[
    {
        "recordid": "GLY_000310_1_735001",
        "row": "[\"Q9Y487-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735002",
        "row": "[\"P04839-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735003",
        "row": "[\"Q9Y5K8-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735004",
        "row": "[\"Q15080-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735005",
        "row": "[\"P36543-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735006",
        "row": "[\"Q8NHE4-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735007",
        "row": "[\"P35228-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735008",
        "row": "[\"P13498-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735009",
        "row": "[\"P21281-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735010",
        "row": "[\"P21283-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735011",
        "row": "[\"Q8NEY4-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735012",
        "row": "[\"P38606-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735013",
        "row": "[\"O15342-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735014",
        "row": "[\"Q16864-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735015",
        "row": "[\"Q9UI12-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735016",
        "row": "[\"Q96A05-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735017",
        "row": "[\"Q96LB4-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735018",
        "row": "[\"P29474-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735019",
        "row": "[\"P29475-1\", \"The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel.\", \"The Biochemical journal\", \"1987 Sep 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2825632\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735020",
        "row": "[\"P49279-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735021",
        "row": "[\"P27449-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735022",
        "row": "[\"O95670-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735023",
        "row": "[\"P61421-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735024",
        "row": "[\"Q9HBG4-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735025",
        "row": "[\"Q96D96-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735026",
        "row": "[\"Q8N8Y2-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735027",
        "row": "[\"Q13488-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735028",
        "row": "[\"P15153-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735029",
        "row": "[\"Q93050-2\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735030",
        "row": "[\"P19878-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735031",
        "row": "[\"Q99437-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735032",
        "row": "[\"P15313-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735033",
        "row": "[\"P14598-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735034",
        "row": "[\"O75348-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735035",
        "row": "[\"Q9Y487-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735036",
        "row": "[\"P04839-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735037",
        "row": "[\"Q9Y5K8-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735038",
        "row": "[\"Q15080-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735039",
        "row": "[\"P36543-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735040",
        "row": "[\"Q8NHE4-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735041",
        "row": "[\"P35228-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735042",
        "row": "[\"P13498-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735043",
        "row": "[\"P21281-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735044",
        "row": "[\"P21283-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735045",
        "row": "[\"Q8NEY4-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735046",
        "row": "[\"P38606-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735047",
        "row": "[\"O15342-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735048",
        "row": "[\"Q16864-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735049",
        "row": "[\"Q9UI12-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735050",
        "row": "[\"Q96A05-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735051",
        "row": "[\"Q96LB4-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735052",
        "row": "[\"P29474-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735053",
        "row": "[\"P29475-1\", \"Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge.\", \"The Biochemical journal\", \"1988 Oct 1\", \"Henderson LM, Chappell JB, Jones OT\", \"protein_xref_pubmed\", \"2848506\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735054",
        "row": "[\"P22079-1\", \"Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome: implications for microbial killing.\", \"The Journal of biological chemistry\", \"2006 Dec 29\", \"Winterbourn CC, Hampton MB, Livesey JH, Kettle AJ\", \"protein_xref_pubmed\", \"17074761\", \"protein_xref_reactome\", \"R-HSA-8941413\"]"
    },
    {
        "recordid": "GLY_000310_1_735055",
        "row": "[\"P05164-1\", \"Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome: implications for microbial killing.\", \"The Journal of biological chemistry\", \"2006 Dec 29\", \"Winterbourn CC, Hampton MB, Livesey JH, Kettle AJ\", \"protein_xref_pubmed\", \"17074761\", \"protein_xref_reactome\", \"R-HSA-8941413\"]"
    },
    {
        "recordid": "GLY_000310_1_735056",
        "row": "[\"P22079-1\", \"Reactions and reactivity of myeloperoxidase-derived oxidants: differential biological effects of hypochlorous and hypothiocyanous acids.\", \"Free radical research\", \"2012 Aug\", \"Pattison DI, Davies MJ, Hawkins CL\", \"protein_xref_pubmed\", \"22348603\", \"protein_xref_reactome\", \"R-HSA-8941413\"]"
    },
    {
        "recordid": "GLY_000310_1_735057",
        "row": "[\"P05164-1\", \"Reactions and reactivity of myeloperoxidase-derived oxidants: differential biological effects of hypochlorous and hypothiocyanous acids.\", \"Free radical research\", \"2012 Aug\", \"Pattison DI, Davies MJ, Hawkins CL\", \"protein_xref_pubmed\", \"22348603\", \"protein_xref_reactome\", \"R-HSA-8941413\"]"
    },
    {
        "recordid": "GLY_000310_1_735058",
        "row": "[\"P49279-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735059",
        "row": "[\"P27449-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735060",
        "row": "[\"O95670-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735061",
        "row": "[\"P61421-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735062",
        "row": "[\"Q9HBG4-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735063",
        "row": "[\"Q96D96-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735064",
        "row": "[\"Q8N8Y2-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735065",
        "row": "[\"Q13488-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735066",
        "row": "[\"P15153-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735067",
        "row": "[\"Q93050-2\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735068",
        "row": "[\"Q99437-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735069",
        "row": "[\"P15313-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735070",
        "row": "[\"O75348-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735071",
        "row": "[\"Q9Y487-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735072",
        "row": "[\"Q9Y5K8-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735073",
        "row": "[\"P36543-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735074",
        "row": "[\"Q8NHE4-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735075",
        "row": "[\"P35228-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735076",
        "row": "[\"P21281-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735077",
        "row": "[\"P21283-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735078",
        "row": "[\"Q8NEY4-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735079",
        "row": "[\"P38606-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735080",
        "row": "[\"O15342-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735081",
        "row": "[\"Q16864-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735082",
        "row": "[\"Q9UI12-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735083",
        "row": "[\"Q96A05-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735084",
        "row": "[\"Q96LB4-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735085",
        "row": "[\"P29474-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735086",
        "row": "[\"P29475-1\", \"NADPH oxidase: an update.\", \"Blood\", \"1999 Mar 1\", \"Babior BM\", \"protein_xref_pubmed\", \"10029572\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735087",
        "row": "[\"P49279-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735088",
        "row": "[\"P27449-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735089",
        "row": "[\"O95670-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735090",
        "row": "[\"P61421-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735091",
        "row": "[\"Q9HBG4-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735092",
        "row": "[\"Q96D96-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735093",
        "row": "[\"Q8N8Y2-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735094",
        "row": "[\"Q13488-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735095",
        "row": "[\"P15153-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735096",
        "row": "[\"Q93050-2\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735097",
        "row": "[\"P19878-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735098",
        "row": "[\"Q99437-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735099",
        "row": "[\"P15313-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735100",
        "row": "[\"P14598-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735101",
        "row": "[\"O75348-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735102",
        "row": "[\"Q9Y487-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735103",
        "row": "[\"P04839-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735104",
        "row": "[\"Q9Y5K8-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735105",
        "row": "[\"Q15080-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735106",
        "row": "[\"P36543-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735107",
        "row": "[\"Q8NHE4-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735108",
        "row": "[\"P35228-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735109",
        "row": "[\"P13498-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735110",
        "row": "[\"P21281-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735111",
        "row": "[\"P21283-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735112",
        "row": "[\"Q8NEY4-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735113",
        "row": "[\"P38606-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735114",
        "row": "[\"O15342-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735115",
        "row": "[\"Q16864-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735116",
        "row": "[\"Q9UI12-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735117",
        "row": "[\"Q96A05-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735118",
        "row": "[\"Q96LB4-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735119",
        "row": "[\"P29474-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735120",
        "row": "[\"P29475-1\", \"Assembly and activation of the neutrophil NADPH oxidase in granule membranes.\", \"Antioxidants &amp; redox signaling\", \"2002 Feb\", \"Karlsson A, Dahlgren C\", \"protein_xref_pubmed\", \"11970843\", \"protein_xref_reactome\", \"R-HSA-1222556\"]"
    },
    {
        "recordid": "GLY_000310_1_735121",
        "row": "[\"P22079-1\", \"X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.\", \"The Journal of biological chemistry\", \"2000 Apr 21\", \"Fiedler TJ, Davey CA, Fenna RE\", \"protein_xref_pubmed\", \"10766826\", \"protein_xref_reactome\", \"R-HSA-8941413\"]"
    },
    {
        "recordid": "GLY_000310_1_735122",
        "row": "[\"P05164-1\", \"X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.\", \"The Journal of biological chemistry\", \"2000 Apr 21\", \"Fiedler TJ, Davey CA, Fenna RE\", \"protein_xref_pubmed\", \"10766826\", \"protein_xref_reactome\", \"R-HSA-8941413\"]"
    },
    {
        "recordid": "GLY_000310_1_735123",
        "row": "[\"P22079-1\", \"Myeloperoxidase-derived oxidation: mechanisms of biological damage and its prevention.\", \"Journal of clinical biochemistry and nutrition\", \"2011 Jan\", \"Davies MJ\", \"protein_xref_pubmed\", \"21297906\", \"protein_xref_reactome\", \"R-HSA-8941413\"]"
    },
    {
        "recordid": "GLY_000310_1_735124",
        "row": "[\"P05164-1\", \"Myeloperoxidase-derived oxidation: mechanisms of biological damage and its prevention.\", \"Journal of clinical biochemistry and nutrition\", \"2011 Jan\", \"Davies MJ\", \"protein_xref_pubmed\", \"21297906\", \"protein_xref_reactome\", \"R-HSA-8941413\"]"
    },
    {
        "recordid": "GLY_000310_1_735125",
        "row": "[\"P22079-1\", \"Myeloperoxidase: a front-line defender against phagocytosed microorganisms.\", \"Journal of leukocyte biology\", \"2013 Feb\", \"Klebanoff SJ, Kettle AJ, Rosen H, Winterbourn CC, Nauseef WM\", \"protein_xref_pubmed\", \"23066164\", \"protein_xref_reactome\", \"R-HSA-8941413\"]"
    },
    {
        "recordid": "GLY_000310_1_735126",
        "row": "[\"P05164-1\", \"Myeloperoxidase: a front-line defender against phagocytosed microorganisms.\", \"Journal of leukocyte biology\", \"2013 Feb\", \"Klebanoff SJ, Kettle AJ, Rosen H, Winterbourn CC, Nauseef WM\", \"protein_xref_pubmed\", \"23066164\", \"protein_xref_reactome\", \"R-HSA-8941413\"]"
    },
    {
        "recordid": "GLY_000310_1_735127",
        "row": "[\"P22079-1\", \"Myeloperoxidase.\", \"Proceedings of the Association of American Physicians\", \"1999 Sep-Oct\", \"Klebanoff SJ\", \"protein_xref_pubmed\", \"10519157\", \"protein_xref_reactome\", \"R-HSA-8941413\"]"
    },
    {
        "recordid": "GLY_000310_1_735128",
        "row": "[\"P05164-1\", \"Myeloperoxidase.\", \"Proceedings of the Association of American Physicians\", \"1999 Sep-Oct\", \"Klebanoff SJ\", \"protein_xref_pubmed\", \"10519157\", \"protein_xref_reactome\", \"R-HSA-8941413\"]"
    },
    {
        "recordid": "GLY_000310_1_735129",
        "row": "[\"P22079-1\", \"Enhanced killing of myeloperoxidase-coated bacteria in the myeloperoxidase-H2O2-Cl- system.\", \"The Journal of infectious diseases\", \"1978 Apr\", \"Selvaraj RJ, Zgliczynski JM, Paul BB, Sbarra AJ\", \"protein_xref_pubmed\", \"206633\", \"protein_xref_reactome\", \"R-HSA-8941413\"]"
    },
    {
        "recordid": "GLY_000310_1_735130",
        "row": "[\"P05164-1\", \"Enhanced killing of myeloperoxidase-coated bacteria in the myeloperoxidase-H2O2-Cl- system.\", \"The Journal of infectious diseases\", \"1978 Apr\", \"Selvaraj RJ, Zgliczynski JM, Paul BB, Sbarra AJ\", \"protein_xref_pubmed\", \"206633\", \"protein_xref_reactome\", \"R-HSA-8941413\"]"
    },
    {
        "recordid": "GLY_000310_1_735131",
        "row": "[\"P22079-1\", \"Role of high-avidity binding of human neutrophil myeloperoxidase in the killing of Actinobacillus actinomycetemcomitans.\", \"Infection and immunity\", \"1987 May\", \"Miyasaki KT, Zambon JJ, Jones CA, Wilson ME\", \"protein_xref_pubmed\", \"3032796\", \"protein_xref_reactome\", \"R-HSA-8941413\"]"
    },
    {
        "recordid": "GLY_000310_1_735132",
        "row": "[\"P05164-1\", \"Role of high-avidity binding of human neutrophil myeloperoxidase in the killing of Actinobacillus actinomycetemcomitans.\", \"Infection and immunity\", \"1987 May\", \"Miyasaki KT, Zambon JJ, Jones CA, Wilson ME\", \"protein_xref_pubmed\", \"3032796\", \"protein_xref_reactome\", \"R-HSA-8941413\"]"
    },
    {
        "recordid": "GLY_000310_1_735133",
        "row": "[\"P30307-1\", \"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase.\", \"The Journal of biological chemistry\", \"2010 Jul 16\", \"Sanchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ\", \"protein_xref_pubmed\", \"20460379\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735134",
        "row": "[\"P31947-1\", \"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase.\", \"The Journal of biological chemistry\", \"2010 Jul 16\", \"Sanchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ\", \"protein_xref_pubmed\", \"20460379\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735135",
        "row": "[\"Q07812-1\", \"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase.\", \"The Journal of biological chemistry\", \"2010 Jul 16\", \"Sanchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ\", \"protein_xref_pubmed\", \"20460379\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735136",
        "row": "[\"Q96PM9-4\", \"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase.\", \"The Journal of biological chemistry\", \"2010 Jul 16\", \"Sanchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ\", \"protein_xref_pubmed\", \"20460379\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735137",
        "row": "[\"P28749-1\", \"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase.\", \"The Journal of biological chemistry\", \"2010 Jul 16\", \"Sanchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ\", \"protein_xref_pubmed\", \"20460379\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735138",
        "row": "[\"Q16254-1\", \"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase.\", \"The Journal of biological chemistry\", \"2010 Jul 16\", \"Sanchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ\", \"protein_xref_pubmed\", \"20460379\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735139",
        "row": "[\"P04637-1\", \"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase.\", \"The Journal of biological chemistry\", \"2010 Jul 16\", \"Sanchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ\", \"protein_xref_pubmed\", \"20460379\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735140",
        "row": "[\"Q09472-1\", \"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase.\", \"The Journal of biological chemistry\", \"2010 Jul 16\", \"Sanchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ\", \"protein_xref_pubmed\", \"20460379\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735141",
        "row": "[\"P12004-1\", \"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase.\", \"The Journal of biological chemistry\", \"2010 Jul 16\", \"Sanchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ\", \"protein_xref_pubmed\", \"20460379\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735142",
        "row": "[\"O14965-1\", \"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase.\", \"The Journal of biological chemistry\", \"2010 Jul 16\", \"Sanchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ\", \"protein_xref_pubmed\", \"20460379\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735143",
        "row": "[\"Q86X55-3\", \"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase.\", \"The Journal of biological chemistry\", \"2010 Jul 16\", \"Sanchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ\", \"protein_xref_pubmed\", \"20460379\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735144",
        "row": "[\"Q14186-1\", \"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase.\", \"The Journal of biological chemistry\", \"2010 Jul 16\", \"Sanchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ\", \"protein_xref_pubmed\", \"20460379\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735145",
        "row": "[\"Q14188-1\", \"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase.\", \"The Journal of biological chemistry\", \"2010 Jul 16\", \"Sanchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ\", \"protein_xref_pubmed\", \"20460379\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735146",
        "row": "[\"Q99873-1\", \"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase.\", \"The Journal of biological chemistry\", \"2010 Jul 16\", \"Sanchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ\", \"protein_xref_pubmed\", \"20460379\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735147",
        "row": "[\"P24522-1\", \"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase.\", \"The Journal of biological chemistry\", \"2010 Jul 16\", \"Sanchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ\", \"protein_xref_pubmed\", \"20460379\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735148",
        "row": "[\"Q08999-1\", \"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase.\", \"The Journal of biological chemistry\", \"2010 Jul 16\", \"Sanchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ\", \"protein_xref_pubmed\", \"20460379\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735149",
        "row": "[\"P14635-1\", \"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase.\", \"The Journal of biological chemistry\", \"2010 Jul 16\", \"Sanchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ\", \"protein_xref_pubmed\", \"20460379\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735150",
        "row": "[\"P06493-1\", \"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase.\", \"The Journal of biological chemistry\", \"2010 Jul 16\", \"Sanchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ\", \"protein_xref_pubmed\", \"20460379\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735151",
        "row": "[\"P30307-1\", \"Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen.\", \"Science (New York, N.Y.)\", \"1994 Nov 25\", \"Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ Jr\", \"protein_xref_pubmed\", \"7973727\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735152",
        "row": "[\"P31947-1\", \"Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen.\", \"Science (New York, N.Y.)\", \"1994 Nov 25\", \"Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ Jr\", \"protein_xref_pubmed\", \"7973727\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735153",
        "row": "[\"Q07812-1\", \"Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen.\", \"Science (New York, N.Y.)\", \"1994 Nov 25\", \"Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ Jr\", \"protein_xref_pubmed\", \"7973727\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735154",
        "row": "[\"Q96PM9-4\", \"Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen.\", \"Science (New York, N.Y.)\", \"1994 Nov 25\", \"Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ Jr\", \"protein_xref_pubmed\", \"7973727\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735155",
        "row": "[\"P28749-1\", \"Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen.\", \"Science (New York, N.Y.)\", \"1994 Nov 25\", \"Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ Jr\", \"protein_xref_pubmed\", \"7973727\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735156",
