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Volumn 16, Issue 11, 2015, Pages 691-698

The discovery of modular binding domains: Building blocks of cell signalling

Author keywords

[No Author keywords available]

Indexed keywords

LIPID; PHOSPHOTYROSINE; PROTEIN; PROTEIN SH2; PROTEIN SH3; PROTEIN BINDING;

EID: 84945436554     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm4068     Document Type: Review
Times cited : (66)

References (94)
  • 1
    • 48249141040 scopus 로고    scopus 로고
    • Allostery and cooperativity revisited
    • Cui, Q. & Karplus, M. Allostery and cooperativity revisited. Protein Sci. 17, 1295-1307 (2008).
    • (2008) Protein Sci. , vol.17 , pp. 1295-1307
    • Cui, Q.1    Karplus, M.2
  • 2
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J. & Changeux, J. P. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12, 88-118 (1965).
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 4
    • 0018580807 scopus 로고
    • An activity phosphorylating tyrosine in polyoma T antigen immunoprecipitates
    • Eckhart, W., Hutchinson, M. A. & Hunter, T. An activity phosphorylating tyrosine in polyoma T antigen immunoprecipitates. Cell 18, 925-933 (1979).
    • (1979) Cell , vol.18 , pp. 925-933
    • Eckhart, W.1    Hutchinson, M.A.2    Hunter, T.3
  • 5
    • 0000109995 scopus 로고
    • Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
    • Hunter, T. & Sefton, B. M. Transforming gene product of Rous sarcoma virus phosphorylates tyrosine. Proc. Natl Acad. Sci. USA 77, 1311-1315 (1980).
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 1311-1315
    • Hunter, T.1    Sefton, B.M.2
  • 6
    • 0021924895 scopus 로고
    • The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signalling
    • Ebina, Y. et al. The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signalling. Cell 40, 747-758 (1985).
    • (1985) Cell , vol.40 , pp. 747-758
    • Ebina, Y.1
  • 7
    • 0021985413 scopus 로고
    • Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes
    • Ullrich, A. et al. Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes. Nature 313, 756-761 (1985).
    • (1985) Nature , vol.313 , pp. 756-761
    • Ullrich, A.1
  • 8
    • 0021273420 scopus 로고
    • Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells
    • Ullrich, A. et al. Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells. Nature 309, 418-425 (1984).
    • (1984) Nature , vol.309 , pp. 418-425
    • Ullrich, A.1
  • 9
    • 0021281324 scopus 로고
    • Close similarity of epidermal growth factor receptor and v-erb-B oncogene protein sequences
    • Downward, J. et al. Close similarity of epidermal growth factor receptor and v-erb-B oncogene protein sequences. Nature 307, 521-527 (1984).
    • (1984) Nature , vol.307 , pp. 521-527
    • Downward, J.1
  • 10
    • 0022390516 scopus 로고
    • Low level of cellular protein phosphorylation by nontransforming overproduced p60c-src
    • Iba, H., Cross, F. R., Garber, E. A. & Hanafusa, H. Low level of cellular protein phosphorylation by nontransforming overproduced p60c-src. Mol. Cell. Biol. 5, 1058-1066 (1985).
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 1058-1066
    • Iba, H.1    Cross, F.R.2    Garber, E.A.3    Hanafusa, H.4
  • 11
    • 0022372043 scopus 로고
    • Restriction of the in vitro and in vivo tyrosine protein kinase activities of pp60c-src relative to pp60v-src
    • Coussens, P. M., Cooper, J. A., Hunter, T. & Shalloway, D. Restriction of the in vitro and in vivo tyrosine protein kinase activities of pp60c-src relative to pp60v-src. Mol. Cell. Biol. 5, 2753-2763 (1985).
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 2753-2763
    • Coussens, P.M.1    Cooper, J.A.2    Hunter, T.3    Shalloway, D.4
  • 12
    • 0021259445 scopus 로고
    • Analysis of the catalytic domain of phosphotransferase activity of two avian sarcoma virus-transforming proteins
    • Brugge, J. S. & Darrow, D. Analysis of the catalytic domain of phosphotransferase activity of two avian sarcoma virus-transforming proteins. J. Biol. Chem. 259, 4550-4557 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 4550-4557
    • Brugge, J.S.1    Darrow, D.2
  • 13
    • 0019432795 scopus 로고
    • Structural and functional domains of the Rous sarcoma virus transforming protein (pp60src)
    • Levinson, A. D., Courtneidge, S. A. & Bishop, J. M. Structural and functional domains of the Rous sarcoma virus transforming protein (pp60src). Proc. Natl Acad. Sci. USA 78, 1624-1628 (1981).
