[
    {
        "recordid": "GLY_000310_1_196001",
        "row": "[\"Q7LG56-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196002",
        "row": "[\"P10599-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196003",
        "row": "[\"P35754-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196004",
        "row": "[\"Q5TCS8-4\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196005",
        "row": "[\"P23919-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196006",
        "row": "[\"O00746-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196007",
        "row": "[\"Q9NRF8-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196008",
        "row": "[\"Q13232-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196009",
        "row": "[\"Q86X67-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196010",
        "row": "[\"Q9Y6K8-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196011",
        "row": "[\"P00568-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196012",
        "row": "[\"O60361-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196013",
        "row": "[\"P54819-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196014",
        "row": "[\"Q16774-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196015",
        "row": "[\"Q9Y3D8-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196016",
        "row": "[\"P04818-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196017",
        "row": "[\"P22392-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196018",
        "row": "[\"P15531-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196019",
        "row": "[\"P17812-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196020",
        "row": "[\"P27144-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196021",
        "row": "[\"Q9H773-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196022",
        "row": "[\"Q96M32-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196023",
        "row": "[\"P32321-1\", \"A dityrosyl-diiron radical cofactor center is essential for human ribonucleotide reductases.\", \"Molecular cancer therapeutics\", \"2005 Dec\", \"Zhou B, Shao J, Su L, Yuan YC, Qi C, Shih J, Xi B, Chu B, Yen Y\", \"protein_xref_pubmed\", \"16373698\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196024",
        "row": "[\"P30085-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196025",
        "row": "[\"P31350-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196026",
        "row": "[\"P23921-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196027",
        "row": "[\"Q96MA6-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196028",
        "row": "[\"Q16881-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196029",
        "row": "[\"Q7LG56-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196030",
        "row": "[\"P10599-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196031",
        "row": "[\"P35754-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196032",
        "row": "[\"Q5TCS8-4\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196033",
        "row": "[\"P23919-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196034",
        "row": "[\"O00746-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196035",
        "row": "[\"Q9NRF8-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196036",
        "row": "[\"Q13232-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196037",
        "row": "[\"Q86X67-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196038",
        "row": "[\"Q9Y6K8-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196039",
        "row": "[\"P00568-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196040",
        "row": "[\"O60361-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196041",
        "row": "[\"P54819-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196042",
        "row": "[\"Q16774-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196043",
        "row": "[\"Q9Y3D8-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196044",
        "row": "[\"P04818-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196045",
        "row": "[\"P22392-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196046",
        "row": "[\"P15531-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196047",
        "row": "[\"P17812-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196048",
        "row": "[\"P27144-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196049",
        "row": "[\"Q9H773-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196050",
        "row": "[\"Q96M32-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196051",
        "row": "[\"P32321-1\", \"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2008 Nov 18\", \"Pontarin G, Fijolek A, Pizzo P, Ferraro P, Rampazzo C, Pozzan T, Thelander L, Reichard PA, Bianchi V\", \"protein_xref_pubmed\", \"18997010\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196052",
        "row": "[\"P30085-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196053",
        "row": "[\"P31350-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196054",
        "row": "[\"P23921-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196055",
        "row": "[\"Q96MA6-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196056",
        "row": "[\"Q16881-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196057",
        "row": "[\"Q7LG56-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196058",
        "row": "[\"P10599-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196059",
        "row": "[\"P35754-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196060",
        "row": "[\"Q5TCS8-4\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196061",
        "row": "[\"P23919-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196062",
        "row": "[\"O00746-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196063",
        "row": "[\"Q9NRF8-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196064",
        "row": "[\"Q13232-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196065",
        "row": "[\"Q86X67-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196066",
        "row": "[\"Q9Y6K8-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196067",
        "row": "[\"P00568-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196068",
        "row": "[\"O60361-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196069",
        "row": "[\"P54819-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196070",
        "row": "[\"Q16774-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196071",
        "row": "[\"Q9Y3D8-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196072",
        "row": "[\"P04818-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196073",
        "row": "[\"P22392-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196074",
        "row": "[\"P15531-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196075",
        "row": "[\"P17812-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196076",
        "row": "[\"P27144-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196077",
        "row": "[\"Q9H773-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196078",
        "row": "[\"Q96M32-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196079",
        "row": "[\"P32321-1\", \"Thioredoxin and glutaredoxin systems.\", \"The Journal of biological chemistry\", \"1989 Aug 25\", \"Holmgren A\", \"protein_xref_pubmed\", \"2668278\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196080",
        "row": "[\"P30085-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196081",
        "row": "[\"P31350-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196082",
        "row": "[\"P23921-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196083",
        "row": "[\"Q96MA6-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196084",
        "row": "[\"Q16881-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196085",
        "row": "[\"Q7LG56-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196086",
        "row": "[\"P10599-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196087",
        "row": "[\"P35754-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196088",
        "row": "[\"Q5TCS8-4\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196089",
        "row": "[\"P23919-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196090",
        "row": "[\"O00746-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196091",
        "row": "[\"Q9NRF8-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196092",
        "row": "[\"Q13232-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196093",
        "row": "[\"Q86X67-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196094",
        "row": "[\"Q9Y6K8-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196095",
        "row": "[\"P00568-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196096",
        "row": "[\"O60361-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196097",
        "row": "[\"P54819-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196098",
        "row": "[\"Q16774-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196099",
        "row": "[\"Q9Y3D8-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196100",
        "row": "[\"P04818-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196101",
        "row": "[\"P22392-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196102",
        "row": "[\"P15531-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196103",
        "row": "[\"P17812-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196104",
        "row": "[\"P27144-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196105",
        "row": "[\"Q9H773-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196106",
        "row": "[\"Q96M32-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196107",
        "row": "[\"P32321-1\", \"Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin.\", \"European journal of biochemistry\", \"1995 Jan 15\", \"Padilla CA, Martinez-Galisteo E, Barcena JA, Spyrou G, Holmgren A\", \"protein_xref_pubmed\", \"7851394\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196108",
        "row": "[\"P30085-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196109",
        "row": "[\"P31350-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196110",
        "row": "[\"P23921-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196111",
        "row": "[\"Q96MA6-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196112",
        "row": "[\"Q16881-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196113",
        "row": "[\"Q7LG56-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196114",
        "row": "[\"P10599-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196115",
        "row": "[\"P35754-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196116",
        "row": "[\"Q5TCS8-4\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196117",
        "row": "[\"P23919-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196118",
        "row": "[\"O00746-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196119",
        "row": "[\"Q9NRF8-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196120",
        "row": "[\"Q13232-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196121",
        "row": "[\"Q86X67-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196122",