        "row": "[\"Q16254-1\", \"Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen.\", \"Science (New York, N.Y.)\", \"1994 Nov 25\", \"Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ Jr\", \"protein_xref_pubmed\", \"7973727\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735157",
        "row": "[\"P04637-1\", \"Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen.\", \"Science (New York, N.Y.)\", \"1994 Nov 25\", \"Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ Jr\", \"protein_xref_pubmed\", \"7973727\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735158",
        "row": "[\"Q09472-1\", \"Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen.\", \"Science (New York, N.Y.)\", \"1994 Nov 25\", \"Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ Jr\", \"protein_xref_pubmed\", \"7973727\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735159",
        "row": "[\"P12004-1\", \"Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen.\", \"Science (New York, N.Y.)\", \"1994 Nov 25\", \"Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ Jr\", \"protein_xref_pubmed\", \"7973727\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735160",
        "row": "[\"O14965-1\", \"Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen.\", \"Science (New York, N.Y.)\", \"1994 Nov 25\", \"Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ Jr\", \"protein_xref_pubmed\", \"7973727\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735161",
        "row": "[\"Q86X55-3\", \"Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen.\", \"Science (New York, N.Y.)\", \"1994 Nov 25\", \"Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ Jr\", \"protein_xref_pubmed\", \"7973727\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735162",
        "row": "[\"Q14186-1\", \"Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen.\", \"Science (New York, N.Y.)\", \"1994 Nov 25\", \"Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ Jr\", \"protein_xref_pubmed\", \"7973727\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735163",
        "row": "[\"Q14188-1\", \"Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen.\", \"Science (New York, N.Y.)\", \"1994 Nov 25\", \"Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ Jr\", \"protein_xref_pubmed\", \"7973727\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735164",
        "row": "[\"Q99873-1\", \"Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen.\", \"Science (New York, N.Y.)\", \"1994 Nov 25\", \"Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ Jr\", \"protein_xref_pubmed\", \"7973727\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735165",
        "row": "[\"P24522-1\", \"Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen.\", \"Science (New York, N.Y.)\", \"1994 Nov 25\", \"Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ Jr\", \"protein_xref_pubmed\", \"7973727\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735166",
        "row": "[\"Q08999-1\", \"Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen.\", \"Science (New York, N.Y.)\", \"1994 Nov 25\", \"Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ Jr\", \"protein_xref_pubmed\", \"7973727\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735167",
        "row": "[\"P14635-1\", \"Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen.\", \"Science (New York, N.Y.)\", \"1994 Nov 25\", \"Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ Jr\", \"protein_xref_pubmed\", \"7973727\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735168",
        "row": "[\"P06493-1\", \"Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen.\", \"Science (New York, N.Y.)\", \"1994 Nov 25\", \"Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ Jr\", \"protein_xref_pubmed\", \"7973727\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735169",
        "row": "[\"P30307-1\", \"A novel role for Gadd45alpha in base excision repair: modulation of APE1 activity by the direct interaction of Gadd45alpha with PCNA.\", \"Biochemical and biophysical research communications\", \"2013 May 3\", \"Kim HL, Kim SU, Seo YR\", \"protein_xref_pubmed\", \"23485469\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735170",
        "row": "[\"P31947-1\", \"A novel role for Gadd45alpha in base excision repair: modulation of APE1 activity by the direct interaction of Gadd45alpha with PCNA.\", \"Biochemical and biophysical research communications\", \"2013 May 3\", \"Kim HL, Kim SU, Seo YR\", \"protein_xref_pubmed\", \"23485469\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735171",
        "row": "[\"Q07812-1\", \"A novel role for Gadd45alpha in base excision repair: modulation of APE1 activity by the direct interaction of Gadd45alpha with PCNA.\", \"Biochemical and biophysical research communications\", \"2013 May 3\", \"Kim HL, Kim SU, Seo YR\", \"protein_xref_pubmed\", \"23485469\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735172",
        "row": "[\"Q96PM9-4\", \"A novel role for Gadd45alpha in base excision repair: modulation of APE1 activity by the direct interaction of Gadd45alpha with PCNA.\", \"Biochemical and biophysical research communications\", \"2013 May 3\", \"Kim HL, Kim SU, Seo YR\", \"protein_xref_pubmed\", \"23485469\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735173",
        "row": "[\"P28749-1\", \"A novel role for Gadd45alpha in base excision repair: modulation of APE1 activity by the direct interaction of Gadd45alpha with PCNA.\", \"Biochemical and biophysical research communications\", \"2013 May 3\", \"Kim HL, Kim SU, Seo YR\", \"protein_xref_pubmed\", \"23485469\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735174",
        "row": "[\"Q16254-1\", \"A novel role for Gadd45alpha in base excision repair: modulation of APE1 activity by the direct interaction of Gadd45alpha with PCNA.\", \"Biochemical and biophysical research communications\", \"2013 May 3\", \"Kim HL, Kim SU, Seo YR\", \"protein_xref_pubmed\", \"23485469\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735175",
        "row": "[\"P04637-1\", \"A novel role for Gadd45alpha in base excision repair: modulation of APE1 activity by the direct interaction of Gadd45alpha with PCNA.\", \"Biochemical and biophysical research communications\", \"2013 May 3\", \"Kim HL, Kim SU, Seo YR\", \"protein_xref_pubmed\", \"23485469\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735176",
        "row": "[\"Q09472-1\", \"A novel role for Gadd45alpha in base excision repair: modulation of APE1 activity by the direct interaction of Gadd45alpha with PCNA.\", \"Biochemical and biophysical research communications\", \"2013 May 3\", \"Kim HL, Kim SU, Seo YR\", \"protein_xref_pubmed\", \"23485469\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735177",
        "row": "[\"P12004-1\", \"A novel role for Gadd45alpha in base excision repair: modulation of APE1 activity by the direct interaction of Gadd45alpha with PCNA.\", \"Biochemical and biophysical research communications\", \"2013 May 3\", \"Kim HL, Kim SU, Seo YR\", \"protein_xref_pubmed\", \"23485469\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735178",
        "row": "[\"O14965-1\", \"A novel role for Gadd45alpha in base excision repair: modulation of APE1 activity by the direct interaction of Gadd45alpha with PCNA.\", \"Biochemical and biophysical research communications\", \"2013 May 3\", \"Kim HL, Kim SU, Seo YR\", \"protein_xref_pubmed\", \"23485469\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735179",
        "row": "[\"Q86X55-3\", \"A novel role for Gadd45alpha in base excision repair: modulation of APE1 activity by the direct interaction of Gadd45alpha with PCNA.\", \"Biochemical and biophysical research communications\", \"2013 May 3\", \"Kim HL, Kim SU, Seo YR\", \"protein_xref_pubmed\", \"23485469\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735180",
        "row": "[\"Q14186-1\", \"A novel role for Gadd45alpha in base excision repair: modulation of APE1 activity by the direct interaction of Gadd45alpha with PCNA.\", \"Biochemical and biophysical research communications\", \"2013 May 3\", \"Kim HL, Kim SU, Seo YR\", \"protein_xref_pubmed\", \"23485469\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735181",
        "row": "[\"Q14188-1\", \"A novel role for Gadd45alpha in base excision repair: modulation of APE1 activity by the direct interaction of Gadd45alpha with PCNA.\", \"Biochemical and biophysical research communications\", \"2013 May 3\", \"Kim HL, Kim SU, Seo YR\", \"protein_xref_pubmed\", \"23485469\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735182",
        "row": "[\"Q99873-1\", \"A novel role for Gadd45alpha in base excision repair: modulation of APE1 activity by the direct interaction of Gadd45alpha with PCNA.\", \"Biochemical and biophysical research communications\", \"2013 May 3\", \"Kim HL, Kim SU, Seo YR\", \"protein_xref_pubmed\", \"23485469\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735183",
        "row": "[\"P24522-1\", \"A novel role for Gadd45alpha in base excision repair: modulation of APE1 activity by the direct interaction of Gadd45alpha with PCNA.\", \"Biochemical and biophysical research communications\", \"2013 May 3\", \"Kim HL, Kim SU, Seo YR\", \"protein_xref_pubmed\", \"23485469\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735184",
        "row": "[\"Q08999-1\", \"A novel role for Gadd45alpha in base excision repair: modulation of APE1 activity by the direct interaction of Gadd45alpha with PCNA.\", \"Biochemical and biophysical research communications\", \"2013 May 3\", \"Kim HL, Kim SU, Seo YR\", \"protein_xref_pubmed\", \"23485469\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735185",
        "row": "[\"P14635-1\", \"A novel role for Gadd45alpha in base excision repair: modulation of APE1 activity by the direct interaction of Gadd45alpha with PCNA.\", \"Biochemical and biophysical research communications\", \"2013 May 3\", \"Kim HL, Kim SU, Seo YR\", \"protein_xref_pubmed\", \"23485469\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735186",
        "row": "[\"P06493-1\", \"A novel role for Gadd45alpha in base excision repair: modulation of APE1 activity by the direct interaction of Gadd45alpha with PCNA.\", \"Biochemical and biophysical research communications\", \"2013 May 3\", \"Kim HL, Kim SU, Seo YR\", \"protein_xref_pubmed\", \"23485469\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735187",
        "row": "[\"P30307-1\", \"Characterisation of the interaction between PCNA and Gadd45.\", \"Oncogene\", \"1995 Jun 15\", \"Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS\", \"protein_xref_pubmed\", \"7784094\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735188",
        "row": "[\"P31947-1\", \"Characterisation of the interaction between PCNA and Gadd45.\", \"Oncogene\", \"1995 Jun 15\", \"Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS\", \"protein_xref_pubmed\", \"7784094\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735189",
        "row": "[\"Q07812-1\", \"Characterisation of the interaction between PCNA and Gadd45.\", \"Oncogene\", \"1995 Jun 15\", \"Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS\", \"protein_xref_pubmed\", \"7784094\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735190",
        "row": "[\"Q96PM9-4\", \"Characterisation of the interaction between PCNA and Gadd45.\", \"Oncogene\", \"1995 Jun 15\", \"Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS\", \"protein_xref_pubmed\", \"7784094\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735191",
        "row": "[\"P28749-1\", \"Characterisation of the interaction between PCNA and Gadd45.\", \"Oncogene\", \"1995 Jun 15\", \"Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS\", \"protein_xref_pubmed\", \"7784094\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735192",
        "row": "[\"Q16254-1\", \"Characterisation of the interaction between PCNA and Gadd45.\", \"Oncogene\", \"1995 Jun 15\", \"Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS\", \"protein_xref_pubmed\", \"7784094\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735193",
        "row": "[\"P04637-1\", \"Characterisation of the interaction between PCNA and Gadd45.\", \"Oncogene\", \"1995 Jun 15\", \"Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS\", \"protein_xref_pubmed\", \"7784094\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735194",
        "row": "[\"Q09472-1\", \"Characterisation of the interaction between PCNA and Gadd45.\", \"Oncogene\", \"1995 Jun 15\", \"Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS\", \"protein_xref_pubmed\", \"7784094\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735195",
        "row": "[\"P12004-1\", \"Characterisation of the interaction between PCNA and Gadd45.\", \"Oncogene\", \"1995 Jun 15\", \"Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS\", \"protein_xref_pubmed\", \"7784094\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735196",
        "row": "[\"O14965-1\", \"Characterisation of the interaction between PCNA and Gadd45.\", \"Oncogene\", \"1995 Jun 15\", \"Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS\", \"protein_xref_pubmed\", \"7784094\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735197",
        "row": "[\"Q86X55-3\", \"Characterisation of the interaction between PCNA and Gadd45.\", \"Oncogene\", \"1995 Jun 15\", \"Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS\", \"protein_xref_pubmed\", \"7784094\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735198",
        "row": "[\"Q14186-1\", \"Characterisation of the interaction between PCNA and Gadd45.\", \"Oncogene\", \"1995 Jun 15\", \"Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS\", \"protein_xref_pubmed\", \"7784094\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735199",
        "row": "[\"Q14188-1\", \"Characterisation of the interaction between PCNA and Gadd45.\", \"Oncogene\", \"1995 Jun 15\", \"Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS\", \"protein_xref_pubmed\", \"7784094\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735200",
        "row": "[\"Q99873-1\", \"Characterisation of the interaction between PCNA and Gadd45.\", \"Oncogene\", \"1995 Jun 15\", \"Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS\", \"protein_xref_pubmed\", \"7784094\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735201",
        "row": "[\"P24522-1\", \"Characterisation of the interaction between PCNA and Gadd45.\", \"Oncogene\", \"1995 Jun 15\", \"Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS\", \"protein_xref_pubmed\", \"7784094\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735202",
        "row": "[\"Q08999-1\", \"Characterisation of the interaction between PCNA and Gadd45.\", \"Oncogene\", \"1995 Jun 15\", \"Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS\", \"protein_xref_pubmed\", \"7784094\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735203",
        "row": "[\"P14635-1\", \"Characterisation of the interaction between PCNA and Gadd45.\", \"Oncogene\", \"1995 Jun 15\", \"Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS\", \"protein_xref_pubmed\", \"7784094\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735204",
        "row": "[\"P06493-1\", \"Characterisation of the interaction between PCNA and Gadd45.\", \"Oncogene\", \"1995 Jun 15\", \"Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS\", \"protein_xref_pubmed\", \"7784094\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735205",
        "row": "[\"P30307-1\", \"Gadd45a interacts with aurora-A and inhibits its kinase activity.\", \"The Journal of biological chemistry\", \"2006 Sep 29\", \"Shao S, Wang Y, Jin S, Song Y, Wang X, Fan W, Zhao Z, Fu M, Tong T, Dong L, Fan F, Xu N, Zhan Q\", \"protein_xref_pubmed\", \"16772293\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735206",
        "row": "[\"P31947-1\", \"Gadd45a interacts with aurora-A and inhibits its kinase activity.\", \"The Journal of biological chemistry\", \"2006 Sep 29\", \"Shao S, Wang Y, Jin S, Song Y, Wang X, Fan W, Zhao Z, Fu M, Tong T, Dong L, Fan F, Xu N, Zhan Q\", \"protein_xref_pubmed\", \"16772293\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735207",
        "row": "[\"Q07812-1\", \"Gadd45a interacts with aurora-A and inhibits its kinase activity.\", \"The Journal of biological chemistry\", \"2006 Sep 29\", \"Shao S, Wang Y, Jin S, Song Y, Wang X, Fan W, Zhao Z, Fu M, Tong T, Dong L, Fan F, Xu N, Zhan Q\", \"protein_xref_pubmed\", \"16772293\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735208",
        "row": "[\"Q96PM9-4\", \"Gadd45a interacts with aurora-A and inhibits its kinase activity.\", \"The Journal of biological chemistry\", \"2006 Sep 29\", \"Shao S, Wang Y, Jin S, Song Y, Wang X, Fan W, Zhao Z, Fu M, Tong T, Dong L, Fan F, Xu N, Zhan Q\", \"protein_xref_pubmed\", \"16772293\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735209",
        "row": "[\"P28749-1\", \"Gadd45a interacts with aurora-A and inhibits its kinase activity.\", \"The Journal of biological chemistry\", \"2006 Sep 29\", \"Shao S, Wang Y, Jin S, Song Y, Wang X, Fan W, Zhao Z, Fu M, Tong T, Dong L, Fan F, Xu N, Zhan Q\", \"protein_xref_pubmed\", \"16772293\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735210",
        "row": "[\"Q16254-1\", \"Gadd45a interacts with aurora-A and inhibits its kinase activity.\", \"The Journal of biological chemistry\", \"2006 Sep 29\", \"Shao S, Wang Y, Jin S, Song Y, Wang X, Fan W, Zhao Z, Fu M, Tong T, Dong L, Fan F, Xu N, Zhan Q\", \"protein_xref_pubmed\", \"16772293\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735211",
        "row": "[\"P04637-1\", \"Gadd45a interacts with aurora-A and inhibits its kinase activity.\", \"The Journal of biological chemistry\", \"2006 Sep 29\", \"Shao S, Wang Y, Jin S, Song Y, Wang X, Fan W, Zhao Z, Fu M, Tong T, Dong L, Fan F, Xu N, Zhan Q\", \"protein_xref_pubmed\", \"16772293\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735212",
        "row": "[\"Q09472-1\", \"Gadd45a interacts with aurora-A and inhibits its kinase activity.\", \"The Journal of biological chemistry\", \"2006 Sep 29\", \"Shao S, Wang Y, Jin S, Song Y, Wang X, Fan W, Zhao Z, Fu M, Tong T, Dong L, Fan F, Xu N, Zhan Q\", \"protein_xref_pubmed\", \"16772293\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735213",
        "row": "[\"P12004-1\", \"Gadd45a interacts with aurora-A and inhibits its kinase activity.\", \"The Journal of biological chemistry\", \"2006 Sep 29\", \"Shao S, Wang Y, Jin S, Song Y, Wang X, Fan W, Zhao Z, Fu M, Tong T, Dong L, Fan F, Xu N, Zhan Q\", \"protein_xref_pubmed\", \"16772293\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735214",
        "row": "[\"O14965-1\", \"Gadd45a interacts with aurora-A and inhibits its kinase activity.\", \"The Journal of biological chemistry\", \"2006 Sep 29\", \"Shao S, Wang Y, Jin S, Song Y, Wang X, Fan W, Zhao Z, Fu M, Tong T, Dong L, Fan F, Xu N, Zhan Q\", \"protein_xref_pubmed\", \"16772293\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735215",
        "row": "[\"Q86X55-3\", \"Gadd45a interacts with aurora-A and inhibits its kinase activity.\", \"The Journal of biological chemistry\", \"2006 Sep 29\", \"Shao S, Wang Y, Jin S, Song Y, Wang X, Fan W, Zhao Z, Fu M, Tong T, Dong L, Fan F, Xu N, Zhan Q\", \"protein_xref_pubmed\", \"16772293\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735216",
        "row": "[\"Q14186-1\", \"Gadd45a interacts with aurora-A and inhibits its kinase activity.\", \"The Journal of biological chemistry\", \"2006 Sep 29\", \"Shao S, Wang Y, Jin S, Song Y, Wang X, Fan W, Zhao Z, Fu M, Tong T, Dong L, Fan F, Xu N, Zhan Q\", \"protein_xref_pubmed\", \"16772293\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735217",
        "row": "[\"Q14188-1\", \"Gadd45a interacts with aurora-A and inhibits its kinase activity.\", \"The Journal of biological chemistry\", \"2006 Sep 29\", \"Shao S, Wang Y, Jin S, Song Y, Wang X, Fan W, Zhao Z, Fu M, Tong T, Dong L, Fan F, Xu N, Zhan Q\", \"protein_xref_pubmed\", \"16772293\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735218",
        "row": "[\"Q99873-1\", \"Gadd45a interacts with aurora-A and inhibits its kinase activity.\", \"The Journal of biological chemistry\", \"2006 Sep 29\", \"Shao S, Wang Y, Jin S, Song Y, Wang X, Fan W, Zhao Z, Fu M, Tong T, Dong L, Fan F, Xu N, Zhan Q\", \"protein_xref_pubmed\", \"16772293\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735219",
        "row": "[\"P24522-1\", \"Gadd45a interacts with aurora-A and inhibits its kinase activity.\", \"The Journal of biological chemistry\", \"2006 Sep 29\", \"Shao S, Wang Y, Jin S, Song Y, Wang X, Fan W, Zhao Z, Fu M, Tong T, Dong L, Fan F, Xu N, Zhan Q\", \"protein_xref_pubmed\", \"16772293\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735220",
        "row": "[\"Q08999-1\", \"Gadd45a interacts with aurora-A and inhibits its kinase activity.\", \"The Journal of biological chemistry\", \"2006 Sep 29\", \"Shao S, Wang Y, Jin S, Song Y, Wang X, Fan W, Zhao Z, Fu M, Tong T, Dong L, Fan F, Xu N, Zhan Q\", \"protein_xref_pubmed\", \"16772293\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735221",
        "row": "[\"P14635-1\", \"Gadd45a interacts with aurora-A and inhibits its kinase activity.\", \"The Journal of biological chemistry\", \"2006 Sep 29\", \"Shao S, Wang Y, Jin S, Song Y, Wang X, Fan W, Zhao Z, Fu M, Tong T, Dong L, Fan F, Xu N, Zhan Q\", \"protein_xref_pubmed\", \"16772293\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735222",
        "row": "[\"P06493-1\", \"Gadd45a interacts with aurora-A and inhibits its kinase activity.\", \"The Journal of biological chemistry\", \"2006 Sep 29\", \"Shao S, Wang Y, Jin S, Song Y, Wang X, Fan W, Zhao Z, Fu M, Tong T, Dong L, Fan F, Xu N, Zhan Q\", \"protein_xref_pubmed\", \"16772293\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735223",
        "row": "[\"Q13625-1\", \"Bcl-G, a novel pro-apoptotic member of the Bcl-2 family.\", \"The Journal of biological chemistry\", \"2001 Jan 26\", \"Guo B, Godzik A, Reed JC\", \"protein_xref_pubmed\", \"11054413\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735224",
        "row": "[\"Q96FX8-1\", \"Bcl-G, a novel pro-apoptotic member of the Bcl-2 family.\", \"The Journal of biological chemistry\", \"2001 Jan 26\", \"Guo B, Godzik A, Reed JC\", \"protein_xref_pubmed\", \"11054413\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735225",
        "row": "[\"Q53FA7-1\", \"Bcl-G, a novel pro-apoptotic member of the Bcl-2 family.\", \"The Journal of biological chemistry\", \"2001 Jan 26\", \"Guo B, Godzik A, Reed JC\", \"protein_xref_pubmed\", \"11054413\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735226",
        "row": "[\"Q92696-1\", \"Bcl-G, a novel pro-apoptotic member of the Bcl-2 family.\", \"The Journal of biological chemistry\", \"2001 Jan 26\", \"Guo B, Godzik A, Reed JC\", \"protein_xref_pubmed\", \"11054413\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735227",
        "row": "[\"P53611-1\", \"Bcl-G, a novel pro-apoptotic member of the Bcl-2 family.\", \"The Journal of biological chemistry\", \"2001 Jan 26\", \"Guo B, Godzik A, Reed JC\", \"protein_xref_pubmed\", \"11054413\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735228",
        "row": "[\"P41182-1\", \"Bcl-G, a novel pro-apoptotic member of the Bcl-2 family.\", \"The Journal of biological chemistry\", \"2001 Jan 26\", \"Guo B, Godzik A, Reed JC\", \"protein_xref_pubmed\", \"11054413\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735229",
        "row": "[\"P04637-1\", \"Bcl-G, a novel pro-apoptotic member of the Bcl-2 family.\", \"The Journal of biological chemistry\", \"2001 Jan 26\", \"Guo B, Godzik A, Reed JC\", \"protein_xref_pubmed\", \"11054413\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735230",
