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Volumn 10, Issue , 2012, Pages

SRC Homology 2 Domain Binding Sites in Insulin, IGF-1 and FGF receptor mediated signaling networks reveal an extensive potential interactome

Author keywords

[No Author keywords available]

Indexed keywords

FIBROBLAST GROWTH FACTOR RECEPTOR; INSULIN; PEPTIDE; PHOSPHOTYROSINE; PROTEIN SH2; SOMATOMEDIN C;

EID: 84870521139     PISSN: None     EISSN: 1478811X     Source Type: Journal    
DOI: 10.1186/1478-811X-10-27     Document Type: Article
Times cited : (33)

References (124)
  • 1
    • 0028170817 scopus 로고
    • Receptor protein-tyrosine kinases and their signal transduction pathways
    • Receptor protein-tyrosine kinases and their signal transduction pathways. van der Geer P, Hunter T, Lindberg RA, Annu Rev Cell Biol 1994 10 251 337 10.1146/annurev.cb.10.110194.001343 7888178 (Pubitemid 24372822)
    • (1994) Annual Review of Cell Biology , vol.10 , pp. 251-337
    • Van Der Geer, P.1    Hunter, T.2    Lindberg, R.A.3
  • 3
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • 10.1016/j.cell.2010.06.011 20602996
    • Cell signaling by receptor tyrosine kinases. Lemmon MA, Schlessinger J, Cell 2010 141 1117 1134 10.1016/j.cell.2010.06.011 20602996
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 4
    • 0036518996 scopus 로고    scopus 로고
    • Phosphotyrosine-binding domains in signal transduction
    • 10.1038/nrm759 11994738
    • Phosphotyrosine-binding domains in signal transduction. Yaffe MB, Nat Rev Mol Cell Biol 2002 3 177 186 10.1038/nrm759 11994738
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 177-186
    • Yaffe, M.B.1
  • 5
    • 0842346438 scopus 로고    scopus 로고
    • Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems
    • DOI 10.1016/S0092-8674(03)01077-8
    • Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems. Pawson T, Cell 2004 116 191 203 10.1016/S0092-8674(03)01077-8 14744431 (Pubitemid 38167312)
    • (2004) Cell , vol.116 , Issue.2 , pp. 191-203
    • Pawson, T.1
  • 6
    • 0035575586 scopus 로고    scopus 로고
    • SH2 domains, interaction modules and cellular wiring
    • DOI 10.1016/S0962-8924(01)02154-7, PII S0962892401021547
    • SH2 domains, interaction modules and cellular wiring. Pawson T, Gish GD, Nash P, Trends Cell Biol 2001 11 504 511 10.1016/S0962-8924(01)02154-7 11719057 (Pubitemid 33079144)
    • (2001) Trends in Cell Biology , vol.11 , Issue.12 , pp. 504-511
    • Pawson, T.1    Gish, G.D.2    Nash, P.3
  • 7
    • 0025298967 scopus 로고
    • Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins
    • 10.1126/science.1694307 1694307
    • Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins. Matsuda M, Mayer BJ, Fukui Y, Hanafusa H, Science 1990 248 1537 1539 10.1126/science.1694307 1694307
    • (1990) Science , vol.248 , pp. 1537-1539
    • Matsuda, M.1    Mayer, B.J.2    Fukui, Y.3    Hanafusa, H.4
  • 9
    • 0025119824 scopus 로고
    • Src homology region 2 domains direct protein-protein interactions in signal transduction
    • 10.1073/pnas.87.21.8622 2236073
    • Src homology region 2 domains direct protein-protein interactions in signal transduction. Moran MF, Koch CA, Anderson D, Ellis C, England L, Martin GS, Pawson T, Proc Natl Acad Sci USA 1990 87 8622 8626 10.1073/pnas.87.21.8622 2236073
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 8622-8626
    • Moran, M.F.1    Koch, C.A.2    Anderson, D.3    Ellis, C.4    England, L.5    Martin, G.S.6    Pawson, T.7
  • 10
    • 0025765803 scopus 로고
    • SH2 and SH3 Domains: Elements that control interactions of cytoplasmic signaling proteins
    • SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Koch CA, Anderson D, Moran MF, Ellis C, Pawson T, Science 1991 252 668 674 10.1126/science.1708916 1708916 (Pubitemid 21916987)
    • (1991) Science , vol.252 , Issue.5006 , pp. 668-674
    • Koch, C.A.1    Anderson, D.2    Moran, M.F.3    Ellis, C.4    Pawson, T.5
  • 11
    • 84864622162 scopus 로고    scopus 로고
    • The language of SH2 domain interactions defines phosphotyrosine-mediated signal transduction
    • 10.1016/j.febslet.2012.04.054 22569091
    • The language of SH2 domain interactions defines phosphotyrosine-mediated signal transduction. Liu BA, Engelmann BW, Nash PD, FEBS Lett 2012 586 2597 2605 10.1016/j.febslet.2012.04.054 22569091
    • (2012) FEBS Lett , vol.586 , pp. 2597-2605
    • Liu, B.A.1    Engelmann, B.W.2    Nash, P.D.3
  • 12
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • DOI 10.1126/science.1083653
    • Assembly of cell regulatory systems through protein interaction domains. Pawson T, Nash P, Science 2003 300 445 452 10.1126/science.1083653 12702867 (Pubitemid 36444318)
    • (2003) Science , vol.300 , Issue.5618 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 13
    • 0034193568 scopus 로고    scopus 로고
    • Protein-protein interactions define specificity in signal transduction
    • Protein-protein interactions define specificity in signal transduction. Pawson T, Nash P, Genes Dev 2000 14 1027 1047 10809663 (Pubitemid 30324418)
    • (2000) Genes and Development , vol.14 , Issue.9 , pp. 1027-1047
    • Pawson, T.1    Nash, P.2
  • 14
    • 33745185987 scopus 로고    scopus 로고
    • The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling
    • 10.1016/j.molcel.2006.06.001 16793553
    • The Human and Mouse Complement of SH2 Domain Proteins-Establishing the Boundaries of Phosphotyrosine Signaling. Liu BA, Jablonowski K, Raina M, Arce M, Pawson T, Nash PD, Mol Cell 2006 22 851 868 10.1016/j.molcel.2006.06.001 16793553
