[
    {
        "recordid": "GLY_000310_1_84001",
        "row": "[\"P04211-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84002",
        "row": "[\"P01619-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84003",
        "row": "[\"P01614-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84004",
        "row": "[\"P01615-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84005",
        "row": "[\"P01611-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84006",
        "row": "[\"P19174-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84007",
        "row": "[\"P01768-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84008",
        "row": "[\"P01762-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84009",
        "row": "[\"P01763-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84010",
        "row": "[\"P01764-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84011",
        "row": "[\"P01767-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84012",
        "row": "[\"P28482-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84013",
        "row": "[\"P0DOY2-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84014",
        "row": "[\"P0DOY3-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84015",
        "row": "[\"A0M8Q6-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84016",
        "row": "[\"P01624-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84017",
        "row": "[\"P01597-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84018",
        "row": "[\"P01593-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84019",
        "row": "[\"P01599-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84020",
        "row": "[\"P01766-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84021",
        "row": "[\"P0CG04-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84022",
        "row": "[\"P27361-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84023",
        "row": "[\"P80748-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84024",
        "row": "[\"Q01362-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84025",
        "row": "[\"P01854-2\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84026",
        "row": "[\"P23083-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84027",
        "row": "[\"P01742-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84028",
        "row": "[\"P01743-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84029",
        "row": "[\"P04430-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84030",
        "row": "[\"P01825-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84031",
        "row": "[\"P01824-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84032",
        "row": "[\"P0CF74-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84033",
        "row": "[\"Q13153-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84034",
        "row": "[\"A0A0C4DH73-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84035",
        "row": "[\"A2NJV5-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84036",
        "row": "[\"P01834-1\", \"Adapters in the organization of mast cell signaling.\", \"Immunological reviews\", \"2009 Nov\", \"Alvarez-Errico D, Lessmann E, Rivera J\", \"protein_xref_pubmed\", \"19909365\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84037",
        "row": "[\"P45984-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84038",
        "row": "[\"P05412-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84039",
        "row": "[\"P15498-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84040",
        "row": "[\"P04433-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84041",
        "row": "[\"P04432-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84042",
        "row": "[\"P07948-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84043",
        "row": "[\"P06315-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84044",
        "row": "[\"Q13177-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84045",
        "row": "[\"P12319-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84046",
        "row": "[\"P01817-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84047",
        "row": "[\"P01814-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84048",
        "row": "[\"P16885-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84049",
        "row": "[\"P01718-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84050",
        "row": "[\"P01782-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84051",
        "row": "[\"P01780-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84052",
        "row": "[\"A0A0C4DH25-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84053",
        "row": "[\"P01111-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84054",
        "row": "[\"P53779-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84055",
        "row": "[\"Q9UKW4-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84056",
        "row": "[\"A0A075B6S6-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84057",
        "row": "[\"P43405-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84058",
        "row": "[\"P01112-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84059",
        "row": "[\"P01721-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84060",
        "row": "[\"Q13094-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84061",
        "row": "[\"P63000-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84062",
        "row": "[\"P01100-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84063",
        "row": "[\"P01594-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84064",
        "row": "[\"P45985-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84065",
        "row": "[\"P45983-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84066",
        "row": "[\"O14733-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84067",
        "row": "[\"P01715-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84068",
        "row": "[\"P01714-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84069",
        "row": "[\"P01717-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84070",
        "row": "[\"P01699-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84071",
        "row": "[\"P06310-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84072",
        "row": "[\"P06312-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84073",
        "row": "[\"P01703-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84074",
        "row": "[\"P01700-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84075",
        "row": "[\"P01701-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84076",
        "row": "[\"P01706-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84077",
        "row": "[\"P01704-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84078",
        "row": "[\"P01705-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84079",
        "row": "[\"P01709-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84080",
        "row": "[\"P52735-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84081",
        "row": "[\"Q07889-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84082",
        "row": "[\"A0A075B6P5-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84083",
        "row": "[\"O75791-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84084",
        "row": "[\"P01602-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84085",
        "row": "[\"P01601-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84086",
        "row": "[\"P30273-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84087",
        "row": "[\"P01772-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84088",
        "row": "[\"P06331-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84089",
        "row": "[\"Q13233-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84090",
        "row": "[\"P04211-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84091",
        "row": "[\"P01619-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84092",
        "row": "[\"P01614-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84093",
        "row": "[\"P01615-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84094",
        "row": "[\"P01611-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84095",
        "row": "[\"P19174-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84096",
        "row": "[\"P01768-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84097",
        "row": "[\"P01762-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84098",
        "row": "[\"P01763-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84099",
        "row": "[\"P01764-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84100",
        "row": "[\"P01767-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84101",
        "row": "[\"P28482-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84102",
        "row": "[\"P0DOY2-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84103",
        "row": "[\"P0DOY3-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84104",
        "row": "[\"A0M8Q6-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84105",
        "row": "[\"P01624-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84106",
        "row": "[\"P01597-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84107",
        "row": "[\"P01593-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84108",
        "row": "[\"P01599-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84109",
        "row": "[\"P01766-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84110",
        "row": "[\"P0CG04-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84111",
        "row": "[\"P27361-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84112",
        "row": "[\"P80748-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84113",
        "row": "[\"Q01362-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84114",
        "row": "[\"P01854-2\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84115",
        "row": "[\"P23083-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84116",
        "row": "[\"P01742-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84117",
        "row": "[\"P01743-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84118",
        "row": "[\"P04430-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84119",
        "row": "[\"P01825-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84120",
        "row": "[\"P01824-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84121",
        "row": "[\"P0CF74-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84122",
        "row": "[\"Q13153-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84123",
        "row": "[\"A0A0C4DH73-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84124",
        "row": "[\"A2NJV5-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84125",
        "row": "[\"P01834-1\", \"Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes.\", \"Molecular and cellular biology\", \"1997 Jul\", \"Harmer SL, DeFranco AL\", \"protein_xref_pubmed\", \"9199344\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84126",
