메뉴 건너뛰기




Volumn 28, Issue 5, 2010, Pages 329-350

Structural elements and allosteric mechanisms governing regulation and catalysis of CSK-family kinases and their inhibition of Src-family kinases

Author keywords

Allosteric regulation; Catalysis; CHK; CSK; Protein kinase; Src family kinases

Indexed keywords

ADENOSINE TRIPHOSPHATE; PEPTIDE YY; PROTEIN SH2; PROTEIN SH3; PROTEIN TYROSINE KINASE;

EID: 77957763100     PISSN: 08977194     EISSN: 10292292     Source Type: Journal    
DOI: 10.3109/08977194.2010.484424     Document Type: Review
Times cited : (24)

References (97)
  • 1
    • 0035413606 scopus 로고    scopus 로고
    • Kinetic and catalytic mechanisms of protein kinases
    • Adams JA. 2001. Kinetic and catalytic mechanisms of protein kinases. Chem Rev 101:2271-2290.
    • (2001) Chem Rev , vol.101 , pp. 2271-2290
    • Adams, J.A.1
  • 4
    • 0037422596 scopus 로고    scopus 로고
    • Structural basis and prediction of substrate specificity in protein serine/threonine kinases
    • Brinkworth RI, Breinl RA, Kobe B. 2003. Structural basis and prediction of substrate specificity in protein serine/threonine kinases. Proc Natl Acad Sci USA 100:74-79.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 74-79
    • Brinkworth, R.I.1    Breinl, R.A.2    Kobe, B.3
  • 5
    • 0029131489 scopus 로고
    • Interactions between the amino-terminal domain ofp56lck and cytoplasmic domains of CD4 and CD8 alpha in yeast
    • Campbell KS, Buder A, Deuschle U. 1995. Interactions between the amino-terminal domain ofp56lck and cytoplasmic domains of CD4 and CD8 alpha in yeast. Eur J Immunol 25:2408-2412.
    • (1995) Eur J Immunol , vol.25 , pp. 2408-2412
    • Campbell, K.S.1    Buder, A.2    Deuschle, U.3
  • 7
    • 74049104885 scopus 로고    scopus 로고
    • Allosteric networks governing regulation and catalysis ofsrc-family protein tyrosine kinases-implications for disease-associated kinases
    • Cheng HC, Johnson TM, Mills RD, Chong YP, Chan KC, Culvenor JG. 2010. Allosteric networks governing regulation and catalysis ofsrc-family protein tyrosine kinases-implications for disease-associated kinases. Clin Exp Pharmacol Physiol 37: 93-101.
    • (2010) Clin Exp Pharmacol Physiol , vol.37 , pp. 93-101
    • Cheng, H.C.1    Johnson, T.M.2    Mills, R.D.3    Chong, Y.P.4    Chan, K.C.5    Culvenor, J.G.6
  • 9
    • 32144460477 scopus 로고    scopus 로고
    • C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK)-endogenous negative regulators of Src-family protein kinases
    • Chong YP, Mulhern TD, Cheng HC. 2005a. C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK)-endogenous negative regulators of Src-family protein kinases. Growth Factors 23:233-244.
    • (2005) Growth Factors , vol.23 , pp. 233-244
    • Chong, Y.P.1    Mulhern, T.D.2    Cheng, H.C.3
  • 10
    • 29144452123 scopus 로고    scopus 로고
    • Endogenous and synthetic inhibitors of the Src-family protein tyrosine kinases
    • Chong YP, Ia KK, Mulhern TD, Cheng HC. 2005b. Endogenous and synthetic inhibitors of the Src-family protein tyrosine kinases. Biochim Biophys Acta 1754:210-220.
    • (2005) Biochim Biophys Acta , vol.1754 , pp. 210-220
    • Chong, Y.P.1    Ia, K.K.2    Mulhern, T.D.3    Cheng, H.C.4
  • 12
    • 30044441052 scopus 로고    scopus 로고
    • KESTREL: A powerful method for identifying the physiological substrates of protein kinases
    • Cohen P, Knebel A. 2006. KESTREL: A powerful method for identifying the physiological substrates of protein kinases. Biochem J 393:1-6.
    • (2006) Biochem J , vol.393 , pp. 1-6
    • Cohen, P.1    Knebel, A.2
  • 13
    • 0142138254 scopus 로고    scopus 로고
    • Protein tyrosine kinases Src and Csk: A tail's tale
    • Cole PA, Shen K, Qiao Y, Wang D. 2003. Protein tyrosine kinases Src and Csk: A tail's tale. Curr Opin Chem Biol 7:580-585.
