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Volumn 81, Issue , 2013, Pages 56-69

Systematic characterization of the specificity of the SH2 domains of cytoplasmic tyrosine kinases

Author keywords

Cytoplasmic tyrosine kinase (CTK); OBOC; Peptide binding; Protein kinase; Src homology 2 (SH2) domain; Support vector machine (SVM)

Indexed keywords

PHOSPHOTYROSINE; PROTEIN TYROSINE KINASE;

EID: 84877817038     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.12.021     Document Type: Article
Times cited : (8)

References (65)
  • 1
    • 0025681492 scopus 로고
    • Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors
    • Anderson D., Koch C.A., Grey L., Ellis C., Moran M.F., Pawson T. Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors. Science 1990, 250:979-982.
    • (1990) Science , vol.250 , pp. 979-982
    • Anderson, D.1    Koch, C.A.2    Grey, L.3    Ellis, C.4    Moran, M.F.5    Pawson, T.6
  • 4
    • 0034693799 scopus 로고    scopus 로고
    • The protein tyrosine kinase family of the human genome
    • Robinson D.R., Wu Y.M., Lin S.F. The protein tyrosine kinase family of the human genome. Oncogene 2000, 19:5548-5557.
    • (2000) Oncogene , vol.19 , pp. 5548-5557
    • Robinson, D.R.1    Wu, Y.M.2    Lin, S.F.3
  • 5
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon M.A., Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell 2010, 141:1117-1134.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 6
    • 1542673243 scopus 로고    scopus 로고
    • Non-receptor protein tyrosine kinases
    • Tsygankov A.Y. Non-receptor protein tyrosine kinases. Front Biosci 2003, 8:s595-s635.
    • (2003) Front Biosci , vol.8
    • Tsygankov, A.Y.1
  • 7
    • 84859357364 scopus 로고    scopus 로고
    • Activation of receptor protein-tyrosine kinases from the cytoplasmic compartment
    • Yamanashi Y., Tezuka T., Yokoyama K. Activation of receptor protein-tyrosine kinases from the cytoplasmic compartment. J Biochem 2012, 151:353-359.
    • (2012) J Biochem , vol.151 , pp. 353-359
    • Yamanashi, Y.1    Tezuka, T.2    Yokoyama, K.3
  • 8
    • 0035575586 scopus 로고    scopus 로고
    • SH2 domains, interaction modules and cellular wiring
    • Pawson T., Gish G.D., Nash P. SH2 domains, interaction modules and cellular wiring. Trends Cell Biol 2001, 11:504-511.
    • (2001) Trends Cell Biol , vol.11 , pp. 504-511
    • Pawson, T.1    Gish, G.D.2    Nash, P.3
  • 9
    • 33745185987 scopus 로고    scopus 로고
    • The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling
    • Liu B.A., Jablonowski K., Raina M., Arce M., Pawson T., Nash P.D. The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling. Mol Cell 2006, 22:851-868.
    • (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
  • 10
    • 2142758178 scopus 로고    scopus 로고
    • Structure and specificity of the SH2 domain
    • [3 p following S8]
    • Waksman G., Kuriyan J. Structure and specificity of the SH2 domain. Cell 2004, 116:S45-S48. [3 p following S8].
    • (2004) Cell , vol.116
    • Waksman, G.1    Kuriyan, J.2
  • 11
    • 70649096122 scopus 로고    scopus 로고
    • SH2 domains: modulators of nonreceptor tyrosine kinase activity
    • Filippakopoulos P., Muller S., Knapp S. SH2 domains: modulators of nonreceptor tyrosine kinase activity. Curr Opin Struct Biol 2009, 19:643-649.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 643-649
    • Filippakopoulos, P.1    Muller, S.2    Knapp, S.3
  • 12
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson T. Protein modules and signalling networks. Nature 1995, 373:573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 13
    • 0035815288 scopus 로고    scopus 로고
    • Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation
    • Young M.A., Gonfloni S., Superti-Furga G., Roux B., Kuriyan J. Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation. Cell 2001, 105:115-126.