        "row": "[\"P45984-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84127",
        "row": "[\"P05412-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84128",
        "row": "[\"P15498-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84129",
        "row": "[\"P04433-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84130",
        "row": "[\"P04432-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84131",
        "row": "[\"P07948-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84132",
        "row": "[\"P06315-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84133",
        "row": "[\"Q13177-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84134",
        "row": "[\"P12319-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84135",
        "row": "[\"P01817-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84136",
        "row": "[\"P01814-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84137",
        "row": "[\"P01718-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84138",
        "row": "[\"P01782-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84139",
        "row": "[\"P01780-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84140",
        "row": "[\"A0A0C4DH25-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84141",
        "row": "[\"P53779-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84142",
        "row": "[\"A0A075B6S6-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84143",
        "row": "[\"P01721-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84144",
        "row": "[\"P01100-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84145",
        "row": "[\"P01594-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84146",
        "row": "[\"P45985-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84147",
        "row": "[\"P45983-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84148",
        "row": "[\"O14733-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84149",
        "row": "[\"P01715-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84150",
        "row": "[\"P01714-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84151",
        "row": "[\"P01717-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84152",
        "row": "[\"P01699-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84153",
        "row": "[\"P06310-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84154",
        "row": "[\"P06312-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84155",
        "row": "[\"P01703-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84156",
        "row": "[\"P01700-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84157",
        "row": "[\"P01701-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84158",
        "row": "[\"P01706-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84159",
        "row": "[\"P01704-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84160",
        "row": "[\"P01705-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84161",
        "row": "[\"P01709-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84162",
        "row": "[\"A0A075B6P5-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84163",
        "row": "[\"P01602-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84164",
        "row": "[\"P01601-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84165",
        "row": "[\"P30273-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84166",
        "row": "[\"P01772-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84167",
        "row": "[\"P06331-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84168",
        "row": "[\"Q13233-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84169",
        "row": "[\"P04211-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84170",
        "row": "[\"P01619-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84171",
        "row": "[\"P01614-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84172",
        "row": "[\"P01615-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84173",
        "row": "[\"P01611-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84174",
        "row": "[\"P01768-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84175",
        "row": "[\"P01762-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84176",
        "row": "[\"P01763-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84177",
        "row": "[\"P01764-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84178",
        "row": "[\"P01767-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84179",
        "row": "[\"P28482-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84180",
        "row": "[\"P0DOY2-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84181",
        "row": "[\"P0DOY3-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84182",
        "row": "[\"A0M8Q6-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84183",
        "row": "[\"P01624-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84184",
        "row": "[\"P01597-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84185",
        "row": "[\"P01593-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84186",
        "row": "[\"P01599-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84187",
        "row": "[\"P01766-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84188",
        "row": "[\"P0CG04-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84189",
        "row": "[\"P27361-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84190",
        "row": "[\"P80748-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84191",
        "row": "[\"Q01362-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84192",
        "row": "[\"P01854-2\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84193",
        "row": "[\"P23083-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84194",
        "row": "[\"P01742-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84195",
        "row": "[\"P01743-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84196",
        "row": "[\"P04430-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84197",
        "row": "[\"P01825-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84198",
        "row": "[\"P01824-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84199",
        "row": "[\"P0CF74-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84200",
        "row": "[\"Q13153-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84201",
        "row": "[\"A0A0C4DH73-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84202",
        "row": "[\"A2NJV5-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84203",
        "row": "[\"P01834-1\", \"Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function.\", \"The Journal of biological chemistry\", \"1996 Aug 16\", \"Bubeck Wardenburg J, Fu C, Jackman JK, Flotow H, Wilkinson SE, Williams DH, Johnson R, Kong G, Chan AC, Findell PR\", \"protein_xref_pubmed\", \"8702662\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84204",
        "row": "[\"P45984-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84205",
        "row": "[\"P05412-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84206",
        "row": "[\"P15498-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84207",
        "row": "[\"P04433-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84208",
        "row": "[\"P04432-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84209",
        "row": "[\"P07948-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84210",
        "row": "[\"P06315-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84211",
        "row": "[\"Q13177-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84212",
        "row": "[\"P12319-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84213",
        "row": "[\"P01817-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84214",
        "row": "[\"P01814-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84215",
        "row": "[\"P01718-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84216",
        "row": "[\"P01782-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84217",
        "row": "[\"P01780-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84218",
        "row": "[\"A0A0C4DH25-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84219",
        "row": "[\"P53779-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84220",
        "row": "[\"A0A075B6S6-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84221",
        "row": "[\"P01721-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84222",
        "row": "[\"P01100-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84223",
        "row": "[\"P01594-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84224",
        "row": "[\"P45985-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84225",
        "row": "[\"P45983-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84226",
        "row": "[\"O14733-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84227",
        "row": "[\"P01715-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84228",
        "row": "[\"P01714-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84229",
        "row": "[\"P01717-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84230",
        "row": "[\"P01699-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84231",
        "row": "[\"P06310-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84232",
        "row": "[\"P06312-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84233",
        "row": "[\"P01703-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84234",
        "row": "[\"P01700-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84235",
        "row": "[\"P01701-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84236",
        "row": "[\"P01706-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84237",
        "row": "[\"P01704-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84238",
        "row": "[\"P01705-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84239",
        "row": "[\"P01709-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84240",
        "row": "[\"A0A075B6P5-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84241",
        "row": "[\"P01602-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84242",
        "row": "[\"P01601-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84243",
        "row": "[\"P30273-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84244",
        "row": "[\"P01772-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84245",
        "row": "[\"P06331-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84246",
        "row": "[\"Q13233-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84247",
        "row": "[\"P04211-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84248",
        "row": "[\"P01619-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84249",
        "row": "[\"P01614-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84250",
        "row": "[\"P01615-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84251",
        "row": "[\"P01611-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84252",