        "row": "[\"Q9Y6K8-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196123",
        "row": "[\"P00568-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196124",
        "row": "[\"O60361-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196125",
        "row": "[\"P54819-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196126",
        "row": "[\"Q16774-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196127",
        "row": "[\"Q9Y3D8-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196128",
        "row": "[\"P04818-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196129",
        "row": "[\"P22392-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196130",
        "row": "[\"P15531-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196131",
        "row": "[\"P17812-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196132",
        "row": "[\"P27144-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196133",
        "row": "[\"Q9H773-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196134",
        "row": "[\"Q96M32-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196135",
        "row": "[\"P32321-1\", \"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.\", \"Nature\", \"2000 Mar 2\", \"Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y\", \"protein_xref_pubmed\", \"10716435\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196136",
        "row": "[\"P30085-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196137",
        "row": "[\"P31350-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196138",
        "row": "[\"P23921-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196139",
        "row": "[\"Q96MA6-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196140",
        "row": "[\"Q16881-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196141",
        "row": "[\"Q7LG56-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196142",
        "row": "[\"P10599-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196143",
        "row": "[\"P35754-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196144",
        "row": "[\"Q5TCS8-4\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196145",
        "row": "[\"P23919-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196146",
        "row": "[\"O00746-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196147",
        "row": "[\"Q9NRF8-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196148",
        "row": "[\"Q13232-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196149",
        "row": "[\"Q86X67-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196150",
        "row": "[\"Q9Y6K8-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196151",
        "row": "[\"P00568-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196152",
        "row": "[\"O60361-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196153",
        "row": "[\"P54819-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196154",
        "row": "[\"Q16774-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196155",
        "row": "[\"Q9Y3D8-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196156",
        "row": "[\"P04818-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196157",
        "row": "[\"P22392-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196158",
        "row": "[\"P15531-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196159",
        "row": "[\"P17812-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196160",
        "row": "[\"P27144-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196161",
        "row": "[\"Q9H773-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196162",
        "row": "[\"Q96M32-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196163",
        "row": "[\"P32321-1\", \"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.\", \"The Journal of biological chemistry\", \"2001 Nov 2\", \"Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L\", \"protein_xref_pubmed\", \"11517226\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196164",
        "row": "[\"P30085-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196165",
        "row": "[\"P31350-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196166",
        "row": "[\"P23921-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196167",
        "row": "[\"Q96MA6-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196168",
        "row": "[\"Q16881-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196169",
        "row": "[\"Q7LG56-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196170",
        "row": "[\"P10599-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196171",
        "row": "[\"P35754-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196172",
        "row": "[\"Q5TCS8-4\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196173",
        "row": "[\"P23919-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196174",
        "row": "[\"O00746-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196175",
        "row": "[\"Q9NRF8-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196176",
        "row": "[\"Q13232-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196177",
        "row": "[\"Q86X67-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196178",
        "row": "[\"Q9Y6K8-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196179",
        "row": "[\"P00568-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196180",
        "row": "[\"O60361-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196181",
        "row": "[\"P54819-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196182",
        "row": "[\"Q16774-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196183",
        "row": "[\"Q9Y3D8-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196184",
        "row": "[\"P04818-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196185",
        "row": "[\"P22392-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196186",
        "row": "[\"P15531-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196187",
        "row": "[\"P17812-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196188",
        "row": "[\"P27144-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196189",
        "row": "[\"Q9H773-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196190",
        "row": "[\"Q96M32-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196191",
        "row": "[\"P32321-1\", \"In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase.\", \"Cancer research\", \"2004 Jan 1\", \"Shao J, Zhou B, Zhu L, Qiu W, Yuan YC, Xi B, Yen Y\", \"protein_xref_pubmed\", \"14729598\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196192",
        "row": "[\"P30085-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196193",
        "row": "[\"P31350-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196194",
        "row": "[\"P23921-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196195",
        "row": "[\"Q96MA6-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196196",
        "row": "[\"Q16881-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196197",
        "row": "[\"Q7LG56-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196198",
        "row": "[\"P10599-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196199",
        "row": "[\"P35754-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196200",
        "row": "[\"Q5TCS8-4\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196201",
        "row": "[\"P23919-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196202",
        "row": "[\"O00746-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196203",
        "row": "[\"Q9NRF8-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196204",
        "row": "[\"Q13232-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196205",
        "row": "[\"Q86X67-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196206",
        "row": "[\"Q9Y6K8-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196207",
        "row": "[\"P00568-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196208",
        "row": "[\"O60361-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196209",
        "row": "[\"P54819-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196210",
        "row": "[\"Q16774-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196211",
        "row": "[\"Q9Y3D8-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196212",
        "row": "[\"P04818-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196213",
        "row": "[\"P22392-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196214",
        "row": "[\"P15531-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196215",
        "row": "[\"P17812-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196216",
        "row": "[\"P27144-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196217",
        "row": "[\"Q9H773-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196218",
        "row": "[\"Q96M32-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196219",
        "row": "[\"P32321-1\", \"Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"2012 Aug 14\", \"Pontarin G, Ferraro P, Bee L, Reichard P, Bianchi V\", \"protein_xref_pubmed\", \"22847445\", \"protein_xref_reactome\", \"R-HSA-499943\"]"
    },
    {
        "recordid": "GLY_000310_1_196220",
        "row": "[\"Q96RU7-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196221",
        "row": "[\"P15498-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196222",
        "row": "[\"P15514-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196223",
        "row": "[\"O15520-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196224",
        "row": "[\"Q9Y243-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196225",
        "row": "[\"O76093-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196226",
        "row": "[\"P12931-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196227",
        "row": "[\"P31751-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196228",
        "row": "[\"Q9Y4H2-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196229",
        "row": "[\"Q9GZV9-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196230",
        "row": "[\"Q9NWZ3-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196231",
        "row": "[\"Q9BPZ7-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196232",
        "row": "[\"P11487-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196233",
        "row": "[\"P10767-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196234",
        "row": "[\"Q92731-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196235",
        "row": "[\"Q99075-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196236",
        "row": "[\"O95750-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196237",
        "row": "[\"Q6R327-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196238",
        "row": "[\"O14944-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196239",
        "row": "[\"Q06124-2\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196240",
        "row": "[\"P21781-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196241",
        "row": "[\"P49771-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196242",
        "row": "[\"P03372-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196243",
        "row": "[\"P42338-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196244",