    • (2006) Mol Cell , vol.22 , pp. 851-868
    • Liu, B.A.1    Jablonowski, K.2    Raina, M.3    Arce, M.4    Pawson, T.5    Nash, P.D.6
  • 15
    • 83155181907 scopus 로고    scopus 로고
    • The SH2 domain-containing proteins in 21 extant species establish the provenance and scope of phosphotyrosine signaling in Eukaryotes
    • 10.1126/scisignal.2002105 22155787
    • The SH2 domain-containing proteins in 21 extant species establish the provenance and scope of phosphotyrosine signaling in Eukaryotes. Liu BA, Shah E, Jablonowski K, Stergachis A, Engelmann BW, Nash PD, Sci Signal 2011 4 a83 10.1126/scisignal.2002105 22155787
    • (2011) Sci Signal , vol.4
    • Liu, B.A.1    Shah, E.2    Jablonowski, K.3    Stergachis, A.4    Engelmann, B.W.5    Nash, P.D.6
  • 17
    • 0033527682 scopus 로고    scopus 로고
    • Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinase
    • DOI 10.1006/jmbi.1999.3190
    • Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinase. Bradshaw JM, Mitaxov V, Waksman G, J Mol Biol 1999 293 971 985 10.1006/jmbi.1999.3190 10543978 (Pubitemid 29527677)
    • (1999) Journal of Molecular Biology , vol.293 , Issue.4 , pp. 971-985
    • Bradshaw, J.M.1    Mitaxov, V.2    Waksman, G.3
  • 18
    • 0036417094 scopus 로고    scopus 로고
    • Molecular recognition by SH2 domains
    • DOI 10.1016/S0065-3233(02)61005-8
    • Molecular recognition by SH2 domains. Bradshaw JM, Waksman G, Adv Protein Chem 2002 61 161 210 12461824 (Pubitemid 35303457)
    • (2002) Advances in Protein Chemistry , vol.61 , pp. 161-210
    • Bradshaw, J.M.1    Waksman, G.2
  • 21
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: Proteome-wide prediction of cell signalling interactions using short sequence motifs
    • DOI 10.1093/nar/gkg584
    • Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs. Obenauer JC, Cantley LC, Yaffe MB, Nucleic Acids Res 2003 31 3635 3641 10.1093/nar/gkg584 12824383 (Pubitemid 37442212)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3635-3641
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3
  • 22
    • 78149333493 scopus 로고    scopus 로고
    • SH2 domains recognize contextual peptide sequence information to determine selectivity
    • 10.1074/mcp.M110.001586 20627867
    • SH2 domains recognize contextual peptide sequence information to determine selectivity. Liu BA, Jablonowski K, Shah EE, Engelmann BW, Jones RB, Nash PD, Mol Cell Proteomics 2010 9 2391 2404 10.1074/mcp.M110.001586 20627867
    • (2010) Mol Cell Proteomics , vol.9 , pp. 2391-2404
    • Liu, B.A.1    Jablonowski, K.2    Shah, E.E.3    Engelmann, B.W.4    Jones, R.B.5    Nash, P.D.6
  • 24
    • 33747769612 scopus 로고    scopus 로고
    • Quantitative multiplexed profiling of cellular signaling networks using phosphotyrosine-specific DNA-tagged SH2 domains
    • DOI 10.1038/nmeth917, PII NMETH917
    • Quantitative multiplexed profiling of cellular signaling networks using phosphotyrosine-specific DNA-tagged SH2 domains. Dierck K, Machida K, Voigt A, Thimm J, Horstmann M, Fiedler W, Mayer BJ, Nollau P, Nat Methods 2006 3 737 744 10.1038/nmeth917 16929320 (Pubitemid 44275743)
    • (2006) Nature Methods , vol.3 , Issue.9 , pp. 737-744
    • Dierck, K.1    Machida, K.2    Voigt, A.3    Thimm, J.4    Horstmann, M.5    Fiedler, W.6    Mayer, B.J.7    Nollau, P.8
  • 25
    • 12844283323 scopus 로고    scopus 로고
    • The SH2 domain: Versatile signaling module and pharmaceutical target
    • DOI 10.1016/j.bbapap.2004.10.005, PII S1570963904002882
    • The SH2 domain: versatile signaling module and pharmaceutical target. Machida K, Mayer BJ, Biochim Biophys Acta 2005 1747 1 25 10.1016/j.bbapap.2004. 10.005 15680235 (Pubitemid 40170450)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1747 , Issue.1 , pp. 1-25
    • Machida, K.1    Mayer, B.J.2
  • 26
    • 10944257339 scopus 로고    scopus 로고
    • Profiling the global tyrosine phosphorylation state
    • 12754303
    • Profiling the global tyrosine phosphorylation state. Machida K, Mayer BJ, Nollau P, Mol Cell Proteomics 2003 2 215 233 12754303
    • (2003) Mol Cell Proteomics , vol.2 , pp. 215-233
    • Machida, K.1    Mayer, B.J.2    Nollau, P.3
  • 27
    • 78149463029 scopus 로고    scopus 로고
    • Characterizing tyrosine phosphorylation signaling in lung cancer using SH2 profiling
    • 10.1371/journal.pone.0013470 20976048
    • Characterizing tyrosine phosphorylation signaling in lung cancer using SH2 profiling. Machida K, Eschrich S, Li J, Bai Y, Koomen J, Mayer BJ, Haura EB, PLoS One 2010 5 13470 10.1371/journal.pone.0013470 20976048
    • (2010) PLoS One , vol.5 , pp. 513470
    • Machida, K.1    Eschrich, S.2    Li, J.3    Bai, Y.4    Koomen, J.5    Mayer, B.J.6    Haura, E.B.7
  • 28
    • 0035996750 scopus 로고    scopus 로고
    • Probing the phosphopeptide specificities of protein tyrosine phosphatases, SH2 and PTB domains with combinatorial library methods
    • DOI 10.2174/1389203023380594
    • Probing the phosphopeptide specificities of protein tyrosine phosphatases, SH2 and PTB domains with combinatorial library methods. Vetter SW, Zhang ZY, Curr Protein Pept Sci 2002 3 365 397 10.2174/1389203023380594 12370002 (Pubitemid 34778182)
    • (2002) Current Protein and Peptide Science , vol.3 , Issue.4 , pp. 365-397
    • Vetter, S.W.1    Zhang, Z.-Y.2
  • 30
    • 1542305566 scopus 로고    scopus 로고
    • An Oriented Peptide Array Library (OPAL) Strategy to Study Protem-Protein Interactions