    • (2001) Cell , vol.105 , pp. 115-126
    • Young, M.A.1    Gonfloni, S.2    Superti-Furga, G.3    Roux, B.4    Kuriyan, J.5
  • 14
    • 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 1997, 385:602-609.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 15
    • 0031452274 scopus 로고    scopus 로고
    • Structures of Src-family tyrosine kinases
    • Sicheri F., Kuriyan J. Structures of Src-family tyrosine kinases. Curr Opin Struct Biol 1997, 7:777-785.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 777-785
    • Sicheri, F.1    Kuriyan, J.2
  • 16
    • 0031017838 scopus 로고    scopus 로고
    • Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement
    • Moarefi I., LaFevreBernt M., Sicheri F., Huse M., Lee C.H., Kuriyan J., et al. Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement. Nature 1997, 385:650-653.
    • (1997) Nature , vol.385 , pp. 650-653
    • Moarefi, I.1    LaFevreBernt, M.2    Sicheri, F.3    Huse, M.4    Lee, C.H.5    Kuriyan, J.6
  • 17
    • 46349099824 scopus 로고    scopus 로고
    • Structural basis for the recognition of c-Src by its inactivator Csk
    • Levinson N.M., Seeliger M.A., Cole P.A., Kuriyan J. Structural basis for the recognition of c-Src by its inactivator Csk. Cell 2008, 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
  • 18
    • 13544256790 scopus 로고    scopus 로고
    • Src protein-tyrosine kinase structure and regulation
    • Roskoski R. Src protein-tyrosine kinase structure and regulation. Biochem Biophys Res Commun 2004, 324:1155-1164.
    • (2004) Biochem Biophys Res Commun , vol.324 , pp. 1155-1164
    • Roskoski, R.1
  • 19
    • 42649123723 scopus 로고    scopus 로고
    • Defining the specificity space of the human SRC homology 2 domain
    • Huang H., Li L., Wu C., Schibli D., Colwill K., Ma S., et al. Defining the specificity space of the human SRC homology 2 domain. Mol Cell Proteomics 2008, 7:768-784.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 768-784
    • Huang, H.1    Li, L.2    Wu, C.3    Schibli, D.4    Colwill, K.5    Ma, S.6
  • 20
    • 0032560583 scopus 로고    scopus 로고
    • Statistical analysis of protein kinase specificity determinants
    • Kreegipuu A., Blom N., Brunak S., Jarv J. Statistical analysis of protein kinase specificity determinants. FEBS Lett 1998, 430:45-50.
    • (1998) FEBS Lett , vol.430 , pp. 45-50
    • Kreegipuu, A.1    Blom, N.2    Brunak, S.3    Jarv, J.4
  • 21
    • 75549086174 scopus 로고    scopus 로고
    • Eukaryotic protein domains as functional units of cellular evolution
    • Jin J., Xie X.Y., Chen C., Park J.G., Stark C., James D.A., et al. Eukaryotic protein domains as functional units of cellular evolution. Sci Signal 2009, 2.
    • (2009) Sci Signal , vol.2
    • Jin, J.1    Xie, X.Y.2    Chen, C.3    Park, J.G.4    Stark, C.5    James, D.A.6
  • 22
    • 0028875162 scopus 로고
    • Recognition and specificity in protein tyrosine kinase-mediated signalling
    • Songyang Z., Cantley L.C. Recognition and specificity in protein tyrosine kinase-mediated signalling. Trends Biochem Sci 1995, 20:470-475.
    • (1995) Trends Biochem Sci , vol.20 , pp. 470-475
    • Songyang, Z.1    Cantley, L.C.2
  • 23
    • 50249132542 scopus 로고    scopus 로고
    • Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation
    • Filippakopoulos P., Kofler M., Hantschel O., Gish G.D., Grebien F., Salah E., et al. Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation. Cell 2008, 134:793-803.
    • (2008) Cell , vol.134 , pp. 793-803
    • Filippakopoulos, P.1    Kofler, M.2    Hantschel, O.3    Gish, G.D.4    Grebien, F.5    Salah, E.6
  • 24
    • 33644871166 scopus 로고    scopus 로고
    • Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase
    • Nagar B., Hantschel O., Seeliger M., Davies J.M., Weis W.I., Superti-Furga G., et al. Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase. Mol Cell 2006, 21:787-798.