        "row": "[\"P42336-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196245",
        "row": "[\"O14511-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196246",
        "row": "[\"P63000-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196247",
        "row": "[\"Q86Z14-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196248",
        "row": "[\"Q9HCT0-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196249",
        "row": "[\"Q99836-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196250",
        "row": "[\"Q9UQC2-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196251",
        "row": "[\"P00533-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196252",
        "row": "[\"P05230-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196253",
        "row": "[\"Q13480-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196254",
        "row": "[\"P15153-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196255",
        "row": "[\"P01133-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196256",
        "row": "[\"P01135-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196257",
        "row": "[\"P42345-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196258",
        "row": "[\"P09038-4\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196259",
        "row": "[\"P16234-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196260",
        "row": "[\"P85299-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196261",
        "row": "[\"P08620-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196262",
        "row": "[\"P14210-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196263",
        "row": "[\"P01127-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196264",
        "row": "[\"P10721-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196265",
        "row": "[\"P35070-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196266",
        "row": "[\"Q8WU20-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196267",
        "row": "[\"Q9NP95-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196268",
        "row": "[\"P33681-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196269",
        "row": "[\"P42081-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196270",
        "row": "[\"O95760-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196271",
        "row": "[\"O43320-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196272",
        "row": "[\"O00329-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196273",
        "row": "[\"P36888-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196274",
        "row": "[\"P56975-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196275",
        "row": "[\"Q6ZUJ8-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196276",
        "row": "[\"Q6PIZ9-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196277",
        "row": "[\"Q01638-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196278",
        "row": "[\"O00141-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196279",
        "row": "[\"P15391-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196280",
        "row": "[\"P04626-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196281",
        "row": "[\"P84095-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196282",
        "row": "[\"P27986-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196283",
        "row": "[\"P09619-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196284",
        "row": "[\"Q02297-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196285",
        "row": "[\"Q9Y4K3-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196286",
        "row": "[\"O00459-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196287",
        "row": "[\"Q8WWG1-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196288",
        "row": "[\"P22455-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196289",
        "row": "[\"P06241-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196290",
        "row": "[\"P31371-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196291",
        "row": "[\"Q92569-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196292",
        "row": "[\"P06239-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196293",
        "row": "[\"O15530-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196294",
        "row": "[\"Q5T1C6-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196295",
        "row": "[\"P10747-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196296",
        "row": "[\"O43815-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196297",
        "row": "[\"Q9BVC4-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196298",
        "row": "[\"P51617-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196299",
        "row": "[\"P31749-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196300",
        "row": "[\"P08581-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196301",
        "row": "[\"Q6UW88-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196302",
        "row": "[\"P35568-1\", \"Rac1 and RhoG promote cell survival by the activation of PI3K and Akt, independently of their ability to stimulate JNK and NF-kappaB.\", \"Oncogene\", \"2002 Jan 10\", \"Murga C, Zohar M, Teramoto H, Gutkind JS\", \"protein_xref_pubmed\", \"11803464\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196303",
        "row": "[\"Q96RU7-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196304",
        "row": "[\"P15498-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196305",
        "row": "[\"P15514-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196306",
        "row": "[\"O15520-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196307",
        "row": "[\"Q9Y243-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196308",
        "row": "[\"O76093-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196309",
        "row": "[\"P12931-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196310",
        "row": "[\"P31751-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196311",
        "row": "[\"Q9Y4H2-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196312",
        "row": "[\"Q9GZV9-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196313",
        "row": "[\"Q9NWZ3-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196314",
        "row": "[\"Q9BPZ7-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196315",
        "row": "[\"P11487-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196316",
        "row": "[\"P10767-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196317",
        "row": "[\"Q92731-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196318",
        "row": "[\"Q99075-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196319",
        "row": "[\"O95750-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196320",
        "row": "[\"Q6R327-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196321",
        "row": "[\"O14944-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196322",
        "row": "[\"Q06124-2\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196323",
        "row": "[\"P21781-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196324",
        "row": "[\"P49771-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196325",
        "row": "[\"P03372-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196326",
        "row": "[\"P42338-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196327",
        "row": "[\"P42336-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196328",
        "row": "[\"O14511-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196329",
        "row": "[\"P63000-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196330",
        "row": "[\"Q86Z14-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196331",
        "row": "[\"Q9HCT0-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196332",
        "row": "[\"Q99836-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196333",
        "row": "[\"Q9UQC2-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196334",
        "row": "[\"P00533-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196335",
        "row": "[\"P05230-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196336",
        "row": "[\"Q13480-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196337",
        "row": "[\"P15153-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196338",
        "row": "[\"P01133-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196339",
        "row": "[\"P01135-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196340",
        "row": "[\"P42345-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196341",
        "row": "[\"P09038-4\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196342",
        "row": "[\"P16234-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196343",
        "row": "[\"P85299-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196344",
        "row": "[\"P08620-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196345",
        "row": "[\"P14210-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196346",
        "row": "[\"P01127-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196347",
        "row": "[\"P10721-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196348",
        "row": "[\"P35070-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196349",
        "row": "[\"Q8WU20-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196350",
        "row": "[\"Q9NP95-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196351",
        "row": "[\"P33681-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196352",
        "row": "[\"P42081-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196353",
        "row": "[\"O95760-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196354",
        "row": "[\"O43320-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196355",
        "row": "[\"O00329-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196356",
        "row": "[\"P36888-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196357",
        "row": "[\"P56975-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196358",
        "row": "[\"Q6ZUJ8-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196359",
        "row": "[\"Q6PIZ9-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196360",
        "row": "[\"Q01638-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196361",
        "row": "[\"O00141-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196362",
        "row": "[\"P15391-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196363",
        "row": "[\"P04626-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196364",
        "row": "[\"P84095-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196365",
        "row": "[\"P27986-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196366",
        "row": "[\"P09619-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196367",
        "row": "[\"Q02297-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196368",
        "row": "[\"Q9Y4K3-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196369",
        "row": "[\"O00459-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196370",
        "row": "[\"Q8WWG1-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196371",
        "row": "[\"P22455-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196372",