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 1624-1628
    • Levinson, A.D.1    Courtneidge, S.A.2    Bishop, J.M.3
  • 14
    • 0020440877 scopus 로고
    • Site-directed mutagenesis of the src gene of Rous sarcoma virus: Construction and characterization of a deletion mutant temperature sensitive for transformation
    • Bryant, D. & Parsons, J. T. Site-directed mutagenesis of the src gene of Rous sarcoma virus: construction and characterization of a deletion mutant temperature sensitive for transformation. J. Virol. 44, 683-691 (1982).
    • (1982) J. Virol. , vol.44 , pp. 683-691
    • Bryant, D.1    Parsons, J.T.2
  • 15
    • 0024537128 scopus 로고
    • Linker insertion-deletion mutagenesis of the v-src gene: Isolation of host-and temperature-dependent mutants
    • DeClue, J. E. & Martin, G. S. Linker insertion-deletion mutagenesis of the v-src gene: isolation of host-and temperature-dependent mutants. J. Virol. 63, 542-554 (1989).
    • (1989) J. Virol. , vol.63 , pp. 542-554
    • DeClue, J.E.1    Martin, G.S.2
  • 16
    • 0023497801 scopus 로고
    • A conserved domain regulates interactions of the v-fps protein-tyrosine kinase with the host cell
    • DeClue, J. E., Sadowski, I., Martin, G. S. & Pawson, T. A conserved domain regulates interactions of the v-fps protein-tyrosine kinase with the host cell. Proc. Natl Acad. Sci. USA 84, 9064-9068 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 9064-9068
    • DeClue, J.E.1    Sadowski, I.2    Martin, G.S.3    Pawson, T.4
  • 18
    • 0020596699 scopus 로고
    • Molecular events leading to fusiform morphological transformation by partial src deletion mutant of Rous sarcoma virus
    • Iwashita, S., Kitamura, N. & Yoshida, M. Molecular events leading to fusiform morphological transformation by partial src deletion mutant of Rous sarcoma virus. Virology 125, 419-431 (1983).
    • (1983) Virology , vol.125 , pp. 419-431
    • Iwashita, S.1    Kitamura, N.2    Yoshida, M.3
  • 20
  • 21
    • 0020806880 scopus 로고
    • Characterization and use of monoclonal antibodies for isolation of phosphotyrosyl proteins from retrovirus-transformed cells and growth factor-stimulated cells
    • Frackelton, A. R. J., Ross, A. H. & Eisen, H. N. Characterization and use of monoclonal antibodies for isolation of phosphotyrosyl proteins from retrovirus-transformed cells and growth factor-stimulated cells. Mol. Cell. Biol. 3, 1343-1352 (1983).
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 1343-1352
    • Frackelton, A.R.J.1    Ross, A.H.2    Eisen, H.N.3
  • 22
    • 0025252220 scopus 로고
    • PDGF β-receptor stimulates tyrosine phosphorylation of GAP and association of GAP with signalling complex
    • Kaplan, D. R., Morrison, D. K., Wong, G., McKormick, F. & Williams, L. T. PDGF β-receptor stimulates tyrosine phosphorylation of GAP and association of GAP with signalling complex. Cell 61, 125-133 (1990).
    • (1990) Cell , vol.61 , pp. 125-133
    • Kaplan, D.R.1    Morrison, D.K.2    Wong, G.3    McKormick, F.4    Williams, L.T.5
  • 23
    • 0024434183 scopus 로고
    • Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins
    • Kazlauskas, A. & Cooper, J. Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins. Cell 58, 1121-1133 (1989).