    • DOI 10.1074/jbc.M311886200
    • An oriented peptide array library (OPAL) strategy to study protein-protein interactions. Rodriguez M, Li SS, Harper JW, Songyang Z, J Biol Chem 2004 279 8802 8807 10.1074/jbc.M311886200 14679191 (Pubitemid 38295938)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.10 , pp. 8802-8807
    • Rodriguez, M.1    Li, S.S.-C.2    Harper, J.W.3    Songyang, Z.4
  • 31
    • 0034677670 scopus 로고    scopus 로고
    • Identification of natural ligands for SH2 domains from a phage display cDNA library
    • 10.1006/jmbi.2000.3561 10704309
    • Identification of natural ligands for SH2 domains from a phage display cDNA library. Cochrane D, Webster C, Masih G, McCafferty J, J Mol Biol 2000 297 89 97 10.1006/jmbi.2000.3561 10704309
    • (2000) J Mol Biol , vol.297 , pp. 89-97
    • Cochrane, D.1    Webster, C.2    Masih, G.3    McCafferty, J.4
  • 34
    • 70350469056 scopus 로고    scopus 로고
    • The complexity of cell signaling and the need for a new mechanics
    • 10.1126/scisignal.281pe46 19638613
    • The complexity of cell signaling and the need for a new mechanics. Hlavacek WS, Faeder JR, Sci Signal 2009 2 e46 10.1126/scisignal.281pe46 19638613
    • (2009) Sci Signal , vol.2
    • Hlavacek, W.S.1    Faeder, J.R.2
  • 35
    • 79960137914 scopus 로고    scopus 로고
    • Scaffold-mediated nucleation of protein signaling complexes: Elementary principles
    • 10.1016/j.mbs.2011.06.003 21683720
    • Scaffold-mediated nucleation of protein signaling complexes: Elementary principles. Yang J, Hlavacek WS, Math Biosci 2011 232 164 173 10.1016/j.mbs.2011.06.003 21683720
    • (2011) Math Biosci , vol.232 , pp. 164-173
    • Yang, J.1    Hlavacek, W.S.2
  • 40
    • 0035969559 scopus 로고    scopus 로고
    • Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication
    • DOI 10.1038/35107009
    • Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication. Nash P, Tang X, Orlicky S, Chen Q, Gertler FB, Mendenhall MD, Sicheri F, Pawson T, Tyers M, Nature 2001 414 514 521 10.1038/35107009 11734846 (Pubitemid 33131529)
    • (2001) Nature , vol.414 , Issue.6863 , pp. 514-521
    • Nash, P.1    Tang, X.2    Orlicky, S.3    Chen, Q.4    Gertler, F.B.5    Mendenhall, M.D.6    Sicheri, F.7    Pawson, T.8    Tyers, M.9
  • 41
    • 0036721834 scopus 로고    scopus 로고
    • The SPOT-synthesis technique: Synthetic peptide arrays on membrane supports - Principles and applications
    • DOI 10.1016/S0022-1759(02)00137-0, PII S0022175902001370
    • The SPOT-synthesis technique. Synthetic peptide arrays on membrane supports - principles and applications. Frank R, J Immunol Methods 2002 267 13 26 10.1016/S0022-1759(02)00137-0 12135797 (Pubitemid 34804809)
    • (2002) Journal of Immunological Methods , vol.267 , Issue.1 , pp. 13-26
    • Frank, R.1
  • 42
    • 0030329981 scopus 로고    scopus 로고
    • SPOT synthesis. Epitope analysis with arrays of synthetic peptides prepared on cellulose membranes
    • 8959713
    • SPOT synthesis. Epitope analysis with arrays of synthetic peptides prepared on cellulose membranes. Frank R, Overwin H, Methods Mol Biol 1996 66 149 169 8959713
    • (1996) Methods Mol Biol , vol.66 , pp. 149-169
    • Frank, R.1    Overwin, H.2
  • 43
    • 0033518296 scopus 로고    scopus 로고
    • Novel mode of ligand binding by the SH2 domain of the human XLP disease gene product SAP/SH2D1A
    • 10.1016/S0960-9822(00)80080-9 10607564
    • Novel mode of ligand binding by the SH2 domain of the human XLP disease gene product SAP/SH2D1A. Li SC, Gish G, Yang D, Coffey AJ, Forman-Kay JD, Ernberg I, Kay LE, Pawson T, Curr Biol 1999 9 1355 1362 10.1016/S0960-9822(00) 80080-9 10607564
    • (1999) Curr Biol , vol.9 , pp. 1355-1362
    • Li, S.C.1    Gish, G.2    Yang, D.3    Coffey, A.J.4    Forman-Kay, J.D.5    Ernberg, I.6    Kay, L.E.7    Pawson, T.8
  • 44
    • 77953424518 scopus 로고    scopus 로고
    • A study to assess the cross-reactivity of cellulose membrane-bound peptides with detection systems: An analysis at the amino acid level
    • 20474041
    • A study to assess the cross-reactivity of cellulose membrane-bound peptides with detection systems: an analysis at the amino acid level. Mahrenholz CC, Tapia V, Stigler RD, Volkmer R, J Pept Sci 2010 16 297 302 20474041
    • (2010) J Pept Sci , vol.16 , pp. 297-302
    • Mahrenholz, C.C.1    Tapia, V.2    Stigler, R.D.3    Volkmer, R.4
  • 46
    • 15844409347 scopus 로고    scopus 로고
    • The Fyn tyrosine kinase binds Irs-1 and forms a distinct signaling complex during insulin stimulation
    • DOI 10.1074/jbc.271.18.10583
    • The Fyn tyrosine kinase binds Irs-1 and forms a distinct signaling complex during insulin stimulation. Sun XJ, Pons S, Asano T, Myers MG Jr, Glasheen E, White MF, J Biol Chem 1996 271 10583 10587 10.1074/jbc.271.18.10583 8631859 (Pubitemid 26149894)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.18 , pp. 10583-10587
    • Sun, X.J.1    Pons, S.2    Asano, T.3    Myers Jr., M.G.4    Glasheen, E.5    White, M.F.6
  • 48
    • 0022977712 scopus 로고
    • A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130(gag-fps)
    • A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps. Sadowski I, Stone JC, Pawson T, Mol Cell Biol 1986 6 4396 4408 3025655 (Pubitemid 17217381)
    • (1986) Molecular and Cellular Biology , vol.6 , Issue.12 , pp. 4396-4408
    • Sadowski, I.1    Stone, J.C.2    Pawson, T.3
  • 51
    • 0037245913 scopus 로고    scopus 로고