        "row": "[\"P06241-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196373",
        "row": "[\"P31371-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196374",
        "row": "[\"Q92569-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196375",
        "row": "[\"P06239-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196376",
        "row": "[\"O15530-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196377",
        "row": "[\"Q5T1C6-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196378",
        "row": "[\"P10747-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196379",
        "row": "[\"O43815-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196380",
        "row": "[\"Q9BVC4-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196381",
        "row": "[\"P51617-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196382",
        "row": "[\"P31749-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196383",
        "row": "[\"P08581-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196384",
        "row": "[\"Q6UW88-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196385",
        "row": "[\"P35568-1\", \"Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation.\", \"The Journal of biological chemistry\", \"1995 May 12\", \"Kovacsovics TJ, Bachelot C, Toker A, Vlahos CJ, Duckworth B, Cantley LC, Hartwig JH\", \"protein_xref_pubmed\", \"7744773\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196386",
        "row": "[\"Q96RU7-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196387",
        "row": "[\"P15498-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196388",
        "row": "[\"P15514-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196389",
        "row": "[\"O15520-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196390",
        "row": "[\"Q9Y243-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196391",
        "row": "[\"O76093-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196392",
        "row": "[\"P12931-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196393",
        "row": "[\"P31751-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196394",
        "row": "[\"Q9Y4H2-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196395",
        "row": "[\"Q9GZV9-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196396",
        "row": "[\"Q9NWZ3-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196397",
        "row": "[\"Q9BPZ7-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196398",
        "row": "[\"P11487-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196399",
        "row": "[\"P10767-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196400",
        "row": "[\"Q92731-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196401",
        "row": "[\"Q99075-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196402",
        "row": "[\"O95750-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196403",
        "row": "[\"Q6R327-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196404",
        "row": "[\"O14944-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196405",
        "row": "[\"Q06124-2\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196406",
        "row": "[\"P21781-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196407",
        "row": "[\"P49771-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196408",
        "row": "[\"P03372-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196409",
        "row": "[\"P42338-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196410",
        "row": "[\"P42336-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196411",
        "row": "[\"O14511-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196412",
        "row": "[\"P63000-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196413",
        "row": "[\"Q86Z14-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196414",
        "row": "[\"Q9HCT0-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196415",
        "row": "[\"Q99836-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196416",
        "row": "[\"Q9UQC2-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196417",
        "row": "[\"P00533-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196418",
        "row": "[\"P05230-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196419",
        "row": "[\"Q13480-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196420",
        "row": "[\"P15153-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196421",
        "row": "[\"P01133-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196422",
        "row": "[\"P01135-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196423",
        "row": "[\"P42345-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196424",
        "row": "[\"P09038-4\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196425",
        "row": "[\"P16234-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196426",
        "row": "[\"P85299-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196427",
        "row": "[\"P08620-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196428",
        "row": "[\"P14210-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196429",
        "row": "[\"P01127-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196430",
        "row": "[\"P10721-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196431",
        "row": "[\"P35070-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196432",
        "row": "[\"Q8WU20-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196433",
        "row": "[\"Q9NP95-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196434",
        "row": "[\"P33681-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196435",
        "row": "[\"P42081-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196436",
        "row": "[\"O95760-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196437",
        "row": "[\"O43320-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196438",
        "row": "[\"O00329-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196439",
        "row": "[\"P36888-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196440",
        "row": "[\"P56975-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196441",
        "row": "[\"Q6ZUJ8-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196442",
        "row": "[\"Q6PIZ9-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196443",
        "row": "[\"Q01638-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196444",
        "row": "[\"O00141-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196445",
        "row": "[\"P15391-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196446",
        "row": "[\"P04626-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196447",
        "row": "[\"P84095-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196448",
        "row": "[\"P27986-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196449",
        "row": "[\"P09619-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196450",
        "row": "[\"Q02297-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196451",
        "row": "[\"Q9Y4K3-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196452",
        "row": "[\"O00459-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196453",
        "row": "[\"Q8WWG1-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196454",
        "row": "[\"P22455-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196455",
        "row": "[\"P06241-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196456",
        "row": "[\"P31371-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196457",
        "row": "[\"Q92569-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196458",
        "row": "[\"P06239-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196459",
        "row": "[\"O15530-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196460",
        "row": "[\"Q5T1C6-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196461",
        "row": "[\"P10747-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196462",
        "row": "[\"O43815-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196463",
        "row": "[\"Q9BVC4-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196464",
        "row": "[\"P51617-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196465",
        "row": "[\"P31749-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196466",
        "row": "[\"P08581-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196467",
        "row": "[\"Q6UW88-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196468",
        "row": "[\"P35568-1\", \"Rac GTPase interacts specifically with phosphatidylinositol 3-kinase.\", \"The Biochemical journal\", \"1996 May 1\", \"Bokoch GM, Vlahos CJ, Wang Y, Knaus UG, Traynor-Kaplan AE\", \"protein_xref_pubmed\", \"8645157\", \"protein_xref_reactome\", \"R-HSA-1257604\"]"
    },
    {
        "recordid": "GLY_000310_1_196469",
        "row": "[\"P16520-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196470",
        "row": "[\"P15498-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196471",
        "row": "[\"A5YM69-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196472",
        "row": "[\"Q8N5V2-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196473",
        "row": "[\"Q12802-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196474",
        "row": "[\"P10911-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196475",
        "row": "[\"Q96DR7-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196476",
        "row": "[\"O60262-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196477",
        "row": "[\"Q5JSP0-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196478",
        "row": "[\"P21731-3\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196479",
        "row": "[\"Q92888-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196480",
        "row": "[\"O43157-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196481",
        "row": "[\"P61952-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196482",
        "row": "[\"Q8IVF5-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196483",
        "row": "[\"Q7Z6J4-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196484",
        "row": "[\"P08134-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196485",
        "row": "[\"Q12774-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196486",
        "row": "[\"P63211-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196487",
        "row": "[\"P63215-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196488",
        "row": "[\"P63218-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196489",
        "row": "[\"Q9UKW4-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196490",
        "row": "[\"Q9P2W3-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196491",
        "row": "[\"O15085-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196492",
        "row": "[\"Q9HAV0-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196493",
        "row": "[\"O94989-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196494",
        "row": "[\"P98174-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196495",
        "row": "[\"Q9H7P9-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196496",
        "row": "[\"A8MVX0-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196497",