        "row": "[\"Q9H3D4-1\", \"Bcl-G, a novel pro-apoptotic member of the Bcl-2 family.\", \"The Journal of biological chemistry\", \"2001 Jan 26\", \"Guo B, Godzik A, Reed JC\", \"protein_xref_pubmed\", \"11054413\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735231",
        "row": "[\"Q92597-1\", \"Bcl-G, a novel pro-apoptotic member of the Bcl-2 family.\", \"The Journal of biological chemistry\", \"2001 Jan 26\", \"Guo B, Godzik A, Reed JC\", \"protein_xref_pubmed\", \"11054413\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735232",
        "row": "[\"O15392-1\", \"Bcl-G, a novel pro-apoptotic member of the Bcl-2 family.\", \"The Journal of biological chemistry\", \"2001 Jan 26\", \"Guo B, Godzik A, Reed JC\", \"protein_xref_pubmed\", \"11054413\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735233",
        "row": "[\"Q9BZR8-1\", \"Bcl-G, a novel pro-apoptotic member of the Bcl-2 family.\", \"The Journal of biological chemistry\", \"2001 Jan 26\", \"Guo B, Godzik A, Reed JC\", \"protein_xref_pubmed\", \"11054413\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735234",
        "row": "[\"Q96KQ4-1\", \"Bcl-G, a novel pro-apoptotic member of the Bcl-2 family.\", \"The Journal of biological chemistry\", \"2001 Jan 26\", \"Guo B, Godzik A, Reed JC\", \"protein_xref_pubmed\", \"11054413\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735235",
        "row": "[\"O15350-1\", \"Bcl-G, a novel pro-apoptotic member of the Bcl-2 family.\", \"The Journal of biological chemistry\", \"2001 Jan 26\", \"Guo B, Godzik A, Reed JC\", \"protein_xref_pubmed\", \"11054413\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735236",
        "row": "[\"P24386-1\", \"Bcl-G, a novel pro-apoptotic member of the Bcl-2 family.\", \"The Journal of biological chemistry\", \"2001 Jan 26\", \"Guo B, Godzik A, Reed JC\", \"protein_xref_pubmed\", \"11054413\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735237",
        "row": "[\"Q13625-1\", \"A genomic map of p53 binding sites identifies novel p53 targets involved in an apoptotic network.\", \"Cancer research\", \"2005 Jun 15\", \"Miled C, Pontoglio M, Garbay S, Yaniv M, Weitzman JB\", \"protein_xref_pubmed\", \"15958553\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735238",
        "row": "[\"Q96FX8-1\", \"A genomic map of p53 binding sites identifies novel p53 targets involved in an apoptotic network.\", \"Cancer research\", \"2005 Jun 15\", \"Miled C, Pontoglio M, Garbay S, Yaniv M, Weitzman JB\", \"protein_xref_pubmed\", \"15958553\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735239",
        "row": "[\"Q53FA7-1\", \"A genomic map of p53 binding sites identifies novel p53 targets involved in an apoptotic network.\", \"Cancer research\", \"2005 Jun 15\", \"Miled C, Pontoglio M, Garbay S, Yaniv M, Weitzman JB\", \"protein_xref_pubmed\", \"15958553\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735240",
        "row": "[\"Q92696-1\", \"A genomic map of p53 binding sites identifies novel p53 targets involved in an apoptotic network.\", \"Cancer research\", \"2005 Jun 15\", \"Miled C, Pontoglio M, Garbay S, Yaniv M, Weitzman JB\", \"protein_xref_pubmed\", \"15958553\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735241",
        "row": "[\"P53611-1\", \"A genomic map of p53 binding sites identifies novel p53 targets involved in an apoptotic network.\", \"Cancer research\", \"2005 Jun 15\", \"Miled C, Pontoglio M, Garbay S, Yaniv M, Weitzman JB\", \"protein_xref_pubmed\", \"15958553\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735242",
        "row": "[\"P41182-1\", \"A genomic map of p53 binding sites identifies novel p53 targets involved in an apoptotic network.\", \"Cancer research\", \"2005 Jun 15\", \"Miled C, Pontoglio M, Garbay S, Yaniv M, Weitzman JB\", \"protein_xref_pubmed\", \"15958553\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735243",
        "row": "[\"P04637-1\", \"A genomic map of p53 binding sites identifies novel p53 targets involved in an apoptotic network.\", \"Cancer research\", \"2005 Jun 15\", \"Miled C, Pontoglio M, Garbay S, Yaniv M, Weitzman JB\", \"protein_xref_pubmed\", \"15958553\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735244",
        "row": "[\"Q9H3D4-1\", \"A genomic map of p53 binding sites identifies novel p53 targets involved in an apoptotic network.\", \"Cancer research\", \"2005 Jun 15\", \"Miled C, Pontoglio M, Garbay S, Yaniv M, Weitzman JB\", \"protein_xref_pubmed\", \"15958553\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735245",
        "row": "[\"Q92597-1\", \"A genomic map of p53 binding sites identifies novel p53 targets involved in an apoptotic network.\", \"Cancer research\", \"2005 Jun 15\", \"Miled C, Pontoglio M, Garbay S, Yaniv M, Weitzman JB\", \"protein_xref_pubmed\", \"15958553\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735246",
        "row": "[\"O15392-1\", \"A genomic map of p53 binding sites identifies novel p53 targets involved in an apoptotic network.\", \"Cancer research\", \"2005 Jun 15\", \"Miled C, Pontoglio M, Garbay S, Yaniv M, Weitzman JB\", \"protein_xref_pubmed\", \"15958553\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735247",
        "row": "[\"Q9BZR8-1\", \"A genomic map of p53 binding sites identifies novel p53 targets involved in an apoptotic network.\", \"Cancer research\", \"2005 Jun 15\", \"Miled C, Pontoglio M, Garbay S, Yaniv M, Weitzman JB\", \"protein_xref_pubmed\", \"15958553\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735248",
        "row": "[\"Q96KQ4-1\", \"A genomic map of p53 binding sites identifies novel p53 targets involved in an apoptotic network.\", \"Cancer research\", \"2005 Jun 15\", \"Miled C, Pontoglio M, Garbay S, Yaniv M, Weitzman JB\", \"protein_xref_pubmed\", \"15958553\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735249",
        "row": "[\"O15350-1\", \"A genomic map of p53 binding sites identifies novel p53 targets involved in an apoptotic network.\", \"Cancer research\", \"2005 Jun 15\", \"Miled C, Pontoglio M, Garbay S, Yaniv M, Weitzman JB\", \"protein_xref_pubmed\", \"15958553\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735250",
        "row": "[\"P24386-1\", \"A genomic map of p53 binding sites identifies novel p53 targets involved in an apoptotic network.\", \"Cancer research\", \"2005 Jun 15\", \"Miled C, Pontoglio M, Garbay S, Yaniv M, Weitzman JB\", \"protein_xref_pubmed\", \"15958553\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735251",
        "row": "[\"Q13625-1\", \"Bcl-2 family member Bcl-G is not a proapoptotic protein.\", \"Cell death &amp; disease\", \"2012 Oct 11\", \"Giam M, Okamoto T, Mintern JD, Strasser A, Bouillet P\", \"protein_xref_pubmed\", \"23059823\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735252",
        "row": "[\"Q96FX8-1\", \"Bcl-2 family member Bcl-G is not a proapoptotic protein.\", \"Cell death &amp; disease\", \"2012 Oct 11\", \"Giam M, Okamoto T, Mintern JD, Strasser A, Bouillet P\", \"protein_xref_pubmed\", \"23059823\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735253",
        "row": "[\"Q53FA7-1\", \"Bcl-2 family member Bcl-G is not a proapoptotic protein.\", \"Cell death &amp; disease\", \"2012 Oct 11\", \"Giam M, Okamoto T, Mintern JD, Strasser A, Bouillet P\", \"protein_xref_pubmed\", \"23059823\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735254",
        "row": "[\"Q92696-1\", \"Bcl-2 family member Bcl-G is not a proapoptotic protein.\", \"Cell death &amp; disease\", \"2012 Oct 11\", \"Giam M, Okamoto T, Mintern JD, Strasser A, Bouillet P\", \"protein_xref_pubmed\", \"23059823\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735255",
        "row": "[\"P53611-1\", \"Bcl-2 family member Bcl-G is not a proapoptotic protein.\", \"Cell death &amp; disease\", \"2012 Oct 11\", \"Giam M, Okamoto T, Mintern JD, Strasser A, Bouillet P\", \"protein_xref_pubmed\", \"23059823\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735256",
        "row": "[\"P41182-1\", \"Bcl-2 family member Bcl-G is not a proapoptotic protein.\", \"Cell death &amp; disease\", \"2012 Oct 11\", \"Giam M, Okamoto T, Mintern JD, Strasser A, Bouillet P\", \"protein_xref_pubmed\", \"23059823\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735257",
        "row": "[\"P04637-1\", \"Bcl-2 family member Bcl-G is not a proapoptotic protein.\", \"Cell death &amp; disease\", \"2012 Oct 11\", \"Giam M, Okamoto T, Mintern JD, Strasser A, Bouillet P\", \"protein_xref_pubmed\", \"23059823\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735258",
        "row": "[\"Q9H3D4-1\", \"Bcl-2 family member Bcl-G is not a proapoptotic protein.\", \"Cell death &amp; disease\", \"2012 Oct 11\", \"Giam M, Okamoto T, Mintern JD, Strasser A, Bouillet P\", \"protein_xref_pubmed\", \"23059823\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735259",
        "row": "[\"Q92597-1\", \"Bcl-2 family member Bcl-G is not a proapoptotic protein.\", \"Cell death &amp; disease\", \"2012 Oct 11\", \"Giam M, Okamoto T, Mintern JD, Strasser A, Bouillet P\", \"protein_xref_pubmed\", \"23059823\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735260",
        "row": "[\"O15392-1\", \"Bcl-2 family member Bcl-G is not a proapoptotic protein.\", \"Cell death &amp; disease\", \"2012 Oct 11\", \"Giam M, Okamoto T, Mintern JD, Strasser A, Bouillet P\", \"protein_xref_pubmed\", \"23059823\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735261",
        "row": "[\"Q9BZR8-1\", \"Bcl-2 family member Bcl-G is not a proapoptotic protein.\", \"Cell death &amp; disease\", \"2012 Oct 11\", \"Giam M, Okamoto T, Mintern JD, Strasser A, Bouillet P\", \"protein_xref_pubmed\", \"23059823\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735262",
        "row": "[\"Q96KQ4-1\", \"Bcl-2 family member Bcl-G is not a proapoptotic protein.\", \"Cell death &amp; disease\", \"2012 Oct 11\", \"Giam M, Okamoto T, Mintern JD, Strasser A, Bouillet P\", \"protein_xref_pubmed\", \"23059823\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735263",
        "row": "[\"O15350-1\", \"Bcl-2 family member Bcl-G is not a proapoptotic protein.\", \"Cell death &amp; disease\", \"2012 Oct 11\", \"Giam M, Okamoto T, Mintern JD, Strasser A, Bouillet P\", \"protein_xref_pubmed\", \"23059823\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735264",
        "row": "[\"P24386-1\", \"Bcl-2 family member Bcl-G is not a proapoptotic protein.\", \"Cell death &amp; disease\", \"2012 Oct 11\", \"Giam M, Okamoto T, Mintern JD, Strasser A, Bouillet P\", \"protein_xref_pubmed\", \"23059823\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735265",
        "row": "[\"Q92851-1\", \"Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis.\", \"The EMBO journal\", \"1999 Jul 1\", \"Hu Y, Benedict MA, Ding L, Nunez G\", \"protein_xref_pubmed\", \"10393175\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735266",
        "row": "[\"O14727-1\", \"Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis.\", \"The EMBO journal\", \"1999 Jul 1\", \"Hu Y, Benedict MA, Ding L, Nunez G\", \"protein_xref_pubmed\", \"10393175\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735267",
        "row": "[\"Q9NPP4-1\", \"Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis.\", \"The EMBO journal\", \"1999 Jul 1\", \"Hu Y, Benedict MA, Ding L, Nunez G\", \"protein_xref_pubmed\", \"10393175\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735268",
        "row": "[\"P04637-1\", \"Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis.\", \"The EMBO journal\", \"1999 Jul 1\", \"Hu Y, Benedict MA, Ding L, Nunez G\", \"protein_xref_pubmed\", \"10393175\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735269",
        "row": "[\"P55212-1\", \"Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis.\", \"The EMBO journal\", \"1999 Jul 1\", \"Hu Y, Benedict MA, Ding L, Nunez G\", \"protein_xref_pubmed\", \"10393175\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735270",
        "row": "[\"Q9H3D4-1\", \"Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis.\", \"The EMBO journal\", \"1999 Jul 1\", \"Hu Y, Benedict MA, Ding L, Nunez G\", \"protein_xref_pubmed\", \"10393175\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735271",
        "row": "[\"P42575-1\", \"Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis.\", \"The EMBO journal\", \"1999 Jul 1\", \"Hu Y, Benedict MA, Ding L, Nunez G\", \"protein_xref_pubmed\", \"10393175\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735272",
        "row": "[\"O15350-1\", \"Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis.\", \"The EMBO journal\", \"1999 Jul 1\", \"Hu Y, Benedict MA, Ding L, Nunez G\", \"protein_xref_pubmed\", \"10393175\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735273",
        "row": "[\"Q13315-1\", \"Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis.\", \"The EMBO journal\", \"1999 Jul 1\", \"Hu Y, Benedict MA, Ding L, Nunez G\", \"protein_xref_pubmed\", \"10393175\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735274",
        "row": "[\"P78560-1\", \"Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis.\", \"The EMBO journal\", \"1999 Jul 1\", \"Hu Y, Benedict MA, Ding L, Nunez G\", \"protein_xref_pubmed\", \"10393175\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735275",
        "row": "[\"P29466-1\", \"Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis.\", \"The EMBO journal\", \"1999 Jul 1\", \"Hu Y, Benedict MA, Ding L, Nunez G\", \"protein_xref_pubmed\", \"10393175\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735276",
        "row": "[\"Q9HB75-1\", \"Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis.\", \"The EMBO journal\", \"1999 Jul 1\", \"Hu Y, Benedict MA, Ding L, Nunez G\", \"protein_xref_pubmed\", \"10393175\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735277",
        "row": "[\"Q92851-1\", \"APAF-1 is a transcriptional target of p53 in DNA damage-induced apoptosis.\", \"Cancer research\", \"2001 Sep 15\", \"Robles AI, Bemmels NA, Foraker AB, Harris CC\", \"protein_xref_pubmed\", \"11559530\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735278",
        "row": "[\"O14727-1\", \"APAF-1 is a transcriptional target of p53 in DNA damage-induced apoptosis.\", \"Cancer research\", \"2001 Sep 15\", \"Robles AI, Bemmels NA, Foraker AB, Harris CC\", \"protein_xref_pubmed\", \"11559530\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735279",
        "row": "[\"Q9NPP4-1\", \"APAF-1 is a transcriptional target of p53 in DNA damage-induced apoptosis.\", \"Cancer research\", \"2001 Sep 15\", \"Robles AI, Bemmels NA, Foraker AB, Harris CC\", \"protein_xref_pubmed\", \"11559530\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735280",
        "row": "[\"P04637-1\", \"APAF-1 is a transcriptional target of p53 in DNA damage-induced apoptosis.\", \"Cancer research\", \"2001 Sep 15\", \"Robles AI, Bemmels NA, Foraker AB, Harris CC\", \"protein_xref_pubmed\", \"11559530\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735281",
        "row": "[\"P55212-1\", \"APAF-1 is a transcriptional target of p53 in DNA damage-induced apoptosis.\", \"Cancer research\", \"2001 Sep 15\", \"Robles AI, Bemmels NA, Foraker AB, Harris CC\", \"protein_xref_pubmed\", \"11559530\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735282",
        "row": "[\"Q9H3D4-1\", \"APAF-1 is a transcriptional target of p53 in DNA damage-induced apoptosis.\", \"Cancer research\", \"2001 Sep 15\", \"Robles AI, Bemmels NA, Foraker AB, Harris CC\", \"protein_xref_pubmed\", \"11559530\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735283",
        "row": "[\"P42575-1\", \"APAF-1 is a transcriptional target of p53 in DNA damage-induced apoptosis.\", \"Cancer research\", \"2001 Sep 15\", \"Robles AI, Bemmels NA, Foraker AB, Harris CC\", \"protein_xref_pubmed\", \"11559530\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735284",
        "row": "[\"O15350-1\", \"APAF-1 is a transcriptional target of p53 in DNA damage-induced apoptosis.\", \"Cancer research\", \"2001 Sep 15\", \"Robles AI, Bemmels NA, Foraker AB, Harris CC\", \"protein_xref_pubmed\", \"11559530\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735285",
        "row": "[\"Q13315-1\", \"APAF-1 is a transcriptional target of p53 in DNA damage-induced apoptosis.\", \"Cancer research\", \"2001 Sep 15\", \"Robles AI, Bemmels NA, Foraker AB, Harris CC\", \"protein_xref_pubmed\", \"11559530\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735286",
        "row": "[\"P78560-1\", \"APAF-1 is a transcriptional target of p53 in DNA damage-induced apoptosis.\", \"Cancer research\", \"2001 Sep 15\", \"Robles AI, Bemmels NA, Foraker AB, Harris CC\", \"protein_xref_pubmed\", \"11559530\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735287",
        "row": "[\"P29466-1\", \"APAF-1 is a transcriptional target of p53 in DNA damage-induced apoptosis.\", \"Cancer research\", \"2001 Sep 15\", \"Robles AI, Bemmels NA, Foraker AB, Harris CC\", \"protein_xref_pubmed\", \"11559530\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735288",
        "row": "[\"Q9HB75-1\", \"APAF-1 is a transcriptional target of p53 in DNA damage-induced apoptosis.\", \"Cancer research\", \"2001 Sep 15\", \"Robles AI, Bemmels NA, Foraker AB, Harris CC\", \"protein_xref_pubmed\", \"11559530\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735289",
        "row": "[\"P78396-1\", \"A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence.\", \"Nature cell biology\", \"2002 Feb\", \"Peeper DS, Shvarts A, Brummelkamp T, Douma S, Koh EY, Daley GQ, Bernards R\", \"protein_xref_pubmed\", \"11812999\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735290",
        "row": "[\"P46527-1\", \"A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence.\", \"Nature cell biology\", \"2002 Feb\", \"Peeper DS, Shvarts A, Brummelkamp T, Douma S, Koh EY, Daley GQ, Bernards R\", \"protein_xref_pubmed\", \"11812999\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735291",
        "row": "[\"Q96PM9-4\", \"A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence.\", \"Nature cell biology\", \"2002 Feb\", \"Peeper DS, Shvarts A, Brummelkamp T, Douma S, Koh EY, Daley GQ, Bernards R\", \"protein_xref_pubmed\", \"11812999\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735292",
        "row": "[\"O96020-1\", \"A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence.\", \"Nature cell biology\", \"2002 Feb\", \"Peeper DS, Shvarts A, Brummelkamp T, Douma S, Koh EY, Daley GQ, Bernards R\", \"protein_xref_pubmed\", \"11812999\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735293",
        "row": "[\"P38936-1\", \"A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence.\", \"Nature cell biology\", \"2002 Feb\", \"Peeper DS, Shvarts A, Brummelkamp T, Douma S, Koh EY, Daley GQ, Bernards R\", \"protein_xref_pubmed\", \"11812999\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735294",
        "row": "[\"P04637-1\", \"A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence.\", \"Nature cell biology\", \"2002 Feb\", \"Peeper DS, Shvarts A, Brummelkamp T, Douma S, Koh EY, Daley GQ, Bernards R\", \"protein_xref_pubmed\", \"11812999\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735295",
        "row": "[\"P24941-1\", \"A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence.\", \"Nature cell biology\", \"2002 Feb\", \"Peeper DS, Shvarts A, Brummelkamp T, Douma S, Koh EY, Daley GQ, Bernards R\", \"protein_xref_pubmed\", \"11812999\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735296",
        "row": "[\"Q99856-1\", \"A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence.\", \"Nature cell biology\", \"2002 Feb\", \"Peeper DS, Shvarts A, Brummelkamp T, Douma S, Koh EY, Daley GQ, Bernards R\", \"protein_xref_pubmed\", \"11812999\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735297",
        "row": "[\"P57723-1\", \"A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence.\", \"Nature cell biology\", \"2002 Feb\", \"Peeper DS, Shvarts A, Brummelkamp T, Douma S, Koh EY, Daley GQ, Bernards R\", \"protein_xref_pubmed\", \"11812999\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735298",
        "row": "[\"Q96AV8-1\", \"A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence.\", \"Nature cell biology\", \"2002 Feb\", \"Peeper DS, Shvarts A, Brummelkamp T, Douma S, Koh EY, Daley GQ, Bernards R\", \"protein_xref_pubmed\", \"11812999\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735299",
        "row": "[\"P24864-1\", \"A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence.\", \"Nature cell biology\", \"2002 Feb\", \"Peeper DS, Shvarts A, Brummelkamp T, Douma S, Koh EY, Daley GQ, Bernards R\", \"protein_xref_pubmed\", \"11812999\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735300",
        "row": "[\"Q01094-1\", \"A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence.\", \"Nature cell biology\", \"2002 Feb\", \"Peeper DS, Shvarts A, Brummelkamp T, Douma S, Koh EY, Daley GQ, Bernards R\", \"protein_xref_pubmed\", \"11812999\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735301",
        "row": "[\"A0AVK6-1\", \"A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence.\", \"Nature cell biology\", \"2002 Feb\", \"Peeper DS, Shvarts A, Brummelkamp T, Douma S, Koh EY, Daley GQ, Bernards R\", \"protein_xref_pubmed\", \"11812999\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735302",
        "row": "[\"P20248-1\", \"A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence.\", \"Nature cell biology\", \"2002 Feb\", \"Peeper DS, Shvarts A, Brummelkamp T, Douma S, Koh EY, Daley GQ, Bernards R\", \"protein_xref_pubmed\", \"11812999\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735303",
        "row": "[\"P78396-1\", \"E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor, is regulated by p53.\", \"Molecular cancer research : MCR\", \"2003 Apr\", \"Ma K, Araki K, Ichwan SJ, Suganuma T, Tamamori-Adachi M, Ikeda MA\", \"protein_xref_pubmed\", \"12692263\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735304",
        "row": "[\"P46527-1\", \"E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor, is regulated by p53.\", \"Molecular cancer research : MCR\", \"2003 Apr\", \"Ma K, Araki K, Ichwan SJ, Suganuma T, Tamamori-Adachi M, Ikeda MA\", \"protein_xref_pubmed\", \"12692263\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735305",
        "row": "[\"Q96PM9-4\", \"E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor, is regulated by p53.\", \"Molecular cancer research : MCR\", \"2003 Apr\", \"Ma K, Araki K, Ichwan SJ, Suganuma T, Tamamori-Adachi M, Ikeda MA\", \"protein_xref_pubmed\", \"12692263\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735306",
        "row": "[\"O96020-1\", \"E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor, is regulated by p53.\", \"Molecular cancer research : MCR\", \"2003 Apr\", \"Ma K, Araki K, Ichwan SJ, Suganuma T, Tamamori-Adachi M, Ikeda MA\", \"protein_xref_pubmed\", \"12692263\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735307",
        "row": "[\"P38936-1\", \"E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor, is regulated by p53.\", \"Molecular cancer research : MCR\", \"2003 Apr\", \"Ma K, Araki K, Ichwan SJ, Suganuma T, Tamamori-Adachi M, Ikeda MA\", \"protein_xref_pubmed\", \"12692263\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735308",
        "row": "[\"P04637-1\", \"E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor, is regulated by p53.\", \"Molecular cancer research : MCR\", \"2003 Apr\", \"Ma K, Araki K, Ichwan SJ, Suganuma T, Tamamori-Adachi M, Ikeda MA\", \"protein_xref_pubmed\", \"12692263\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735309",