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 580-585
    • Cole, P.A.1    Shen, K.2    Qiao, Y.3    Wang, D.4
  • 14
    • 0022559078 scopus 로고
    • Tyr527 is phosphorylated in pp60c-src: Implications for regulation
    • Cooper JA, Gould KL, Cartwright CA, Hunter T. 1986. Tyr527 is phosphorylated in pp60c-src: Implications for regulation. Science 231:1431-1434.
    • (1986) Science , vol.231 , pp. 1431-1434
    • Cooper, J.A.1    Gould, K.L.2    Cartwright, C.A.3    Hunter, T.4
  • 15
    • 20444399897 scopus 로고    scopus 로고
    • The crystal structure of a c-Src complex in an active conformation suggests possible steps in c-Srcactivation
    • Cowan-Jacob SW, Fendrich G, Manley PW, Jahnke W, Fabbro D, Liebetanz J, Meyer T. 2005. The crystal structure of a c-Src complex in an active conformation suggests possible steps in c-Srcactivation. Structure 13:861-871.
    • (2005) Structure , vol.13 , pp. 861-871
    • Cowan-Jacob, S.W.1    Fendrich, G.2    Manley, P.W.3    Jahnke, W.4    Fabbro, D.5    Liebetanz, J.6    Meyer, T.7
  • 16
    • 33751272653 scopus 로고    scopus 로고
    • Structural biology of protein tyrosine kinases
    • Cowan-Jacob SW. 2006. Structural biology of protein tyrosine kinases. Cell Mol Life Sci 63:2608-2625.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 2608-2625
    • Cowan-Jacob, S.W.1
  • 17
    • 69249129036 scopus 로고    scopus 로고
    • The C-terminal Src inhibitory kinase (Csk)-mediated tyrosine phosphorylation is a novel molecular mechanism to limit P2X3 receptor function in mouse sensory neurons
    • D'Arco M, Giniatullin R, Leone V, Carloni P, Birsa N, Nair A, Nistri A, Fabbretti E. 2009. The C-terminal Src inhibitory kinase (Csk)-mediated tyrosine phosphorylation is a novel molecular mechanism to limit P2X3 receptor function in mouse sensory neurons. J Biol Chem 284:21393-21401.
    • (2009) J Biol Chem , vol.284 , pp. 21393-21401
    • D'Arco, M.1    Giniatullin, R.2    Leone, V.3    Carloni, P.4    Birsa, N.5    Nair, A.6    Nistri, A.7    Fabbretti, E.8
  • 19
    • 70649096122 scopus 로고    scopus 로고
    • SH2 domains: Modulators of nonreceptor tyrosine kinase activity
    • Filippakopoulos P, Muller S, Knapp S. 2009. SH2 domains: Modulators of nonreceptor tyrosine kinase activity. Curr Opin Struct Biol 19:643-649.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 643-649
    • Filippakopoulos, P.1    Muller, S.2    Knapp, S.3
  • 21
    • 42049123098 scopus 로고    scopus 로고
    • Target spectrum of the BCR-ABL inhibitors imatinib, nilotinib and dasatinib
    • Hantschel O, Rix U, Superti-Furga G. 2008. Target spectrum of the BCR-ABL inhibitors imatinib, nilotinib and dasatinib. Leuk Lymphoma 49:615-619.
    • (2008) Leuk Lymphoma , vol.49 , pp. 615-619
    • Hantschel, O.1    Rix, U.2    Superti-Furga, G.3
  • 22
    • 60149085253 scopus 로고    scopus 로고
    • Identification of N-terminal lobe motifs that determine the kinase activity of the catalytic domains and regulatory strategies of Src and Csk protein tyrosine kinases
    • Huang K, Wang YH, Brown A, Sun G. 2009. Identification of N-terminal lobe motifs that determine the kinase activity of the catalytic domains and regulatory strategies of Src and Csk protein tyrosine kinases. J Mol Biol 386:1066-1077.
    • (2009) J Mol Biol , vol.386 , pp. 1066-1077
    • Huang, K.1    Wang, Y.H.2    Brown, A.3    Sun, G.4
  • 23
    • 0000109995 scopus 로고
    • Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
    • Hunter T, Sefton BM. 1980. Transforming gene product of Rous sarcoma virus phosphorylates tyrosine. Proc Natl Acad Sci USA 77:1311-1315.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1311-1315
    • Hunter, T.1    Sefton, B.M.2
  • 24
    • 38349014380 scopus 로고    scopus 로고
    • Src family kinases: Regulation of their activities, levels and identification of new pathways
    • Ingley E. 2008. Src family kinases: Regulation of their activities, levels and identification of new pathways. Biochim Biophys Acta 1784:56-65.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 56-65
    • Ingley, E.1
  • 25
    • 0034721860 scopus 로고    scopus 로고
    • Modulation of the catalytic activity of the Src family tyrosine kinase Hck by autophosphorylation at a novel site in the unique domain
    • Johnson TM, Williamson NA, Scholz G, Jaworowski A, Wettenhall RE, Dunn AR, Cheng HC. 2000. Modulation of the catalytic activity of the Src family tyrosine kinase Hck by autophosphorylation at a novel site in the unique domain. J Biol Chem 275:33353-33364.