    • BIND: The biomolecular interaction network database
    • DOI 10.1093/nar/gkg056
    • BIND: the Biomolecular Interaction Network Database. Bader GD, Betel D, Hogue CW, Nucleic Acids Res 2003 31 248 250 10.1093/nar/gkg056 12519993 (Pubitemid 36150376)
    • (2003) Nucleic Acids Research , vol.31 , Issue.1 , pp. 248-250
    • Bader, G.D.1    Betel, D.2    Hogue, C.W.V.3
  • 54
    • 84862642911 scopus 로고    scopus 로고
    • High-throughput analysis of peptide binding modules
    • 10.1002/pmic.201100599 22610655
    • High-throughput analysis of peptide binding modules. Liu BA, Engelmann BW, Nash PD, Proteomics 2012 12 1527 1546 10.1002/pmic.201100599 22610655
    • (2012) Proteomics , vol.12 , pp. 1527-1546
    • Liu, B.A.1    Engelmann, B.W.2    Nash, P.D.3
  • 56
    • 0026731562 scopus 로고
    • Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca2+ flux but not mitogenesis
    • 10.1038/358678a0 1379697
    • Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca2+ flux but not mitogenesis. Peters KG, Marie J, Wilson E, Ives HE, Escobedo J, Del Rosario M, Mirda D, Williams LT, Nature 1992 358 678 681 10.1038/358678a0 1379697
    • (1992) Nature , vol.358 , pp. 678-681
    • Peters, K.G.1    Marie, J.2    Wilson, E.3    Ives, H.E.4    Escobedo, J.5    Del Rosario, M.6    Mirda, D.7    Williams, L.T.8
  • 57
    • 43949125837 scopus 로고    scopus 로고
    • A quantitative study of the recruitment potential of all intracellular tyrosine residues on EGFR, FGFR1 and IGF1R
    • DOI 10.1039/b801018h
    • A quantitative study of the recruitment potential of all intracellular tyrosine residues on EGFR, FGFR1 and IGF1R. Kaushansky A, Gordus A, Chang B, Rush J, MacBeath G, Mol Biosyst 2008 4 643 653 10.1039/b801018h 18493663 (Pubitemid 351706308)
    • (2008) Molecular BioSystems , vol.4 , Issue.6 , pp. 643-653
    • Kaushansky, A.1    Gordus, A.2    Chang, B.3    Rush, J.4    MacBeath, G.5
  • 58
    • 30544449081 scopus 로고    scopus 로고
    • A quantitative protein interaction network for the ErbB receptors using protein microarrays
    • DOI 10.1038/nature04177, PII NATURE04177
    • A quantitative protein interaction network for the ErbB receptors using protein microarrays. Jones RB, Gordus A, Krall JA, MacBeath G, Nature 2006 439 168 174 10.1038/nature04177 16273093 (Pubitemid 43083134)
    • (2006) Nature , vol.439 , Issue.7073 , pp. 168-174
    • Jones, R.B.1    Gordus, A.2    Krall, J.A.3    MacBeath, G.4
  • 59
    • 80052140473 scopus 로고    scopus 로고
    • Application of Celluspots peptide arrays for the analysis of the binding specificity of epigenetic reading domains to modified histone tails
    • 10.1186/1471-2091-12-48 21884582
    • Application of Celluspots peptide arrays for the analysis of the binding specificity of epigenetic reading domains to modified histone tails. Bock I, Kudithipudi S, Tamas R, Kungulovski G, Dhayalan A, Jeltsch A, BMC Biochem 2011 12 48 10.1186/1471-2091-12-48 21884582
    • (2011) BMC Biochem , vol.12 , pp. 48
    • Bock, I.1    Kudithipudi, S.2    Tamas, R.3    Kungulovski, G.4    Dhayalan, A.5    Jeltsch, A.6
  • 62
    • 80053161741 scopus 로고    scopus 로고
    • A systematic family-wide investigation reveals that 30% of mammalian PDZ domains engage in PDZ-PDZ interactions
    • 10.1016/j.chembiol.2011.06.013 21944753
    • A systematic family-wide investigation reveals that 30% of mammalian PDZ domains engage in PDZ-PDZ interactions. Chang BH, Gujral TS, Karp ES, BuKhalid R, Grantcharova VP, MacBeath G, Chem Biol 2011 18 1143 1152 10.1016/j.chembiol. 2011.06.013 21944753
    • (2011) Chem Biol , vol.18 , pp. 1143-1152
    • Chang, B.H.1    Gujral, T.S.2    Karp, E.S.3    Bukhalid, R.4    Grantcharova, V.P.5    MacBeath, G.6
  • 63
    • 0343181431 scopus 로고    scopus 로고
    • The hematopoietic-specific adaptor protein Gads functions in T-cell signaling via interactions with the SLP-76 and LAT adaptors
    • DOI 10.1016/S0960-9822(99)80017-7
    • The hematopoietic-specific adaptor protein gads functions in T-cell signaling via interactions with the SLP-76 and LAT adaptors. Liu SK, Fang N, Koretzky GA, McGlade CJ, Curr Biol 1999 9 67 75 10.1016/S0960-9822(99)80017-7 10021361 (Pubitemid 29083530)
    • (1999) Current Biology , vol.9 , Issue.2 , pp. 67-75
    • Liu, S.K.1    Fang, N.2    Koretzky, G.A.3    McGlade, C.J.4
  • 64
    • 15844388521 scopus 로고    scopus 로고
    • Grap is a novel SH3-SH2-SH3 adaptor protein that couples tyrosine kinases to the Ras pathway
    • DOI 10.1074/jbc.271.21.12129
    • Grap is a novel SH3-SH2-SH3 adaptor protein that couples tyrosine kinases to the Ras pathway. Feng GS, Ouyang YB, Hu DP, Shi ZQ, Gentz R, Ni J, J Biol Chem 1996 271 12129 12132 10.1074/jbc.271.21.12129 8647802 (Pubitemid 26160867)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.21 , pp. 12129-12132
    • Feng, G.-S.1    Ouyang, Y.-B.2    Hu, D.-P.3    Shi, Z.-Q.4    Gentz, R.5    Ni, J.6
  • 65
    • 2942598149 scopus 로고    scopus 로고
    • PhosphoSite: A bioinformatics resource dedicated to physiological protein phosphorylation
    • DOI 10.1002/pmic.200300772
    • PhosphoSite: A bioinformatics resource dedicated to physiological protein phosphorylation. Hornbeck PV, Chabra I, Kornhauser JM, Skrzypek E, Zhang B, Proteomics 2004 4 1551 1561 10.1002/pmic.200300772 15174125 (Pubitemid 38738314)
    • (2004) Proteomics , vol.4 , Issue.6 , pp. 1551-1561
    • Hornbeck, P.V.1    Chabra, I.2    Kornhauser, J.M.3    Skrzypek, E.4    Zhang, B.5
  • 66