        "row": "[\"P24941-1\", \"E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor, is regulated by p53.\", \"Molecular cancer research : MCR\", \"2003 Apr\", \"Ma K, Araki K, Ichwan SJ, Suganuma T, Tamamori-Adachi M, Ikeda MA\", \"protein_xref_pubmed\", \"12692263\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735310",
        "row": "[\"Q99856-1\", \"E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor, is regulated by p53.\", \"Molecular cancer research : MCR\", \"2003 Apr\", \"Ma K, Araki K, Ichwan SJ, Suganuma T, Tamamori-Adachi M, Ikeda MA\", \"protein_xref_pubmed\", \"12692263\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735311",
        "row": "[\"P57723-1\", \"E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor, is regulated by p53.\", \"Molecular cancer research : MCR\", \"2003 Apr\", \"Ma K, Araki K, Ichwan SJ, Suganuma T, Tamamori-Adachi M, Ikeda MA\", \"protein_xref_pubmed\", \"12692263\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735312",
        "row": "[\"Q96AV8-1\", \"E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor, is regulated by p53.\", \"Molecular cancer research : MCR\", \"2003 Apr\", \"Ma K, Araki K, Ichwan SJ, Suganuma T, Tamamori-Adachi M, Ikeda MA\", \"protein_xref_pubmed\", \"12692263\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735313",
        "row": "[\"P24864-1\", \"E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor, is regulated by p53.\", \"Molecular cancer research : MCR\", \"2003 Apr\", \"Ma K, Araki K, Ichwan SJ, Suganuma T, Tamamori-Adachi M, Ikeda MA\", \"protein_xref_pubmed\", \"12692263\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735314",
        "row": "[\"Q01094-1\", \"E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor, is regulated by p53.\", \"Molecular cancer research : MCR\", \"2003 Apr\", \"Ma K, Araki K, Ichwan SJ, Suganuma T, Tamamori-Adachi M, Ikeda MA\", \"protein_xref_pubmed\", \"12692263\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735315",
        "row": "[\"A0AVK6-1\", \"E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor, is regulated by p53.\", \"Molecular cancer research : MCR\", \"2003 Apr\", \"Ma K, Araki K, Ichwan SJ, Suganuma T, Tamamori-Adachi M, Ikeda MA\", \"protein_xref_pubmed\", \"12692263\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735316",
        "row": "[\"P20248-1\", \"E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor, is regulated by p53.\", \"Molecular cancer research : MCR\", \"2003 Apr\", \"Ma K, Araki K, Ichwan SJ, Suganuma T, Tamamori-Adachi M, Ikeda MA\", \"protein_xref_pubmed\", \"12692263\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735317",
        "row": "[\"P78396-1\", \"A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer.\", \"Oncogene\", \"1998 Aug 20\", \"Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K\", \"protein_xref_pubmed\", \"9780002\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735318",
        "row": "[\"P46527-1\", \"A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer.\", \"Oncogene\", \"1998 Aug 20\", \"Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K\", \"protein_xref_pubmed\", \"9780002\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735319",
        "row": "[\"Q96PM9-4\", \"A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer.\", \"Oncogene\", \"1998 Aug 20\", \"Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K\", \"protein_xref_pubmed\", \"9780002\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735320",
        "row": "[\"O96020-1\", \"A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer.\", \"Oncogene\", \"1998 Aug 20\", \"Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K\", \"protein_xref_pubmed\", \"9780002\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735321",
        "row": "[\"P38936-1\", \"A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer.\", \"Oncogene\", \"1998 Aug 20\", \"Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K\", \"protein_xref_pubmed\", \"9780002\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735322",
        "row": "[\"P04637-1\", \"A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer.\", \"Oncogene\", \"1998 Aug 20\", \"Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K\", \"protein_xref_pubmed\", \"9780002\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735323",
        "row": "[\"P24941-1\", \"A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer.\", \"Oncogene\", \"1998 Aug 20\", \"Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K\", \"protein_xref_pubmed\", \"9780002\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735324",
        "row": "[\"Q99856-1\", \"A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer.\", \"Oncogene\", \"1998 Aug 20\", \"Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K\", \"protein_xref_pubmed\", \"9780002\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735325",
        "row": "[\"P57723-1\", \"A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer.\", \"Oncogene\", \"1998 Aug 20\", \"Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K\", \"protein_xref_pubmed\", \"9780002\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735326",
        "row": "[\"Q96AV8-1\", \"A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer.\", \"Oncogene\", \"1998 Aug 20\", \"Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K\", \"protein_xref_pubmed\", \"9780002\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735327",
        "row": "[\"P24864-1\", \"A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer.\", \"Oncogene\", \"1998 Aug 20\", \"Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K\", \"protein_xref_pubmed\", \"9780002\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735328",
        "row": "[\"Q01094-1\", \"A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer.\", \"Oncogene\", \"1998 Aug 20\", \"Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K\", \"protein_xref_pubmed\", \"9780002\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735329",
        "row": "[\"A0AVK6-1\", \"A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer.\", \"Oncogene\", \"1998 Aug 20\", \"Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K\", \"protein_xref_pubmed\", \"9780002\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735330",
        "row": "[\"P20248-1\", \"A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer.\", \"Oncogene\", \"1998 Aug 20\", \"Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K\", \"protein_xref_pubmed\", \"9780002\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735331",
        "row": "[\"P78396-1\", \"Cooperation between ARID3A and p53 in the transcriptional activation of p21WAF1 in response to DNA damage.\", \"Biochemical and biophysical research communications\", \"2012 Jan 13\", \"Lestari W, Ichwan SJ, Otsu M, Yamada S, Iseki S, Shimizu S, Ikeda MA\", \"protein_xref_pubmed\", \"22172947\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735332",
        "row": "[\"P46527-1\", \"Cooperation between ARID3A and p53 in the transcriptional activation of p21WAF1 in response to DNA damage.\", \"Biochemical and biophysical research communications\", \"2012 Jan 13\", \"Lestari W, Ichwan SJ, Otsu M, Yamada S, Iseki S, Shimizu S, Ikeda MA\", \"protein_xref_pubmed\", \"22172947\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735333",
        "row": "[\"Q96PM9-4\", \"Cooperation between ARID3A and p53 in the transcriptional activation of p21WAF1 in response to DNA damage.\", \"Biochemical and biophysical research communications\", \"2012 Jan 13\", \"Lestari W, Ichwan SJ, Otsu M, Yamada S, Iseki S, Shimizu S, Ikeda MA\", \"protein_xref_pubmed\", \"22172947\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735334",
        "row": "[\"O96020-1\", \"Cooperation between ARID3A and p53 in the transcriptional activation of p21WAF1 in response to DNA damage.\", \"Biochemical and biophysical research communications\", \"2012 Jan 13\", \"Lestari W, Ichwan SJ, Otsu M, Yamada S, Iseki S, Shimizu S, Ikeda MA\", \"protein_xref_pubmed\", \"22172947\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735335",
        "row": "[\"P38936-1\", \"Cooperation between ARID3A and p53 in the transcriptional activation of p21WAF1 in response to DNA damage.\", \"Biochemical and biophysical research communications\", \"2012 Jan 13\", \"Lestari W, Ichwan SJ, Otsu M, Yamada S, Iseki S, Shimizu S, Ikeda MA\", \"protein_xref_pubmed\", \"22172947\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735336",
        "row": "[\"P04637-1\", \"Cooperation between ARID3A and p53 in the transcriptional activation of p21WAF1 in response to DNA damage.\", \"Biochemical and biophysical research communications\", \"2012 Jan 13\", \"Lestari W, Ichwan SJ, Otsu M, Yamada S, Iseki S, Shimizu S, Ikeda MA\", \"protein_xref_pubmed\", \"22172947\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735337",
        "row": "[\"P24941-1\", \"Cooperation between ARID3A and p53 in the transcriptional activation of p21WAF1 in response to DNA damage.\", \"Biochemical and biophysical research communications\", \"2012 Jan 13\", \"Lestari W, Ichwan SJ, Otsu M, Yamada S, Iseki S, Shimizu S, Ikeda MA\", \"protein_xref_pubmed\", \"22172947\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735338",
        "row": "[\"Q99856-1\", \"Cooperation between ARID3A and p53 in the transcriptional activation of p21WAF1 in response to DNA damage.\", \"Biochemical and biophysical research communications\", \"2012 Jan 13\", \"Lestari W, Ichwan SJ, Otsu M, Yamada S, Iseki S, Shimizu S, Ikeda MA\", \"protein_xref_pubmed\", \"22172947\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735339",
        "row": "[\"P57723-1\", \"Cooperation between ARID3A and p53 in the transcriptional activation of p21WAF1 in response to DNA damage.\", \"Biochemical and biophysical research communications\", \"2012 Jan 13\", \"Lestari W, Ichwan SJ, Otsu M, Yamada S, Iseki S, Shimizu S, Ikeda MA\", \"protein_xref_pubmed\", \"22172947\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735340",
        "row": "[\"Q96AV8-1\", \"Cooperation between ARID3A and p53 in the transcriptional activation of p21WAF1 in response to DNA damage.\", \"Biochemical and biophysical research communications\", \"2012 Jan 13\", \"Lestari W, Ichwan SJ, Otsu M, Yamada S, Iseki S, Shimizu S, Ikeda MA\", \"protein_xref_pubmed\", \"22172947\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735341",
        "row": "[\"P24864-1\", \"Cooperation between ARID3A and p53 in the transcriptional activation of p21WAF1 in response to DNA damage.\", \"Biochemical and biophysical research communications\", \"2012 Jan 13\", \"Lestari W, Ichwan SJ, Otsu M, Yamada S, Iseki S, Shimizu S, Ikeda MA\", \"protein_xref_pubmed\", \"22172947\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735342",
        "row": "[\"Q01094-1\", \"Cooperation between ARID3A and p53 in the transcriptional activation of p21WAF1 in response to DNA damage.\", \"Biochemical and biophysical research communications\", \"2012 Jan 13\", \"Lestari W, Ichwan SJ, Otsu M, Yamada S, Iseki S, Shimizu S, Ikeda MA\", \"protein_xref_pubmed\", \"22172947\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735343",
        "row": "[\"A0AVK6-1\", \"Cooperation between ARID3A and p53 in the transcriptional activation of p21WAF1 in response to DNA damage.\", \"Biochemical and biophysical research communications\", \"2012 Jan 13\", \"Lestari W, Ichwan SJ, Otsu M, Yamada S, Iseki S, Shimizu S, Ikeda MA\", \"protein_xref_pubmed\", \"22172947\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735344",
        "row": "[\"P20248-1\", \"Cooperation between ARID3A and p53 in the transcriptional activation of p21WAF1 in response to DNA damage.\", \"Biochemical and biophysical research communications\", \"2012 Jan 13\", \"Lestari W, Ichwan SJ, Otsu M, Yamada S, Iseki S, Shimizu S, Ikeda MA\", \"protein_xref_pubmed\", \"22172947\", \"protein_xref_reactome\", \"R-HSA-6804116\"]"
    },
    {
        "recordid": "GLY_000310_1_735345",
        "row": "[\"Q9HCL2-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735346",
        "row": "[\"P47712-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735347",
        "row": "[\"Q9BZM2-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735348",
        "row": "[\"Q9BZM1-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735349",
        "row": "[\"Q6NUI2-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735350",
        "row": "[\"Q86XP0-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735351",
        "row": "[\"Q13393-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735352",
        "row": "[\"Q9NPH0-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735353",
        "row": "[\"Q8NF37-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735354",
        "row": "[\"P39877-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735355",
        "row": "[\"O15496-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735356",
        "row": "[\"Q6UWP7-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735357",
        "row": "[\"P43304-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735358",
        "row": "[\"Q99943-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735359",
        "row": "[\"P21695-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735360",
        "row": "[\"Q6XZB0-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735361",
        "row": "[\"Q53EU6-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735362",
        "row": "[\"Q8NAN2-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735363",
        "row": "[\"Q643R3-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735364",
        "row": "[\"Q9NZK7-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735365",
        "row": "[\"Q8WWY8-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735366",
        "row": "[\"Q86UL3-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735367",
        "row": "[\"O15228-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735368",
        "row": "[\"P09923-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735369",
        "row": "[\"Q13018-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735370",
        "row": "[\"O15120-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735371",
        "row": "[\"Q7L4E1-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735372",
        "row": "[\"P14555-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735373",
        "row": "[\"O94830-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735374",
        "row": "[\"P0C869-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735375",
        "row": "[\"P04054-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735376",
        "row": "[\"Q8N2A8-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735377",
        "row": "[\"Q9UNK4-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735378",
        "row": "[\"O14939-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735379",
        "row": "[\"Q9NRZ7-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735380",
        "row": "[\"Q9NRZ5-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735381",
        "row": "[\"Q8N335-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735382",
        "row": "[\"Q9NUQ2-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735383",
        "row": "[\"Q8NEL9-1\", \"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.\", \"The Journal of biological chemistry\", \"2002 Sep 13\", \"Sonoda H, Aoki J, Hiramatsu T, Ishida M, Bandoh K, Nagai Y, Taguchi R, Inoue K, Arai H\", \"protein_xref_pubmed\", \"12063250\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735384",
        "row": "[\"Q9HCL2-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735385",
        "row": "[\"P47712-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735386",
        "row": "[\"Q9BZM2-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735387",
        "row": "[\"Q9BZM1-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735388",
        "row": "[\"Q6NUI2-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735389",
        "row": "[\"Q86XP0-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735390",
        "row": "[\"Q13393-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735391",
        "row": "[\"Q9NPH0-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735392",
        "row": "[\"Q8NF37-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735393",
        "row": "[\"P39877-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735394",
        "row": "[\"O15496-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735395",
        "row": "[\"Q6UWP7-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735396",
        "row": "[\"P43304-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735397",
        "row": "[\"Q99943-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735398",
        "row": "[\"P21695-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735399",
        "row": "[\"Q6XZB0-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735400",
        "row": "[\"Q53EU6-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735401",
        "row": "[\"Q8NAN2-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735402",
        "row": "[\"Q643R3-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735403",
        "row": "[\"Q9NZK7-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735404",
        "row": "[\"Q8WWY8-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735405",
        "row": "[\"Q86UL3-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735406",
        "row": "[\"O15228-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735407",
        "row": "[\"P09923-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735408",
        "row": "[\"Q13018-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735409",
        "row": "[\"O15120-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735410",
        "row": "[\"Q7L4E1-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735411",
        "row": "[\"P14555-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735412",
        "row": "[\"O94830-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735413",
        "row": "[\"P0C869-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735414",
        "row": "[\"P04054-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735415",
        "row": "[\"Q8N2A8-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735416",
        "row": "[\"Q9UNK4-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735417",
        "row": "[\"O14939-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735418",
        "row": "[\"Q9NRZ7-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735419",
        "row": "[\"Q9NRZ5-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735420",
        "row": "[\"Q8N335-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735421",
        "row": "[\"Q9NUQ2-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735422",
        "row": "[\"Q8NEL9-1\", \"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.\", \"The Journal of biological chemistry\", \"2003 Dec 5\", \"Hiramatsu T, Sonoda H, Takanezawa Y, Morikawa R, Ishida M, Kasahara K, Sanai Y, Taguchi R, Aoki J, Arai H\", \"protein_xref_pubmed\", \"12963729\", \"protein_xref_reactome\", \"R-HSA-1483166\"]"
    },
    {
        "recordid": "GLY_000310_1_735423",
        "row": "[\"Q9NR77-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735424",
        "row": "[\"Q02218-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735425",
        "row": "[\"Q9UJM8-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735426",
        "row": "[\"P10515-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735427",
        "row": "[\"Q86XE5-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735428",
        "row": "[\"P00505-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735429",
        "row": "[\"P36957-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735430",
        "row": "[\"A6NK58-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735431",
        "row": "[\"P21953-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735432",
        "row": "[\"P23434-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735433",
        "row": "[\"Q9UBQ7-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735434",
        "row": "[\"Q99489-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735435",
        "row": "[\"P12694-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735436",
        "row": "[\"P11182-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735437",
        "row": "[\"P11177-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735438",
        "row": "[\"Q96HY7-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735439",
        "row": "[\"Q9UF12-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735440",
        "row": "[\"O00330-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735441",
        "row": "[\"Q14749-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735442",
        "row": "[\"P14920-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735443",
        "row": "[\"Q9Y234-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735444",
        "row": "[\"P08559-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735445",
        "row": "[\"P30038-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735446",
        "row": "[\"P21549-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735447",
        "row": "[\"O14561-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735448",
        "row": "[\"P29803-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735449",
        "row": "[\"P09622-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735450",
        "row": "[\"Q9BYV1-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735451",
        "row": "[\"O43766-1\", \"Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.\", \"European journal of biochemistry\", \"1999 Mar\", \"Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y\", \"protein_xref_pubmed\", \"10103005\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735452",
        "row": "[\"Q9NR77-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735453",
        "row": "[\"Q02218-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735454",
        "row": "[\"Q9UJM8-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735455",
        "row": "[\"P10515-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735456",
        "row": "[\"Q86XE5-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735457",
        "row": "[\"P00505-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735458",
        "row": "[\"P36957-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735459",
        "row": "[\"A6NK58-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735460",
        "row": "[\"P21953-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735461",
        "row": "[\"P23434-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735462",
        "row": "[\"Q9UBQ7-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735463",
        "row": "[\"Q99489-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735464",
        "row": "[\"P12694-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735465",
        "row": "[\"P11182-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735466",
        "row": "[\"P11177-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735467",
        "row": "[\"Q96HY7-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735468",
        "row": "[\"Q9UF12-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735469",
        "row": "[\"O00330-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735470",
        "row": "[\"Q14749-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735471",
        "row": "[\"P14920-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735472",