    • (2000) J Biol Chem , vol.275 , pp. 33353-33364
    • Johnson, T.M.1    Williamson, N.A.2    Scholz, G.3    Jaworowski, A.4    Wettenhall, R.E.5    Dunn, A.R.6    Cheng, H.C.7
  • 26
    • 67649726156 scopus 로고    scopus 로고
    • Protein kinase inhibitors: Contributions from structure to clinical compounds
    • Johnson LN. 2009. Protein kinase inhibitors: Contributions from structure to clinical compounds. Q Rev Biophys 42:1-40.
    • (2009) Q Rev Biophys , vol.42 , pp. 1-40
    • Johnson, L.N.1
  • 27
    • 0022398521 scopus 로고
    • Mutation ofNH2-terminal glycine ofp60src prevents both myristoylation and morphological transformation
    • Kamps MP, Buss JE, Sefton BM. 1985. Mutation ofNH2-terminal glycine ofp60src prevents both myristoylation and morphological transformation. Proc Natl Acad Sci USA 82:4625-4628.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4625-4628
    • Kamps, M.P.1    Buss, J.E.2    Sefton, B.M.3
  • 29
    • 0034720166 scopus 로고    scopus 로고
    • Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases
    • DOI 10.1038/35010121
    • Kawabuchi M, Satomi Y, Takao T, Shimonishi Y, Nada S, Nagai K, Tarakhovsky A, Okada M. 2000. Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases. Nature 404:999-1003. (Pubitemid 30243594)
    • (2000) Nature , vol.404 , Issue.6781 , pp. 999-1003
    • Kawabuchi, M.1    Satomi, Y.2    Takao, T.3    Shimonishi, Y.4    Nada, S.5    Nagal, K.6    Tarakhovsky, A.7    Okada, M.8
  • 30
    • 70349758510 scopus 로고    scopus 로고
    • Src kinases as therapeutic targets for cancer
    • Kim LC, Song L, Haura EB. 2009. Src kinases as therapeutic targets for cancer. Nat Rev Clin Oncol 6:587-595.
    • (2009) Nat Rev Clin Oncol , vol.6 , pp. 587-595
    • Kim, L.C.1    Song, L.2    Haura, E.B.3
  • 33
    • 33845197964 scopus 로고    scopus 로고
    • Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism
    • Kornev AP, Haste NM, Taylor SS, Eyck LF. 2006. Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism. Proc Natl Acad Sci USA 103: 17783-17788.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 17783-17788
    • Kornev, A.P.1    Haste, N.M.2    Taylor, S.S.3    Eyck, L.F.4
  • 34
    • 75349091799 scopus 로고    scopus 로고
    • Defining the conserved internal architecture of a protein kinase
    • Kornev AP, Taylor SS. 2010. Defining the conserved internal architecture of a protein kinase. Biochim Biophys Acta 1804: 440-444.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 440-444
    • Kornev, A.P.1    Taylor, S.S.2
  • 35
    • 55749102720 scopus 로고    scopus 로고
    • A helix scaffold for the assembly ofactive protein kinases
    • Kornev AP, Taylor SS, Ten Eyck LF. 2008. A helix scaffold for the assembly ofactive protein kinases. Proc Natl Acad Sci USA 105: 14377-14382.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14377-14382
    • Kornev, A.P.1    Taylor, S.S.2    Ten Eyck, L.F.3
  • 36
    • 0027965251 scopus 로고
    • Identification and characterization ofBatk, a predominantly brain-specific non-receptor protein tyrosine kinase related to Csk
    • Kuo SS, Moran P, Gripp J, Armanini M, Phillips HS, Goddard A, Caras IW. 1994. Identification and characterization ofBatk, a predominantly brain-specific non-receptor protein tyrosine kinase related to Csk. J Neurosci Res 38:705-715.
    • (1994) J Neurosci Res , vol.38 , pp. 705-715
    • Kuo, S.S.1    Moran, P.2    Gripp, J.3    Armanini, M.4    Phillips, H.S.5    Goddard, A.6    Caras, I.W.7
  • 37
    • 0033555270 scopus 로고    scopus 로고
    • Structure of the protein tyrosine kinase domain of C-terminal Src kinase (CSK) in complex with staurosporine
    • Lamers MB, Antson AA, Hubbard RE, Scott RK, Williams DH. 1999. Structure of the protein tyrosine kinase domain of C-terminal Src kinase (CSK) in complex with staurosporine. J Mol Biol 285:713-725.