    • 13644262131 scopus 로고    scopus 로고
    • Identification of a molecular recognition role for the activation loop phosphotyrosine of the Src tyrosine kinase
    • DOI 10.1021/ja047957c
    • Identification of a molecular recognition role for the activation loop phosphotyrosine of the SRC tyrosine kinase. Videlock EJ, Chung VK, Hall JM, Hines J, Agapakis CM, Austin DJ, J Am Chem Soc 2005 127 1600 1601 10.1021/ja047957c 15700969 (Pubitemid 40229121)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.6 , pp. 1600-1601
    • Videlock, E.J.1    Chung, V.K.2    Hall, J.M.3    Hines, J.4    Agapakis, C.M.5    Austin, D.J.6
  • 68
    • 0033516705 scopus 로고    scopus 로고
    • The packing density in proteins: Standard radii and volumes
    • DOI 10.1006/jmbi.1999.2829
    • The packing density in proteins: standard radii and volumes. Tsai J, Taylor R, Chothia C, Gerstein M, J Mol Biol 1999 290 253 266 10.1006/jmbi.1999.2829 10388571 (Pubitemid 29308589)
    • (1999) Journal of Molecular Biology , vol.290 , Issue.1 , pp. 253-266
    • Tsai, J.1    Taylor, R.2    Chothia, C.3    Gerstein, M.4
  • 69
    • 2142738304 scopus 로고    scopus 로고
    • WebLogo: A sequence logo generator
    • DOI 10.1101/gr.849004
    • WebLogo: a sequence logo generator. Crooks GE, Hon G, Chandonia JM, Brenner SE, Genome Res 2004 14 1188 1190 10.1101/gr.849004 15173120 (Pubitemid 38811555)
    • (2004) Genome Research , vol.14 , Issue.6 , pp. 1188-1190
    • Crooks, G.E.1    Hon, G.2    Chandonia, J.-M.3    Brenner, S.E.4
  • 70
    • 84865105858 scopus 로고    scopus 로고
    • Evolution of SH2 domains and phosphotyrosine signaling networks
    • Evolution of SH2 domains and phosphotyrosine signaling networks. Liu BA, Nash PD, Philos Trans R Soc Lond B Biol Sci 2012 367 2555 2572
    • (2012) Philos Trans R Soc Lond B Biol Sci , vol.367 , pp. 2555-2572
    • Liu, B.A.1    Nash, P.D.2
  • 71
    • 79960245388 scopus 로고    scopus 로고
    • Selected reaction monitoring mass spectrometry reveals the dynamics of signaling through the GRB2 adaptor
    • 10.1038/nbt.1905 21706016
    • Selected reaction monitoring mass spectrometry reveals the dynamics of signaling through the GRB2 adaptor. Bisson N, James DA, Ivosev G, Tate SA, Bonner R, Taylor L, Pawson T, Nat Biotechnol 2011 29 653 658 10.1038/nbt.1905 21706016
    • (2011) Nat Biotechnol , vol.29 , pp. 653-658
    • Bisson, N.1    James, D.A.2    Ivosev, G.3    Tate, S.A.4    Bonner, R.5    Taylor, L.6    Pawson, T.7
  • 72
    • 77957241580 scopus 로고    scopus 로고
    • The proliferating role of insulin and insulin-like growth factors in cancer
    • 10.1016/j.tem.2010.06.007 20663687
    • The proliferating role of insulin and insulin-like growth factors in cancer. Gallagher EJ, LeRoith D, Trends Endocrinol Metab 2010 21 610 618 10.1016/j.tem.2010.06.007 20663687
    • (2010) Trends Endocrinol Metab , vol.21 , pp. 610-618
    • Gallagher, E.J.1    Leroith, D.2
  • 73
    • 79961004321 scopus 로고    scopus 로고
    • Signalling by insulin and IGF receptors: Supporting acts and new players
    • 10.1530/JME-11-0022 21498522
    • Signalling by insulin and IGF receptors: supporting acts and new players. Siddle K, J Mol Endocrinol 2011 47 1 R10 10.1530/JME-11-0022 21498522
    • (2011) J Mol Endocrinol , vol.47
    • Siddle, K.1
  • 74
    • 79954614279 scopus 로고    scopus 로고
    • Targeting the insulin-like growth factor network in cancer therapy
    • 10.4161/cbt.11.8.14689 21311212
    • Targeting the insulin-like growth factor network in cancer therapy. Heidegger I, Pircher A, Klocker H, Massoner P, Cancer Biol Ther 2011 11 701 707 10.4161/cbt.11.8.14689 21311212
    • (2011) Cancer Biol Ther , vol.11 , pp. 701-707
    • Heidegger, I.1    Pircher, A.2    Klocker, H.3    Massoner, P.4
  • 76
    • 84862777882 scopus 로고    scopus 로고
    • Insulin resistance in the nervous system
    • 10.1016/j.tem.2011.12.004 22245457
    • Insulin resistance in the nervous system. Kim B, Feldman EL, Trends Endocrinol Metab 2012 23 133 141 10.1016/j.tem.2011.12.004 22245457
    • (2012) Trends Endocrinol Metab , vol.23 , pp. 133-141
    • Kim, B.1    Feldman, E.L.2
  • 77
    • 0033586726 scopus 로고    scopus 로고
    • Calorimetric examination of high-affinity Src SH2 domain-tyrosyl phosphopeptide binding: Dissection of the phosphopeptide sequence specificity and coupling energetics
    • DOI 10.1021/bi982974y
    • Calorimetric examination of high-affinity Src SH2 domain-tyrosyl phosphopeptide binding: dissection of the phosphopeptide sequence specificity and coupling energetics. Bradshaw JM, Waksman G, Biochemistry 1999 38 5147 5154 10.1021/bi982974y 10213620 (Pubitemid 29196364)
    • (1999) Biochemistry , vol.38 , Issue.16 , pp. 5147-5154
    • Bradshaw, J.M.1    Waksman, G.2
  • 79
    • 0027157785 scopus 로고
    • Phosphatidylinositol 3-kinase p85 SH2 domain specificity defined by direct phosphopeptide/SH2 domain binding
    • Phosphatidylinositol 3-kinase p85 SH2 domain specificity defined by direct phosphopeptide/SH2 domain binding. Piccione E, Case RD, Domchek SM, Hu P, Chaudhuri M, Backer JM, Schlessinger J, Shoelson SE, Biochemistry 1993 32 3197 3202 10.1021/bi00064a001 8384875 (Pubitemid 23126884)
    • (1993) Biochemistry , vol.32 , Issue.13 , pp. 3197-3202
    • Piccione, E.1    Case, R.D.2    Domchek, S.M.3    Hu, P.4    Chaudhuri, M.5    Backer, J.M.6    Schlessinger, J.7    Shoelson, S.E.8
  • 80
    • 0021891894 scopus 로고
    • Protein-tyrosine kinases