        "row": "[\"Q9Y234-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735473",
        "row": "[\"P08559-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735474",
        "row": "[\"P30038-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735475",
        "row": "[\"P21549-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735476",
        "row": "[\"O14561-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735477",
        "row": "[\"P29803-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735478",
        "row": "[\"P09622-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735479",
        "row": "[\"Q9BYV1-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735480",
        "row": "[\"O43766-1\", \"Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.\", \"Human molecular genetics\", \"2014 Apr 1\", \"Tort F, Ferrer-Cortes X, Thio M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, Garcia-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, Garcia-Cazorla A, Briones P, Ribes A\", \"protein_xref_pubmed\", \"24256811\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735481",
        "row": "[\"Q9NR77-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735482",
        "row": "[\"Q02218-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735483",
        "row": "[\"Q9UJM8-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735484",
        "row": "[\"P10515-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735485",
        "row": "[\"Q86XE5-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735486",
        "row": "[\"P00505-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735487",
        "row": "[\"P36957-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735488",
        "row": "[\"A6NK58-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735489",
        "row": "[\"P21953-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735490",
        "row": "[\"P23434-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735491",
        "row": "[\"Q9UBQ7-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735492",
        "row": "[\"Q99489-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735493",
        "row": "[\"P12694-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735494",
        "row": "[\"P11182-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735495",
        "row": "[\"P11177-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735496",
        "row": "[\"Q96HY7-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735497",
        "row": "[\"Q9UF12-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735498",
        "row": "[\"O00330-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735499",
        "row": "[\"Q14749-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735500",
        "row": "[\"P14920-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735501",
        "row": "[\"Q9Y234-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735502",
        "row": "[\"P08559-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735503",
        "row": "[\"P30038-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735504",
        "row": "[\"P21549-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735505",
        "row": "[\"O14561-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735506",
        "row": "[\"P29803-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735507",
        "row": "[\"P09622-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735508",
        "row": "[\"Q9BYV1-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735509",
        "row": "[\"O43766-1\", \"Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.\", \"Orphanet journal of rare diseases\", \"2013 Dec 17\", \"Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P\", \"protein_xref_pubmed\", \"24341803\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735510",
        "row": "[\"P33778-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735511",
        "row": "[\"Q96L91-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735512",
        "row": "[\"P23527-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735513",
        "row": "[\"P78396-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735514",
        "row": "[\"P46527-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735515",
        "row": "[\"Q9NYB0-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735516",
        "row": "[\"O60934-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735517",
        "row": "[\"O60814-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735518",
        "row": "[\"O96020-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735519",
        "row": "[\"P38936-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735520",
        "row": "[\"P16104-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735521",
        "row": "[\"Q92993-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735522",
        "row": "[\"Q99880-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735523",
        "row": "[\"P62807-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735524",
        "row": "[\"Q6FI13-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735525",
        "row": "[\"P04637-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735526",
        "row": "[\"P24941-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735527",
        "row": "[\"Q93077-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735528",
        "row": "[\"Q93079-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735529",
        "row": "[\"P54274-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735530",
        "row": "[\"Q16695-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735531",
        "row": "[\"Q9BTM1-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735532",
        "row": "[\"Q15554-3\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735533",
        "row": "[\"Q92878-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735534",
        "row": "[\"Q8N257-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735535",
        "row": "[\"Q9NUX5-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735536",
        "row": "[\"Q99877-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735537",
        "row": "[\"Q99878-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735538",
        "row": "[\"Q99879-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735539",
        "row": "[\"Q16777-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735540",
        "row": "[\"Q16778-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735541",
        "row": "[\"P62805-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735542",
        "row": "[\"P06899-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735543",
        "row": "[\"Q9BSI4-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735544",
        "row": "[\"P24864-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735545",
        "row": "[\"P20671-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735546",
        "row": "[\"P49959-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735547",
        "row": "[\"P58876-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735548",
        "row": "[\"P57053-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735549",
        "row": "[\"P0C5Y9-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735550",
        "row": "[\"Q13315-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735551",
        "row": "[\"Q96AP0-3\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735552",
        "row": "[\"P04908-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735553",
        "row": "[\"Q71UI9-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735554",
        "row": "[\"Q96A08-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735555",
        "row": "[\"P20248-1\", \"Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity.\", \"EMBO reports\", \"2002 Nov\", \"Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, Brunori M, Brun C, Martins L, Sabatier L, Pulitzer JF, Gilson E\", \"protein_xref_pubmed\", \"12393752\", \"protein_xref_reactome\", \"R-HSA-2559586\"]"
    },
    {
        "recordid": "GLY_000310_1_735556",
        "row": "[\"Q9NR77-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735557",
        "row": "[\"Q02218-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735558",
        "row": "[\"Q9UJM8-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735559",
        "row": "[\"P10515-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735560",
        "row": "[\"Q86XE5-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735561",
        "row": "[\"P00505-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735562",
        "row": "[\"P36957-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735563",
        "row": "[\"A6NK58-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735564",
        "row": "[\"P21953-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735565",
        "row": "[\"P23434-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735566",
        "row": "[\"Q9UBQ7-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735567",
        "row": "[\"Q99489-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735568",
        "row": "[\"P12694-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735569",
        "row": "[\"P11182-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735570",
        "row": "[\"P11177-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735571",
        "row": "[\"Q96HY7-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735572",
        "row": "[\"Q9UF12-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735573",
        "row": "[\"O00330-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735574",
        "row": "[\"Q14749-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735575",
        "row": "[\"P14920-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735576",
        "row": "[\"Q9Y234-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735577",
        "row": "[\"P08559-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735578",
        "row": "[\"P30038-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735579",
        "row": "[\"P21549-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735580",
        "row": "[\"O14561-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735581",
        "row": "[\"P29803-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735582",
        "row": "[\"P09622-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735583",
        "row": "[\"Q9BYV1-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735584",
        "row": "[\"O43766-1\", \"Lipoic acid synthesis and attachment in yeast mitochondria.\", \"The Journal of biological chemistry\", \"2009 Aug 28\", \"Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL\", \"protein_xref_pubmed\", \"19570983\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735585",
        "row": "[\"Q9NR77-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735586",
        "row": "[\"Q02218-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735587",
        "row": "[\"Q9UJM8-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735588",
        "row": "[\"P10515-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735589",
        "row": "[\"Q86XE5-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735590",
        "row": "[\"P00505-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735591",
        "row": "[\"P36957-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735592",
        "row": "[\"A6NK58-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735593",
        "row": "[\"P21953-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735594",
        "row": "[\"P23434-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735595",
        "row": "[\"Q9UBQ7-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735596",
        "row": "[\"Q99489-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735597",
        "row": "[\"P12694-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735598",
        "row": "[\"P11182-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735599",
        "row": "[\"P11177-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735600",
        "row": "[\"Q96HY7-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735601",
        "row": "[\"Q9UF12-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735602",
        "row": "[\"O00330-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735603",
        "row": "[\"Q14749-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735604",
        "row": "[\"P14920-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735605",
        "row": "[\"Q9Y234-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735606",
        "row": "[\"P08559-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735607",
        "row": "[\"P30038-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735608",
        "row": "[\"P21549-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735609",
        "row": "[\"O14561-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735610",
        "row": "[\"P29803-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735611",
        "row": "[\"P09622-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735612",
        "row": "[\"Q9BYV1-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735613",
        "row": "[\"O43766-1\", \"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.\", \"FEBS letters\", \"2001 Jun 1\", \"Morikawa T, Yasuno R, Wada H\", \"protein_xref_pubmed\", \"11389890\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735614",
        "row": "[\"Q9NR77-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735615",
        "row": "[\"Q02218-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735616",
        "row": "[\"Q9UJM8-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735617",
        "row": "[\"P10515-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735618",
        "row": "[\"Q86XE5-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735619",
        "row": "[\"P00505-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735620",
        "row": "[\"P36957-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735621",
        "row": "[\"A6NK58-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735622",
        "row": "[\"P21953-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735623",
        "row": "[\"P23434-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735624",
        "row": "[\"Q9UBQ7-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735625",
        "row": "[\"Q99489-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735626",
        "row": "[\"P12694-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735627",
        "row": "[\"P11182-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735628",
        "row": "[\"P11177-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735629",
        "row": "[\"Q96HY7-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735630",
        "row": "[\"Q9UF12-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735631",
        "row": "[\"O00330-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735632",
        "row": "[\"Q14749-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735633",
        "row": "[\"P14920-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735634",
        "row": "[\"Q9Y234-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735635",
        "row": "[\"P08559-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735636",
        "row": "[\"P30038-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735637",
        "row": "[\"P21549-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735638",
        "row": "[\"O14561-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735639",
        "row": "[\"P29803-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735640",
        "row": "[\"P09622-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735641",
        "row": "[\"Q9BYV1-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735642",
        "row": "[\"O43766-1\", \"Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.\", \"American journal of human genetics\", \"2011 Dec 9\", \"Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W\", \"protein_xref_pubmed\", \"22152680\", \"protein_xref_reactome\", \"R-HSA-389661\"]"
    },
    {
        "recordid": "GLY_000310_1_735643",
        "row": "[\"Q9UL12-1\", \"Structure and analysis of the human dimethylglycine dehydrogenase gene.\", \"Molecular genetics and metabolism\", \"2000 Mar\", \"Binzak BA, Vockley JG, Jenkins RB, Vockley J\", \"protein_xref_pubmed\", \"10767172\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735644",
        "row": "[\"Q93088-1\", \"Structure and analysis of the human dimethylglycine dehydrogenase gene.\", \"Molecular genetics and metabolism\", \"2000 Mar\", \"Binzak BA, Vockley JG, Jenkins RB, Vockley J\", \"protein_xref_pubmed\", \"10767172\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735645",
        "row": "[\"P49419-1\", \"Structure and analysis of the human dimethylglycine dehydrogenase gene.\", \"Molecular genetics and metabolism\", \"2000 Mar\", \"Binzak BA, Vockley JG, Jenkins RB, Vockley J\", \"protein_xref_pubmed\", \"10767172\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735646",
        "row": "[\"Q9UI17-1\", \"Structure and analysis of the human dimethylglycine dehydrogenase gene.\", \"Molecular genetics and metabolism\", \"2000 Mar\", \"Binzak BA, Vockley JG, Jenkins RB, Vockley J\", \"protein_xref_pubmed\", \"10767172\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735647",
        "row": "[\"Q8NE62-1\", \"Structure and analysis of the human dimethylglycine dehydrogenase gene.\", \"Molecular genetics and metabolism\", \"2000 Mar\", \"Binzak BA, Vockley JG, Jenkins RB, Vockley J\", \"protein_xref_pubmed\", \"10767172\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735648",
        "row": "[\"Q8WWI5-1\", \"Structure and analysis of the human dimethylglycine dehydrogenase gene.\", \"Molecular genetics and metabolism\", \"2000 Mar\", \"Binzak BA, Vockley JG, Jenkins RB, Vockley J\", \"protein_xref_pubmed\", \"10767172\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735649",
        "row": "[\"Q9UL12-1\", \"Cloning of dimethylglycine dehydrogenase and a new human inborn error of metabolism, dimethylglycine dehydrogenase deficiency.\", \"American journal of human genetics\", \"2001 Apr\", \"Binzak BA, Wevers RA, Moolenaar SH, Lee YM, Hwu WL, Poggi-Bach J, Engelke UF, Hoard HM, Vockley JG, Vockley J\", \"protein_xref_pubmed\", \"11231903\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735650",
        "row": "[\"Q93088-1\", \"Cloning of dimethylglycine dehydrogenase and a new human inborn error of metabolism, dimethylglycine dehydrogenase deficiency.\", \"American journal of human genetics\", \"2001 Apr\", \"Binzak BA, Wevers RA, Moolenaar SH, Lee YM, Hwu WL, Poggi-Bach J, Engelke UF, Hoard HM, Vockley JG, Vockley J\", \"protein_xref_pubmed\", \"11231903\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735651",
        "row": "[\"P49419-1\", \"Cloning of dimethylglycine dehydrogenase and a new human inborn error of metabolism, dimethylglycine dehydrogenase deficiency.\", \"American journal of human genetics\", \"2001 Apr\", \"Binzak BA, Wevers RA, Moolenaar SH, Lee YM, Hwu WL, Poggi-Bach J, Engelke UF, Hoard HM, Vockley JG, Vockley J\", \"protein_xref_pubmed\", \"11231903\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735652",
        "row": "[\"Q9UI17-1\", \"Cloning of dimethylglycine dehydrogenase and a new human inborn error of metabolism, dimethylglycine dehydrogenase deficiency.\", \"American journal of human genetics\", \"2001 Apr\", \"Binzak BA, Wevers RA, Moolenaar SH, Lee YM, Hwu WL, Poggi-Bach J, Engelke UF, Hoard HM, Vockley JG, Vockley J\", \"protein_xref_pubmed\", \"11231903\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735653",
        "row": "[\"Q8NE62-1\", \"Cloning of dimethylglycine dehydrogenase and a new human inborn error of metabolism, dimethylglycine dehydrogenase deficiency.\", \"American journal of human genetics\", \"2001 Apr\", \"Binzak BA, Wevers RA, Moolenaar SH, Lee YM, Hwu WL, Poggi-Bach J, Engelke UF, Hoard HM, Vockley JG, Vockley J\", \"protein_xref_pubmed\", \"11231903\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735654",
        "row": "[\"Q8WWI5-1\", \"Cloning of dimethylglycine dehydrogenase and a new human inborn error of metabolism, dimethylglycine dehydrogenase deficiency.\", \"American journal of human genetics\", \"2001 Apr\", \"Binzak BA, Wevers RA, Moolenaar SH, Lee YM, Hwu WL, Poggi-Bach J, Engelke UF, Hoard HM, Vockley JG, Vockley J\", \"protein_xref_pubmed\", \"11231903\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735655",
        "row": "[\"Q13625-1\", \"Transcriptional repression of the anti-apoptotic survivin gene by wild type p53.\", \"The Journal of biological chemistry\", \"2002 Feb 1\", \"Hoffman WH, Biade S, Zilfou JT, Chen J, Murphy M\", \"protein_xref_pubmed\", \"11714700\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735656",
        "row": "[\"Q96FX8-1\", \"Transcriptional repression of the anti-apoptotic survivin gene by wild type p53.\", \"The Journal of biological chemistry\", \"2002 Feb 1\", \"Hoffman WH, Biade S, Zilfou JT, Chen J, Murphy M\", \"protein_xref_pubmed\", \"11714700\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735657",
        "row": "[\"Q53FA7-1\", \"Transcriptional repression of the anti-apoptotic survivin gene by wild type p53.\", \"The Journal of biological chemistry\", \"2002 Feb 1\", \"Hoffman WH, Biade S, Zilfou JT, Chen J, Murphy M\", \"protein_xref_pubmed\", \"11714700\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735658",
        "row": "[\"Q92696-1\", \"Transcriptional repression of the anti-apoptotic survivin gene by wild type p53.\", \"The Journal of biological chemistry\", \"2002 Feb 1\", \"Hoffman WH, Biade S, Zilfou JT, Chen J, Murphy M\", \"protein_xref_pubmed\", \"11714700\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735659",
        "row": "[\"P53611-1\", \"Transcriptional repression of the anti-apoptotic survivin gene by wild type p53.\", \"The Journal of biological chemistry\", \"2002 Feb 1\", \"Hoffman WH, Biade S, Zilfou JT, Chen J, Murphy M\", \"protein_xref_pubmed\", \"11714700\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735660",
        "row": "[\"P41182-1\", \"Transcriptional repression of the anti-apoptotic survivin gene by wild type p53.\", \"The Journal of biological chemistry\", \"2002 Feb 1\", \"Hoffman WH, Biade S, Zilfou JT, Chen J, Murphy M\", \"protein_xref_pubmed\", \"11714700\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735661",
        "row": "[\"P04637-1\", \"Transcriptional repression of the anti-apoptotic survivin gene by wild type p53.\", \"The Journal of biological chemistry\", \"2002 Feb 1\", \"Hoffman WH, Biade S, Zilfou JT, Chen J, Murphy M\", \"protein_xref_pubmed\", \"11714700\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735662",
        "row": "[\"Q9H3D4-1\", \"Transcriptional repression of the anti-apoptotic survivin gene by wild type p53.\", \"The Journal of biological chemistry\", \"2002 Feb 1\", \"Hoffman WH, Biade S, Zilfou JT, Chen J, Murphy M\", \"protein_xref_pubmed\", \"11714700\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735663",
        "row": "[\"Q92597-1\", \"Transcriptional repression of the anti-apoptotic survivin gene by wild type p53.\", \"The Journal of biological chemistry\", \"2002 Feb 1\", \"Hoffman WH, Biade S, Zilfou JT, Chen J, Murphy M\", \"protein_xref_pubmed\", \"11714700\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735664",