    • (2006) Mol Cell , vol.21 , pp. 787-798
    • Nagar, B.1    Hantschel, O.2    Seeliger, M.3    Davies, J.M.4    Weis, W.I.5    Superti-Furga, G.6
  • 25
    • 15444372337 scopus 로고    scopus 로고
    • Protein kinase specificity. A strategic collaboration between kinase peptide specificity and substrate recruitment
    • Zhu G., Liu Y., Shaw S. Protein kinase specificity. A strategic collaboration between kinase peptide specificity and substrate recruitment. Cell Cycle 2005, 4:52-56.
    • (2005) Cell Cycle , vol.4 , pp. 52-56
    • Zhu, G.1    Liu, Y.2    Shaw, S.3
  • 27
    • 64949123341 scopus 로고    scopus 로고
    • High-throughput sequencing of peptoids and peptide-peptoid hybrids by partial edman degradation and mass spectrometry
    • Thakkar A., Cohen A.S., Connolly M.D., Zuckermann R.N., Pei D. High-throughput sequencing of peptoids and peptide-peptoid hybrids by partial edman degradation and mass spectrometry. J Comb Chem 2009, 11:294-302.
    • (2009) J Comb Chem , vol.11 , pp. 294-302
    • Thakkar, A.1    Cohen, A.S.2    Connolly, M.D.3    Zuckermann, R.N.4    Pei, D.5
  • 28
    • 80052745646 scopus 로고    scopus 로고
    • High-throughput screening of one-bead-one-compound libraries: identification of cyclic peptidyl inhibitors against calcineurin/NFAT interaction
    • Liu T., Qian Z., Xiao Q., Pei D. High-throughput screening of one-bead-one-compound libraries: identification of cyclic peptidyl inhibitors against calcineurin/NFAT interaction. ACS Comb Sci 2011, 13:537-546.
    • (2011) ACS Comb Sci , vol.13 , pp. 537-546
    • Liu, T.1    Qian, Z.2    Xiao, Q.3    Pei, D.4
  • 29
    • 34249071629 scopus 로고    scopus 로고
    • Defining SH2 domain and PTP specificity by screening combinatorial peptide libraries
    • Wavreille A.S., Garaud M., Zhang Y., Pei D. Defining SH2 domain and PTP specificity by screening combinatorial peptide libraries. Methods 2007, 42:207-219.
    • (2007) Methods , vol.42 , pp. 207-219
    • Wavreille, A.S.1    Garaud, M.2    Zhang, Y.3    Pei, D.4
  • 30
    • 33747621649 scopus 로고    scopus 로고
    • Traceless capping agent for peptide sequencing by partial edman degradation and mass spectrometry
    • Thakkar A., Wavreille A.S., Pei D. Traceless capping agent for peptide sequencing by partial edman degradation and mass spectrometry. Anal Chem 2006, 78:5935-5939.
    • (2006) Anal Chem , vol.78 , pp. 5935-5939
    • Thakkar, A.1    Wavreille, A.S.2    Pei, D.3
  • 31
    • 79952957889 scopus 로고    scopus 로고
    • Substrate specificity of protein tyrosine phosphatases 1B, RPTPalpha, SHP-1, and SHP-2
    • Ren L., Chen X., Luechapanichkul R., Selner N.G., Meyer T.M., Wavreille A.S., et al. Substrate specificity of protein tyrosine phosphatases 1B, RPTPalpha, SHP-1, and SHP-2. Biochemistry 2011, 50:2339-2356.
    • (2011) Biochemistry , vol.50 , pp. 2339-2356
    • Ren, L.1    Chen, X.2    Luechapanichkul, R.3    Selner, N.G.4    Meyer, T.M.5    Wavreille, A.S.6
  • 33
    • 34249753618 scopus 로고
    • Support-vector networks
    • Cortes C., Vapnik V. Support-vector networks. Mach Learn 1995, 20:273-297.
    • (1995) Mach Learn , vol.20 , pp. 273-297
    • Cortes, C.1    Vapnik, V.2
  • 34
    • 0142148183 scopus 로고    scopus 로고
    • Application of support vector machines for T-cell epitopes prediction
    • Zhao Y., Pinilla C., Valmori D., Martin R., Simon R. Application of support vector machines for T-cell epitopes prediction. Bioinformatics 2003, 19:1978-1984.
    • (2003) Bioinformatics , vol.19 , pp. 1978-1984
    • Zhao, Y.1    Pinilla, C.2    Valmori, D.3    Martin, R.4    Simon, R.5
  • 35
    • 0141523251 scopus 로고    scopus 로고
    • Beta edge strands in protein structure prediction and aggregation
    • Siepen J.A., Radford S.E., Westhead D.R. Beta edge strands in protein structure prediction and aggregation. Protein Sci 2003, 12:2348-2359.