        "row": "[\"P01768-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84253",
        "row": "[\"P01762-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84254",
        "row": "[\"P01763-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84255",
        "row": "[\"P01764-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84256",
        "row": "[\"P01767-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84257",
        "row": "[\"P28482-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84258",
        "row": "[\"P0DOY2-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84259",
        "row": "[\"P0DOY3-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84260",
        "row": "[\"A0M8Q6-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84261",
        "row": "[\"P01624-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84262",
        "row": "[\"P01597-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84263",
        "row": "[\"P01593-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84264",
        "row": "[\"P01599-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84265",
        "row": "[\"P01766-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84266",
        "row": "[\"P0CG04-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84267",
        "row": "[\"P27361-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84268",
        "row": "[\"P80748-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84269",
        "row": "[\"Q01362-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84270",
        "row": "[\"P01854-2\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84271",
        "row": "[\"P23083-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84272",
        "row": "[\"P01742-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84273",
        "row": "[\"P01743-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84274",
        "row": "[\"P04430-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84275",
        "row": "[\"P01825-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84276",
        "row": "[\"P01824-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84277",
        "row": "[\"P0CF74-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84278",
        "row": "[\"Q13153-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84279",
        "row": "[\"A0A0C4DH73-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84280",
        "row": "[\"A2NJV5-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84281",
        "row": "[\"P01834-1\", \"Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets.\", \"The Journal of biological chemistry\", \"1999 Feb 26\", \"Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP\", \"protein_xref_pubmed\", \"10026222\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84282",
        "row": "[\"P45984-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84283",
        "row": "[\"P05412-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84284",
        "row": "[\"P15498-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84285",
        "row": "[\"P04433-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84286",
        "row": "[\"P04432-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84287",
        "row": "[\"P07948-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84288",
        "row": "[\"P06315-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84289",
        "row": "[\"Q13177-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84290",
        "row": "[\"P12319-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84291",
        "row": "[\"P01817-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84292",
        "row": "[\"P01814-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84293",
        "row": "[\"P01718-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84294",
        "row": "[\"P01782-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84295",
        "row": "[\"P01780-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84296",
        "row": "[\"A0A0C4DH25-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84297",
        "row": "[\"P53779-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84298",
        "row": "[\"A0A075B6S6-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84299",
        "row": "[\"P01721-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84300",
        "row": "[\"P01100-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84301",
        "row": "[\"P01594-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84302",
        "row": "[\"P45985-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84303",
        "row": "[\"P45983-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84304",
        "row": "[\"O14733-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84305",
        "row": "[\"P01715-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84306",
        "row": "[\"P01714-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84307",
        "row": "[\"P01717-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84308",
        "row": "[\"P01699-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84309",
        "row": "[\"P06310-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84310",
        "row": "[\"P06312-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84311",
        "row": "[\"P01703-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84312",
        "row": "[\"P01700-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84313",
        "row": "[\"P01701-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84314",
        "row": "[\"P01706-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84315",
        "row": "[\"P01704-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84316",
        "row": "[\"P01705-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84317",
        "row": "[\"P01709-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84318",
        "row": "[\"A0A075B6P5-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84319",
        "row": "[\"P01602-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84320",
        "row": "[\"P01601-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84321",
        "row": "[\"P30273-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84322",
        "row": "[\"P01772-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84323",
        "row": "[\"P06331-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84324",
        "row": "[\"Q13233-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84325",
        "row": "[\"P04211-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84326",
        "row": "[\"P01619-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84327",
        "row": "[\"P01614-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84328",
        "row": "[\"P01615-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84329",
        "row": "[\"P01611-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84330",
        "row": "[\"P01768-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84331",
        "row": "[\"P01762-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84332",
        "row": "[\"P01763-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84333",
        "row": "[\"P01764-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84334",
        "row": "[\"P01767-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84335",
        "row": "[\"P28482-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84336",
        "row": "[\"P0DOY2-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84337",
        "row": "[\"P0DOY3-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84338",
        "row": "[\"A0M8Q6-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84339",
        "row": "[\"P01624-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84340",
        "row": "[\"P01597-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84341",
        "row": "[\"P01593-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84342",
        "row": "[\"P01599-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84343",
        "row": "[\"P01766-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84344",
        "row": "[\"P0CG04-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84345",
        "row": "[\"P27361-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84346",
        "row": "[\"P80748-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84347",
        "row": "[\"Q01362-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84348",
        "row": "[\"P01854-2\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84349",
        "row": "[\"P23083-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84350",
        "row": "[\"P01742-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84351",
        "row": "[\"P01743-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84352",
        "row": "[\"P04430-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84353",
        "row": "[\"P01825-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84354",
        "row": "[\"P01824-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84355",
        "row": "[\"P0CF74-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84356",
        "row": "[\"Q13153-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84357",
        "row": "[\"A0A0C4DH73-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84358",
        "row": "[\"A2NJV5-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84359",
        "row": "[\"P01834-1\", \"SLP-76 couples Syk to the osteoclast cytoskeleton.\", \"Journal of immunology (Baltimore, Md. : 1950)\", \"2009 Aug 1\", \"Reeve JL, Zou W, Liu Y, Maltzman JS, Ross FP, Teitelbaum SL\", \"protein_xref_pubmed\", \"19592646\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84360",
        "row": "[\"P45984-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84361",
        "row": "[\"P05412-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84362",
        "row": "[\"P15498-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84363",
        "row": "[\"P04433-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84364",
        "row": "[\"P04432-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84365",
        "row": "[\"P07948-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84366",
        "row": "[\"P06315-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84367",
        "row": "[\"Q13177-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84368",
        "row": "[\"P12319-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84369",
        "row": "[\"P01817-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84370",
        "row": "[\"P01814-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84371",
        "row": "[\"P16885-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84372",
        "row": "[\"P01718-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84373",
        "row": "[\"P01782-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84374",
        "row": "[\"P01780-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84375",
        "row": "[\"A0A0C4DH25-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84376",
