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    {
        "title": "Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization.",
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        "authors": "Stewart S, Sundaram M, Zhang Y, Lee J, Han M, Guan KL",
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    {
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    {
        "title": "Discovery of (S)-1-(1-(4-Chloro-3-fluorophenyl)-2-hydroxyethyl)-4-(2-((1-methyl-1H-pyrazol-5-y l)amino)pyrimidin-4-yl)pyridin-2(1H)-one (GDC-0994), an Extracellular Signal-Regulated Kinase 1/2 (ERK1/2) Inhibitor in Early Clinical Development.",
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        "date": "2016",
        "authors": "Blake JF, Burkard M, Chan J, Chen H, Chou KJ, Diaz D, Dudley DA, Gaudino JJ, Gould SE, Grina J, Hunsaker T, Liu L, Martinson M, Moreno D, Mueller L, Orr C, Pacheco P, Qin A, Rasor K, Ren L, Robarge K, Shahidi-Latham S, Stults J, Sullivan F, Wang W, Yin J, Zhou A, Belvin M, Merchant M, Moffat J, Schwarz JB",
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        "title": "Structural basis for the docking of mTORC1 on the lysosomal surface.",
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        "title": "B-Raf protein isoforms interact with and phosphorylate Mek-1 on serine residues 218 and 222.",
        "journal": "Oncogene",
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        "title": "Overexpression of mitogen-activated protein kinase kinase (MAPKK) and its mutants in NIH 3T3 cells. Evidence that MAPKK involvement in cellular proliferation is regulated by phosphorylation of serine residues in its kinase subdomains VII and VIII.",
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        "title": "MP1: a MEK binding partner that enhances enzymatic activation of the MAP kinase cascade.",
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