    • (2003) Protein Sci , vol.12 , pp. 2348-2359
    • Siepen, J.A.1    Radford, S.E.2    Westhead, D.R.3
  • 36
    • 0142179209 scopus 로고    scopus 로고
    • Prediction of regulatory networks: genome-wide identification of transcription factor targets from gene expression data
    • Qian J., Lin J., Luscombe N.M., Yu H., Gerstein M. Prediction of regulatory networks: genome-wide identification of transcription factor targets from gene expression data. Bioinformatics 2003, 19:1917-1926.
    • (2003) Bioinformatics , vol.19 , pp. 1917-1926
    • Qian, J.1    Lin, J.2    Luscombe, N.M.3    Yu, H.4    Gerstein, M.5
  • 38
    • 78650290837 scopus 로고    scopus 로고
    • SVM classifier to predict genes important for self-renewal and pluripotency of mouse embryonic stem cells
    • Xu H., Lemischka I.R., Ma'ayan A. SVM classifier to predict genes important for self-renewal and pluripotency of mouse embryonic stem cells. BMC Syst Biol 2010, 4:173.
    • (2010) BMC Syst Biol , vol.4 , pp. 173
    • Xu, H.1    Lemischka, I.R.2    Ma'ayan, A.3
  • 39
    • 2942598149 scopus 로고    scopus 로고
    • PhosphoSite: a bioinformatics resource dedicated to physiological protein phosphorylation
    • Hornbeck P.V., Chabra I., Kornhauser J.M., Skrzypek E., Zhang B. PhosphoSite: a bioinformatics resource dedicated to physiological protein phosphorylation. Proteomics 2004, 4:1551-1561.
    • (2004) Proteomics , vol.4 , pp. 1551-1561
    • Hornbeck, P.V.1    Chabra, I.2    Kornhauser, J.M.3    Skrzypek, E.4    Zhang, B.5
  • 40
    • 84857047339 scopus 로고    scopus 로고
    • PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
    • Hornbeck P.V., Kornhauser J.M., Tkachev S., Zhang B., Skrzypek E., Murray B., et al. PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res 2012, 40:D261-D270.
    • (2012) Nucleic Acids Res , vol.40
    • Hornbeck, P.V.1    Kornhauser, J.M.2    Tkachev, S.3    Zhang, B.4    Skrzypek, E.5    Murray, B.6
  • 41
    • 78651320816 scopus 로고    scopus 로고
    • Phospho.ELM: a database of phosphorylation sites - update 2011
    • Dinkel H., Chica C., Via A., Gould C.M., Jensen L.J., Gibson T.J., et al. Phospho.ELM: a database of phosphorylation sites - update 2011. Nucleic Acids Res Jan. 2011, 39(Database issue):D261-D267.
    • (2011) Nucleic Acids Res , vol.39 , Issue.DATABASE ISSUE
    • Dinkel, H.1    Chica, C.2    Via, A.3    Gould, C.M.4    Jensen, L.J.5    Gibson, T.J.6
  • 42
    • 0026419328 scopus 로고
    • A new type of synthetic peptide library for identifying ligand-binding activity
    • Lam K.S., Salmon S.E., Hersh E.M., Hruby V.J., Kazmierski W.M., Knapp R.J. A new type of synthetic peptide library for identifying ligand-binding activity. Nature 1991, 354:82-84.
    • (1991) Nature , vol.354 , pp. 82-84
    • Lam, K.S.1    Salmon, S.E.2    Hersh, E.M.3    Hruby, V.J.4    Kazmierski, W.M.5    Knapp, R.J.6
  • 43
    • 0026419319 scopus 로고
    • Generation and use of synthetic peptide combinatorial libraries for basic research and drug discovery
    • Houghten R.A., Pinilla C., Blondelle S.E., Appel J.R., Dooley C.T., Cuervo J.H. Generation and use of synthetic peptide combinatorial libraries for basic research and drug discovery. Nature 1991, 354:84-86.