        "row": "[\"P01111-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84377",
        "row": "[\"P53779-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84378",
        "row": "[\"Q9UKW4-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84379",
        "row": "[\"A0A075B6S6-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84380",
        "row": "[\"P43405-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84381",
        "row": "[\"P01112-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84382",
        "row": "[\"P01721-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84383",
        "row": "[\"Q13094-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84384",
        "row": "[\"P63000-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84385",
        "row": "[\"P01100-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84386",
        "row": "[\"P01594-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84387",
        "row": "[\"P45985-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84388",
        "row": "[\"P45983-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84389",
        "row": "[\"O14733-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84390",
        "row": "[\"P01715-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84391",
        "row": "[\"P01714-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84392",
        "row": "[\"P01717-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84393",
        "row": "[\"P01699-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84394",
        "row": "[\"P06310-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84395",
        "row": "[\"P06312-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84396",
        "row": "[\"P01703-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84397",
        "row": "[\"P01700-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84398",
        "row": "[\"P01701-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84399",
        "row": "[\"P01706-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84400",
        "row": "[\"P01704-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84401",
        "row": "[\"P01705-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84402",
        "row": "[\"P01709-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84403",
        "row": "[\"P52735-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84404",
        "row": "[\"Q07889-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84405",
        "row": "[\"A0A075B6P5-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84406",
        "row": "[\"O75791-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84407",
        "row": "[\"P01602-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84408",
        "row": "[\"P01601-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84409",
        "row": "[\"P30273-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84410",
        "row": "[\"P01772-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84411",
        "row": "[\"P06331-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84412",
        "row": "[\"Q13233-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84413",
        "row": "[\"P04211-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84414",
        "row": "[\"P01619-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84415",
        "row": "[\"P01614-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84416",
        "row": "[\"P01615-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84417",
        "row": "[\"P01611-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84418",
        "row": "[\"P19174-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84419",
        "row": "[\"P01768-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84420",
        "row": "[\"P01762-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84421",
        "row": "[\"P01763-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84422",
        "row": "[\"P01764-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84423",
        "row": "[\"P01767-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84424",
        "row": "[\"P28482-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84425",
        "row": "[\"P0DOY2-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84426",
        "row": "[\"P0DOY3-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84427",
        "row": "[\"A0M8Q6-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84428",
        "row": "[\"P01624-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84429",
        "row": "[\"P01597-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84430",
        "row": "[\"P01593-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84431",
        "row": "[\"P01599-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84432",
        "row": "[\"P01766-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84433",
        "row": "[\"P0CG04-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84434",
        "row": "[\"P27361-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84435",
        "row": "[\"P80748-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84436",
        "row": "[\"Q01362-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84437",
        "row": "[\"P01854-2\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84438",
        "row": "[\"P23083-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84439",
        "row": "[\"P01742-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84440",
        "row": "[\"P01743-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84441",
        "row": "[\"P04430-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84442",
        "row": "[\"P01825-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84443",
        "row": "[\"P01824-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84444",
        "row": "[\"P0CF74-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84445",
        "row": "[\"Q13153-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84446",
        "row": "[\"A0A0C4DH73-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84447",
        "row": "[\"A2NJV5-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84448",
        "row": "[\"P01834-1\", \"SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells.\", \"The Journal of biological chemistry\", \"1997 Jan 10\", \"Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA\", \"protein_xref_pubmed\", \"8995445\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84449",
        "row": "[\"P45984-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84450",
        "row": "[\"P05412-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84451",
        "row": "[\"P15498-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84452",
        "row": "[\"P04433-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84453",
        "row": "[\"P04432-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84454",
        "row": "[\"P07948-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84455",
        "row": "[\"P06315-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84456",
        "row": "[\"Q13177-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84457",
        "row": "[\"P12319-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84458",
        "row": "[\"P01817-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84459",
        "row": "[\"P01814-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84460",
        "row": "[\"P16885-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84461",
        "row": "[\"P01718-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84462",
        "row": "[\"P01782-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84463",
        "row": "[\"P01780-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84464",
        "row": "[\"A0A0C4DH25-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84465",
        "row": "[\"P01111-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84466",
        "row": "[\"P53779-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84467",
        "row": "[\"Q9UKW4-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84468",
        "row": "[\"A0A075B6S6-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84469",
        "row": "[\"P43405-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84470",
        "row": "[\"P01112-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84471",
        "row": "[\"P01721-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84472",
        "row": "[\"Q13094-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84473",
        "row": "[\"P63000-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84474",
        "row": "[\"P01100-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84475",
        "row": "[\"P01594-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84476",
        "row": "[\"P45985-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84477",
        "row": "[\"P45983-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84478",
        "row": "[\"O14733-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84479",
        "row": "[\"P01715-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84480",
        "row": "[\"P01714-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84481",
        "row": "[\"P01717-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84482",
        "row": "[\"P01699-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84483",
        "row": "[\"P06310-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84484",
        "row": "[\"P06312-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84485",
        "row": "[\"P01703-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84486",
        "row": "[\"P01700-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84487",
        "row": "[\"P01701-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84488",
        "row": "[\"P01706-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84489",
        "row": "[\"P01704-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84490",
        "row": "[\"P01705-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84491",
        "row": "[\"P01709-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84492",
        "row": "[\"P52735-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84493",
        "row": "[\"Q07889-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84494",
        "row": "[\"A0A075B6P5-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84495",
        "row": "[\"O75791-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84496",
        "row": "[\"P01602-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84497",
        "row": "[\"P01601-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84498",
        "row": "[\"P30273-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84499",
        "row": "[\"P01772-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84500",
        "row": "[\"P06331-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84501",
        "row": "[\"Q13233-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84502",
        "row": "[\"P04211-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84503",