    • (1999) J Mol Biol , vol.285 , pp. 713-725
    • Lamers, M.B.1    Antson, A.A.2    Hubbard, R.E.3    Scott, R.K.4    Williams, D.H.5
  • 38
    • 33646379617 scopus 로고    scopus 로고
    • Docking-based substrate recognition by the catalytic domain of a protein tyrosine kinase, C-terminal Src kinase (Csk)
    • Lee S, Ayrapetov MK, Kemble DJ, Parang K, Sun G. 2006. Docking-based substrate recognition by the catalytic domain of a protein tyrosine kinase, C-terminal Src kinase (Csk). J Biol Chem 281:8183-8189.
    • (2006) J Biol Chem , vol.281 , pp. 8183-8189
    • Lee, S.1    Ayrapetov, M.K.2    Kemble, D.J.3    Parang, K.4    Sun, G.5
  • 39
    • 0344736716 scopus 로고    scopus 로고
    • Determination of the substrate-docking site of protein tyrosine kinase C-terminal Src kinase
    • Lee S, Lin X, Nam NH, Parang K, Sun G. 2003. Determination of the substrate-docking site of protein tyrosine kinase C-terminal Src kinase. Proc Natl Acad Sci USA 100:14707-14712.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 14707-14712
    • Lee, S.1    Lin, X.2    Nam, N.H.3    Parang, K.4    Sun, G.5
  • 40
    • 46349099824 scopus 로고    scopus 로고
    • Structural basis for the recognition ofc-Src by its inactivator Csk
    • Levinson NM, Seeliger MA, Cole PA, Kuriyan J. 2008. Structural basis for the recognition ofc-Src by its inactivator Csk. Cell 134: 124-134.
    • (2008) Cell , vol.134 , pp. 124-134
    • Levinson, N.M.1    Seeliger, M.A.2    Cole, P.A.3    Kuriyan, J.4
  • 41
    • 70449435684 scopus 로고    scopus 로고
    • The tyrosine kinase Csk dimerizes through Its SH3 domain
    • Levinson NM, Visperas PR, Kuriyan J. 2009. The tyrosine kinase Csk dimerizes through Its SH3 domain. PLoS One 4:e7683.
    • (2009) PLoS One , vol.4
    • Levinson, N.M.1    Visperas, P.R.2    Kuriyan, J.3
  • 43
    • 14844301680 scopus 로고    scopus 로고
    • Phosphoryl transfer step in the C-terminal Src kinase controls Src recognition
    • Lieser SA, Shindler C, Aubol BE, Lee S, Sun G, Adams JA. 2005b. Phosphoryl transfer step in the C-terminal Src kinase controls Src recognition. J Biol Chem 280:7769-7776.
    • (2005) J Biol Chem , vol.280 , pp. 7769-7776
    • Lieser, S.A.1    Shindler, C.2    Aubol, B.E.3    Lee, S.4    Sun, G.5    Adams, J.A.6
  • 44
    • 33846015040 scopus 로고    scopus 로고
    • SRC tail phosphorylation is limited by structural changes in the regulatory tyrosine kinase Csk
    • Lieser SA, Shaffer J, Adams JA. 2006. SRC tail phosphorylation is limited by structural changes in the regulatory tyrosine kinase Csk. J Biol Chem 281:38004-38012.
    • (2006) J Biol Chem , vol.281 , pp. 38004-38012
    • Lieser, S.A.1    Shaffer, J.2    Adams, J.A.3
  • 45
    • 13444306414 scopus 로고    scopus 로고
    • Probing the communication between the regulatory and catalytic domains of a protein tyrosine kinase, Csk
    • Lin X, Ayrapetov MK, Lee S, Parang K, Sun G. 2005. Probing the communication between the regulatory and catalytic domains of a protein tyrosine kinase, Csk. Biochemistry 44:1561-1567.
    • (2005) Biochemistry , vol.44 , pp. 1561-1567
    • Lin, X.1    Ayrapetov, M.K.2    Lee, S.3    Parang, K.4    Sun, G.5
  • 46
    • 0038267169 scopus 로고    scopus 로고
    • Functions of the activation loop in Csk protein-tyrosine kinase
    • Lin X, Lee S, Sun G. 2003. Functions of the activation loop in Csk protein-tyrosine kinase. J Biol Chem 278:24072-24077.