        "row": "[\"O15392-1\", \"Transcriptional repression of the anti-apoptotic survivin gene by wild type p53.\", \"The Journal of biological chemistry\", \"2002 Feb 1\", \"Hoffman WH, Biade S, Zilfou JT, Chen J, Murphy M\", \"protein_xref_pubmed\", \"11714700\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735665",
        "row": "[\"Q9BZR8-1\", \"Transcriptional repression of the anti-apoptotic survivin gene by wild type p53.\", \"The Journal of biological chemistry\", \"2002 Feb 1\", \"Hoffman WH, Biade S, Zilfou JT, Chen J, Murphy M\", \"protein_xref_pubmed\", \"11714700\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735666",
        "row": "[\"Q96KQ4-1\", \"Transcriptional repression of the anti-apoptotic survivin gene by wild type p53.\", \"The Journal of biological chemistry\", \"2002 Feb 1\", \"Hoffman WH, Biade S, Zilfou JT, Chen J, Murphy M\", \"protein_xref_pubmed\", \"11714700\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735667",
        "row": "[\"O15350-1\", \"Transcriptional repression of the anti-apoptotic survivin gene by wild type p53.\", \"The Journal of biological chemistry\", \"2002 Feb 1\", \"Hoffman WH, Biade S, Zilfou JT, Chen J, Murphy M\", \"protein_xref_pubmed\", \"11714700\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735668",
        "row": "[\"P24386-1\", \"Transcriptional repression of the anti-apoptotic survivin gene by wild type p53.\", \"The Journal of biological chemistry\", \"2002 Feb 1\", \"Hoffman WH, Biade S, Zilfou JT, Chen J, Murphy M\", \"protein_xref_pubmed\", \"11714700\", \"protein_xref_reactome\", \"R-HSA-6803205\"]"
    },
    {
        "recordid": "GLY_000310_1_735669",
        "row": "[\"Q9UL12-1\", \"Cloning and mapping of the cDNA for human sarcosine dehydrogenase, a flavoenzyme defective in patients with sarcosinemia.\", \"Genomics\", \"1999 Aug 1\", \"Eschenbrenner M, Jorns MS\", \"protein_xref_pubmed\", \"10444331\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735670",
        "row": "[\"Q93088-1\", \"Cloning and mapping of the cDNA for human sarcosine dehydrogenase, a flavoenzyme defective in patients with sarcosinemia.\", \"Genomics\", \"1999 Aug 1\", \"Eschenbrenner M, Jorns MS\", \"protein_xref_pubmed\", \"10444331\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735671",
        "row": "[\"P49419-1\", \"Cloning and mapping of the cDNA for human sarcosine dehydrogenase, a flavoenzyme defective in patients with sarcosinemia.\", \"Genomics\", \"1999 Aug 1\", \"Eschenbrenner M, Jorns MS\", \"protein_xref_pubmed\", \"10444331\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735672",
        "row": "[\"Q9UI17-1\", \"Cloning and mapping of the cDNA for human sarcosine dehydrogenase, a flavoenzyme defective in patients with sarcosinemia.\", \"Genomics\", \"1999 Aug 1\", \"Eschenbrenner M, Jorns MS\", \"protein_xref_pubmed\", \"10444331\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735673",
        "row": "[\"Q8NE62-1\", \"Cloning and mapping of the cDNA for human sarcosine dehydrogenase, a flavoenzyme defective in patients with sarcosinemia.\", \"Genomics\", \"1999 Aug 1\", \"Eschenbrenner M, Jorns MS\", \"protein_xref_pubmed\", \"10444331\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735674",
        "row": "[\"Q8WWI5-1\", \"Cloning and mapping of the cDNA for human sarcosine dehydrogenase, a flavoenzyme defective in patients with sarcosinemia.\", \"Genomics\", \"1999 Aug 1\", \"Eschenbrenner M, Jorns MS\", \"protein_xref_pubmed\", \"10444331\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735675",
        "row": "[\"Q9UL12-1\", \"Mutations in the sarcosine dehydrogenase gene in patients with sarcosinemia.\", \"Human genetics\", \"2012 Nov\", \"Bar-joseph I, Pras E, Reznik-Wolf H, Marek-Yagel D, Abu-Horvitz A, Dushnitzky M, Goldstein N, Rienstein S, Dekel M, Pode-Shakked B, Zlotnik J, Benarrosh A, Gillery P, Hofliger N, Auray-Blais C, Garnotel R, Anikster Y\", \"protein_xref_pubmed\", \"22825317\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735676",
        "row": "[\"Q93088-1\", \"Mutations in the sarcosine dehydrogenase gene in patients with sarcosinemia.\", \"Human genetics\", \"2012 Nov\", \"Bar-joseph I, Pras E, Reznik-Wolf H, Marek-Yagel D, Abu-Horvitz A, Dushnitzky M, Goldstein N, Rienstein S, Dekel M, Pode-Shakked B, Zlotnik J, Benarrosh A, Gillery P, Hofliger N, Auray-Blais C, Garnotel R, Anikster Y\", \"protein_xref_pubmed\", \"22825317\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735677",
        "row": "[\"P49419-1\", \"Mutations in the sarcosine dehydrogenase gene in patients with sarcosinemia.\", \"Human genetics\", \"2012 Nov\", \"Bar-joseph I, Pras E, Reznik-Wolf H, Marek-Yagel D, Abu-Horvitz A, Dushnitzky M, Goldstein N, Rienstein S, Dekel M, Pode-Shakked B, Zlotnik J, Benarrosh A, Gillery P, Hofliger N, Auray-Blais C, Garnotel R, Anikster Y\", \"protein_xref_pubmed\", \"22825317\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735678",
        "row": "[\"Q9UI17-1\", \"Mutations in the sarcosine dehydrogenase gene in patients with sarcosinemia.\", \"Human genetics\", \"2012 Nov\", \"Bar-joseph I, Pras E, Reznik-Wolf H, Marek-Yagel D, Abu-Horvitz A, Dushnitzky M, Goldstein N, Rienstein S, Dekel M, Pode-Shakked B, Zlotnik J, Benarrosh A, Gillery P, Hofliger N, Auray-Blais C, Garnotel R, Anikster Y\", \"protein_xref_pubmed\", \"22825317\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735679",
        "row": "[\"Q8NE62-1\", \"Mutations in the sarcosine dehydrogenase gene in patients with sarcosinemia.\", \"Human genetics\", \"2012 Nov\", \"Bar-joseph I, Pras E, Reznik-Wolf H, Marek-Yagel D, Abu-Horvitz A, Dushnitzky M, Goldstein N, Rienstein S, Dekel M, Pode-Shakked B, Zlotnik J, Benarrosh A, Gillery P, Hofliger N, Auray-Blais C, Garnotel R, Anikster Y\", \"protein_xref_pubmed\", \"22825317\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735680",
        "row": "[\"Q8WWI5-1\", \"Mutations in the sarcosine dehydrogenase gene in patients with sarcosinemia.\", \"Human genetics\", \"2012 Nov\", \"Bar-joseph I, Pras E, Reznik-Wolf H, Marek-Yagel D, Abu-Horvitz A, Dushnitzky M, Goldstein N, Rienstein S, Dekel M, Pode-Shakked B, Zlotnik J, Benarrosh A, Gillery P, Hofliger N, Auray-Blais C, Garnotel R, Anikster Y\", \"protein_xref_pubmed\", \"22825317\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735681",
        "row": "[\"Q9UL12-1\", \"Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress.\", \"The Journal of biological chemistry\", \"2010 Jun 11\", \"Brocker C, Lassen N, Estey T, Pappa A, Cantore M, Orlova VV, Chavakis T, Kavanagh KL, Oppermann U, Vasiliou V\", \"protein_xref_pubmed\", \"20207735\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735682",
        "row": "[\"Q93088-1\", \"Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress.\", \"The Journal of biological chemistry\", \"2010 Jun 11\", \"Brocker C, Lassen N, Estey T, Pappa A, Cantore M, Orlova VV, Chavakis T, Kavanagh KL, Oppermann U, Vasiliou V\", \"protein_xref_pubmed\", \"20207735\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735683",
        "row": "[\"P49419-1\", \"Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress.\", \"The Journal of biological chemistry\", \"2010 Jun 11\", \"Brocker C, Lassen N, Estey T, Pappa A, Cantore M, Orlova VV, Chavakis T, Kavanagh KL, Oppermann U, Vasiliou V\", \"protein_xref_pubmed\", \"20207735\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735684",
        "row": "[\"Q9UI17-1\", \"Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress.\", \"The Journal of biological chemistry\", \"2010 Jun 11\", \"Brocker C, Lassen N, Estey T, Pappa A, Cantore M, Orlova VV, Chavakis T, Kavanagh KL, Oppermann U, Vasiliou V\", \"protein_xref_pubmed\", \"20207735\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735685",
        "row": "[\"Q8NE62-1\", \"Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress.\", \"The Journal of biological chemistry\", \"2010 Jun 11\", \"Brocker C, Lassen N, Estey T, Pappa A, Cantore M, Orlova VV, Chavakis T, Kavanagh KL, Oppermann U, Vasiliou V\", \"protein_xref_pubmed\", \"20207735\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735686",
        "row": "[\"Q8WWI5-1\", \"Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress.\", \"The Journal of biological chemistry\", \"2010 Jun 11\", \"Brocker C, Lassen N, Estey T, Pappa A, Cantore M, Orlova VV, Chavakis T, Kavanagh KL, Oppermann U, Vasiliou V\", \"protein_xref_pubmed\", \"20207735\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735687",
        "row": "[\"Q9UL12-1\", \"The solute carrier 44A1 is a mitochondrial protein and mediates choline transport.\", \"FASEB journal : official publication of the Federation of American Societies for Experimental Biology\", \"2009 Aug\", \"Michel V, Bakovic M\", \"protein_xref_pubmed\", \"19357133\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735688",
        "row": "[\"Q93088-1\", \"The solute carrier 44A1 is a mitochondrial protein and mediates choline transport.\", \"FASEB journal : official publication of the Federation of American Societies for Experimental Biology\", \"2009 Aug\", \"Michel V, Bakovic M\", \"protein_xref_pubmed\", \"19357133\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735689",
        "row": "[\"P49419-1\", \"The solute carrier 44A1 is a mitochondrial protein and mediates choline transport.\", \"FASEB journal : official publication of the Federation of American Societies for Experimental Biology\", \"2009 Aug\", \"Michel V, Bakovic M\", \"protein_xref_pubmed\", \"19357133\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735690",
        "row": "[\"Q9UI17-1\", \"The solute carrier 44A1 is a mitochondrial protein and mediates choline transport.\", \"FASEB journal : official publication of the Federation of American Societies for Experimental Biology\", \"2009 Aug\", \"Michel V, Bakovic M\", \"protein_xref_pubmed\", \"19357133\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735691",
        "row": "[\"Q8NE62-1\", \"The solute carrier 44A1 is a mitochondrial protein and mediates choline transport.\", \"FASEB journal : official publication of the Federation of American Societies for Experimental Biology\", \"2009 Aug\", \"Michel V, Bakovic M\", \"protein_xref_pubmed\", \"19357133\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735692",
        "row": "[\"Q8WWI5-1\", \"The solute carrier 44A1 is a mitochondrial protein and mediates choline transport.\", \"FASEB journal : official publication of the Federation of American Societies for Experimental Biology\", \"2009 Aug\", \"Michel V, Bakovic M\", \"protein_xref_pubmed\", \"19357133\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735693",
        "row": "[\"Q9UL12-1\", \"Functional expression and processing of rat choline dehydrogenase precursor.\", \"Biochemical and biophysical research communications\", \"2003 Sep 19\", \"Huang S, Lin Q\", \"protein_xref_pubmed\", \"12951056\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735694",
        "row": "[\"Q93088-1\", \"Functional expression and processing of rat choline dehydrogenase precursor.\", \"Biochemical and biophysical research communications\", \"2003 Sep 19\", \"Huang S, Lin Q\", \"protein_xref_pubmed\", \"12951056\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735695",
        "row": "[\"P49419-1\", \"Functional expression and processing of rat choline dehydrogenase precursor.\", \"Biochemical and biophysical research communications\", \"2003 Sep 19\", \"Huang S, Lin Q\", \"protein_xref_pubmed\", \"12951056\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735696",
        "row": "[\"Q9UI17-1\", \"Functional expression and processing of rat choline dehydrogenase precursor.\", \"Biochemical and biophysical research communications\", \"2003 Sep 19\", \"Huang S, Lin Q\", \"protein_xref_pubmed\", \"12951056\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735697",
        "row": "[\"Q8NE62-1\", \"Functional expression and processing of rat choline dehydrogenase precursor.\", \"Biochemical and biophysical research communications\", \"2003 Sep 19\", \"Huang S, Lin Q\", \"protein_xref_pubmed\", \"12951056\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735698",
        "row": "[\"Q8WWI5-1\", \"Functional expression and processing of rat choline dehydrogenase precursor.\", \"Biochemical and biophysical research communications\", \"2003 Sep 19\", \"Huang S, Lin Q\", \"protein_xref_pubmed\", \"12951056\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735699",
        "row": "[\"Q9UL12-1\", \"Studies on choline dehydrogenase. II. Components of the choline oxidase system and the site of action of amytal.\", \"The Journal of biological chemistry\", \"1960 Feb\", \"PACKER L, ESTABROOK RW, SINGER TP, KIMURA T\", \"protein_xref_pubmed\", \"14429690\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735700",
        "row": "[\"Q93088-1\", \"Studies on choline dehydrogenase. II. Components of the choline oxidase system and the site of action of amytal.\", \"The Journal of biological chemistry\", \"1960 Feb\", \"PACKER L, ESTABROOK RW, SINGER TP, KIMURA T\", \"protein_xref_pubmed\", \"14429690\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735701",
        "row": "[\"P49419-1\", \"Studies on choline dehydrogenase. II. Components of the choline oxidase system and the site of action of amytal.\", \"The Journal of biological chemistry\", \"1960 Feb\", \"PACKER L, ESTABROOK RW, SINGER TP, KIMURA T\", \"protein_xref_pubmed\", \"14429690\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735702",
        "row": "[\"Q9UI17-1\", \"Studies on choline dehydrogenase. II. Components of the choline oxidase system and the site of action of amytal.\", \"The Journal of biological chemistry\", \"1960 Feb\", \"PACKER L, ESTABROOK RW, SINGER TP, KIMURA T\", \"protein_xref_pubmed\", \"14429690\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735703",
        "row": "[\"Q8NE62-1\", \"Studies on choline dehydrogenase. II. Components of the choline oxidase system and the site of action of amytal.\", \"The Journal of biological chemistry\", \"1960 Feb\", \"PACKER L, ESTABROOK RW, SINGER TP, KIMURA T\", \"protein_xref_pubmed\", \"14429690\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735704",
        "row": "[\"Q8WWI5-1\", \"Studies on choline dehydrogenase. II. Components of the choline oxidase system and the site of action of amytal.\", \"The Journal of biological chemistry\", \"1960 Feb\", \"PACKER L, ESTABROOK RW, SINGER TP, KIMURA T\", \"protein_xref_pubmed\", \"14429690\", \"protein_xref_reactome\", \"R-HSA-6798163\"]"
    },
    {
        "recordid": "GLY_000310_1_735705",
        "row": "[\"A5YKK6-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735706",
        "row": "[\"P30307-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735707",
        "row": "[\"Q9UIV1-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735708",
        "row": "[\"Q9H4X1-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735709",
        "row": "[\"Q9UFF9-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735710",
        "row": "[\"Q9UM63-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735711",
        "row": "[\"Q92600-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735712",
        "row": "[\"Q9C0C2-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735713",
        "row": "[\"O75175-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735714",
        "row": "[\"P04637-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735715",
        "row": "[\"Q9H4B4-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735716",
        "row": "[\"Q9HC77-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735717",
        "row": "[\"Q9H9A5-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735718",
        "row": "[\"O95628-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735719",
        "row": "[\"P78543-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735720",
        "row": "[\"Q9UKZ1-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735721",
        "row": "[\"Q96LI5-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735722",
        "row": "[\"Q9NZN8-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735723",
        "row": "[\"Q9ULM6-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735724",
        "row": "[\"P06748-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735725",
        "row": "[\"Q9NYY3-1\", \"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene.\", \"Gene\", \"2002 Jan 9\", \"Duriez C, Falette N, Audoynaud C, Moyret-Lalle C, Bensaad K, Courtois S, Wang Q, Soussi T, Puisieux A\", \"protein_xref_pubmed\", \"11814693\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735726",
        "row": "[\"A5YKK6-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735727",
        "row": "[\"P30307-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735728",
        "row": "[\"Q9UIV1-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735729",
        "row": "[\"Q9H4X1-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735730",
        "row": "[\"Q9UFF9-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735731",
        "row": "[\"Q9UM63-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735732",
        "row": "[\"Q92600-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735733",
        "row": "[\"Q9C0C2-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735734",
        "row": "[\"O75175-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735735",
        "row": "[\"P04637-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735736",
        "row": "[\"Q9H4B4-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735737",
        "row": "[\"Q9HC77-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735738",
        "row": "[\"Q9H9A5-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735739",
        "row": "[\"O95628-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735740",
        "row": "[\"P78543-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735741",
        "row": "[\"Q9UKZ1-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735742",
        "row": "[\"Q96LI5-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735743",
        "row": "[\"Q9NZN8-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735744",
        "row": "[\"Q9ULM6-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735745",
        "row": "[\"P06748-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735746",
        "row": "[\"Q9NYY3-1\", \"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway.\", \"Nature genetics\", \"1996 Dec\", \"Rouault JP, Falette N, Guehenneux F, Guillot C, Rimokh R, Wang Q, Berthet C, Moyret-Lalle C, Savatier P, Pain B, Shaw P, Berger R, Samarut J, Magaud JP, Ozturk M, Samarut C, Puisieux A\", \"protein_xref_pubmed\", \"8944033\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735747",
        "row": "[\"A5YKK6-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735748",
        "row": "[\"P30307-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735749",
        "row": "[\"Q9UIV1-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735750",
        "row": "[\"Q9H4X1-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735751",
        "row": "[\"Q9UFF9-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735752",
        "row": "[\"Q9UM63-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735753",
        "row": "[\"Q92600-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735754",
        "row": "[\"Q9C0C2-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735755",
        "row": "[\"O75175-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735756",
        "row": "[\"P04637-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735757",
        "row": "[\"Q9H4B4-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735758",
        "row": "[\"Q9HC77-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735759",
        "row": "[\"Q9H9A5-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735760",
        "row": "[\"O95628-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735761",
        "row": "[\"P78543-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735762",
        "row": "[\"Q9UKZ1-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735763",
        "row": "[\"Q96LI5-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735764",
        "row": "[\"Q9NZN8-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735765",
        "row": "[\"Q9ULM6-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735766",
        "row": "[\"P06748-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735767",
        "row": "[\"Q9NYY3-1\", \"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex.\", \"The Journal of biological chemistry\", \"2009 May 8\", \"Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F\", \"protein_xref_pubmed\", \"19276069\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735768",
        "row": "[\"A5YKK6-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735769",
        "row": "[\"P30307-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735770",
        "row": "[\"Q9UIV1-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735771",
        "row": "[\"Q9H4X1-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735772",
        "row": "[\"Q9UFF9-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735773",
        "row": "[\"Q9UM63-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735774",
        "row": "[\"Q92600-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735775",
        "row": "[\"Q9C0C2-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735776",
        "row": "[\"O75175-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735777",
        "row": "[\"P04637-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735778",
        "row": "[\"Q9H4B4-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735779",
        "row": "[\"Q9HC77-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735780",
        "row": "[\"Q9H9A5-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735781",
        "row": "[\"O95628-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735782",
        "row": "[\"P78543-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735783",
        "row": "[\"Q9UKZ1-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735784",
        "row": "[\"Q96LI5-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735785",
        "row": "[\"Q9NZN8-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735786",
        "row": "[\"Q9ULM6-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735787",
        "row": "[\"P06748-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735788",
        "row": "[\"Q9NYY3-1\", \"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex.\", \"The Journal of biological chemistry\", \"1998 Aug 28\", \"Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L\", \"protein_xref_pubmed\", \"9712883\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735789",
        "row": "[\"A5YKK6-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735790",
        "row": "[\"P30307-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735791",
        "row": "[\"Q9UIV1-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735792",
        "row": "[\"Q9H4X1-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735793",
        "row": "[\"Q9UFF9-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735794",
        "row": "[\"Q9UM63-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735795",
        "row": "[\"Q92600-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735796",
        "row": "[\"Q9C0C2-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735797",
        "row": "[\"O75175-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735798",
        "row": "[\"P04637-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735799",