    • (1989) Cell , vol.58 , pp. 1121-1133
    • Kazlauskas, A.1    Cooper, J.2
  • 24
    • 0024380391 scopus 로고
    • Phospholipase C-gamma is a substrate for the PDGF and EGF receptor protein-tyrosine kinases in vivo and in vitro
    • Meisenhelder, J., Suh, P.-G., Rhee, S. G. & Hunter, T. Phospholipase C-gamma is a substrate for the PDGF and EGF receptor protein-tyrosine kinases in vivo and in vitro. Cell 57, 1109-1122 (1989).
    • (1989) Cell , vol.57 , pp. 1109-1122
    • Meisenhelder, J.1    Suh, P.-G.2    Rhee, S.G.3    Hunter, T.4
  • 25
    • 0024345772 scopus 로고
    • EGF induces tyrosine phosphorylation of phospholipase C-II: A potential mechanism for EGF receptor signaling
    • Margolis, B. et al. EGF induces tyrosine phosphorylation of phospholipase C-II: a potential mechanism for EGF receptor signaling. Cell 57, 1101-1107 (1989).
    • (1989) Cell , vol.57 , pp. 1101-1107
    • Margolis, B.1
  • 26
    • 0023864050 scopus 로고
    • A novel viral oncogene with structural similarity to phospholipase C
    • Mayer, B. J., Hamaguchi, M. & Hanafusa, H. A novel viral oncogene with structural similarity to phospholipase C. Nature 332, 272-275 (1988).
    • (1988) Nature , vol.332 , pp. 272-275
    • Mayer, B.J.1    Hamaguchi, M.2    Hanafusa, H.3
  • 27
    • 0023860445 scopus 로고
    • Sequence similarity of phospholipase C with the non-catalytic region of src
    • Stahl, M. L., Ferenz, C. R., Kelleher, K. L., Kriz, R. W. & Knopf, J. L. Sequence similarity of phospholipase C with the non-catalytic region of src. Nature 332, 269-272 (1988).
    • (1988) Nature , vol.332 , pp. 269-272
    • Stahl, M.L.1    Ferenz, C.R.2    Kelleher, K.L.3    Kriz, R.W.4    Knopf, J.L.5
  • 28
    • 0024212303 scopus 로고
    • Molecular cloning of two types of GAP cDNA from human placenta
    • Trahey, M. et al. Molecular cloning of two types of GAP cDNA from human placenta. Science 242, 1697-1700 (1988).
    • (1988) Science , vol.242 , pp. 1697-1700
    • Trahey, M.1
  • 29
    • 0025681492 scopus 로고
    • g1, GAP, and src to activated growth factor receptors
    • g1, GAP, and src to activated growth factor receptors. Science 250, 979-982 (1990).
    • (1990) Science , vol.250 , pp. 979-982
    • Anderson, D.1
  • 30
    • 0025630506 scopus 로고
    • The tyrosine-phosphorylated carboxyterminus of the EGF receptor is a binding site for GAP and PLC-γ
    • Margolis, B. et al. The tyrosine-phosphorylated carboxyterminus of the EGF receptor is a binding site for GAP and PLC-γ. EMBO J. 9, 4375-4380 (1990).
    • (1990) EMBO J. , vol.9 , pp. 4375-4380
    • Margolis, B.1
  • 31
    • 0025978644 scopus 로고
    • Identification of domains of the v-crk oncogene product sufficient for association with phosphotyrosine-containing proteins
    • Matsuda, M., Mayer, B. J. & Hanafusa, H. Identification of domains of the v-crk oncogene product sufficient for association with phosphotyrosine-containing proteins. Mol. Cell. Biol. 11, 1607-1613 (1991).
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1607-1613
    • Matsuda, M.1    Mayer, B.J.2    Hanafusa, H.3
  • 32
    • 0026059615 scopus 로고
    • The noncatalytic src homology region 2 segment of abl tyrosine kinase binds to tyrosine-phosphorylated cellular proteins with high affinity
    • Mayer, B. J., Jackson, P. K. & Baltimore, D. The noncatalytic src homology region 2 segment of abl tyrosine kinase binds to tyrosine-phosphorylated cellular proteins with high affinity. Proc. Natl Acad. Sci. USA 88, 627-631 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 627-631
    • Mayer, B.J.1    Jackson, P.K.2    Baltimore, D.3
  • 33
    • 0025119824 scopus 로고
    • Src homology region 2 domains direct protein-protein interactions in signal transduction
    • Moran, M. F. et al. Src homology region 2 domains direct protein-protein interactions in signal transduction. Proc. Natl Acad. Sci. USA 87, 8622-8626 (1990).