    • (1991) Nature , vol.354 , pp. 84-86
    • Houghten, R.A.1    Pinilla, C.2    Blondelle, S.E.3    Appel, J.R.4    Dooley, C.T.5    Cuervo, J.H.6
  • 44
    • 79955702502 scopus 로고    scopus 로고
    • LIBSVM: a library for support vector machines
    • [27]
    • Chang C.C., Lin C.J. LIBSVM: a library for support vector machines. ACM Trans Intell Syst Technol 2011, 2(27):1-27. [27].
    • (2011) ACM Trans Intell Syst Technol , vol.2 , Issue.27 , pp. 1-27
    • Chang, C.C.1    Lin, C.J.2
  • 45
    • 70349909349 scopus 로고    scopus 로고
    • Enhancing the performance of LibSVM classifier by kernel F-score feature selection
    • Sarojini B., Ramaraj N., Nickolas S. Enhancing the performance of LibSVM classifier by kernel F-score feature selection. Commun Comput Inf Sci 2009, 40:533-543.
    • (2009) Commun Comput Inf Sci , vol.40 , pp. 533-543
    • Sarojini, B.1    Ramaraj, N.2    Nickolas, S.3
  • 46
    • 13844275301 scopus 로고    scopus 로고
    • Similarity of position frequency matrices for transcription factor binding sites
    • Schones D.E., Sumazin P., Zhang M.Q. Similarity of position frequency matrices for transcription factor binding sites. Bioinformatics 2005, 21:307-313.
    • (2005) Bioinformatics , vol.21 , pp. 307-313
    • Schones, D.E.1    Sumazin, P.2    Zhang, M.Q.3
  • 47
    • 27644499659 scopus 로고    scopus 로고
    • Measuring similarities between transcription factor binding sites
    • Kielbasa S.M., Gonze D., Herzel H. Measuring similarities between transcription factor binding sites. BMC Bioinformatics 2005, 6:237.
    • (2005) BMC Bioinformatics , vol.6 , pp. 237
    • Kielbasa, S.M.1    Gonze, D.2    Herzel, H.3
  • 49
    • 79960976768 scopus 로고    scopus 로고
    • UniProt Knowledgebase: a hub of integrated protein data
    • bar009
    • Magrane M., Consortium U. UniProt Knowledgebase: a hub of integrated protein data. Database (Oxford) 2011, 2011:bar009.
    • (2011) Database (Oxford) , vol.2011
    • Magrane, M.1    Consortium, U.2
  • 51
    • 0038679485 scopus 로고    scopus 로고
    • Applications of one-bead one-compound combinatorial libraries and chemical microarrays in signal transduction research
    • Lam K.S., Liu R.W., Miyamoto S., Lehman A.L., Tuscano J.M. Applications of one-bead one-compound combinatorial libraries and chemical microarrays in signal transduction research. Acc Chem Res 2003, 36:370-377.
    • (2003) Acc Chem Res , vol.36 , pp. 370-377
    • Lam, K.S.1    Liu, R.W.2    Miyamoto, S.3    Lehman, A.L.4    Tuscano, J.M.5
  • 52
    • 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 1990, 18:6097-6100.
    • (1990) Nucleic Acids Res , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 53
    • 0028351583 scopus 로고
    • Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav
    • Songyang Z., Shoelson S.E., McGlade J., Olivier P., Pawson T., Bustelo X.R., et al. Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav. Mol Cell Biol 1994, 14:2777-2785.
    • (1994) Mol Cell Biol , vol.14 , pp. 2777-2785
    • Songyang, Z.1    Shoelson, S.E.2    McGlade, J.3    Olivier, P.4    Pawson, T.5    Bustelo, X.R.6
  • 54
    • 80053913061 scopus 로고    scopus 로고
    • DomPep - a general method for predicting modular domain-mediated protein-protein interactions
    • Li L., Zhao B., Du J., Zhang K., Ling C.X., Li S.S. DomPep - a general method for predicting modular domain-mediated protein-protein interactions. PLoS One 2011, 6:e25528.
    • (2011) PLoS One , vol.6
    • Li, L.1    Zhao, B.2    Du, J.3    Zhang, K.4    Ling, C.X.5    Li, S.S.6
  • 55
    • 0027368929 scopus 로고
    • SH2 domains of the protein-tyrosine kinases Blk, Lyn, and Fyn(T) bind distinct sets of phosphoproteins from B lymphocytes
    • Malek S.N., Desiderio S. SH2 domains of the protein-tyrosine kinases Blk, Lyn, and Fyn(T) bind distinct sets of phosphoproteins from B lymphocytes. J Biol Chem 1993, 268:22557-22565.