        "row": "[\"P01619-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84504",
        "row": "[\"P01614-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84505",
        "row": "[\"P01615-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84506",
        "row": "[\"P01611-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84507",
        "row": "[\"P19174-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84508",
        "row": "[\"P01768-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84509",
        "row": "[\"P01762-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84510",
        "row": "[\"P01763-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84511",
        "row": "[\"P01764-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84512",
        "row": "[\"P01767-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84513",
        "row": "[\"P28482-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84514",
        "row": "[\"P0DOY2-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84515",
        "row": "[\"P0DOY3-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84516",
        "row": "[\"A0M8Q6-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84517",
        "row": "[\"P01624-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84518",
        "row": "[\"P01597-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84519",
        "row": "[\"P01593-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84520",
        "row": "[\"P01599-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84521",
        "row": "[\"P01766-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84522",
        "row": "[\"P0CG04-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84523",
        "row": "[\"P27361-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84524",
        "row": "[\"P80748-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84525",
        "row": "[\"Q01362-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84526",
        "row": "[\"P01854-2\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84527",
        "row": "[\"P23083-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84528",
        "row": "[\"P01742-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84529",
        "row": "[\"P01743-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84530",
        "row": "[\"P04430-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84531",
        "row": "[\"P01825-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84532",
        "row": "[\"P01824-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84533",
        "row": "[\"P0CF74-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84534",
        "row": "[\"Q13153-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84535",
        "row": "[\"A0A0C4DH73-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84536",
        "row": "[\"A2NJV5-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84537",
        "row": "[\"P01834-1\", \"Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.\", \"Molecular cell\", \"2002 Jan\", \"Parrini MC, Lei M, Harrison SC, Mayer BJ\", \"protein_xref_pubmed\", \"11804587\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84538",
        "row": "[\"P45984-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84539",
        "row": "[\"P05412-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84540",
        "row": "[\"P15498-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84541",
        "row": "[\"P04433-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84542",
        "row": "[\"P04432-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84543",
        "row": "[\"P07948-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84544",
        "row": "[\"P06315-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84545",
        "row": "[\"Q13177-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84546",
        "row": "[\"P12319-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84547",
        "row": "[\"P01817-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84548",
        "row": "[\"P01814-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84549",
        "row": "[\"P16885-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84550",
        "row": "[\"P01718-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84551",
        "row": "[\"P01782-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84552",
        "row": "[\"P01780-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84553",
        "row": "[\"A0A0C4DH25-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84554",
        "row": "[\"P01111-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84555",
        "row": "[\"P53779-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84556",
        "row": "[\"Q9UKW4-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84557",
        "row": "[\"A0A075B6S6-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84558",
        "row": "[\"P43405-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84559",
        "row": "[\"P01112-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84560",
        "row": "[\"P01721-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84561",
        "row": "[\"Q13094-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84562",
        "row": "[\"P63000-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84563",
        "row": "[\"P01100-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84564",
        "row": "[\"P01594-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84565",
        "row": "[\"P45985-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84566",
        "row": "[\"P45983-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84567",
        "row": "[\"O14733-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84568",
        "row": "[\"P01715-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84569",
        "row": "[\"P01714-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84570",
        "row": "[\"P01717-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84571",
        "row": "[\"P01699-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84572",
        "row": "[\"P06310-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84573",
        "row": "[\"P06312-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84574",
        "row": "[\"P01703-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84575",
        "row": "[\"P01700-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84576",
        "row": "[\"P01701-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84577",
        "row": "[\"P01706-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84578",
        "row": "[\"P01704-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84579",
        "row": "[\"P01705-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84580",
        "row": "[\"P01709-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84581",
        "row": "[\"P52735-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84582",
        "row": "[\"Q07889-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84583",
        "row": "[\"A0A075B6P5-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84584",
        "row": "[\"O75791-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84585",
        "row": "[\"P01602-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84586",
        "row": "[\"P01601-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84587",
        "row": "[\"P30273-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84588",
        "row": "[\"P01772-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84589",
        "row": "[\"P06331-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84590",
        "row": "[\"Q13233-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84591",
        "row": "[\"P04211-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84592",
        "row": "[\"P01619-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84593",
        "row": "[\"P01614-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84594",
        "row": "[\"P01615-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84595",
        "row": "[\"P01611-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84596",
        "row": "[\"P19174-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84597",
        "row": "[\"P01768-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84598",
        "row": "[\"P01762-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84599",
        "row": "[\"P01763-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84600",
        "row": "[\"P01764-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84601",
        "row": "[\"P01767-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84602",
        "row": "[\"P28482-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84603",
        "row": "[\"P0DOY2-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84604",
        "row": "[\"P0DOY3-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84605",
        "row": "[\"A0M8Q6-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84606",
        "row": "[\"P01624-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84607",
        "row": "[\"P01597-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84608",
        "row": "[\"P01593-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84609",
        "row": "[\"P01599-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84610",
        "row": "[\"P01766-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84611",
        "row": "[\"P0CG04-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84612",
        "row": "[\"P27361-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84613",
        "row": "[\"P80748-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84614",
        "row": "[\"Q01362-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84615",
        "row": "[\"P01854-2\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84616",
        "row": "[\"P23083-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84617",
        "row": "[\"P01742-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84618",
        "row": "[\"P01743-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84619",
        "row": "[\"P04430-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84620",
        "row": "[\"P01825-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84621",
        "row": "[\"P01824-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84622",
        "row": "[\"P0CF74-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84623",
        "row": "[\"Q13153-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84624",
        "row": "[\"A0A0C4DH73-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84625",
        "row": "[\"A2NJV5-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84626",
        "row": "[\"P01834-1\", \"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.\", \"The Journal of biological chemistry\", \"2001 May 18\", \"Chong C, Tan L, Lim L, Manser E\", \"protein_xref_pubmed\", \"11278486\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84627",
        "row": "[\"P45984-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84628",