    • Protein-tyrosine kinases. Hunter T, Cooper JA, Annu Rev Biochem 1985 54 897 930 10.1146/annurev.bi.54.070185.004341 2992362 (Pubitemid 15073667)
    • (1985) Annual Review of Biochemistry , vol.VOL. 54 , pp. 897-930
    • Hunter, T.1    Cooper, J.A.2
  • 83
    • 0346555269 scopus 로고    scopus 로고
    • Optimization of specificity in a cellular protein interaction network by negative selection
    • DOI 10.1038/nature02178
    • Optimization of specificity in a cellular protein interaction network by negative selection. Zarrinpar A, Park SH, Lim WA, Nature 2003 426 676 680 10.1038/nature02178 14668868 (Pubitemid 38009377)
    • (2003) Nature , vol.426 , Issue.6967 , pp. 676-680
    • Zarrinpar, A.1    Park, S.-H.2    Lim, W.A.3
  • 84
    • 0023864050 scopus 로고
    • A novel viral oncogene with structural similarity to phospholipase C
    • DOI 10.1038/332272a0
    • A novel viral oncogene with structural similarity to phospholipase C. Mayer BJ, Hamaguchi M, Hanafusa H, Nature 1988 332 272 275 10.1038/332272a0 2450282 (Pubitemid 18076660)
    • (1988) Nature , vol.332 , Issue.6161 , pp. 272-275
    • Mayer, B.J.1    Hamaguchi, M.2    Hanafusa, H.3
  • 85
    • 0000122573 scopus 로고
    • PHYLIP - Phylogeny Inference Package (Version 3.2)
    • PHYLIP - Phylogeny Inference Package (Version 3.2). Felsenstein J, Cladistics 1989 5 164 166
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 86
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • DOI 10.1093/molbev/msm092
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Tamura K, Dudley J, Nei M, Kumar S, Mol Biol Evol 2007 24 1596 1599 10.1093/molbev/msm092 17488738 (Pubitemid 47236692)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.8 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 87
    • 4644305806 scopus 로고    scopus 로고
    • Subsets of the major tyrosine phosphorylation sites in Crk-associated substrate (CAS) are sufficient to promote cell migration
    • DOI 10.1074/jbc.M404675200
    • Subsets of the major tyrosine phosphorylation sites in Crk-associated substrate (CAS) are sufficient to promote cell migration. Shin NY, Dise RS, Schneider-Mergener J, Ritchie MD, Kilkenny DM, Hanks SK, J Biol Chem 2004 279 38331 38337 10.1074/jbc.M404675200 15247284 (Pubitemid 39295981)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.37 , pp. 38331-38337
    • Shin, N.-Y.1    Dise, R.S.2    Schneider-Mergener, J.3    Ritchie, M.D.4    Kilkenny, D.M.5    Hanks, S.K.6
  • 90
    • 0033593322 scopus 로고    scopus 로고
    • Fyn associates with Cbl and phosphorylates tyrosine 731 in Cbl, a binding site for phosphatidylinositol 3-kinase
    • DOI 10.1074/jbc.274.4.2097
    • Fyn associates with Cbl and phosphorylates tyrosine 731 in Cbl, a binding site for phosphatidylinositol 3-kinase. Hunter S, Burton EA, Wu SC, Anderson SM, J Biol Chem 1999 274 2097 2106 10.1074/jbc.274.4.2097 9890970 (Pubitemid 29061362)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.4 , pp. 2097-2106
    • Hunter, S.1    Burton, E.A.2    Wu, S.C.3    Anderson, S.M.4
  • 95
    • 0031964602 scopus 로고    scopus 로고
    • Tandem SH2 domains confer high specificity in tyrosine kinase signaling
    • DOI 10.1074/jbc.273.2.729
    • Tandem SH2 domains confer high specificity in tyrosine kinase signaling. Ottinger EA, Botfield MC, Shoelson SE, J Biol Chem 1998 273 729 735 10.1074/jbc.273.2.729 9422724 (Pubitemid 28049159)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.2 , pp. 729-735
    • Ottinger, E.A.1    Botfield, M.C.2    Shoelson, S.E.3
  • 96
    • 0028354446 scopus 로고
    • Nuclear magnetic resonance structure of an SH2 domain of phospholipase C- γ1 complexed with a high affinity binding peptide
    • DOI 10.1016/0092-8674(94)90160-0
    • Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide. Pascal SM, Singer AU, Gish G, Yamazaki T, Shoelson SE, Pawson T, Kay LE, Forman-Kay JD, Cell 1994 77 461 472 10.1016/0092-8674(94)90160-0 8181064 (Pubitemid 24145206)
    • (1994) Cell , vol.77 , Issue.3 , pp. 461-472
    • Pascal, S.M.1    Singer, A.U.2    Gish, G.3    Yamazaki, T.4    Shoelson, S.E.5    Pawson, T.6    Kay, L.E.7    Forman-Kay, J.D.8
  • 97
    • 12144259853 scopus 로고    scopus 로고
    • NMR dynamics-derived insights into the binding properties of a peptide interacting with an SH2 domain
    • DOI 10.1021/bi048641k
    • NMR dynamics-derived insights into the binding properties of a peptide interacting with an SH2 domain. Finerty PJ Jr, Mittermaier AK, Muhandiram R, Kay LE, Forman-Kay JD, Biochemistry 2005 44 694 703 10.1021/bi048641k 15641795 (Pubitemid 40105500)
    • (2005) Biochemistry , vol.44 , Issue.2 , pp. 694-703
    • Finerty Jr., P.J.1    Mittermaier, A.K.2    Muhandiram, R.3    Kay, L.E.4    Forman-Kay, J.D.5
  • 98
    • 0035939843 scopus 로고    scopus 로고
    • A repertoire library that allows the selection of synthetic SH2ITALT with altered binding specificities
    • DOI 10.1038/sj.onc.1204654
    • A repertoire library that allows the selection of synthetic SH2s with altered binding specificities. Malabarba MG, Milia E, Faretta M, Zamponi R, Pelicci PG, Di Fiore PP, Oncogene 2001 20 5186 5194 10.1038/sj.onc.1204654 11526507 (Pubitemid 32844047)
    • (2001) Oncogene , vol.20 , Issue.37 , pp. 5186-5194
    • Malabarba, M.G.1    Milia, E.2    Faretta, M.3    Zamponi, R.4    Pelicci, P.G.5    Di Fiore, P.P.6
  • 101
    • 0029121483 scopus 로고
    • Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor
    • 10.1073/pnas.92.17.7784 7544002
    • Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor. Zhou MM, Meadows RP, Logan TM, Yoon HS, Wade WS, Ravichandran KS, Burakoff SJ, Fesik SW, Proc Natl Acad Sci USA 1995 92 7784 7788 10.1073/pnas.92.17.7784 7544002
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7784-7788
    • Zhou, M.M.1    Meadows, R.P.2    Logan, T.M.3    Yoon, H.S.4    Wade, W.S.5    Ravichandran, K.S.6    Burakoff, S.J.7    Fesik, S.W.8
  • 102
    • 0031239913 scopus 로고    scopus 로고
    • The protein tyrosine phosphatase SHP-2 negatively regulates ciliary neurotrophic factor induction of gene expression
    • The protein tyrosine phosphatase SHP-2 negatively regulates ciliary neurotrophic factor induction of gene expression. Symes A, Stahl N, Reeves SA, Farruggella T, Servidei T, Gearan T, Yancopoulos G, Fink JS, Curr Biol 1997 7 697 700 10.1016/S0960-9822(06)00298-3 9285712 (Pubitemid 27408869)
    • (1997) Current Biology , vol.7 , Issue.9 , pp. 697-700
    • Symes, A.1    Stahl, N.2    Reeves, S.A.3    Farruggella, T.4    Servidei, T.5    Gearan, T.6    Yancopoulos, G.7    Stephen Fink, J.8
  • 103
    • 0035853839 scopus 로고    scopus 로고
    • From consensus sequence peptide to high affinity ligand, a "library scan" strategy
    • 10.1074/jbc.M011232200 11278862
    • From consensus sequence peptide to high affinity ligand, a "library scan" strategy. Yeh RH, Lee TR, Lawrence DS, J Biol Chem 2001 276 12235 12240 10.1074/jbc.M011232200 11278862
    • (2001) J Biol Chem , vol.276 , pp. 12235-12240
    • Yeh, R.H.1    Lee, T.R.2    Lawrence, D.S.3
  • 104
    • 23344436170 scopus 로고    scopus 로고
    • Functional interactions of HPK1 with adaptor proteins
    • DOI 10.1002/jcb.20401
    • Functional interactions of HPK1 with adaptor proteins. Boomer JS, Tan TH, J Cell Biochem 2005 95 34 44 10.1002/jcb.20401 15770651 (Pubitemid 41420213)
    • (2005) Journal of Cellular Biochemistry , vol.95 , Issue.1 , pp. 34-44
    • Boomer, J.S.1    Tan, T.-H.2
  • 105
    • 0032577464 scopus 로고    scopus 로고
    • Association of the insulin receptor with phospholipase C-γ/(PLCγ) in 3T3-L1 adipocytes suggests a role for PLCγ in metabolic signaling by insulin
    • DOI 10.1074/jbc.273.22.13808
    • Association of the insulin receptor with phospholipase C-gamma (PLCgamma) in 3 T3-L1 adipocytes suggests a role for PLCgamma in metabolic signaling by insulin. Kayali AG, Eichhorn J, Haruta T, Morris AJ, Nelson JG, Vollenweider P, Olefsky JM, Webster NJ, J Biol Chem 1998 273 13808 13818 10.1074/jbc.273.22. 13808 9593725 (Pubitemid 28268431)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.22 , pp. 13808-13818
    • Kayali, A.G.1    Eichhorn, J.2    Haruta, T.3    Morris, A.J.4    Nelson, J.G.5    Vollenweider, P.6    Olefsky, J.M.7    Webster, N.J.G.8
  • 107
    • 0028342948 scopus 로고
    • SH-PTP2/Syp SH2 domain binding specificity is defined by direct interactions with platelet-derived growth factor beta-receptor, epidermal growth factor receptor, and insulin receptor substrate-1-derived phosphopeptides
    • 8144631
    • SH-PTP2/Syp SH2 domain binding specificity is defined by direct interactions with platelet-derived growth factor beta-receptor, epidermal growth factor receptor, and insulin receptor substrate-1-derived phosphopeptides. Case RD, Piccione E, Wolf G, Benett AM, Lechleider RJ, Neel BG, Shoelson SE, J Biol Chem 1994 269 10467 10474 8144631
    • (1994) J Biol Chem , vol.269 , pp. 10467-10474
    • Case, R.D.1    Piccione, E.2    Wolf, G.3    Benett, A.M.4    Lechleider, R.J.5    Neel, B.G.6    Shoelson, S.E.7
  • 110
    • 15644368839 scopus 로고    scopus 로고
    • The COOH-terminal tyrosine phosphorylation sites on IRS-1 bind SHP-2 and negatively regulate insulin signaling
    • DOI 10.1074/jbc.273.41.26908
    • The COOH-terminal tyrosine phosphorylation sites on IRS-1 bind SHP-2 and negatively regulate insulin signaling. Myers MG Jr, Mendez R, Shi P, Pierce JH, Rhoads R, White MF, J Biol Chem 1998 273 26908 26914 10.1074/jbc.273.41.26908 9756938 (Pubitemid 28471711)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.41 , pp. 26908-26914
    • Myers Jr., M.G.1    Mendez, R.2    Shi, P.3    Pierce, J.H.4    Rhoads, R.5    White, M.F.6
  • 111
    • 0032571078 scopus 로고    scopus 로고
    • IL-13 induces tyrosine phosphorylation of phospholipase Cγ-1 following IRS-2 association in human monocytes: Relationship with the inhibitory effect of IL-13 on ROI production
    • DOI 10.1006/bbrc.1998.8314
    • IL-13 induces tyrosine phosphorylation of phospholipase C gamma-1 following IRS-2 association in human monocytes: relationship with the inhibitory effect of IL-13 on ROI production. Sozzani P, Hasan L, Seguelas MH, Caput D, Ferrara P, Pipy B, Cambon C, Biochem Biophys Res Commun 1998 244 665 670 10.1006/bbrc.1998.8314 9535722 (Pubitemid 28418125)
    • (1998) Biochemical and Biophysical Research Communications , vol.244 , Issue.3 , pp. 665-670
    • Sozzani, P.1    Hasan, L.2    Seguelas, M.-H.3    Caput, D.4    Ferrara, P.5    Pipy, B.6    Cambon, C.7
  • 112
    • 0028810236 scopus 로고
    • 4PS/insulin receptor substrate (IRS)-2 is the alternative substrate of the insulin receptor in IRS-1-deficient mice
    • 10.1074/jbc.270.42.24670 7559579
    • 4PS/insulin receptor substrate (IRS)-2 is the alternative substrate of the insulin receptor in IRS-1-deficient mice. Patti ME, Sun XJ, Bruening JC, Araki E, Lipes MA, White MF, Kahn CR, J Biol Chem 1995 270 24670 24673 10.1074/jbc.270.42.24670 7559579
    • (1995) J Biol Chem , vol.270 , pp. 24670-24673