        "row": "[\"O14827-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196498",
        "row": "[\"Q8TER5-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196499",
        "row": "[\"O14775-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196500",
        "row": "[\"Q07890-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196501",
        "row": "[\"P61586-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196502",
        "row": "[\"Q5VV41-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196503",
        "row": "[\"Q9NZN5-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196504",
        "row": "[\"Q9UBI6-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196505",
        "row": "[\"Q13009-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196506",
        "row": "[\"O60229-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196507",
        "row": "[\"A1IGU5-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196508",
        "row": "[\"Q8N4T4-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196509",
        "row": "[\"P52735-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196510",
        "row": "[\"Q15811-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196511",
        "row": "[\"O75962-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196512",
        "row": "[\"Q07889-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196513",
        "row": "[\"O43307-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196514",
        "row": "[\"Q96M96-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196515",
        "row": "[\"Q8TCU6-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196516",
        "row": "[\"P59768-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196517",
        "row": "[\"Q92974-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196518",
        "row": "[\"Q13464-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196519",
        "row": "[\"Q14344-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196520",
        "row": "[\"Q6ZSZ5-4\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196521",
        "row": "[\"O15013-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196522",
        "row": "[\"Q8IW93-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196523",
        "row": "[\"P62745-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196524",
        "row": "[\"Q96PE2-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196525",
        "row": "[\"O14610-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196526",
        "row": "[\"Q9UK08-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196527",
        "row": "[\"Q03113-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196528",
        "row": "[\"Q15052-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196529",
        "row": "[\"Q9H8V3-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196530",
        "row": "[\"O94827-5\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196531",
        "row": "[\"Q12979-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196532",
        "row": "[\"P50151-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196533",
        "row": "[\"P50150-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196534",
        "row": "[\"P35368-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196535",
        "row": "[\"Q14155-4\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196536",
        "row": "[\"Q9NR80-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196537",
        "row": "[\"Q9NR81-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196538",
        "row": "[\"P25100-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196539",
        "row": "[\"Q9NXL2-2\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196540",
        "row": "[\"O75116-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196541",
        "row": "[\"Q5VST9-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196542",
        "row": "[\"Q9HCE6-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196543",
        "row": "[\"Q7Z628-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196544",
        "row": "[\"Q06187-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196545",
        "row": "[\"O15068-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196546",
        "row": "[\"P35348-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196547",
        "row": "[\"P62879-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196548",
        "row": "[\"P62873-1\", \"Activation of p115-RhoGEF requires direct association of Galpha13 and the Dbl homology domain.\", \"The Journal of biological chemistry\", \"2012 Jul 20\", \"Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC\", \"protein_xref_pubmed\", \"22661716\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196549",
        "row": "[\"P16520-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196550",
        "row": "[\"P15498-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196551",
        "row": "[\"A5YM69-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196552",
        "row": "[\"Q8N5V2-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196553",
        "row": "[\"Q12802-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196554",
        "row": "[\"P10911-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196555",
        "row": "[\"Q96DR7-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196556",
        "row": "[\"O60262-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196557",
        "row": "[\"Q5JSP0-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196558",
        "row": "[\"P21731-3\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196559",
        "row": "[\"Q92888-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196560",
        "row": "[\"O43157-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196561",
        "row": "[\"P61952-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196562",
        "row": "[\"Q8IVF5-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196563",
        "row": "[\"Q7Z6J4-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196564",
        "row": "[\"P08134-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196565",
        "row": "[\"Q12774-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196566",
        "row": "[\"P63211-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196567",
        "row": "[\"P63215-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196568",
        "row": "[\"P63218-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196569",
        "row": "[\"Q9UKW4-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196570",
        "row": "[\"Q9P2W3-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196571",
        "row": "[\"O15085-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196572",
        "row": "[\"Q9HAV0-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196573",
        "row": "[\"O94989-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196574",
        "row": "[\"P98174-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196575",
        "row": "[\"Q9H7P9-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196576",
        "row": "[\"A8MVX0-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196577",
        "row": "[\"O14827-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196578",
        "row": "[\"Q8TER5-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196579",
        "row": "[\"O14775-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196580",
        "row": "[\"Q07890-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196581",
        "row": "[\"P61586-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196582",
        "row": "[\"Q5VV41-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196583",
        "row": "[\"Q9NZN5-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196584",
        "row": "[\"Q9UBI6-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196585",
        "row": "[\"Q13009-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196586",
        "row": "[\"O60229-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196587",
        "row": "[\"A1IGU5-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196588",
        "row": "[\"Q8N4T4-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196589",
        "row": "[\"P52735-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196590",
        "row": "[\"Q15811-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196591",
        "row": "[\"O75962-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196592",
        "row": "[\"Q07889-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196593",
        "row": "[\"O43307-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196594",
        "row": "[\"Q96M96-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196595",
        "row": "[\"Q8TCU6-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196596",
        "row": "[\"P59768-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196597",
        "row": "[\"Q92974-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196598",
        "row": "[\"Q13464-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196599",
        "row": "[\"Q14344-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196600",
        "row": "[\"Q6ZSZ5-4\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196601",
        "row": "[\"O15013-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196602",
        "row": "[\"Q8IW93-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196603",
        "row": "[\"P62745-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196604",
        "row": "[\"Q96PE2-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196605",
        "row": "[\"O14610-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196606",
        "row": "[\"Q9UK08-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196607",
        "row": "[\"Q03113-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196608",
        "row": "[\"Q15052-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196609",
        "row": "[\"Q9H8V3-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196610",
        "row": "[\"O94827-5\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196611",
        "row": "[\"Q12979-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196612",
        "row": "[\"P50151-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196613",
        "row": "[\"P50150-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196614",
        "row": "[\"P35368-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196615",
        "row": "[\"Q14155-4\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196616",
        "row": "[\"Q9NR80-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196617",
        "row": "[\"Q9NR81-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196618",
        "row": "[\"P25100-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196619",
        "row": "[\"Q9NXL2-2\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196620",
        "row": "[\"O75116-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196621",
        "row": "[\"Q5VST9-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196622",
        "row": "[\"Q9HCE6-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196623",
        "row": "[\"Q7Z628-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196624",
        "row": "[\"Q06187-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196625",
        "row": "[\"O15068-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196626",