    • (2003) J Biol Chem , vol.278 , pp. 24072-24077
    • Lin, X.1    Lee, S.2    Sun, G.3
  • 47
    • 33644832576 scopus 로고    scopus 로고
    • Structural basis for domain-domain communication in a protein tyrosine kinase, the C-terminal Src kinase
    • DOI 10.1016/j.jmb.2006.01.046, PII S0022283606000751
    • Lin X, Wang Y, Ahmadibeni Y, Parang K, Sun G. 2006. Structural basis for domain-domain communication in a protein tyrosine kinase, the C-terminal Src kinase. J Mol Biol 357:1263-1273. (Pubitemid 43357986)
    • (2006) Journal of Molecular Biology , vol.357 , Issue.4 , pp. 1263-1273
    • Lin, X.1    Wang, Y.2    Ahmadibeni, Y.3    Parang, K.4    Sun, G.5
  • 48
    • 47249122274 scopus 로고    scopus 로고
    • Signaling properties of a non-metazoan Src kinase and the evolutionary history of Src negative regulation
    • Li W, Young SL, King N, Miller WT 2008. Signaling properties of a non-metazoan Src kinase and the evolutionary history of Src negative regulation. J Biol Chem 283:15491-15501.
    • (2008) J Biol Chem , vol.283 , pp. 15491-15501
    • Li, W.1    Young, S.L.2    King, N.3    Miller, W.T.4
  • 49
    • 0035374609 scopus 로고    scopus 로고
    • The hunting of the Src
    • Martin GS. 2001. The hunting of the Src. Nat Rev Mol Cell Biol 2: 467-475.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 467-475
    • Martin, G.S.1
  • 50
    • 7944231535 scopus 로고    scopus 로고
    • The road to Src
    • Martin GS. 2004. The road to Src. Oncogene 23:7910-7917.
    • (2004) Oncogene , vol.23 , pp. 7910-7917
    • Martin, G.S.1
  • 53
    • 33846008333 scopus 로고    scopus 로고
    • A novel disulfide bond in the SH2 Domain of the C-terminal Src kinase controls catalytic activity
    • Mills JE, Whitford PC, Shaffer J, Onuchic JN, Adams JA, Jennings PA. 2007. A novel disulfide bond in the SH2 Domain of the C-terminal Src kinase controls catalytic activity. J Mol Biol 365:1460-1468.
    • (2007) J Mol Biol , vol.365 , pp. 1460-1468
    • Mills, J.E.1    Whitford, P.C.2    Shaffer, J.3    Onuchic, J.N.4    Adams, J.A.5    Jennings, P.A.6
  • 54
    • 41149180888 scopus 로고    scopus 로고
    • Csk-homologous kinase interacts with SHPS-1 and enhances neurite outgrowth ofPC12 cells
    • Mitsuhashi H, Futai E, Sasagawa N, Hayashi Y, Nishino I, Ishiura S. 2008. Csk-homologous kinase interacts with SHPS-1 and enhances neurite outgrowth ofPC12 cells. J Neurochem 105: 101-112.
    • (2008) J Neurochem , vol.105 , pp. 101-112
    • Mitsuhashi, H.1    Futai, E.2    Sasagawa, N.3    Hayashi, Y.4    Nishino, I.5    Ishiura, S.6
  • 56
    • 0025881470 scopus 로고
    • Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src
    • Nada S, Okada M, Mac Auley A, Cooper JA, Nakagawa H. 1991. Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src. Nature 351:69-72.
    • (1991) Nature , vol.351 , pp. 69-72
    • Nada, S.1    Okada, M.2    Mac Auley, A.3    Cooper, J.A.4    Nakagawa, H.5
  • 57
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases; Controlling activity through activation segment conformation
    • Nolen B, Taylor S, Ghosh G. 2004. Regulation of protein kinases; controlling activity through activation segment conformation. Mol Cell 15:661-675.
    • (2004) Mol Cell , vol.15 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 59
    • 0026355723 scopus 로고
    • CSK: A protein-tyrosine kinase involved in regulation of src family kinases
    • Okada M, Nada S, Yamanashi Y, Yamamoto T, Nakagawa H. 1991. CSK: A protein-tyrosine kinase involved in regulation of src family kinases. J Biol Chem 266:24249-24252.
    • (1991) J Biol Chem , vol.266 , pp. 24249-24252
    • Okada, M.1    Nada, S.2    Yamanashi, Y.3    Yamamoto, T.4    Nakagawa, H.5
  • 60
    • 0023722245 scopus 로고
    • Protein tyrosine kinase in rat brain: Neonatal rat brain expresses two types ofpp60c-src and a novel protein tyrosine kinase
    • Okada M, Nakagawa H. 1988a. Protein tyrosine kinase in rat brain: Neonatal rat brain expresses two types ofpp60c-src and a novel protein tyrosine kinase. J Biochem 104:297-305.