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 8622-8626
    • Moran, M.F.1
  • 35
    • 0026698924 scopus 로고
    • Crystal structure of the phosphotyrosine recognition domain (SH2) of the v-src tyrosine kinase complexed with tyrosine phosphorylated peptides
    • Waksman, G. et al. Crystal structure of the phosphotyrosine recognition domain (SH2) of the v-src tyrosine kinase complexed with tyrosine phosphorylated peptides. Nature 358, 646-653 (1992).
    • (1992) Nature , vol.358 , pp. 646-653
    • Waksman, G.1
  • 36
    • 0027409064 scopus 로고
    • Binding of a high affinity phosphotyrosyl psptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free forms
    • Waksman, G., Shoelson, S. E., Pant, N., Cowburn, D. & Kuriyan, D. Binding of a high affinity phosphotyrosyl psptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell 72, 779-790 (1993).
    • (1993) Cell , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3    Cowburn, D.4    Kuriyan, D.5
  • 37
    • 0027403027 scopus 로고
    • SH2 domains recognize specific phosphopeptide sequences
    • Songyang, Z. et al. SH2 domains recognize specific phosphopeptide sequences. Cell 72, 767-778 (1993).
    • (1993) Cell , vol.72 , pp. 767-778
    • Songyang, Z.1
  • 38
    • 0028351583 scopus 로고
    • Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav
    • Songyang, Z. et al. Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav. Mol. Cell. Biol. 14, 2777-2785 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2777-2785
    • Songyang, Z.1
  • 39
    • 0026669472 scopus 로고
    • Three dimensional solution structure of the src homology 2 domain of c-abl
    • Overduin, M., Rios, C. B., Mayer, B. J., Baltimore, D. & Cowburn, D. Three dimensional solution structure of the src homology 2 domain of c-abl. Cell 70, 697-704 (1992).
    • (1992) Cell , vol.70 , pp. 697-704
    • Overduin, M.1    Rios, C.B.2    Mayer, B.J.3    Baltimore, D.4    Cowburn, D.5
  • 40
    • 33745185987 scopus 로고    scopus 로고
    • The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling
    • Liu, B. A. et al. The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling. Mol. Cell 22, 851-868 (2006).
    • (2006) Mol. Cell , vol.22 , pp. 851-868
    • Liu, B.A.1
  • 43
    • 70349441058 scopus 로고    scopus 로고
    • Ubiquitin-binding domains-from structures to functions
    • Dikic, I., Wakatsuki, S. & Walters, K. J. Ubiquitin-binding domains-from structures to functions. Nat. Rev. Mol. Cell Biol. 10, 659-671 (2009).
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 659-671
    • Dikic, I.1    Wakatsuki, S.2    Walters, K.J.3
  • 44
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T. & Allis, C. D. Translating the histone code. Science 293, 1074-1080 (2001).
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 45
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4, 5-bisphosphate
    • Harlan, J. E., Hajduk, P. J., Yoon, H. S. & Fesik, S. W. Pleckstrin homology domains bind to phosphatidylinositol-4, 5-bisphosphate. Nature 371, 168-170 (1994).
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 46
    • 0028874438 scopus 로고
    • Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain
    • Lemmon, M. A., Ferguson, K. M., Sigler, P. B. & Schlessinger, J. Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain. Proc. Natl Acad. Sci. USA 92, 10472-10476 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10472-10476
    • Lemmon, M.A.1    Ferguson, K.M.2    Sigler, P.B.3    Schlessinger, J.4
  • 47
    • 1642367563 scopus 로고    scopus 로고
    • Genome-wide analysis of membrane targeting by S. Cerevisiae pleckstrin homology domains
    • Yu, J. W. et al. Genome-wide analysis of membrane targeting by S. cerevisiae pleckstrin homology domains. Mol. Cell 13, 677-688 (2004).
    • (2004) Mol. Cell , vol.13 , pp. 677-688
    • Yu, J.W.1
  • 48
    • 42949124488 scopus 로고    scopus 로고
    • Comprehensive identification of PIP3-regulated PH domains from C. Elegans to H. Sapiens by model prediction and live imaging
    • Park, W. S. et al. Comprehensive identification of PIP3-regulated PH domains from C. elegans to H. sapiens by model prediction and live imaging. Mol. Cell 30, 381-392 (2008).