        "row": "[\"P35348-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196627",
        "row": "[\"P62879-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196628",
        "row": "[\"P62873-1\", \"RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?\", \"Oncogene\", \"2001 Mar 26\", \"Fukuhara S, Chikumi H, Gutkind JS\", \"protein_xref_pubmed\", \"11313914\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196629",
        "row": "[\"P15498-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196630",
        "row": "[\"A5YM69-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196631",
        "row": "[\"Q8N5V2-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196632",
        "row": "[\"Q12802-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196633",
        "row": "[\"P10911-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196634",
        "row": "[\"Q96DR7-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196635",
        "row": "[\"Q5JSP0-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196636",
        "row": "[\"Q92888-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196637",
        "row": "[\"O43157-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196638",
        "row": "[\"Q8IVF5-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196639",
        "row": "[\"Q7Z6J4-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196640",
        "row": "[\"P08134-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196641",
        "row": "[\"Q12774-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196642",
        "row": "[\"Q9UKW4-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196643",
        "row": "[\"O15085-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196644",
        "row": "[\"O94989-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196645",
        "row": "[\"P98174-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196646",
        "row": "[\"Q9H7P9-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196647",
        "row": "[\"A8MVX0-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196648",
        "row": "[\"O14827-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196649",
        "row": "[\"Q8TER5-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196650",
        "row": "[\"Q07890-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196651",
        "row": "[\"P61586-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196652",
        "row": "[\"Q5VV41-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196653",
        "row": "[\"Q9NZN5-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196654",
        "row": "[\"Q13009-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196655",
        "row": "[\"A1IGU5-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196656",
        "row": "[\"Q8N4T4-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196657",
        "row": "[\"P52735-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196658",
        "row": "[\"Q15811-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196659",
        "row": "[\"Q07889-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196660",
        "row": "[\"O43307-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196661",
        "row": "[\"Q96M96-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196662",
        "row": "[\"Q8TCU6-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196663",
        "row": "[\"Q92974-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196664",
        "row": "[\"Q13464-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196665",
        "row": "[\"Q14344-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196666",
        "row": "[\"Q6ZSZ5-4\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196667",
        "row": "[\"O15013-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196668",
        "row": "[\"Q8IW93-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196669",
        "row": "[\"P62745-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196670",
        "row": "[\"Q96PE2-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196671",
        "row": "[\"Q03113-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196672",
        "row": "[\"Q15052-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196673",
        "row": "[\"Q9H8V3-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196674",
        "row": "[\"O94827-5\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196675",
        "row": "[\"Q12979-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196676",
        "row": "[\"Q14155-4\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196677",
        "row": "[\"Q9NR80-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196678",
        "row": "[\"Q9NR81-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196679",
        "row": "[\"Q9NXL2-2\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196680",
        "row": "[\"O75116-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196681",
        "row": "[\"Q5VST9-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196682",
        "row": "[\"Q9HCE6-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196683",
        "row": "[\"Q7Z628-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196684",
        "row": "[\"O15068-1\", \"The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.\", \"International journal of biological sciences\", \"2005\", \"Siderovski DP, Willard FS\", \"protein_xref_pubmed\", \"15951850\", \"protein_xref_reactome\", \"R-HSA-416482\"]"
    },
    {
        "recordid": "GLY_000310_1_196685",
        "row": "[\"P11912-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196686",
        "row": "[\"P15498-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196687",
        "row": "[\"Q96SN7-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196688",
        "row": "[\"P04433-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196689",
        "row": "[\"P04432-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196690",
        "row": "[\"P07948-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196691",
        "row": "[\"P06315-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196692",
        "row": "[\"P48995-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196693",
        "row": "[\"P40259-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196694",
        "row": "[\"P01817-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196695",
        "row": "[\"P01814-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196696",
        "row": "[\"P16885-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196697",
        "row": "[\"P01718-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196698",
        "row": "[\"P01782-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196699",
        "row": "[\"P01780-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196700",
        "row": "[\"A0A0C4DH25-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196701",
        "row": "[\"A0A075B6S6-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196702",
        "row": "[\"P43405-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196703",
        "row": "[\"Q9UN19-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196704",
        "row": "[\"P01721-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196705",
        "row": "[\"P20273-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196706",
        "row": "[\"P01594-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196707",
        "row": "[\"Q8WV28-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196708",
        "row": "[\"P01715-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196709",
        "row": "[\"P01714-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196710",
        "row": "[\"P01717-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196711",
        "row": "[\"P01699-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196712",
        "row": "[\"P06310-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196713",
        "row": "[\"O43865-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196714",
        "row": "[\"P06312-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196715",
        "row": "[\"P01703-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196716",
        "row": "[\"P01700-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196717",
        "row": "[\"P01701-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196718",
        "row": "[\"P01706-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196719",
        "row": "[\"P01704-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196720",
        "row": "[\"P01705-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196721",
        "row": "[\"P01709-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196722",
        "row": "[\"Q14643-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196723",
        "row": "[\"Q07889-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196724",
        "row": "[\"P01880-2\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196725",
        "row": "[\"A0A075B6P5-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196726",
        "row": "[\"P0DP23-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196727",
        "row": "[\"P01602-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196728",
        "row": "[\"P01601-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196729",
        "row": "[\"P01772-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196730",
        "row": "[\"P06331-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196731",
        "row": "[\"P04211-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196732",
        "row": "[\"Q14571-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196733",
        "row": "[\"Q14573-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196734",
        "row": "[\"P01871-2\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196735",
        "row": "[\"O00329-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196736",
        "row": "[\"P01619-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196737",
        "row": "[\"P01614-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196738",
        "row": "[\"P01615-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196739",
        "row": "[\"P01611-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196740",
        "row": "[\"Q6ZUJ8-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196741",
        "row": "[\"P01768-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196742",
        "row": "[\"P01762-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196743",
        "row": "[\"P01763-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196744",
        "row": "[\"P01764-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196745",
        "row": "[\"P01767-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196746",
        "row": "[\"Q96B97-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196747",
        "row": "[\"Q13586-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196748",
        "row": "[\"P0DOY2-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196749",
        "row": "[\"P0DOY3-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196750",
        "row": "[\"P15391-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196751",
        "row": "[\"A0M8Q6-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196752",