    • (1988) J Biochem , vol.104 , pp. 297-305
    • Okada, M.1    Nakagawa, H.2
  • 61
    • 0023787831 scopus 로고
    • Identification of a novel protein tyrosine kinase that phosphorylates pp60c-src and regulates its activity in neonatal rat brain
    • Okada M, Nakagawa H. 1988b. Identification of a novel protein tyrosine kinase that phosphorylates pp60c-src and regulates its activity in neonatal rat brain. Biochem Biophys Res Commun 154:796-802.
    • (1988) Biochem Biophys Res Commun , vol.154 , pp. 796-802
    • Okada, M.1    Nakagawa, H.2
  • 62
    • 0024829259 scopus 로고
    • Aprotein tyrosine kinaseinvolved in regulation of pp60c-src function
    • Okada M, Nakagawa H. 1989. Aprotein tyrosine kinaseinvolved in regulation of pp60c-src function. J Biol Chem 264: 20886-20893.
    • (1989) J Biol Chem , vol.264 , pp. 20886-20893
    • Okada, M.1    Nakagawa, H.2
  • 63
    • 7944236785 scopus 로고    scopus 로고
    • Src family kinases, key regulators of signal transduction
    • Parsons SJ, Parsons JT. 2004. Src family kinases, key regulators of signal transduction. Oncogene 23:7906-7909.
    • (2004) Oncogene , vol.23 , pp. 7906-7909
    • Parsons, S.J.1    Parsons, J.T.2
  • 64
    • 0035958959 scopus 로고    scopus 로고
    • Processive phosphorylation of p130Cas by Src depends on SH3-polyproline interactions
    • Pellicena P, Miller WT. 2001. Processive phosphorylation of p130Cas by Src depends on SH3-polyproline interactions. J Biol Chem 276:28190-28196.
    • (2001) J Biol Chem , vol.276 , pp. 28190-28196
    • Pellicena, P.1    Miller, W.T.2
  • 65
    • 47749097979 scopus 로고    scopus 로고
    • Evolution of the phospho-tyrosine signaling machinery in premetazoan lineages
    • Pincus D, Letunic I, Bork P, Lim WA. 2008. Evolution of the phospho-tyrosine signaling machinery in premetazoan lineages. Proc Natl Acad Sci USA 105:9680-9684.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 9680-9684
    • Pincus, D.1    Letunic, I.2    Bork, P.3    Lim, W.A.4
  • 66
    • 0027408247 scopus 로고
    • Identificationof a ten-amino acid proline-rich SH3 binding site
    • Ren R, Mayer BJ, Cicchetti P, Baltimore D. 1993. Identificationof a ten-amino acid proline-rich SH3 binding site. Science 259: 1157-1161.
    • (1993) Science , vol.259 , pp. 1157-1161
    • Ren, R.1    Mayer, B.J.2    Cicchetti, P.3    Baltimore, D.4
  • 67
    • 0027772325 scopus 로고
    • Interaction of tyrosine kinase oncoproteins with cellular membranes
    • Resh MD. 1993. Interaction of tyrosine kinase oncoproteins with cellular membranes. Biochim Biophys Acta 1155:307-322.
    • (1993) Biochim Biophys Acta , vol.1155 , pp. 307-322
    • Resh, M.D.1
  • 69
    • 0022977712 scopus 로고
    • 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 1986. A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps. Mol Cell Biol 6:4396-4408.
    • (1986) Mol Cell Biol , vol.6 , pp. 4396-4408
    • Sadowski, I.1    Stone, J.C.2    Pawson, T.3
  • 70
    • 0028347585 scopus 로고
    • Molecular cloning of a novel non-receptor tyrosine kinase, HYL (hematopoietic consensus tyrosine-lacking kinase)
    • Sakano S, Iwama A, Inazawa J, Ariyama T, Ohno M, Suda T 1994. Molecular cloning of a novel non-receptor tyrosine kinase, HYL (hematopoietic consensus tyrosine-lacking kinase). Oncogene 9: 1155-1161. (Pubitemid 24095024)
    • (1994) Oncogene , vol.9 , Issue.4 , pp. 1155-1161
    • Sakano, S.1    Iwama, A.2    Inazawa, J.3    Ariyama, T.4    Ohno, M.5    Suda, T.6
  • 71
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction ofspatial restraints
    • Sali A, Blundell TL. 1993. Comparative protein modelling by satisfaction ofspatial restraints. J Mol Biol 234:779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 72
    • 44849086809 scopus 로고    scopus 로고
    • Predikin and Predikin DB: A computational framework for the prediction of protein kinase peptide specificity and an associated database of phosphorylation sites
    • Saunders NF, Brinkworth RI, Huber T, Kemp BE, Kobe B. 2008. Predikin and Predikin DB: A computational framework for the prediction of protein kinase peptide specificity and an associated database of phosphorylation sites. BMC Bioinformatics 9:245.