    • (2008) Mol. Cell , vol.30 , pp. 381-392
    • Park, W.S.1
  • 49
    • 78649853031 scopus 로고    scopus 로고
    • A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae
    • Gallego, O. et al. A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae. Mol. Syst. Biol. 6, 430 (2010).
    • (2010) Mol. Syst. Biol. , vol.6 , pp. 430
    • Gallego, O.1
  • 50
    • 0026743906 scopus 로고
    • Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho
    • Cicchetti, P., Mayer, B. J., Thiel, G. & Baltimore, D. Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho. Science 257, 803-806 (1992).
    • (1992) Science , vol.257 , pp. 803-806
    • Cicchetti, P.1    Mayer, B.J.2    Thiel, G.3    Baltimore, D.4
  • 51
    • 0027408247 scopus 로고
    • Identification of a 10-amino acid proline-rich SH3 binding site
    • Ren, R., Mayer, B. J., Cicchetti, P. & Baltimore, D. Identification of a 10-amino acid proline-rich SH3 binding site. Science 259, 1157-1161 (1993).
    • (1993) Science , vol.259 , pp. 1157-1161
    • Ren, R.1    Mayer, B.J.2    Cicchetti, P.3    Baltimore, D.4
  • 52
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay, B. K., Williamson, M. P. & Sudol, M. The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 14, 231-241 (2000).
    • (2000) FASEB J. , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 53
    • 0013033597 scopus 로고    scopus 로고
    • The structure and function of proline recognition domains
    • Zarrinpar, A., Bhattacharyya, R. P. & Lim, W. A. The structure and function of proline recognition domains. Sci. STKE 2003, RE8 (2003).
    • (2003) Sci. STKE 2003 , pp. RE8
    • Zarrinpar, A.1    Bhattacharyya, R.P.2    Lim, W.A.3
  • 54
    • 33645828833 scopus 로고    scopus 로고
    • Identification of preferred protein interactions by phage-display of the human Src homology-3 proteome
    • Kärkkäinen, S. et al. Identification of preferred protein interactions by phage-display of the human Src homology-3 proteome. EMBO Rep. 7, 186-191 (2006).
    • (2006) EMBO Rep. , vol.7 , pp. 186-191
    • Kärkkäinen, S.1
  • 55
    • 0027962645 scopus 로고
    • Tw o binding orientations for peptides to the Src SH3 domain: Development of a general model for SH3-ligand interactions
    • Feng, S., Chen, J. K., Yu, H., Simon, J. A. & Schreiber, S. L. Tw o binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions. Science 266, 1241-1247 (1994).
    • (1994) Science , vol.266 , pp. 1241-1247
    • Feng, S.1    Chen, J.K.2    Yu, H.3    Simon, J.A.4    Schreiber, S.L.5
  • 56
    • 0028148629 scopus 로고
    • Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains
    • Lim, W. A., Richards, F. M. & Fox, R. O. Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains. Nature 372, 375-379 (1994).
    • (1994) Nature , vol.372 , pp. 375-379
    • Lim, W.A.1    Richards, F.M.2    Fox, R.O.3
  • 57
    • 0029374716 scopus 로고
    • Origin of PDZ (DHR, GLGF) domains
    • Kennedy, M. B. Origin of PDZ (DHR, GLGF) domains. Trends Biochem. Sci. 20, 350 (1995).
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 350
    • Kennedy, M.B.1
  • 58
    • 0028902098 scopus 로고
    • DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins
    • Ponting, C. P. & Phillips, C. DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins. Trends Biochem. Sci. 20, 102-103 (1995).
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 102-103
    • Ponting, C.P.1    Phillips, C.2
  • 59
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • Sheng, M. & Sala, C. PDZ domains and the organization of supramolecular complexes. Annu. Rev. Neurosci. 24, 1-29 (2001).
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 60
    • 0026015023 scopus 로고
    • Signal transduction and the fate of the R7 photoreceptor in Drosophila
    • Rubin, G. M. Signal transduction and the fate of the R7 photoreceptor in Drosophila. Trends Genet. 7, 372-377 (1990).