        "row": "[\"P05412-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84629",
        "row": "[\"P15498-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84630",
        "row": "[\"P04433-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84631",
        "row": "[\"P04432-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84632",
        "row": "[\"P07948-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84633",
        "row": "[\"P06315-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84634",
        "row": "[\"Q13177-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84635",
        "row": "[\"P12319-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84636",
        "row": "[\"P01817-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84637",
        "row": "[\"P01814-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84638",
        "row": "[\"P16885-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84639",
        "row": "[\"P01718-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84640",
        "row": "[\"P01782-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84641",
        "row": "[\"P01780-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84642",
        "row": "[\"A0A0C4DH25-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84643",
        "row": "[\"P01111-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84644",
        "row": "[\"P53779-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84645",
        "row": "[\"Q9UKW4-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84646",
        "row": "[\"A0A075B6S6-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84647",
        "row": "[\"P43405-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84648",
        "row": "[\"P01112-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84649",
        "row": "[\"P01721-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84650",
        "row": "[\"Q13094-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84651",
        "row": "[\"P63000-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84652",
        "row": "[\"P01100-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84653",
        "row": "[\"P01594-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84654",
        "row": "[\"P45985-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84655",
        "row": "[\"P45983-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84656",
        "row": "[\"O14733-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84657",
        "row": "[\"P01715-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84658",
        "row": "[\"P01714-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84659",
        "row": "[\"P01717-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84660",
        "row": "[\"P01699-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84661",
        "row": "[\"P06310-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84662",
        "row": "[\"P06312-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84663",
        "row": "[\"P01703-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84664",
        "row": "[\"P01700-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84665",
        "row": "[\"P01701-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84666",
        "row": "[\"P01706-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84667",
        "row": "[\"P01704-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84668",
        "row": "[\"P01705-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84669",
        "row": "[\"P01709-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84670",
        "row": "[\"P52735-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84671",
        "row": "[\"Q07889-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84672",
        "row": "[\"A0A075B6P5-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84673",
        "row": "[\"O75791-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84674",
        "row": "[\"P01602-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84675",
        "row": "[\"P01601-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84676",
        "row": "[\"P30273-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84677",
        "row": "[\"P01772-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84678",
        "row": "[\"P06331-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84679",
        "row": "[\"Q13233-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84680",
        "row": "[\"P04211-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84681",
        "row": "[\"P01619-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84682",
        "row": "[\"P01614-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84683",
        "row": "[\"P01615-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84684",
        "row": "[\"P01611-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84685",
        "row": "[\"P19174-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84686",
        "row": "[\"P01768-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84687",
        "row": "[\"P01762-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84688",
        "row": "[\"P01763-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84689",
        "row": "[\"P01764-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84690",
        "row": "[\"P01767-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84691",
        "row": "[\"P28482-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84692",
        "row": "[\"P0DOY2-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84693",
        "row": "[\"P0DOY3-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84694",
        "row": "[\"A0M8Q6-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84695",
        "row": "[\"P01624-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84696",
        "row": "[\"P01597-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84697",
        "row": "[\"P01593-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84698",
        "row": "[\"P01599-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84699",
        "row": "[\"P01766-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84700",
        "row": "[\"P0CG04-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84701",
        "row": "[\"P27361-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84702",
        "row": "[\"P80748-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84703",
        "row": "[\"Q01362-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84704",
        "row": "[\"P01854-2\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84705",
        "row": "[\"P23083-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84706",
        "row": "[\"P01742-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84707",
        "row": "[\"P01743-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84708",
        "row": "[\"P04430-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84709",
        "row": "[\"P01825-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84710",
        "row": "[\"P01824-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84711",
        "row": "[\"P0CF74-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84712",
        "row": "[\"Q13153-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84713",
        "row": "[\"A0A0C4DH73-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84714",
        "row": "[\"A2NJV5-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84715",
        "row": "[\"P01834-1\", \"Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1.\", \"The Biochemical journal\", \"1998 Jul 1\", \"Cuenda A, Dorow DS\", \"protein_xref_pubmed\", \"9639556\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84716",
        "row": "[\"P45984-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84717",
        "row": "[\"P05412-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84718",
        "row": "[\"P15498-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84719",
        "row": "[\"P04433-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84720",
        "row": "[\"P04432-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84721",
        "row": "[\"P07948-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84722",
        "row": "[\"P06315-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84723",
        "row": "[\"Q13177-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84724",
        "row": "[\"P12319-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84725",
        "row": "[\"P01817-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84726",
        "row": "[\"P01814-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84727",
        "row": "[\"P16885-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84728",
        "row": "[\"P01718-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84729",
        "row": "[\"P01782-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84730",
        "row": "[\"P01780-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84731",
        "row": "[\"A0A0C4DH25-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84732",
        "row": "[\"P01111-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84733",
        "row": "[\"P53779-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84734",
        "row": "[\"Q9UKW4-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84735",
        "row": "[\"A0A075B6S6-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84736",
        "row": "[\"P43405-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84737",
        "row": "[\"P01112-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84738",
        "row": "[\"P01721-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84739",
        "row": "[\"Q13094-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84740",
        "row": "[\"P63000-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84741",
        "row": "[\"P01100-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84742",
        "row": "[\"P01594-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84743",
        "row": "[\"P45985-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84744",
        "row": "[\"P45983-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84745",
        "row": "[\"O14733-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84746",
        "row": "[\"P01715-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84747",
        "row": "[\"P01714-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84748",
        "row": "[\"P01717-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84749",
        "row": "[\"P01699-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84750",
        "row": "[\"P06310-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84751",
        "row": "[\"P06312-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84752",
        "row": "[\"P01703-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84753",
        "row": "[\"P01700-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84754",
        "row": "[\"P01701-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84755",