        "row": "[\"Q9H4B4-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735800",
        "row": "[\"Q9HC77-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735801",
        "row": "[\"Q9H9A5-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735802",
        "row": "[\"O95628-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735803",
        "row": "[\"P78543-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735804",
        "row": "[\"Q9UKZ1-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735805",
        "row": "[\"Q96LI5-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735806",
        "row": "[\"Q9NZN8-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735807",
        "row": "[\"Q9ULM6-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735808",
        "row": "[\"P06748-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735809",
        "row": "[\"Q9NYY3-1\", \"The BTG2 protein is a general activator of mRNA deadenylation.\", \"The EMBO journal\", \"2008 Apr 9\", \"Mauxion F, Faux C, Seraphin B\", \"protein_xref_pubmed\", \"18337750\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735810",
        "row": "[\"A5YKK6-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735811",
        "row": "[\"P30307-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735812",
        "row": "[\"Q9UIV1-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735813",
        "row": "[\"Q9H4X1-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735814",
        "row": "[\"Q9UFF9-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735815",
        "row": "[\"Q9UM63-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735816",
        "row": "[\"Q92600-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735817",
        "row": "[\"Q9C0C2-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735818",
        "row": "[\"O75175-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735819",
        "row": "[\"P04637-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735820",
        "row": "[\"Q9H4B4-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735821",
        "row": "[\"Q9HC77-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735822",
        "row": "[\"Q9H9A5-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735823",
        "row": "[\"O95628-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735824",
        "row": "[\"P78543-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735825",
        "row": "[\"Q9UKZ1-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735826",
        "row": "[\"Q96LI5-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735827",
        "row": "[\"Q9NZN8-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735828",
        "row": "[\"Q9ULM6-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735829",
        "row": "[\"P06748-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735830",
        "row": "[\"Q9NYY3-1\", \"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex.\", \"PloS one\", \"2012\", \"Doidge R, Mittal S, Aslam A, Winkler GS\", \"protein_xref_pubmed\", \"23236473\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735831",
        "row": "[\"A5YKK6-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735832",
        "row": "[\"P30307-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735833",
        "row": "[\"Q9UIV1-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735834",
        "row": "[\"Q9H4X1-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735835",
        "row": "[\"Q9UFF9-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735836",
        "row": "[\"Q9UM63-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735837",
        "row": "[\"Q92600-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735838",
        "row": "[\"Q9C0C2-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735839",
        "row": "[\"O75175-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735840",
        "row": "[\"P04637-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735841",
        "row": "[\"Q9H4B4-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735842",
        "row": "[\"Q9HC77-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735843",
        "row": "[\"Q9H9A5-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735844",
        "row": "[\"O95628-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735845",
        "row": "[\"P78543-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735846",
        "row": "[\"Q9UKZ1-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735847",
        "row": "[\"Q96LI5-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735848",
        "row": "[\"Q9NZN8-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735849",
        "row": "[\"Q9ULM6-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735850",
        "row": "[\"P06748-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735851",
        "row": "[\"Q9NYY3-1\", \"Evidence providing new insights into TOB-promoted deadenylation and supporting a link between TOB's deadenylation-enhancing and antiproliferative activities.\", \"Molecular and cellular biology\", \"2012 Mar\", \"Ezzeddine N, Chen CY, Shyu AB\", \"protein_xref_pubmed\", \"22252318\", \"protein_xref_reactome\", \"R-HSA-6804115\"]"
    },
    {
        "recordid": "GLY_000310_1_735852",
        "row": "[\"Q92851-1\", \"Molecular cloning of the interleukin-1 beta converting enzyme.\", \"Science (New York, N.Y.)\", \"1992 Apr 3\", \"Cerretti DP, Kozlosky CJ, Mosley B, Nelson N, Van Ness K, Greenstreet TA, March CJ, Kronheim SR, Druck T, Cannizzaro LA, et al.\", \"protein_xref_pubmed\", \"1373520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735853",
        "row": "[\"O14727-1\", \"Molecular cloning of the interleukin-1 beta converting enzyme.\", \"Science (New York, N.Y.)\", \"1992 Apr 3\", \"Cerretti DP, Kozlosky CJ, Mosley B, Nelson N, Van Ness K, Greenstreet TA, March CJ, Kronheim SR, Druck T, Cannizzaro LA, et al.\", \"protein_xref_pubmed\", \"1373520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735854",
        "row": "[\"Q9NPP4-1\", \"Molecular cloning of the interleukin-1 beta converting enzyme.\", \"Science (New York, N.Y.)\", \"1992 Apr 3\", \"Cerretti DP, Kozlosky CJ, Mosley B, Nelson N, Van Ness K, Greenstreet TA, March CJ, Kronheim SR, Druck T, Cannizzaro LA, et al.\", \"protein_xref_pubmed\", \"1373520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735855",
        "row": "[\"P04637-1\", \"Molecular cloning of the interleukin-1 beta converting enzyme.\", \"Science (New York, N.Y.)\", \"1992 Apr 3\", \"Cerretti DP, Kozlosky CJ, Mosley B, Nelson N, Van Ness K, Greenstreet TA, March CJ, Kronheim SR, Druck T, Cannizzaro LA, et al.\", \"protein_xref_pubmed\", \"1373520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735856",
        "row": "[\"P55212-1\", \"Molecular cloning of the interleukin-1 beta converting enzyme.\", \"Science (New York, N.Y.)\", \"1992 Apr 3\", \"Cerretti DP, Kozlosky CJ, Mosley B, Nelson N, Van Ness K, Greenstreet TA, March CJ, Kronheim SR, Druck T, Cannizzaro LA, et al.\", \"protein_xref_pubmed\", \"1373520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735857",
        "row": "[\"Q9H3D4-1\", \"Molecular cloning of the interleukin-1 beta converting enzyme.\", \"Science (New York, N.Y.)\", \"1992 Apr 3\", \"Cerretti DP, Kozlosky CJ, Mosley B, Nelson N, Van Ness K, Greenstreet TA, March CJ, Kronheim SR, Druck T, Cannizzaro LA, et al.\", \"protein_xref_pubmed\", \"1373520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735858",
        "row": "[\"P42575-1\", \"Molecular cloning of the interleukin-1 beta converting enzyme.\", \"Science (New York, N.Y.)\", \"1992 Apr 3\", \"Cerretti DP, Kozlosky CJ, Mosley B, Nelson N, Van Ness K, Greenstreet TA, March CJ, Kronheim SR, Druck T, Cannizzaro LA, et al.\", \"protein_xref_pubmed\", \"1373520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735859",
        "row": "[\"O15350-1\", \"Molecular cloning of the interleukin-1 beta converting enzyme.\", \"Science (New York, N.Y.)\", \"1992 Apr 3\", \"Cerretti DP, Kozlosky CJ, Mosley B, Nelson N, Van Ness K, Greenstreet TA, March CJ, Kronheim SR, Druck T, Cannizzaro LA, et al.\", \"protein_xref_pubmed\", \"1373520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735860",
        "row": "[\"Q13315-1\", \"Molecular cloning of the interleukin-1 beta converting enzyme.\", \"Science (New York, N.Y.)\", \"1992 Apr 3\", \"Cerretti DP, Kozlosky CJ, Mosley B, Nelson N, Van Ness K, Greenstreet TA, March CJ, Kronheim SR, Druck T, Cannizzaro LA, et al.\", \"protein_xref_pubmed\", \"1373520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735861",
        "row": "[\"P78560-1\", \"Molecular cloning of the interleukin-1 beta converting enzyme.\", \"Science (New York, N.Y.)\", \"1992 Apr 3\", \"Cerretti DP, Kozlosky CJ, Mosley B, Nelson N, Van Ness K, Greenstreet TA, March CJ, Kronheim SR, Druck T, Cannizzaro LA, et al.\", \"protein_xref_pubmed\", \"1373520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735862",
        "row": "[\"P29466-1\", \"Molecular cloning of the interleukin-1 beta converting enzyme.\", \"Science (New York, N.Y.)\", \"1992 Apr 3\", \"Cerretti DP, Kozlosky CJ, Mosley B, Nelson N, Van Ness K, Greenstreet TA, March CJ, Kronheim SR, Druck T, Cannizzaro LA, et al.\", \"protein_xref_pubmed\", \"1373520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735863",
        "row": "[\"Q9HB75-1\", \"Molecular cloning of the interleukin-1 beta converting enzyme.\", \"Science (New York, N.Y.)\", \"1992 Apr 3\", \"Cerretti DP, Kozlosky CJ, Mosley B, Nelson N, Van Ness K, Greenstreet TA, March CJ, Kronheim SR, Druck T, Cannizzaro LA, et al.\", \"protein_xref_pubmed\", \"1373520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735864",
        "row": "[\"Q92851-1\", \"Caspase-1-dependent processing of pro-interleukin-1beta is cytosolic and precedes cell death.\", \"Journal of cell science\", \"2007 Mar 1\", \"Brough D, Rothwell NJ\", \"protein_xref_pubmed\", \"17284521\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735865",
        "row": "[\"O14727-1\", \"Caspase-1-dependent processing of pro-interleukin-1beta is cytosolic and precedes cell death.\", \"Journal of cell science\", \"2007 Mar 1\", \"Brough D, Rothwell NJ\", \"protein_xref_pubmed\", \"17284521\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735866",
        "row": "[\"Q9NPP4-1\", \"Caspase-1-dependent processing of pro-interleukin-1beta is cytosolic and precedes cell death.\", \"Journal of cell science\", \"2007 Mar 1\", \"Brough D, Rothwell NJ\", \"protein_xref_pubmed\", \"17284521\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735867",
        "row": "[\"P04637-1\", \"Caspase-1-dependent processing of pro-interleukin-1beta is cytosolic and precedes cell death.\", \"Journal of cell science\", \"2007 Mar 1\", \"Brough D, Rothwell NJ\", \"protein_xref_pubmed\", \"17284521\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735868",
        "row": "[\"P55212-1\", \"Caspase-1-dependent processing of pro-interleukin-1beta is cytosolic and precedes cell death.\", \"Journal of cell science\", \"2007 Mar 1\", \"Brough D, Rothwell NJ\", \"protein_xref_pubmed\", \"17284521\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735869",
        "row": "[\"Q9H3D4-1\", \"Caspase-1-dependent processing of pro-interleukin-1beta is cytosolic and precedes cell death.\", \"Journal of cell science\", \"2007 Mar 1\", \"Brough D, Rothwell NJ\", \"protein_xref_pubmed\", \"17284521\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735870",
        "row": "[\"P42575-1\", \"Caspase-1-dependent processing of pro-interleukin-1beta is cytosolic and precedes cell death.\", \"Journal of cell science\", \"2007 Mar 1\", \"Brough D, Rothwell NJ\", \"protein_xref_pubmed\", \"17284521\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735871",
        "row": "[\"O15350-1\", \"Caspase-1-dependent processing of pro-interleukin-1beta is cytosolic and precedes cell death.\", \"Journal of cell science\", \"2007 Mar 1\", \"Brough D, Rothwell NJ\", \"protein_xref_pubmed\", \"17284521\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735872",
        "row": "[\"Q13315-1\", \"Caspase-1-dependent processing of pro-interleukin-1beta is cytosolic and precedes cell death.\", \"Journal of cell science\", \"2007 Mar 1\", \"Brough D, Rothwell NJ\", \"protein_xref_pubmed\", \"17284521\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735873",
        "row": "[\"P78560-1\", \"Caspase-1-dependent processing of pro-interleukin-1beta is cytosolic and precedes cell death.\", \"Journal of cell science\", \"2007 Mar 1\", \"Brough D, Rothwell NJ\", \"protein_xref_pubmed\", \"17284521\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735874",
        "row": "[\"P29466-1\", \"Caspase-1-dependent processing of pro-interleukin-1beta is cytosolic and precedes cell death.\", \"Journal of cell science\", \"2007 Mar 1\", \"Brough D, Rothwell NJ\", \"protein_xref_pubmed\", \"17284521\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735875",
        "row": "[\"Q9HB75-1\", \"Caspase-1-dependent processing of pro-interleukin-1beta is cytosolic and precedes cell death.\", \"Journal of cell science\", \"2007 Mar 1\", \"Brough D, Rothwell NJ\", \"protein_xref_pubmed\", \"17284521\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735876",
        "row": "[\"Q92851-1\", \"Direct transcriptional activation of human caspase-1 by tumor suppressor p53.\", \"The Journal of biological chemistry\", \"2001 Apr 6\", \"Gupta S, Radha V, Furukawa Y, Swarup G\", \"protein_xref_pubmed\", \"11278253\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735877",
        "row": "[\"O14727-1\", \"Direct transcriptional activation of human caspase-1 by tumor suppressor p53.\", \"The Journal of biological chemistry\", \"2001 Apr 6\", \"Gupta S, Radha V, Furukawa Y, Swarup G\", \"protein_xref_pubmed\", \"11278253\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735878",
        "row": "[\"Q9NPP4-1\", \"Direct transcriptional activation of human caspase-1 by tumor suppressor p53.\", \"The Journal of biological chemistry\", \"2001 Apr 6\", \"Gupta S, Radha V, Furukawa Y, Swarup G\", \"protein_xref_pubmed\", \"11278253\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735879",
        "row": "[\"P04637-1\", \"Direct transcriptional activation of human caspase-1 by tumor suppressor p53.\", \"The Journal of biological chemistry\", \"2001 Apr 6\", \"Gupta S, Radha V, Furukawa Y, Swarup G\", \"protein_xref_pubmed\", \"11278253\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735880",
        "row": "[\"P55212-1\", \"Direct transcriptional activation of human caspase-1 by tumor suppressor p53.\", \"The Journal of biological chemistry\", \"2001 Apr 6\", \"Gupta S, Radha V, Furukawa Y, Swarup G\", \"protein_xref_pubmed\", \"11278253\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735881",
        "row": "[\"Q9H3D4-1\", \"Direct transcriptional activation of human caspase-1 by tumor suppressor p53.\", \"The Journal of biological chemistry\", \"2001 Apr 6\", \"Gupta S, Radha V, Furukawa Y, Swarup G\", \"protein_xref_pubmed\", \"11278253\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735882",
        "row": "[\"P42575-1\", \"Direct transcriptional activation of human caspase-1 by tumor suppressor p53.\", \"The Journal of biological chemistry\", \"2001 Apr 6\", \"Gupta S, Radha V, Furukawa Y, Swarup G\", \"protein_xref_pubmed\", \"11278253\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735883",
        "row": "[\"O15350-1\", \"Direct transcriptional activation of human caspase-1 by tumor suppressor p53.\", \"The Journal of biological chemistry\", \"2001 Apr 6\", \"Gupta S, Radha V, Furukawa Y, Swarup G\", \"protein_xref_pubmed\", \"11278253\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735884",
        "row": "[\"Q13315-1\", \"Direct transcriptional activation of human caspase-1 by tumor suppressor p53.\", \"The Journal of biological chemistry\", \"2001 Apr 6\", \"Gupta S, Radha V, Furukawa Y, Swarup G\", \"protein_xref_pubmed\", \"11278253\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735885",
        "row": "[\"P78560-1\", \"Direct transcriptional activation of human caspase-1 by tumor suppressor p53.\", \"The Journal of biological chemistry\", \"2001 Apr 6\", \"Gupta S, Radha V, Furukawa Y, Swarup G\", \"protein_xref_pubmed\", \"11278253\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735886",
        "row": "[\"P29466-1\", \"Direct transcriptional activation of human caspase-1 by tumor suppressor p53.\", \"The Journal of biological chemistry\", \"2001 Apr 6\", \"Gupta S, Radha V, Furukawa Y, Swarup G\", \"protein_xref_pubmed\", \"11278253\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735887",
        "row": "[\"Q9HB75-1\", \"Direct transcriptional activation of human caspase-1 by tumor suppressor p53.\", \"The Journal of biological chemistry\", \"2001 Apr 6\", \"Gupta S, Radha V, Furukawa Y, Swarup G\", \"protein_xref_pubmed\", \"11278253\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735888",
        "row": "[\"Q92851-1\", \"Role of p73 in regulating human caspase-1 gene transcription induced by interferon-{gamma} and cisplatin.\", \"The Journal of biological chemistry\", \"2005 Nov 4\", \"Jain N, Gupta S, Sudhakar Ch, Radha V, Swarup G\", \"protein_xref_pubmed\", \"16135520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735889",
        "row": "[\"O14727-1\", \"Role of p73 in regulating human caspase-1 gene transcription induced by interferon-{gamma} and cisplatin.\", \"The Journal of biological chemistry\", \"2005 Nov 4\", \"Jain N, Gupta S, Sudhakar Ch, Radha V, Swarup G\", \"protein_xref_pubmed\", \"16135520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735890",
        "row": "[\"Q9NPP4-1\", \"Role of p73 in regulating human caspase-1 gene transcription induced by interferon-{gamma} and cisplatin.\", \"The Journal of biological chemistry\", \"2005 Nov 4\", \"Jain N, Gupta S, Sudhakar Ch, Radha V, Swarup G\", \"protein_xref_pubmed\", \"16135520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735891",
        "row": "[\"P04637-1\", \"Role of p73 in regulating human caspase-1 gene transcription induced by interferon-{gamma} and cisplatin.\", \"The Journal of biological chemistry\", \"2005 Nov 4\", \"Jain N, Gupta S, Sudhakar Ch, Radha V, Swarup G\", \"protein_xref_pubmed\", \"16135520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735892",
        "row": "[\"P55212-1\", \"Role of p73 in regulating human caspase-1 gene transcription induced by interferon-{gamma} and cisplatin.\", \"The Journal of biological chemistry\", \"2005 Nov 4\", \"Jain N, Gupta S, Sudhakar Ch, Radha V, Swarup G\", \"protein_xref_pubmed\", \"16135520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735893",
        "row": "[\"Q9H3D4-1\", \"Role of p73 in regulating human caspase-1 gene transcription induced by interferon-{gamma} and cisplatin.\", \"The Journal of biological chemistry\", \"2005 Nov 4\", \"Jain N, Gupta S, Sudhakar Ch, Radha V, Swarup G\", \"protein_xref_pubmed\", \"16135520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735894",
        "row": "[\"P42575-1\", \"Role of p73 in regulating human caspase-1 gene transcription induced by interferon-{gamma} and cisplatin.\", \"The Journal of biological chemistry\", \"2005 Nov 4\", \"Jain N, Gupta S, Sudhakar Ch, Radha V, Swarup G\", \"protein_xref_pubmed\", \"16135520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735895",
        "row": "[\"O15350-1\", \"Role of p73 in regulating human caspase-1 gene transcription induced by interferon-{gamma} and cisplatin.\", \"The Journal of biological chemistry\", \"2005 Nov 4\", \"Jain N, Gupta S, Sudhakar Ch, Radha V, Swarup G\", \"protein_xref_pubmed\", \"16135520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735896",
        "row": "[\"Q13315-1\", \"Role of p73 in regulating human caspase-1 gene transcription induced by interferon-{gamma} and cisplatin.\", \"The Journal of biological chemistry\", \"2005 Nov 4\", \"Jain N, Gupta S, Sudhakar Ch, Radha V, Swarup G\", \"protein_xref_pubmed\", \"16135520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735897",
        "row": "[\"P78560-1\", \"Role of p73 in regulating human caspase-1 gene transcription induced by interferon-{gamma} and cisplatin.\", \"The Journal of biological chemistry\", \"2005 Nov 4\", \"Jain N, Gupta S, Sudhakar Ch, Radha V, Swarup G\", \"protein_xref_pubmed\", \"16135520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735898",
        "row": "[\"P29466-1\", \"Role of p73 in regulating human caspase-1 gene transcription induced by interferon-{gamma} and cisplatin.\", \"The Journal of biological chemistry\", \"2005 Nov 4\", \"Jain N, Gupta S, Sudhakar Ch, Radha V, Swarup G\", \"protein_xref_pubmed\", \"16135520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735899",
        "row": "[\"Q9HB75-1\", \"Role of p73 in regulating human caspase-1 gene transcription induced by interferon-{gamma} and cisplatin.\", \"The Journal of biological chemistry\", \"2005 Nov 4\", \"Jain N, Gupta S, Sudhakar Ch, Radha V, Swarup G\", \"protein_xref_pubmed\", \"16135520\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735900",
        "row": "[\"Q92851-1\", \"Caspase-1 is a novel target of p63 in tumor suppression.\", \"Cell death &amp; disease\", \"2013 May 23\", \"Celardo I, Grespi F, Antonov A, Bernassola F, Garabadgiu AV, Melino G, Amelio I\", \"protein_xref_pubmed\", \"23703390\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735901",
        "row": "[\"O14727-1\", \"Caspase-1 is a novel target of p63 in tumor suppression.\", \"Cell death &amp; disease\", \"2013 May 23\", \"Celardo I, Grespi F, Antonov A, Bernassola F, Garabadgiu AV, Melino G, Amelio I\", \"protein_xref_pubmed\", \"23703390\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735902",
        "row": "[\"Q9NPP4-1\", \"Caspase-1 is a novel target of p63 in tumor suppression.\", \"Cell death &amp; disease\", \"2013 May 23\", \"Celardo I, Grespi F, Antonov A, Bernassola F, Garabadgiu AV, Melino G, Amelio I\", \"protein_xref_pubmed\", \"23703390\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735903",
        "row": "[\"P04637-1\", \"Caspase-1 is a novel target of p63 in tumor suppression.\", \"Cell death &amp; disease\", \"2013 May 23\", \"Celardo I, Grespi F, Antonov A, Bernassola F, Garabadgiu AV, Melino G, Amelio I\", \"protein_xref_pubmed\", \"23703390\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735904",
        "row": "[\"P55212-1\", \"Caspase-1 is a novel target of p63 in tumor suppression.\", \"Cell death &amp; disease\", \"2013 May 23\", \"Celardo I, Grespi F, Antonov A, Bernassola F, Garabadgiu AV, Melino G, Amelio I\", \"protein_xref_pubmed\", \"23703390\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735905",
        "row": "[\"Q9H3D4-1\", \"Caspase-1 is a novel target of p63 in tumor suppression.\", \"Cell death &amp; disease\", \"2013 May 23\", \"Celardo I, Grespi F, Antonov A, Bernassola F, Garabadgiu AV, Melino G, Amelio I\", \"protein_xref_pubmed\", \"23703390\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735906",
        "row": "[\"P42575-1\", \"Caspase-1 is a novel target of p63 in tumor suppression.\", \"Cell death &amp; disease\", \"2013 May 23\", \"Celardo I, Grespi F, Antonov A, Bernassola F, Garabadgiu AV, Melino G, Amelio I\", \"protein_xref_pubmed\", \"23703390\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735907",
        "row": "[\"O15350-1\", \"Caspase-1 is a novel target of p63 in tumor suppression.\", \"Cell death &amp; disease\", \"2013 May 23\", \"Celardo I, Grespi F, Antonov A, Bernassola F, Garabadgiu AV, Melino G, Amelio I\", \"protein_xref_pubmed\", \"23703390\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735908",