    • (1990) Trends Genet. , vol.7 , pp. 372-377
    • Rubin, G.M.1
  • 61
    • 0026423579 scopus 로고
    • Multiple intercellular signalling systems control the development of the Caenorhabditis elegans vulva
    • Horvitz, H. R. & Sternberg, P. W. Multiple intercellular signalling systems control the development of the Caenorhabditis elegans vulva. Nature 351, 535-541 (1991).
    • (1991) Nature , vol.351 , pp. 535-541
    • Horvitz, H.R.1    Sternberg, P.W.2
  • 62
    • 0026608178 scopus 로고
    • Elegans cell-signalling gene sem-5 encodes a protein with SH2 and SH3 domains
    • Clark, S. G., Stern, M. J. & Horvitz, H. R. C. elegans cell-signalling gene sem-5 encodes a protein with SH2 and SH3 domains. Nature 356, 340-344 (1992).
    • (1992) Nature , vol.356 , pp. 340-344
    • Clark, S.G.1    Stern, M.J.2    Horvitz, H.R.C.3
  • 63
    • 0026608238 scopus 로고
    • The Son of sevenless gene product: A putative activator of Ras
    • Bonfini, L., Karlovich, C. A., Dasgupta, C. & Bannerjee, U. The Son of sevenless gene product: a putative activator of Ras. Science 255, 603-606 (1992).
    • (1992) Science , vol.255 , pp. 603-606
    • Bonfini, L.1    Karlovich, C.A.2    Dasgupta, C.3    Bannerjee, U.4
  • 64
    • 0025997867 scopus 로고
    • Ras1 and a putative guanine nucleotide exchange factor perform crucial steps in signaling by the sevenless protein tyrosine kinase
    • Simon, M. A., Bowtell, D. D., Dodson, G. S., Laverty, T. R. & Rubin, G. M. Ras1 and a putative guanine nucleotide exchange factor perform crucial steps in signaling by the sevenless protein tyrosine kinase. Cell 67, 701-716 (1991).
    • (1991) Cell , vol.67 , pp. 701-716
    • Simon, M.A.1    Bowtell, D.D.2    Dodson, G.S.3    Laverty, T.R.4    Rubin, G.M.5
  • 65
    • 78649474147 scopus 로고    scopus 로고
    • Ras history: The saga continues
    • Cox, A. D. & Der, C. J. Ras history: the saga continues. Small GTPases 1, 2-27 (2010).
    • (2010) Small GTPases , vol.1 , pp. 2-27
    • Cox, A.D.1    Der, C.J.2
  • 66
    • 0027212082 scopus 로고
    • How receptors turn Ras on
    • McCormick, F. How receptors turn Ras on. Nature 363, 15-16 (1993).
    • (1993) Nature , vol.363 , pp. 15-16
    • McCormick, F.1
  • 67
    • 0027931640 scopus 로고
    • Membrane targeting of the nucleotide exchange factor Sos is sufficient for activating the Ras signaling pathway
    • Aronheim, A. et al. Membrane targeting of the nucleotide exchange factor Sos is sufficient for activating the Ras signaling pathway. Cell 78, 949-961 (1994).
    • (1994) Cell , vol.78 , pp. 949-961
    • Aronheim, A.1
  • 68
    • 0027999033 scopus 로고
    • Membrane-targeting potentiates guanine nucleotide exchange factor CDC25 and SOS1 activation of Ras transforming activity
    • Quilliam, L. A. et al. Membrane-targeting potentiates guanine nucleotide exchange factor CDC25 and SOS1 activation of Ras transforming activity. Proc. Natl Acad. Sci. USA 91, 8512-8516 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8512-8516
    • Quilliam, L.A.1
  • 69
    • 0032438571 scopus 로고    scopus 로고
    • Mammalian Grb2 regulates multiple steps in embryonic development and malignant transformation
    • Cheng, A. M. et al. Mammalian Grb2 regulates multiple steps in embryonic development and malignant transformation. Cell 95, 793-803 (1998).
    • (1998) Cell , vol.95 , pp. 793-803
    • Cheng, A.M.1
  • 70
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri, F., Moarefi, I. & Kuriyan, J. Crystal structure of the Src family tyrosine kinase Hck. Nature 385, 602-609 (1997).