    • (1993) J Biol Chem , vol.268 , pp. 22557-22565
    • Malek, S.N.1    Desiderio, S.2
  • 56
    • 0034874786 scopus 로고    scopus 로고
    • Structure and function of Syk protein-tyrosine kinase
    • Sada K., Takano T., Yanagi S., Yamamura H. Structure and function of Syk protein-tyrosine kinase. J Biochem 2001, 130:177-186.
    • (2001) J Biochem , vol.130 , pp. 177-186
    • Sada, K.1    Takano, T.2    Yanagi, S.3    Yamamura, H.4
  • 57
    • 0033786922 scopus 로고    scopus 로고
    • Protein tyrosine kinase structure and function
    • Hubbard S.R., Till J.H. Protein tyrosine kinase structure and function. Annu Rev Biochem 2000, 69:373-398.
    • (2000) Annu Rev Biochem , vol.69 , pp. 373-398
    • Hubbard, S.R.1    Till, J.H.2
  • 58
    • 84877796331 scopus 로고    scopus 로고
    • Structure and function of protein kinases and protein phosphatases
    • Musgrave I.F. Structure and function of protein kinases and protein phosphatases. IDrugs 1998, 1:617-619.
    • (1998) IDrugs , vol.1 , pp. 617-619
    • Musgrave, I.F.1
  • 59
    • 33746359639 scopus 로고    scopus 로고
    • The death-associated protein kinases: structure, function, and beyond
    • Bialik S., Kimchi A. The death-associated protein kinases: structure, function, and beyond. Annu Rev Biochem 2006, 75:189-210.
    • (2006) Annu Rev Biochem , vol.75 , pp. 189-210
    • Bialik, S.1    Kimchi, A.2
  • 60
    • 77956691818 scopus 로고    scopus 로고
    • Crystal structure of the ALK (anaplastic lymphoma kinase) catalytic domain
    • Lee C.C., Jia Y., Li N., Sun X., Ng K., Ambing E., et al. Crystal structure of the ALK (anaplastic lymphoma kinase) catalytic domain. Biochem J 2010, 430:425-437.
    • (2010) Biochem J , vol.430 , pp. 425-437
    • Lee, C.C.1    Jia, Y.2    Li, N.3    Sun, X.4    Ng, K.5    Ambing, E.6
  • 62
    • 0037422596 scopus 로고    scopus 로고
    • Structural basis and prediction of substrate specificity in protein serine/threonine kinases
    • Brinkworth R.I., Breinl R.A., Kobe B. Structural basis and prediction of substrate specificity in protein serine/threonine kinases. Proc Natl Acad Sci U S A 2003, 100:74-79.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 74-79
    • Brinkworth, R.I.1    Breinl, R.A.2    Kobe, B.3
  • 63
    • 67650281206 scopus 로고    scopus 로고
    • A machine learning based method for the prediction of G protein-coupled receptor-binding PDZ domain proteins
    • Eo H.S., Kim S., Koo H., Kim W. A machine learning based method for the prediction of G protein-coupled receptor-binding PDZ domain proteins. Mol Cells 2009, 27:629-634.
    • (2009) Mol Cells , vol.27 , pp. 629-634
    • Eo, H.S.1    Kim, S.2    Koo, H.3    Kim, W.4
  • 64
    • 77957737014 scopus 로고    scopus 로고
    • Proteome scanning to predict PDZ domain interactions using support vector machines
    • Hui S., Bader G.D. Proteome scanning to predict PDZ domain interactions using support vector machines. BMC Bioinformatics 2010, 11:507.
    • (2010) BMC Bioinformatics , vol.11 , pp. 507
    • Hui, S.1    Bader, G.D.2
  • 65
    • 39149136524 scopus 로고    scopus 로고
    • The Bead blot: a method for selecting small molecule ligands for protein capture and purification
    • Lathrop J.T., Hammond D. The Bead blot: a method for selecting small molecule ligands for protein capture and purification. Nat Protoc 2007, 2:3102-3110.
    • (2007) Nat Protoc , vol.2 , pp. 3102-3110
    • Lathrop, J.T.1    Hammond, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.