        "row": "[\"Q13315-1\", \"Caspase-1 is a novel target of p63 in tumor suppression.\", \"Cell death &amp; disease\", \"2013 May 23\", \"Celardo I, Grespi F, Antonov A, Bernassola F, Garabadgiu AV, Melino G, Amelio I\", \"protein_xref_pubmed\", \"23703390\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735909",
        "row": "[\"P78560-1\", \"Caspase-1 is a novel target of p63 in tumor suppression.\", \"Cell death &amp; disease\", \"2013 May 23\", \"Celardo I, Grespi F, Antonov A, Bernassola F, Garabadgiu AV, Melino G, Amelio I\", \"protein_xref_pubmed\", \"23703390\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735910",
        "row": "[\"P29466-1\", \"Caspase-1 is a novel target of p63 in tumor suppression.\", \"Cell death &amp; disease\", \"2013 May 23\", \"Celardo I, Grespi F, Antonov A, Bernassola F, Garabadgiu AV, Melino G, Amelio I\", \"protein_xref_pubmed\", \"23703390\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735911",
        "row": "[\"Q9HB75-1\", \"Caspase-1 is a novel target of p63 in tumor suppression.\", \"Cell death &amp; disease\", \"2013 May 23\", \"Celardo I, Grespi F, Antonov A, Bernassola F, Garabadgiu AV, Melino G, Amelio I\", \"protein_xref_pubmed\", \"23703390\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735912",
        "row": "[\"Q92851-1\", \"Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3.\", \"Cell\", \"1993 Nov 19\", \"Miura M, Zhu H, Rotello R, Hartwieg EA, Yuan J\", \"protein_xref_pubmed\", \"8242741\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735913",
        "row": "[\"O14727-1\", \"Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3.\", \"Cell\", \"1993 Nov 19\", \"Miura M, Zhu H, Rotello R, Hartwieg EA, Yuan J\", \"protein_xref_pubmed\", \"8242741\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735914",
        "row": "[\"Q9NPP4-1\", \"Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3.\", \"Cell\", \"1993 Nov 19\", \"Miura M, Zhu H, Rotello R, Hartwieg EA, Yuan J\", \"protein_xref_pubmed\", \"8242741\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735915",
        "row": "[\"P04637-1\", \"Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3.\", \"Cell\", \"1993 Nov 19\", \"Miura M, Zhu H, Rotello R, Hartwieg EA, Yuan J\", \"protein_xref_pubmed\", \"8242741\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735916",
        "row": "[\"P55212-1\", \"Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3.\", \"Cell\", \"1993 Nov 19\", \"Miura M, Zhu H, Rotello R, Hartwieg EA, Yuan J\", \"protein_xref_pubmed\", \"8242741\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735917",
        "row": "[\"Q9H3D4-1\", \"Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3.\", \"Cell\", \"1993 Nov 19\", \"Miura M, Zhu H, Rotello R, Hartwieg EA, Yuan J\", \"protein_xref_pubmed\", \"8242741\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735918",
        "row": "[\"P42575-1\", \"Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3.\", \"Cell\", \"1993 Nov 19\", \"Miura M, Zhu H, Rotello R, Hartwieg EA, Yuan J\", \"protein_xref_pubmed\", \"8242741\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735919",
        "row": "[\"O15350-1\", \"Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3.\", \"Cell\", \"1993 Nov 19\", \"Miura M, Zhu H, Rotello R, Hartwieg EA, Yuan J\", \"protein_xref_pubmed\", \"8242741\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735920",
        "row": "[\"Q13315-1\", \"Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3.\", \"Cell\", \"1993 Nov 19\", \"Miura M, Zhu H, Rotello R, Hartwieg EA, Yuan J\", \"protein_xref_pubmed\", \"8242741\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735921",
        "row": "[\"P78560-1\", \"Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3.\", \"Cell\", \"1993 Nov 19\", \"Miura M, Zhu H, Rotello R, Hartwieg EA, Yuan J\", \"protein_xref_pubmed\", \"8242741\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735922",
        "row": "[\"P29466-1\", \"Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3.\", \"Cell\", \"1993 Nov 19\", \"Miura M, Zhu H, Rotello R, Hartwieg EA, Yuan J\", \"protein_xref_pubmed\", \"8242741\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735923",
        "row": "[\"Q9HB75-1\", \"Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3.\", \"Cell\", \"1993 Nov 19\", \"Miura M, Zhu H, Rotello R, Hartwieg EA, Yuan J\", \"protein_xref_pubmed\", \"8242741\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735924",
        "row": "[\"Q92851-1\", \"Apoptotic threshold is lowered by p53 transactivation of caspase-6.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2002 Jul 9\", \"MacLachlan TK, El-Deiry WS\", \"protein_xref_pubmed\", \"12089322\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735925",
        "row": "[\"O14727-1\", \"Apoptotic threshold is lowered by p53 transactivation of caspase-6.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2002 Jul 9\", \"MacLachlan TK, El-Deiry WS\", \"protein_xref_pubmed\", \"12089322\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735926",
        "row": "[\"Q9NPP4-1\", \"Apoptotic threshold is lowered by p53 transactivation of caspase-6.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2002 Jul 9\", \"MacLachlan TK, El-Deiry WS\", \"protein_xref_pubmed\", \"12089322\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735927",
        "row": "[\"P04637-1\", \"Apoptotic threshold is lowered by p53 transactivation of caspase-6.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2002 Jul 9\", \"MacLachlan TK, El-Deiry WS\", \"protein_xref_pubmed\", \"12089322\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735928",
        "row": "[\"P55212-1\", \"Apoptotic threshold is lowered by p53 transactivation of caspase-6.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2002 Jul 9\", \"MacLachlan TK, El-Deiry WS\", \"protein_xref_pubmed\", \"12089322\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735929",
        "row": "[\"Q9H3D4-1\", \"Apoptotic threshold is lowered by p53 transactivation of caspase-6.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2002 Jul 9\", \"MacLachlan TK, El-Deiry WS\", \"protein_xref_pubmed\", \"12089322\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735930",
        "row": "[\"P42575-1\", \"Apoptotic threshold is lowered by p53 transactivation of caspase-6.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2002 Jul 9\", \"MacLachlan TK, El-Deiry WS\", \"protein_xref_pubmed\", \"12089322\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735931",
        "row": "[\"O15350-1\", \"Apoptotic threshold is lowered by p53 transactivation of caspase-6.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2002 Jul 9\", \"MacLachlan TK, El-Deiry WS\", \"protein_xref_pubmed\", \"12089322\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735932",
        "row": "[\"Q13315-1\", \"Apoptotic threshold is lowered by p53 transactivation of caspase-6.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2002 Jul 9\", \"MacLachlan TK, El-Deiry WS\", \"protein_xref_pubmed\", \"12089322\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735933",
        "row": "[\"P78560-1\", \"Apoptotic threshold is lowered by p53 transactivation of caspase-6.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2002 Jul 9\", \"MacLachlan TK, El-Deiry WS\", \"protein_xref_pubmed\", \"12089322\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735934",
        "row": "[\"P29466-1\", \"Apoptotic threshold is lowered by p53 transactivation of caspase-6.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2002 Jul 9\", \"MacLachlan TK, El-Deiry WS\", \"protein_xref_pubmed\", \"12089322\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735935",
        "row": "[\"Q9HB75-1\", \"Apoptotic threshold is lowered by p53 transactivation of caspase-6.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2002 Jul 9\", \"MacLachlan TK, El-Deiry WS\", \"protein_xref_pubmed\", \"12089322\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735936",
        "row": "[\"Q92851-1\", \"Caspase 10 levels are increased following DNA damage in a p53-dependent manner.\", \"Cancer biology &amp; therapy\", \"2003 Nov-Dec\", \"Rikhof B, Corn PG, El-Deiry WS\", \"protein_xref_pubmed\", \"14688482\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735937",
        "row": "[\"O14727-1\", \"Caspase 10 levels are increased following DNA damage in a p53-dependent manner.\", \"Cancer biology &amp; therapy\", \"2003 Nov-Dec\", \"Rikhof B, Corn PG, El-Deiry WS\", \"protein_xref_pubmed\", \"14688482\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735938",
        "row": "[\"Q9NPP4-1\", \"Caspase 10 levels are increased following DNA damage in a p53-dependent manner.\", \"Cancer biology &amp; therapy\", \"2003 Nov-Dec\", \"Rikhof B, Corn PG, El-Deiry WS\", \"protein_xref_pubmed\", \"14688482\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735939",
        "row": "[\"P04637-1\", \"Caspase 10 levels are increased following DNA damage in a p53-dependent manner.\", \"Cancer biology &amp; therapy\", \"2003 Nov-Dec\", \"Rikhof B, Corn PG, El-Deiry WS\", \"protein_xref_pubmed\", \"14688482\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735940",
        "row": "[\"P55212-1\", \"Caspase 10 levels are increased following DNA damage in a p53-dependent manner.\", \"Cancer biology &amp; therapy\", \"2003 Nov-Dec\", \"Rikhof B, Corn PG, El-Deiry WS\", \"protein_xref_pubmed\", \"14688482\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735941",
        "row": "[\"Q9H3D4-1\", \"Caspase 10 levels are increased following DNA damage in a p53-dependent manner.\", \"Cancer biology &amp; therapy\", \"2003 Nov-Dec\", \"Rikhof B, Corn PG, El-Deiry WS\", \"protein_xref_pubmed\", \"14688482\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735942",
        "row": "[\"P42575-1\", \"Caspase 10 levels are increased following DNA damage in a p53-dependent manner.\", \"Cancer biology &amp; therapy\", \"2003 Nov-Dec\", \"Rikhof B, Corn PG, El-Deiry WS\", \"protein_xref_pubmed\", \"14688482\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735943",
        "row": "[\"O15350-1\", \"Caspase 10 levels are increased following DNA damage in a p53-dependent manner.\", \"Cancer biology &amp; therapy\", \"2003 Nov-Dec\", \"Rikhof B, Corn PG, El-Deiry WS\", \"protein_xref_pubmed\", \"14688482\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735944",
        "row": "[\"Q13315-1\", \"Caspase 10 levels are increased following DNA damage in a p53-dependent manner.\", \"Cancer biology &amp; therapy\", \"2003 Nov-Dec\", \"Rikhof B, Corn PG, El-Deiry WS\", \"protein_xref_pubmed\", \"14688482\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735945",
        "row": "[\"P78560-1\", \"Caspase 10 levels are increased following DNA damage in a p53-dependent manner.\", \"Cancer biology &amp; therapy\", \"2003 Nov-Dec\", \"Rikhof B, Corn PG, El-Deiry WS\", \"protein_xref_pubmed\", \"14688482\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735946",
        "row": "[\"P29466-1\", \"Caspase 10 levels are increased following DNA damage in a p53-dependent manner.\", \"Cancer biology &amp; therapy\", \"2003 Nov-Dec\", \"Rikhof B, Corn PG, El-Deiry WS\", \"protein_xref_pubmed\", \"14688482\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735947",
        "row": "[\"Q9HB75-1\", \"Caspase 10 levels are increased following DNA damage in a p53-dependent manner.\", \"Cancer biology &amp; therapy\", \"2003 Nov-Dec\", \"Rikhof B, Corn PG, El-Deiry WS\", \"protein_xref_pubmed\", \"14688482\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735948",
        "row": "[\"O14727-1\", \"Caspase-10 is an initiator caspase in death receptor signaling.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2001 Nov 20\", \"Wang J, Chun HJ, Wong W, Spencer DM, Lenardo MJ\", \"protein_xref_pubmed\", \"11717445\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735949",
        "row": "[\"Q9NPP4-1\", \"Caspase-10 is an initiator caspase in death receptor signaling.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2001 Nov 20\", \"Wang J, Chun HJ, Wong W, Spencer DM, Lenardo MJ\", \"protein_xref_pubmed\", \"11717445\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735950",
        "row": "[\"P04637-1\", \"Caspase-10 is an initiator caspase in death receptor signaling.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2001 Nov 20\", \"Wang J, Chun HJ, Wong W, Spencer DM, Lenardo MJ\", \"protein_xref_pubmed\", \"11717445\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735951",
        "row": "[\"P55212-1\", \"Caspase-10 is an initiator caspase in death receptor signaling.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2001 Nov 20\", \"Wang J, Chun HJ, Wong W, Spencer DM, Lenardo MJ\", \"protein_xref_pubmed\", \"11717445\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735952",
        "row": "[\"Q9H3D4-1\", \"Caspase-10 is an initiator caspase in death receptor signaling.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2001 Nov 20\", \"Wang J, Chun HJ, Wong W, Spencer DM, Lenardo MJ\", \"protein_xref_pubmed\", \"11717445\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735953",
        "row": "[\"P42575-1\", \"Caspase-10 is an initiator caspase in death receptor signaling.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2001 Nov 20\", \"Wang J, Chun HJ, Wong W, Spencer DM, Lenardo MJ\", \"protein_xref_pubmed\", \"11717445\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735954",
        "row": "[\"O15350-1\", \"Caspase-10 is an initiator caspase in death receptor signaling.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2001 Nov 20\", \"Wang J, Chun HJ, Wong W, Spencer DM, Lenardo MJ\", \"protein_xref_pubmed\", \"11717445\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735955",
        "row": "[\"Q13315-1\", \"Caspase-10 is an initiator caspase in death receptor signaling.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2001 Nov 20\", \"Wang J, Chun HJ, Wong W, Spencer DM, Lenardo MJ\", \"protein_xref_pubmed\", \"11717445\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735956",
        "row": "[\"P78560-1\", \"Caspase-10 is an initiator caspase in death receptor signaling.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2001 Nov 20\", \"Wang J, Chun HJ, Wong W, Spencer DM, Lenardo MJ\", \"protein_xref_pubmed\", \"11717445\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735957",
        "row": "[\"P29466-1\", \"Caspase-10 is an initiator caspase in death receptor signaling.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2001 Nov 20\", \"Wang J, Chun HJ, Wong W, Spencer DM, Lenardo MJ\", \"protein_xref_pubmed\", \"11717445\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735958",
        "row": "[\"Q9HB75-1\", \"Caspase-10 is an initiator caspase in death receptor signaling.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2001 Nov 20\", \"Wang J, Chun HJ, Wong W, Spencer DM, Lenardo MJ\", \"protein_xref_pubmed\", \"11717445\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735959",
        "row": "[\"O14727-1\", \"Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8.\", \"The EMBO journal\", \"2002 Sep 2\", \"Sprick MR, Rieser E, Stahl H, Grosse-Wilde A, Weigand MA, Walczak H\", \"protein_xref_pubmed\", \"12198154\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735960",
        "row": "[\"Q9NPP4-1\", \"Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8.\", \"The EMBO journal\", \"2002 Sep 2\", \"Sprick MR, Rieser E, Stahl H, Grosse-Wilde A, Weigand MA, Walczak H\", \"protein_xref_pubmed\", \"12198154\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735961",
        "row": "[\"P04637-1\", \"Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8.\", \"The EMBO journal\", \"2002 Sep 2\", \"Sprick MR, Rieser E, Stahl H, Grosse-Wilde A, Weigand MA, Walczak H\", \"protein_xref_pubmed\", \"12198154\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735962",
        "row": "[\"P55212-1\", \"Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8.\", \"The EMBO journal\", \"2002 Sep 2\", \"Sprick MR, Rieser E, Stahl H, Grosse-Wilde A, Weigand MA, Walczak H\", \"protein_xref_pubmed\", \"12198154\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735963",
        "row": "[\"Q9H3D4-1\", \"Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8.\", \"The EMBO journal\", \"2002 Sep 2\", \"Sprick MR, Rieser E, Stahl H, Grosse-Wilde A, Weigand MA, Walczak H\", \"protein_xref_pubmed\", \"12198154\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735964",
        "row": "[\"P42575-1\", \"Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8.\", \"The EMBO journal\", \"2002 Sep 2\", \"Sprick MR, Rieser E, Stahl H, Grosse-Wilde A, Weigand MA, Walczak H\", \"protein_xref_pubmed\", \"12198154\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735965",
        "row": "[\"O15350-1\", \"Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8.\", \"The EMBO journal\", \"2002 Sep 2\", \"Sprick MR, Rieser E, Stahl H, Grosse-Wilde A, Weigand MA, Walczak H\", \"protein_xref_pubmed\", \"12198154\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735966",
        "row": "[\"Q13315-1\", \"Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8.\", \"The EMBO journal\", \"2002 Sep 2\", \"Sprick MR, Rieser E, Stahl H, Grosse-Wilde A, Weigand MA, Walczak H\", \"protein_xref_pubmed\", \"12198154\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735967",
        "row": "[\"P78560-1\", \"Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8.\", \"The EMBO journal\", \"2002 Sep 2\", \"Sprick MR, Rieser E, Stahl H, Grosse-Wilde A, Weigand MA, Walczak H\", \"protein_xref_pubmed\", \"12198154\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735968",
        "row": "[\"P29466-1\", \"Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8.\", \"The EMBO journal\", \"2002 Sep 2\", \"Sprick MR, Rieser E, Stahl H, Grosse-Wilde A, Weigand MA, Walczak H\", \"protein_xref_pubmed\", \"12198154\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735969",
        "row": "[\"Q9HB75-1\", \"Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8.\", \"The EMBO journal\", \"2002 Sep 2\", \"Sprick MR, Rieser E, Stahl H, Grosse-Wilde A, Weigand MA, Walczak H\", \"protein_xref_pubmed\", \"12198154\", \"protein_xref_reactome\", \"R-HSA-6803207\"]"
    },
    {
        "recordid": "GLY_000310_1_735970",
        "row": "[\"Q13526-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735971",
        "row": "[\"P05109-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735972",
        "row": "[\"P63000-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735973",
        "row": "[\"Q05513-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735974",
        "row": "[\"P15153-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735975",
        "row": "[\"P19878-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735976",
        "row": "[\"Q8NEB9-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735977",
        "row": "[\"Q99570-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735978",
        "row": "[\"P14598-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735979",
        "row": "[\"Q16539-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735980",
        "row": "[\"P04839-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735981",
        "row": "[\"P05771-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735982",
        "row": "[\"P06702-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735983",
        "row": "[\"Q05655-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735984",
        "row": "[\"Q9HBY0-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735985",
        "row": "[\"Q15080-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735986",
        "row": "[\"P28482-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735987",
        "row": "[\"P13498-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735988",
        "row": "[\"P27361-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735989",
        "row": "[\"Q8NFA2-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735990",
        "row": "[\"P17252-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735991",
        "row": "[\"Q9Y5S8-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735992",
        "row": "[\"Q86UR1-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735993",
        "row": "[\"Q15759-1\", \"Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic.\", \"The FEBS journal\", \"2013 Jun\", \"Raiborg C, Schink KO, Stenmark H\", \"protein_xref_pubmed\", \"23289851\", \"protein_xref_reactome\", \"R-HSA-5668599\"]"
    },
    {
        "recordid": "GLY_000310_1_735994",
        "row": "[\"P30307-1\", \"DNA damage-induced downregulation of Cdc25C is mediated by p53 via two independent mechanisms: one involves direct binding to the cdc25C promoter.\", \"Molecular cell\", \"2004 Dec 3\", \"St Clair S, Giono L, Varmeh-Ziaie S, Resnick-Silverman L, Liu WJ, Padi A, Dastidar J, DaCosta A, Mattia M, Manfredi JJ\", \"protein_xref_pubmed\", \"15574328\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735995",
        "row": "[\"P31947-1\", \"DNA damage-induced downregulation of Cdc25C is mediated by p53 via two independent mechanisms: one involves direct binding to the cdc25C promoter.\", \"Molecular cell\", \"2004 Dec 3\", \"St Clair S, Giono L, Varmeh-Ziaie S, Resnick-Silverman L, Liu WJ, Padi A, Dastidar J, DaCosta A, Mattia M, Manfredi JJ\", \"protein_xref_pubmed\", \"15574328\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735996",
        "row": "[\"Q07812-1\", \"DNA damage-induced downregulation of Cdc25C is mediated by p53 via two independent mechanisms: one involves direct binding to the cdc25C promoter.\", \"Molecular cell\", \"2004 Dec 3\", \"St Clair S, Giono L, Varmeh-Ziaie S, Resnick-Silverman L, Liu WJ, Padi A, Dastidar J, DaCosta A, Mattia M, Manfredi JJ\", \"protein_xref_pubmed\", \"15574328\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735997",
        "row": "[\"Q96PM9-4\", \"DNA damage-induced downregulation of Cdc25C is mediated by p53 via two independent mechanisms: one involves direct binding to the cdc25C promoter.\", \"Molecular cell\", \"2004 Dec 3\", \"St Clair S, Giono L, Varmeh-Ziaie S, Resnick-Silverman L, Liu WJ, Padi A, Dastidar J, DaCosta A, Mattia M, Manfredi JJ\", \"protein_xref_pubmed\", \"15574328\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735998",
        "row": "[\"P28749-1\", \"DNA damage-induced downregulation of Cdc25C is mediated by p53 via two independent mechanisms: one involves direct binding to the cdc25C promoter.\", \"Molecular cell\", \"2004 Dec 3\", \"St Clair S, Giono L, Varmeh-Ziaie S, Resnick-Silverman L, Liu WJ, Padi A, Dastidar J, DaCosta A, Mattia M, Manfredi JJ\", \"protein_xref_pubmed\", \"15574328\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_735999",
        "row": "[\"Q16254-1\", \"DNA damage-induced downregulation of Cdc25C is mediated by p53 via two independent mechanisms: one involves direct binding to the cdc25C promoter.\", \"Molecular cell\", \"2004 Dec 3\", \"St Clair S, Giono L, Varmeh-Ziaie S, Resnick-Silverman L, Liu WJ, Padi A, Dastidar J, DaCosta A, Mattia M, Manfredi JJ\", \"protein_xref_pubmed\", \"15574328\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    },
    {
        "recordid": "GLY_000310_1_736000",
        "row": "[\"P04637-1\", \"DNA damage-induced downregulation of Cdc25C is mediated by p53 via two independent mechanisms: one involves direct binding to the cdc25C promoter.\", \"Molecular cell\", \"2004 Dec 3\", \"St Clair S, Giono L, Varmeh-Ziaie S, Resnick-Silverman L, Liu WJ, Padi A, Dastidar J, DaCosta A, Mattia M, Manfredi JJ\", \"protein_xref_pubmed\", \"15574328\", \"protein_xref_reactome\", \"R-HSA-6804114\"]"
    }
]