        "row": "[\"P01624-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196753",
        "row": "[\"P27986-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196754",
        "row": "[\"P01597-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196755",
        "row": "[\"P01593-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196756",
        "row": "[\"P01599-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196757",
        "row": "[\"P51451-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196758",
        "row": "[\"P01766-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196759",
        "row": "[\"P0CG04-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196760",
        "row": "[\"P80748-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196761",
        "row": "[\"P23083-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196762",
        "row": "[\"P16333-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196763",
        "row": "[\"P01742-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196764",
        "row": "[\"P01743-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196765",
        "row": "[\"P06241-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196766",
        "row": "[\"P04430-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196767",
        "row": "[\"Q96D31-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196768",
        "row": "[\"P01825-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196769",
        "row": "[\"P01824-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196770",
        "row": "[\"P0CF74-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196771",
        "row": "[\"Q06187-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196772",
        "row": "[\"A0A0C4DH73-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196773",
        "row": "[\"P29350-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196774",
        "row": "[\"A2NJV5-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196775",
        "row": "[\"P01834-1\", \"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1.\", \"Cell\", \"2009 Mar 6\", \"Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, Raunser S, Walz T, Garcia KC, Dolmetsch RE, Lewis RS\", \"protein_xref_pubmed\", \"19249086\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196776",
        "row": "[\"P11912-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196777",
        "row": "[\"P15498-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196778",
        "row": "[\"Q96SN7-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196779",
        "row": "[\"P04433-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196780",
        "row": "[\"P04432-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196781",
        "row": "[\"P07948-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196782",
        "row": "[\"P06315-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196783",
        "row": "[\"P48995-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196784",
        "row": "[\"P40259-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196785",
        "row": "[\"P01817-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196786",
        "row": "[\"P01814-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196787",
        "row": "[\"P16885-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196788",
        "row": "[\"P01718-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196789",
        "row": "[\"P01782-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196790",
        "row": "[\"P01780-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196791",
        "row": "[\"A0A0C4DH25-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196792",
        "row": "[\"A0A075B6S6-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196793",
        "row": "[\"P43405-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196794",
        "row": "[\"Q9UN19-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196795",
        "row": "[\"P01721-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196796",
        "row": "[\"P20273-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196797",
        "row": "[\"P01594-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196798",
        "row": "[\"Q8WV28-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196799",
        "row": "[\"P01715-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196800",
        "row": "[\"P01714-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196801",
        "row": "[\"P01717-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196802",
        "row": "[\"P01699-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196803",
        "row": "[\"P06310-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196804",
        "row": "[\"O43865-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196805",
        "row": "[\"P06312-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196806",
        "row": "[\"P01703-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196807",
        "row": "[\"P01700-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196808",
        "row": "[\"P01701-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196809",
        "row": "[\"P01706-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196810",
        "row": "[\"P01704-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196811",
        "row": "[\"P01705-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196812",
        "row": "[\"P01709-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196813",
        "row": "[\"Q14643-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196814",
        "row": "[\"Q07889-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196815",
        "row": "[\"P01880-2\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196816",
        "row": "[\"A0A075B6P5-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196817",
        "row": "[\"P0DP23-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196818",
        "row": "[\"P01602-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196819",
        "row": "[\"P01601-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196820",
        "row": "[\"P01772-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196821",
        "row": "[\"P06331-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196822",
        "row": "[\"P04211-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196823",
        "row": "[\"Q14571-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196824",
        "row": "[\"Q14573-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196825",
        "row": "[\"P01871-2\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196826",
        "row": "[\"O00329-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196827",
        "row": "[\"P01619-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196828",
        "row": "[\"P01614-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196829",
        "row": "[\"P01615-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196830",
        "row": "[\"P01611-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196831",
        "row": "[\"Q6ZUJ8-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196832",
        "row": "[\"P01768-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196833",
        "row": "[\"P01762-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196834",
        "row": "[\"P01763-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196835",
        "row": "[\"P01764-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196836",
        "row": "[\"P01767-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196837",
        "row": "[\"Q96B97-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196838",
        "row": "[\"Q13586-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196839",
        "row": "[\"P0DOY2-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196840",
        "row": "[\"P0DOY3-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196841",
        "row": "[\"P15391-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196842",
        "row": "[\"A0M8Q6-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196843",
        "row": "[\"P01624-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196844",
        "row": "[\"P27986-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196845",
        "row": "[\"P01597-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196846",
        "row": "[\"P01593-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196847",
        "row": "[\"P01599-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196848",
        "row": "[\"P51451-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196849",
        "row": "[\"P01766-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196850",
        "row": "[\"P0CG04-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196851",
        "row": "[\"P80748-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196852",
        "row": "[\"P23083-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196853",
        "row": "[\"P16333-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196854",
        "row": "[\"P01742-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196855",
        "row": "[\"P01743-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196856",
        "row": "[\"P06241-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196857",
        "row": "[\"P04430-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196858",
        "row": "[\"Q96D31-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196859",
        "row": "[\"P01825-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196860",
        "row": "[\"P01824-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196861",
        "row": "[\"P0CF74-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196862",
        "row": "[\"Q06187-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196863",
        "row": "[\"A0A0C4DH73-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196864",
        "row": "[\"P29350-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196865",
        "row": "[\"A2NJV5-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196866",
        "row": "[\"P01834-1\", \"Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation.\", \"The Journal of biological chemistry\", \"2008 Mar 21\", \"Muik M, Frischauf I, Derler I, Fahrner M, Bergsmann J, Eder P, Schindl R, Hesch C, Polzinger B, Fritsch R, Kahr H, Madl J, Gruber H, Groschner K, Romanin C\", \"protein_xref_pubmed\", \"18187424\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196867",
        "row": "[\"P11912-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196868",
        "row": "[\"P15498-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196869",
        "row": "[\"Q96SN7-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196870",
        "row": "[\"P04433-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196871",
        "row": "[\"P04432-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196872",
        "row": "[\"P07948-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196873",
        "row": "[\"P06315-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196874",
        "row": "[\"P48995-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196875",
        "row": "[\"P40259-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196876",
        "row": "[\"P01817-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196877",