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 71
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu, W., Harrison, S. C. & Eck, M. J. Three-dimensional structure of the tyrosine kinase c-Src. Nature 385, 595-602 (1997).
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 72
    • 0036468436 scopus 로고    scopus 로고
    • The modular logic of signaling proteins: Building allosteric switches from simple binding domains
    • Lim, W. A. The modular logic of signaling proteins: building allosteric switches from simple binding domains. Curr. Opin. Struct. Biol. 12, 61-68 (2002).
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 61-68
    • Lim, W.A.1
  • 73
    • 0141757323 scopus 로고    scopus 로고
    • Reprogramming control of an allosteric signaling switch through modular recombination
    • Dueber, J. E., Yeh, B. J., Chak, K. & Lim, W. A. Reprogramming control of an allosteric signaling switch through modular recombination. Science 301, 1904-1908 (2003).
    • (2003) Science , vol.301 , pp. 1904-1908
    • Dueber, J.E.1    Yeh, B.J.2    Chak, K.3    Lim, W.A.4
  • 74
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson, T. & Nash, P. Assembly of cell regulatory systems through protein interaction domains. Science 300, 445-452 (2003).
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 75
    • 70350364712 scopus 로고    scopus 로고
    • Molecular machines or pleiomorphic ensembles: Signaling complexes revisited
    • Mayer, B. J., Blinov, M. L. & Loew, L. M. Molecular machines or pleiomorphic ensembles: signaling complexes revisited. J. Biol. 8, 81 (2009).
    • (2009) J. Biol. , vol.8 , pp. 81
    • Mayer, B.J.1    Blinov, M.L.2    Loew, L.M.3
  • 76
    • 70349308508 scopus 로고    scopus 로고
    • Cell regulation: Determined to signal discrete cooperation
    • Gibson, T. J. Cell regulation: determined to signal discrete cooperation. Trends Biochem. Sci. 34, 471-482 (2009).
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 471-482
    • Gibson, T.J.1
  • 77
    • 84862776582 scopus 로고    scopus 로고
    • Phase transitions in the assembly of multi-valent signaling proteins
    • Li, P. et al. Phase transitions in the assembly of multi-valent signaling proteins. Nature 483, 336-340 (2012).
    • (2012) Nature , vol.483 , pp. 336-340
    • Li, P.1
  • 79
    • 84862950678 scopus 로고    scopus 로고
    • Visualizing dynamic activities of signaling enzymes using genetically encodable FRET-based biosensors from designs to applications
    • Zhou, X., Herbst-Robinson, K. J. & Zhang, J. Visualizing dynamic activities of signaling enzymes using genetically encodable FRET-based biosensors from designs to applications. Methods Enzymol. 504, 317-340 (2012).
    • (2012) Methods Enzymol. , vol.504 , pp. 317-340
    • Zhou, X.1    Herbst-Robinson, K.J.2    Zhang, J.3
  • 80
    • 84874787934 scopus 로고    scopus 로고
    • Interaction domains of Sos1/Grb2 are finely tuned for cooperative control of embryonic stem cell fate
    • Findlay, G. M. et al. Interaction domains of Sos1/Grb2 are finely tuned for cooperative control of embryonic stem cell fate. Cell 152, 1008-1020 (2013).
    • (2013) Cell , vol.152 , pp. 1008-1020
    • Findlay, G.M.1
  • 81
    • 84880441014 scopus 로고    scopus 로고
    • Temporal regulation of EGF signalling networks by the scaffold protein Shc1
    • Zheng, Y. et al. Temporal regulation of EGF signalling networks by the scaffold protein Shc1. Nature 499, 166-171 (2013).
    • (2013) Nature , vol.499 , pp. 166-171
    • Zheng, Y.1
  • 82
    • 84864577164 scopus 로고    scopus 로고
    • The application of modular protein domains in proteomics
    • Jadwin, J. A., Ogiue-Ikeda, M. & Machida, K. The application of modular protein domains in proteomics. FEBS Lett. 586, 2586-2596 (2012).
    • (2012) FEBS Lett. , vol.586 , pp. 2586-2596
    • Jadwin, J.A.1    Ogiue-Ikeda, M.2    Machida, K.3
  • 83
    • 12144287536 scopus 로고    scopus 로고
    • A map of WW domain family interactions
    • Hu, H. et al. A map of WW domain family interactions. Proteomics 4, 643-655 (2004).