        "row": "[\"P01706-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84756",
        "row": "[\"P01704-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84757",
        "row": "[\"P01705-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84758",
        "row": "[\"P01709-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84759",
        "row": "[\"P52735-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84760",
        "row": "[\"Q07889-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84761",
        "row": "[\"A0A075B6P5-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84762",
        "row": "[\"O75791-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84763",
        "row": "[\"P01602-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84764",
        "row": "[\"P01601-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84765",
        "row": "[\"P30273-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84766",
        "row": "[\"P01772-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84767",
        "row": "[\"P06331-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84768",
        "row": "[\"Q13233-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84769",
        "row": "[\"P04211-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84770",
        "row": "[\"P01619-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84771",
        "row": "[\"P01614-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84772",
        "row": "[\"P01615-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84773",
        "row": "[\"P01611-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84774",
        "row": "[\"P19174-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84775",
        "row": "[\"P01768-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84776",
        "row": "[\"P01762-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84777",
        "row": "[\"P01763-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84778",
        "row": "[\"P01764-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84779",
        "row": "[\"P01767-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84780",
        "row": "[\"P28482-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84781",
        "row": "[\"P0DOY2-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84782",
        "row": "[\"P0DOY3-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84783",
        "row": "[\"A0M8Q6-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84784",
        "row": "[\"P01624-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84785",
        "row": "[\"P01597-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84786",
        "row": "[\"P01593-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84787",
        "row": "[\"P01599-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84788",
        "row": "[\"P01766-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84789",
        "row": "[\"P0CG04-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84790",
        "row": "[\"P27361-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84791",
        "row": "[\"P80748-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84792",
        "row": "[\"Q01362-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84793",
        "row": "[\"P01854-2\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84794",
        "row": "[\"P23083-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84795",
        "row": "[\"P01742-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84796",
        "row": "[\"P01743-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84797",
        "row": "[\"P04430-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84798",
        "row": "[\"P01825-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84799",
        "row": "[\"P01824-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84800",
        "row": "[\"P0CF74-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84801",
        "row": "[\"Q13153-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84802",
        "row": "[\"A0A0C4DH73-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84803",
        "row": "[\"A2NJV5-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84804",
        "row": "[\"P01834-1\", \"Mitogen-activated protein kinase kinase 4 metastasis suppressor gene expression is inversely related to histological pattern in advancing human prostatic cancers.\", \"Cancer research\", \"2001 Apr 1\", \"Kim HL, Vander Griend DJ, Yang X, Benson DA, Dubauskas Z, Yoshida BA, Chekmareva MA, Ichikawa Y, Sokoloff MH, Zhan P, Karrison T, Lin A, Stadler WM, Ichikawa T, Rubin MA, Rinker-Schaeffer CW\", \"protein_xref_pubmed\", \"11306453\", \"protein_xref_reactome\", \"R-HSA-2871796\"]"
    },
    {
        "recordid": "GLY_000310_1_84805",
        "row": "[\"P04433-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84806",
        "row": "[\"P04432-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84807",
        "row": "[\"P07948-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84808",
        "row": "[\"P06315-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84809",
        "row": "[\"P12319-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84810",
        "row": "[\"P01817-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84811",
        "row": "[\"P01814-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84812",
        "row": "[\"P01718-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84813",
        "row": "[\"P01782-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84814",
        "row": "[\"P01780-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84815",
        "row": "[\"A0A0C4DH25-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84816",
        "row": "[\"A0A075B6S6-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84817",
        "row": "[\"P43405-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84818",
        "row": "[\"P01721-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84819",
        "row": "[\"P42338-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84820",
        "row": "[\"P42336-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84821",
        "row": "[\"Q9UQC2-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84822",
        "row": "[\"P01594-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84823",
        "row": "[\"P01715-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84824",
        "row": "[\"P01714-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84825",
        "row": "[\"P01717-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84826",
        "row": "[\"P01699-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84827",
        "row": "[\"P06310-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84828",
        "row": "[\"P06312-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84829",
        "row": "[\"P01703-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84830",
        "row": "[\"P01700-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84831",
        "row": "[\"P01701-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84832",
        "row": "[\"P01706-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84833",
        "row": "[\"P01704-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84834",
        "row": "[\"P01705-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84835",
        "row": "[\"P01709-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84836",
        "row": "[\"Q07889-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84837",
        "row": "[\"A0A075B6P5-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84838",
        "row": "[\"P01602-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84839",
        "row": "[\"P01601-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84840",
        "row": "[\"P30273-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84841",
        "row": "[\"P01772-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84842",
        "row": "[\"P06331-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84843",
        "row": "[\"P04211-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84844",
        "row": "[\"Q9GZY6-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84845",
        "row": "[\"P01619-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84846",
        "row": "[\"P01614-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84847",
        "row": "[\"P01615-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84848",
        "row": "[\"P01611-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84849",
        "row": "[\"P01768-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84850",
        "row": "[\"P01762-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84851",
        "row": "[\"P01763-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84852",
        "row": "[\"P01764-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84853",
        "row": "[\"P01767-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84854",
        "row": "[\"P0DOY2-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84855",
        "row": "[\"P0DOY3-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84856",
        "row": "[\"A0M8Q6-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84857",
        "row": "[\"P01624-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84858",
        "row": "[\"P27986-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84859",
        "row": "[\"P01597-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84860",
        "row": "[\"P01593-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84861",
        "row": "[\"P01599-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84862",
        "row": "[\"P01766-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84863",
        "row": "[\"P0CG04-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84864",
        "row": "[\"P80748-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84865",
        "row": "[\"Q01362-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84866",
        "row": "[\"P01854-2\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84867",
        "row": "[\"P23083-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84868",
        "row": "[\"O00459-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84869",
        "row": "[\"P01742-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84870",
        "row": "[\"P01743-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84871",
        "row": "[\"P06241-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84872",
        "row": "[\"P04430-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84873",
        "row": "[\"P01825-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84874",
        "row": "[\"P01824-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84875",
        "row": "[\"P0CF74-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84876",
        "row": "[\"A0A0C4DH73-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84877",
        "row": "[\"O15530-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84878",
        "row": "[\"A2NJV5-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84879",