    • (2008) BMC Bioinformatics , vol.9 , pp. 245
    • Saunders, N.F.1    Brinkworth, R.I.2    Huber, T.3    Kemp, B.E.4    Kobe, B.5
  • 73
    • 48449084853 scopus 로고    scopus 로고
    • The Predikin webserver: Improved prediction of protein kinase peptide specificity using structural information
    • Saunders NF, Kobe B. 2008. The Predikin webserver: Improved prediction of protein kinase peptide specificity using structural information. Nucleic Acids Res 36; W286-W290.
    • (2008) Nucleic Acids Res , vol.36
    • Saunders, N.F.1    Kobe, B.2
  • 75
    • 33747071203 scopus 로고    scopus 로고
    • Functional development of Src tyrosine kinases during evolution from a unicellular ancestor to multicellular animals
    • Segawa Y, Suga H, Iwabe N, Oneyama C, Akagi T, Miyata T, Okada M. 2006. Functional development of Src tyrosine kinases during evolution from a unicellular ancestor to multicellular animals. Proc Natl Acad Sci USA 103:12021-12026.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 12021-12026
    • Segawa, Y.1    Suga, H.2    Iwabe, N.3    Oneyama, C.4    Akagi, T.5    Miyata, T.6    Okada, M.7
  • 76
    • 0035900556 scopus 로고    scopus 로고
    • Novel mechanism of regulation of the non-receptor protein tyrosine kinase Csk: Insights from NMR mapping studies and site-directed mutagenesis
    • Shekhtman A, Ghose R, Wang D, Cole PA, Cowburn D. 2001. Novel mechanism of regulation of the non-receptor protein tyrosine kinase Csk: Insights from NMR mapping studies and site-directed mutagenesis. J Mol Biol 314:129-138.
    • (2001) J Mol Biol , vol.314 , pp. 129-138
    • Shekhtman, A.1    Ghose, R.2    Wang, D.3    Cole, P.A.4    Cowburn, D.5
  • 78
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri F, Moarefi I, Kuriyan J. 1997. Crystal structure of the Src family tyrosine kinase Hck. Nature 385:602-609.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 79
    • 0033600568 scopus 로고    scopus 로고
    • Domain interactions in protein tyrosine kinase Csk
    • Sondhi D, Cole PA. 1999. Domain interactions in protein tyrosine kinase Csk. Biochemistry 38:11147-11155.
    • (1999) Biochemistry , vol.38 , pp. 11147-11155
    • Sondhi, D.1    Cole, P.A.2
  • 80
    • 0032488592 scopus 로고    scopus 로고
    • Peptide and protein phosphorylation by protein tyrosine kinase Csk: Insights into specificity and mechanism
    • Sondhi D, Xu W, Songyang Z, Eck MJ, Cole PA. 1998. Peptide and protein phosphorylation by protein tyrosine kinase Csk: Insights into specificity and mechanism. Biochemistry 37:165-172.
    • (1998) Biochemistry , vol.37 , pp. 165-172
    • Sondhi, D.1    Xu, W.2    Songyang, Z.3    Eck, M.J.4    Cole, P.A.5
  • 82
    • 0029615453 scopus 로고
    • Autophosphorylation induces autoactivation and a decrease in the Src homology 2 domain accessibility of the Lyn protein kinase
    • Sotirellis N, Johnson TM, Hibbs ML, Stanley IJ, Stanley E, Dunn AR, Cheng HC. 1995. Autophosphorylation induces autoactivation and a decrease in the Src homology 2 domain accessibility of the Lyn protein kinase. J Biol Chem 270: 29773-29780.
    • (1995) J Biol Chem , vol.270 , pp. 29773-29780
    • Sotirellis, N.1    Johnson, T.M.2    Hibbs, M.L.3    Stanley, I.J.4    Stanley, E.5    Dunn, A.R.6    Cheng, H.C.7
  • 83
    • 0034703099 scopus 로고    scopus 로고
    • Transmembrane phosphoprotein Cbp positively regulates the activity of the carboxyl-terminal Src kinase, Csk
    • Takeuchi S, Takayama Y, Ogawa A, Tamura K, Okada M. 2000. Transmembrane phosphoprotein Cbp positively regulates the activity of the carboxyl-terminal Src kinase, Csk. J Biol Chem 275:29183-29186.
    • (2000) J Biol Chem , vol.275 , pp. 29183-29186
    • Takeuchi, S.1    Takayama, Y.2    Ogawa, A.3    Tamura, K.4    Okada, M.5
  • 84
    • 67650713930 scopus 로고    scopus 로고
    • The chemical biology of protein phosphorylation
    • Tarrant MK, Cole PA. 2009. The chemical biology of protein phosphorylation. Annu Rev Biochem 78:797-825.