    • (2004) Proteomics , vol.4 , pp. 643-655
    • Hu, H.1
  • 84
    • 33745037938 scopus 로고    scopus 로고
    • Comparative analysis of Saccharomyces cerevisiae WW domains and their interacting proteins
    • Hesselberth, J. R. et al. Comparative analysis of Saccharomyces cerevisiae WW domains and their interacting proteins. Genome Biol. 7, R30 (2006).
    • (2006) Genome Biol. , vol.7 , pp. R30
    • Hesselberth, J.R.1
  • 85
    • 42649123723 scopus 로고    scopus 로고
    • Defining the specificity space of the human SRC homology 2 domain
    • Huang, H. et al. Defining the specificity space of the human SRC homology 2 domain. Mol. Cell. Proteomics 7, 768-784 (2008).
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 768-784
    • Huang, H.1
  • 86
    • 30544449081 scopus 로고    scopus 로고
    • A quantitative protein interaction network for the ERBB receptors using protein microarrays
    • Jones, R. B., Gordus, A., Krall, J. A. & MacBeath, G. A quantitative protein interaction network for the ErbB receptors using protein microarrays. Nature 439, 168-174 (2006).
    • (2006) Nature , vol.439 , pp. 168-174
    • Jones, R.B.1    Gordus, A.2    Krall, J.A.3    MacBeath, G.4
  • 87
    • 34547127612 scopus 로고    scopus 로고
    • PDZ domain binding selectivity is optimized across the mouse proteome
    • Stiffler, M. A. et al. PDZ domain binding selectivity is optimized across the mouse proteome. Science 317, 364-369 (2007).
    • (2007) Science , vol.317 , pp. 364-369
    • Stiffler, M.A.1
  • 88
    • 84876957035 scopus 로고    scopus 로고
    • The human SH2 interaction landscape
    • Tinti, M. et al. The human SH2 interaction landscape. Cell Rep. 3, 1293-1305 (2013).
    • (2013) Cell Rep. , vol.3 , pp. 1293-1305
    • Tinti, M.1
  • 89
    • 70350404403 scopus 로고    scopus 로고
    • Bayesian modeling of the yeast SH3 domain interactome predicts spatiotemporal dynamics of endocytosis proteins
    • Tonikian, R. et al. Bayesian modeling of the yeast SH3 domain interactome predicts spatiotemporal dynamics of endocytosis proteins. PLoS Biol. 7, e1000218 (2009).
    • (2009) PLoS Biol. , vol.7 , pp. e1000218
    • Tonikian, R.1
  • 90
    • 54749086397 scopus 로고    scopus 로고
    • A specificity map for the PDZ domain family
    • Tonikian, R. et al. A specificity map for the PDZ domain family. PLoS Biol. 6, 239 (2008).
    • (2008) PLoS Biol. , vol.6 , pp. 239
    • Tonikian, R.1
  • 91
    • 0025008168 scopus 로고
    • Sequence logos: A new way to display consensus sequences
    • Schneider, T. D. & Stephens, R. M. Sequence logos: a new way to display consensus sequences. Nucleic Acids Res. 18, 6097-6100 (1990).
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 92
    • 0019311793 scopus 로고
    • Nucleotide sequence of an avian sarcoma virus oncogene (src) and proposed amino acid sequence for gene product
    • Czernilofsky, A. P. et al. Nucleotide sequence of an avian sarcoma virus oncogene (src) and proposed amino acid sequence for gene product. Nature 287, 198-203 (1980).
    • (1980) Nature , vol.287 , pp. 198-203
    • Czernilofsky, A.P.1
  • 93
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin, A. J., Tanner, J. W., Allen, P. M. & Shaw, A. S. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 84, 889-897 (1996).
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 94
    • 0031470652 scopus 로고    scopus 로고
    • The structural basis for 14-3-3:phosphopeptide binding specificity
    • Yaffe, M. B. et al. The structural basis for 14-3-3:phosphopeptide binding specificity. Cell 91, 961-971 (1997).
    • (1997) Cell , vol.91 , pp. 961-971
    • Yaffe, M.B.1


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