        "row": "[\"P01834-1\", \"Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate.\", \"Nature\", \"1988 Apr 14\", \"Whitman M, Downes CP, Keeler M, Keller T, Cantley L\", \"protein_xref_pubmed\", \"2833705\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84880",
        "row": "[\"P04433-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84881",
        "row": "[\"P04432-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84882",
        "row": "[\"P06315-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84883",
        "row": "[\"P12319-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84884",
        "row": "[\"P01817-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84885",
        "row": "[\"P01814-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84886",
        "row": "[\"P01718-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84887",
        "row": "[\"P01782-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84888",
        "row": "[\"P01780-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84889",
        "row": "[\"A0A0C4DH25-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84890",
        "row": "[\"A0A075B6S6-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84891",
        "row": "[\"P01721-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84892",
        "row": "[\"P01594-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84893",
        "row": "[\"P01715-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84894",
        "row": "[\"P01714-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84895",
        "row": "[\"P01717-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84896",
        "row": "[\"P01699-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84897",
        "row": "[\"P06310-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84898",
        "row": "[\"P06312-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84899",
        "row": "[\"P01703-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84900",
        "row": "[\"P01700-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84901",
        "row": "[\"P01701-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84902",
        "row": "[\"P01706-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84903",
        "row": "[\"P01704-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84904",
        "row": "[\"P01705-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84905",
        "row": "[\"P01709-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84906",
        "row": "[\"A0A075B6P5-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84907",
        "row": "[\"P01602-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84908",
        "row": "[\"P01601-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84909",
        "row": "[\"P30273-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84910",
        "row": "[\"P01772-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84911",
        "row": "[\"P06331-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84912",
        "row": "[\"P04211-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84913",
        "row": "[\"Q9GZY6-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84914",
        "row": "[\"P01619-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84915",
        "row": "[\"P01614-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84916",
        "row": "[\"P01615-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84917",
        "row": "[\"P01611-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84918",
        "row": "[\"P01768-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84919",
        "row": "[\"P01762-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84920",
        "row": "[\"P01763-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84921",
        "row": "[\"P01764-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84922",
        "row": "[\"P01767-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84923",
        "row": "[\"P0DOY2-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84924",
        "row": "[\"P0DOY3-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84925",
        "row": "[\"A0M8Q6-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84926",
        "row": "[\"P01624-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84927",
        "row": "[\"P01597-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84928",
        "row": "[\"P01593-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84929",
        "row": "[\"P01599-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84930",
        "row": "[\"P01766-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84931",
        "row": "[\"P0CG04-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84932",
        "row": "[\"P80748-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84933",
        "row": "[\"Q01362-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84934",
        "row": "[\"P01854-2\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84935",
        "row": "[\"P23083-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84936",
        "row": "[\"P01742-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84937",
        "row": "[\"P01743-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84938",
        "row": "[\"P04430-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84939",
        "row": "[\"P01825-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84940",
        "row": "[\"P01824-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84941",
        "row": "[\"P0CF74-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84942",
        "row": "[\"A0A0C4DH73-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84943",
        "row": "[\"O15530-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84944",
        "row": "[\"A2NJV5-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84945",
        "row": "[\"P01834-1\", \"The role of PI3K in immune cells.\", \"Nature immunology\", \"2003 Apr\", \"Koyasu S\", \"protein_xref_pubmed\", \"12660731\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84946",
        "row": "[\"P04433-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84947",
        "row": "[\"P04432-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84948",
        "row": "[\"P07948-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84949",
        "row": "[\"P06315-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84950",
        "row": "[\"P12319-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84951",
        "row": "[\"P01817-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84952",
        "row": "[\"P01814-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84953",
        "row": "[\"P01718-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84954",
        "row": "[\"P01782-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84955",
        "row": "[\"P01780-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84956",
        "row": "[\"A0A0C4DH25-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84957",
        "row": "[\"A0A075B6S6-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84958",
        "row": "[\"P43405-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84959",
        "row": "[\"P01721-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84960",
        "row": "[\"P42338-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84961",
        "row": "[\"P42336-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84962",
        "row": "[\"Q9UQC2-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84963",
        "row": "[\"P01594-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84964",
        "row": "[\"P01715-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84965",
        "row": "[\"P01714-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84966",
        "row": "[\"P01717-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84967",
        "row": "[\"P01699-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84968",
        "row": "[\"P06310-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84969",
        "row": "[\"P06312-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84970",
        "row": "[\"P01703-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84971",
        "row": "[\"P01700-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84972",
        "row": "[\"P01701-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84973",
        "row": "[\"P01706-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84974",
        "row": "[\"P01704-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84975",
        "row": "[\"P01705-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84976",
        "row": "[\"P01709-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84977",
        "row": "[\"Q07889-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84978",
        "row": "[\"A0A075B6P5-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84979",
        "row": "[\"P01602-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84980",
        "row": "[\"P01601-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84981",
        "row": "[\"P30273-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84982",
        "row": "[\"P01772-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84983",
        "row": "[\"P06331-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84984",
        "row": "[\"P04211-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84985",
        "row": "[\"Q9GZY6-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84986",
        "row": "[\"P01619-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84987",
        "row": "[\"P01614-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84988",
        "row": "[\"P01615-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84989",
        "row": "[\"P01611-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84990",
        "row": "[\"P01768-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84991",
        "row": "[\"P01762-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84992",
        "row": "[\"P01763-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84993",
        "row": "[\"P01764-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84994",
        "row": "[\"P01767-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84995",
        "row": "[\"P0DOY2-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84996",
        "row": "[\"P0DOY3-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84997",
        "row": "[\"A0M8Q6-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84998",
        "row": "[\"P01624-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_84999",
        "row": "[\"P27986-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    },
    {
        "recordid": "GLY_000310_1_85000",
        "row": "[\"P01597-1\", \"NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.\", \"Blood\", \"2004 Jul 1\", \"Tkaczyk C, Horejsi V, Iwaki S, Draber P, Samelson LE, Satterthwaite AB, Nahm DH, Metcalfe DD, Gilfillan AM\", \"protein_xref_pubmed\", \"15010370\", \"protein_xref_reactome\", \"R-HSA-2730905\"]"
    }
]