    • Patti, M.E.1    Sun, X.J.2    Bruening, J.C.3    Araki, E.4    Lipes, M.A.5    White, M.F.6    Kahn, C.R.7
  • 113
    • 0036679107 scopus 로고    scopus 로고
    • The Shb adaptor protein binds to tyrosine 766 in the FGFR-1 and regulates the Ras/MEK/MAPK pathway via FRS2 phosphorylation in endothelial cells
    • 10.1091/mbc.E02-02-0103 12181353
    • The Shb adaptor protein binds to tyrosine 766 in the FGFR-1 and regulates the Ras/MEK/MAPK pathway via FRS2 phosphorylation in endothelial cells. Cross MJ, Lu L, Magnusson P, Nyqvist D, Holmqvist K, Welsh M, Claesson-Welsh L, Mol Biol Cell 2002 13 2881 2893 10.1091/mbc.E02-02-0103 12181353
    • (2002) Mol Biol Cell , vol.13 , pp. 2881-2893
    • Cross, M.J.1    Lu, L.2    Magnusson, P.3    Nyqvist, D.4    Holmqvist, K.5    Welsh, M.6    Claesson-Welsh, L.7
  • 114
    • 0037013284 scopus 로고    scopus 로고
    • Interaction of fibroblast growth factor receptor 3 and the adapter protein SH2-B. A role in Stat5 activation
    • DOI 10.1074/jbc.M102777200
    • Interaction of fibroblast growth factor receptor 3 and the adapter protein SH2-B. A role in STAT5 activation. Kong M, Wang CS, Donoghue DJ, J Biol Chem 2002 277 15962 15970 10.1074/jbc.M102777200 11827956 (Pubitemid 34967878)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.18 , pp. 15962-15970
    • Kong, M.1    Wang, C.S.2    Donoghue, D.J.3
  • 116
    • 0030706168 scopus 로고    scopus 로고
    • A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway
    • A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway. Kouhara H, Hadari YR, Spivak-Kroizman T, Schilling J, Bar-Sagi D, Lax I, Schlessinger J, Cell 1997 89 693 702 10.1016/S0092-8674(00)80252-4 9182757 (Pubitemid 27516172)
    • (1997) Cell , vol.89 , Issue.5 , pp. 693-702
    • Kouhara, H.1    Hadari, Y.R.2    Spivak-Kroizman, T.3    Schilling, J.4    Bar-Sagi, D.5    Lax, I.6    Schlessinger, J.7
  • 117
    • 0031835659 scopus 로고    scopus 로고
    • Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation
    • Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation. Hadari YR, Kouhara H, Lax I, Schlessinger J, Mol Cell Biol 1998 18 3966 3973 9632781 (Pubitemid 28287920)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.7 , pp. 3966-3973
    • Hadari, Y.R.1    Kouhara, H.2    Lax, I.3    Schlessinger, J.4
  • 118
    • 15444377640 scopus 로고    scopus 로고
    • Intramolecular interaction between phosphorylated tyrosine-783 and the C-terminal Src homology 2 domain activates phospholipase C-γ1
    • DOI 10.1073/pnas.0409590102
    • Intramolecular interaction between phosphorylated tyrosine-783 and the C-terminal Src homology 2 domain activates phospholipase C-gamma1. Poulin B, Sekiya F, Rhee SG, Proc Natl Acad Sci USA 2005 102 4276 4281 10.1073/pnas.0409590102 15764700 (Pubitemid 40397102)
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.12 , pp. 4276-4281
    • Poulin, B.1    Sekiya, F.2    Rhee, S.G.3
  • 119
    • 0031032777 scopus 로고    scopus 로고
    • Fibronectin-stimulated signaling from a focal adhesion kinase-c-Src complex: Involvement of the Grb2, p130(cas) and Nck adaptor proteins
    • Fibronectin-stimulated signaling from a focal adhesion kinase-c-Src complex: involvement of the Grb2, p130cas, and Nck adaptor proteins. Schlaepfer DD, Broome MA, Hunter T, Mol Cell Biol 1997 17 1702 1713 9032297 (Pubitemid 27097399)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.3 , pp. 1702-1713
    • Schlaepfer, D.D.1    Broome, M.A.2    Hunter, T.3
  • 120
    • 0041816053 scopus 로고    scopus 로고
    • Cas couples the tyrosine kinase Bmx/Etk with regulation of the actin cytoskeleton and cell migration
    • DOI 10.1074/jbc.M306438200
    • p130Cas Couples the tyrosine kinase Bmx/Etk with regulation of the actin cytoskeleton and cell migration. Abassi YA, Rehn M, Ekman N, Alitalo K, Vuori K, J Biol Chem 2003 278 35636 35643 10.1074/jbc.M306438200 12832404 (Pubitemid 37102337)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.37 , pp. 35636-35643
    • Abassi, Y.A.1    Rehn, M.2    Ekman, N.3    Alitalo, K.4    Vuori, K.5
  • 123
    • 0035900720 scopus 로고    scopus 로고
    • Insulin receptor-mediated p62dok tyrosine phosphorylation at residues 362 and 398 plays distinct roles for binding GTPase-activating protein and Nck and is essential for inhibiting insulin-stimulated activation of Ras and Akt
    • 10.1074/jbc.M102116200 11551902
    • Insulin receptor-mediated p62dok tyrosine phosphorylation at residues 362 and 398 plays distinct roles for binding GTPase-activating protein and Nck and is essential for inhibiting insulin-stimulated activation of Ras and Akt. Wick MJ, Dong LQ, Hu D, Langlais P, Liu F, J Biol Chem 2001 276 42843 42850 10.1074/jbc.M102116200 11551902
    • (2001) J Biol Chem , vol.276 , pp. 42843-42850
    • Wick, M.J.1    Dong, L.Q.2    Hu, D.3    Langlais, P.4    Liu, F.5
  • 124
    • 0033529502 scopus 로고    scopus 로고
    • Independent SH2-binding sites mediate interaction of Dok-related protein with RasGTPase-activating protein and Nck
    • DOI 10.1074/jbc.274.32.22775
    • Independent SH2-binding sites mediate interaction of Dok-related protein with RasGTPase-activating protein and Nck. Lock P, Casagranda F, Dunn AR, J Biol Chem 1999 274 22775 22784 10.1074/jbc.274.32.22775 10428862 (Pubitemid 29379327)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.32 , pp. 22775-22784
    • Lock, P.1    Casagranda, F.2    Dunn, A.R.3


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