    • (2009) Annu Rev Biochem , vol.78 , pp. 797-825
    • Tarrant, M.K.1    Cole, P.A.2
  • 86
    • 34250638276 scopus 로고    scopus 로고
    • Determining protein kinase substrate specificity by parallel solution-phase assay of large numbers ofpeptide substrates
    • Turk BE, Hutti JE, Cantley LC. 2006. Determining protein kinase substrate specificity by parallel solution-phase assay of large numbers ofpeptide substrates. Nat Protoc 1:375-379.
    • (2006) Nat Protoc , vol.1 , pp. 375-379
    • Turk, B.E.1    Hutti, J.E.2    Cantley, L.C.3
  • 87
    • 0035916292 scopus 로고    scopus 로고
    • Molecular determinants for Csk-catalyzed tyrosine phosphorylation of the Src tail
    • DOI 10.1021/bi002342n
    • Wang D, Huang XY, Cole PA. 2001. Molecular determinants for Csk-catalyzed tyrosine phosphorylation of the Src tail. Biochemistry 40:2004-2010. (Pubitemid 32165669)
    • (2001) Biochemistry , vol.40 , Issue.7 , pp. 2004-2010
    • Wang, D.1    Huang, X.-Y.2    Cole, P.A.3
  • 88
    • 0029761755 scopus 로고    scopus 로고
    • The purification and characterization of the catalytic domain of Src expressed in Schizosaccharomyces pombe. Comparison of unphosphorylated and tyrosine phos-phorylated species
    • Weijland A, Neubauer G, Courtneidge SA, Mann M, Wierenga RK, Superti-Furga G. 1996. The purification and characterization of the catalytic domain of Src expressed in Schizosaccharomyces pombe. Comparison of unphosphorylated and tyrosine phos-phorylated species. Eur J Biochem 240:756-764.
    • (1996) Eur J Biochem , vol.240 , pp. 756-764
    • Weijland, A.1    Neubauer, G.2    Courtneidge, S.A.3    Mann, M.4    Wierenga, R.K.5    Superti-Furga, G.6
  • 89
    • 0034623991 scopus 로고    scopus 로고
    • Chemical rescue of a mutantprotein-tyrosine kinase
    • Williams DM, Wang D, Cole PA. 2000. Chemical rescue of a mutantprotein-tyrosine kinase. J Biol Chem 275:38127-38130.
    • (2000) J Biol Chem , vol.275 , pp. 38127-38130
    • Williams, D.M.1    Wang, D.2    Cole, P.A.3
  • 92
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu W, Harrison SC, Eck MJ. 1997. Three-dimensional structure of the tyrosine kinase c-Src. Nature 385:595-602.
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 94
    • 2942618768 scopus 로고    scopus 로고
    • A renaissance for SRC
    • Yeatman TJ. 2004. A renaissance for SRC. Nat Rev Cancer 4: 470-480.
    • (2004) Nat Rev Cancer , vol.4 , pp. 470-480
    • Yeatman, T.J.1
  • 95
    • 32144437781 scopus 로고    scopus 로고
    • Csk homologous kinase (CHK), unlike Csk, enhances MAPK activation via Ras-mediated signaling in a Src-independentmanner
    • Zagozdzon R, Kaminski R, Fu Y, Fu W, Bougeret C, Avraham HK. 2006. Csk homologous kinase (CHK), unlike Csk, enhances MAPK activation via Ras-mediated signaling in a Src-independentmanner. Cell Signal 18:871-881.
    • (2006) Cell Signal , vol.18 , pp. 871-881
    • Zagozdzon, R.1    Kaminski, R.2    Fu, Y.3    Fu, W.4    Bougeret, C.5    Avraham, H.K.6
  • 96
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • Zhang J, Yang PL, Gray NS. 2009. Targeting cancer with small molecule kinase inhibitors. Nat Rev Cancer 9:28-39.
    • (2009) Nat Rev Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 97
    • 33745242921 scopus 로고    scopus 로고
    • COOH-terminal Src kinase-mediated c-Jun phosphorylation promotes c-Jun degra-dation and inhibits cell transformation
    • Zhu F, Choi BY, Ma WY, Zhao Z, Zhang Y, Cho YY, Choi HS, Imamoto A, Bode AM, Dong Z. 2006. COOH-terminal Src kinase-mediated c-Jun phosphorylation promotes c-Jun degra-dation and inhibits cell transformation. Cancer Res 66: 5729-5736.
    • (2006) Cancer Res , vol.66 , pp. 5729-5736
    • Zhu, F.1    Choi, B.Y.2    Ma, W.Y.3    Zhao, Z.4    Zhang, Y.5    Cho, Y.Y.6    Choi, H.S.7    Imamoto, A.8    Bode, A.M.9    Dong, Z.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.