        "row": "[\"P01814-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196878",
        "row": "[\"P16885-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196879",
        "row": "[\"P01718-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196880",
        "row": "[\"P01782-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196881",
        "row": "[\"P01780-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196882",
        "row": "[\"A0A0C4DH25-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196883",
        "row": "[\"A0A075B6S6-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196884",
        "row": "[\"P43405-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196885",
        "row": "[\"Q9UN19-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196886",
        "row": "[\"P01721-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196887",
        "row": "[\"P20273-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196888",
        "row": "[\"P01594-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196889",
        "row": "[\"Q8WV28-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196890",
        "row": "[\"P01715-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196891",
        "row": "[\"P01714-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196892",
        "row": "[\"P01717-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196893",
        "row": "[\"P01699-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196894",
        "row": "[\"P06310-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196895",
        "row": "[\"O43865-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196896",
        "row": "[\"P06312-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196897",
        "row": "[\"P01703-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196898",
        "row": "[\"P01700-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196899",
        "row": "[\"P01701-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196900",
        "row": "[\"P01706-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196901",
        "row": "[\"P01704-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196902",
        "row": "[\"P01705-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196903",
        "row": "[\"P01709-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196904",
        "row": "[\"Q14643-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196905",
        "row": "[\"Q07889-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196906",
        "row": "[\"P01880-2\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196907",
        "row": "[\"A0A075B6P5-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196908",
        "row": "[\"P0DP23-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196909",
        "row": "[\"P01602-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196910",
        "row": "[\"P01601-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196911",
        "row": "[\"P01772-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196912",
        "row": "[\"P06331-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196913",
        "row": "[\"P04211-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196914",
        "row": "[\"Q14571-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196915",
        "row": "[\"Q14573-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196916",
        "row": "[\"P01871-2\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196917",
        "row": "[\"O00329-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196918",
        "row": "[\"P01619-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196919",
        "row": "[\"P01614-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196920",
        "row": "[\"P01615-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196921",
        "row": "[\"P01611-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196922",
        "row": "[\"Q6ZUJ8-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196923",
        "row": "[\"P01768-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196924",
        "row": "[\"P01762-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196925",
        "row": "[\"P01763-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196926",
        "row": "[\"P01764-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196927",
        "row": "[\"P01767-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196928",
        "row": "[\"Q96B97-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196929",
        "row": "[\"Q13586-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196930",
        "row": "[\"P0DOY2-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196931",
        "row": "[\"P0DOY3-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196932",
        "row": "[\"P15391-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196933",
        "row": "[\"A0M8Q6-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196934",
        "row": "[\"P01624-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196935",
        "row": "[\"P27986-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196936",
        "row": "[\"P01597-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196937",
        "row": "[\"P01593-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196938",
        "row": "[\"P01599-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196939",
        "row": "[\"P51451-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196940",
        "row": "[\"P01766-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196941",
        "row": "[\"P0CG04-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196942",
        "row": "[\"P80748-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196943",
        "row": "[\"P23083-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196944",
        "row": "[\"P16333-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196945",
        "row": "[\"P01742-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196946",
        "row": "[\"P01743-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196947",
        "row": "[\"P06241-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196948",
        "row": "[\"P04430-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196949",
        "row": "[\"Q96D31-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196950",
        "row": "[\"P01825-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196951",
        "row": "[\"P01824-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196952",
        "row": "[\"P0CF74-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196953",
        "row": "[\"Q06187-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196954",
        "row": "[\"A0A0C4DH73-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196955",
        "row": "[\"P29350-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196956",
        "row": "[\"A2NJV5-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196957",
        "row": "[\"P01834-1\", \"Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.\", \"Nature\", \"2008 Jul 24\", \"Luik RM, Wang B, Prakriya M, Wu MM, Lewis RS\", \"protein_xref_pubmed\", \"18596693\", \"protein_xref_reactome\", \"R-HSA-983695\"]"
    },
    {
        "recordid": "GLY_000310_1_196958",
        "row": "[\"Q9Y2X0-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196959",
        "row": "[\"Q9Y2W1-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196960",
        "row": "[\"P11802-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196961",
        "row": "[\"Q9ULK4-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196962",
        "row": "[\"P49336-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196963",
        "row": "[\"Q92793-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196964",
        "row": "[\"O60907-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196965",
        "row": "[\"Q14686-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196966",
        "row": "[\"Q71SY5-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196967",
        "row": "[\"Q15528-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196968",
        "row": "[\"Q9Y3C7-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196969",
        "row": "[\"Q15788-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196970",
        "row": "[\"Q96G25-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196971",
        "row": "[\"Q96RN5-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196972",
        "row": "[\"Q12772-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196973",
        "row": "[\"Q93074-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196974",
        "row": "[\"Q96EK7-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196975",
        "row": "[\"Q9UBK2-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196976",
        "row": "[\"Q9H204-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196977",
        "row": "[\"Q6STE5-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196978",
        "row": "[\"Q9BWU1-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196979",
        "row": "[\"O60240-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196980",
        "row": "[\"Q9NX70-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196981",
        "row": "[\"P37231-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196982",
        "row": "[\"P06858-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196983",
        "row": "[\"Q9UHV7-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196984",
        "row": "[\"P30281-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196985",
        "row": "[\"Q71F56-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196986",
        "row": "[\"Q9BYK8-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196987",
        "row": "[\"P11161-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196988",
        "row": "[\"A0JLT2-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196989",
        "row": "[\"Q09472-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196990",
        "row": "[\"Q9NVC6-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196991",
        "row": "[\"P01137-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196992",
        "row": "[\"Q14966-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196993",
        "row": "[\"Q15596-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196994",
        "row": "[\"P04628-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196995",
        "row": "[\"Q6P2C8-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196996",
        "row": "[\"Q9Y618-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196997",
        "row": "[\"O43513-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196998",
        "row": "[\"Q9UH73-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_196999",
        "row": "[\"P24468-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    },
    {
        "recordid": "GLY_000310_1_197000",
        "row": "[\"P01375-1\", \"The adipocyte specific transcription factor C/EBPalpha modulates human ob gene expression.\", \"Proceedings of the National Academy of Sciences of the United States of America\", \"1996 May 28\", \"Miller SG, De Vos P, Guerre-Millo M, Wong K, Hermann T, Staels B, Briggs MR, Auwerx J\", \"protein_xref_pubmed\", \"8643605\", \"protein_xref_reactome\", \"R-HSA-381340\"]"
    }
]