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Volumn 407, Issue 6802, 2000, Pages 395-401

A chemical switch for inhibitor-sensitive alleles of any protein kinase

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN KINASE INHIBITOR;

EID: 0034699382     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35030148     Document Type: Article
Times cited : (913)

References (30)
  • 1
    • 0032563315 scopus 로고    scopus 로고
    • Exploiting chemical libraries, structure, and genomics in the search for kinase inhibitions
    • Gray, N. S. et al. Exploiting chemical libraries, structure, and genomics in the search for kinase inhibitions. Science 281, 533-538 (1998).
    • (1998) Science , vol.281 , pp. 533-538
    • Gray, N.S.1
  • 2
    • 0033518610 scopus 로고    scopus 로고
    • Generation of monospecific nanomolar tyrosine kinase inhibitors via a chemical genetic approach
    • Bishop, A. C. et al. Generation of monospecific nanomolar tyrosine kinase inhibitors via a chemical genetic approach. J. Am. Chem. Soc. 121, 627-631 (1999).
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 627-631
    • Bishop, A.C.1
  • 3
    • 0019162297 scopus 로고
    • The selection of S. cerevisiae mutants defective in the start event of cell division
    • Reed, S. I. The selection of S. cerevisiae mutants defective in the start event of cell division. Genetics 95, 561-577 (1980).
    • (1980) Genetics , vol.95 , pp. 561-577
    • Reed, S.I.1
  • 4
    • 0032008085 scopus 로고    scopus 로고
    • Engineering Src family protein kinases with unnatural nucleotide specificity
    • Liu, Y., Shah, K., Yang, F., Witucki, L. & Shokat, K. M. Engineering Src family protein kinases with unnatural nucleotide specificity. Chem. Biol. 5, 91-101 (1998).
    • (1998) Chem. Biol. , vol.5 , pp. 91-101
    • Liu, Y.1    Shah, K.2    Yang, F.3    Witucki, L.4    Shokat, K.M.5
  • 5
    • 0030029143 scopus 로고    scopus 로고
    • Discovery of a novel, potent, and Src family-selective tyrosine kinase inhibitor
    • Hanke, J. H. et al. Discovery of a novel, potent, and Src family-selective tyrosine kinase inhibitor. J. Biol. Chem. 271, 695-701 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 695-701
    • Hanke, J.H.1
  • 6
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of src
    • Brown, M. T. & Cooper, J. A. Regulation, substrates and functions of src. Biochim. Biophys. Acta 1287, 121-149 (1996).
    • (1996) Biochim. Biophys. Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 7
    • 0032211806 scopus 로고    scopus 로고
    • Fyn, a Src family tyrosine kinase
    • Resh, M. D. Fyn, a Src family tyrosine kinase. Int. J. Biochem. Cell Biol. 30, 1159-1162 (1998).
    • (1998) Int. J. Biochem. Cell Biol. , vol.30 , pp. 1159-1162
    • Resh, M.D.1
  • 8
    • 0029348008 scopus 로고
    • Abl tyrosine protein kinase
    • Laneuville, P. Abl tyrosine protein kinase. Semin. Immunol. 7, 255-266 (1995).
    • (1995) Semin. Immunol. , vol.7 , pp. 255-266
    • Laneuville, P.1
  • 9
    • 0026294146 scopus 로고
    • Calmodulin-dependent protein kinase II. Multifunctional roles in neuronal differentiation and synaptic plasticity
    • Kelly, P. T. Calmodulin-dependent protein kinase II. Multifunctional roles in neuronal differentiation and synaptic plasticity. Mol. Neurobiol. 5, 153-177 (1991).
    • (1991) Mol. Neurobiol. , vol.5 , pp. 153-177
    • Kelly, P.T.1
  • 10
    • 0028931265 scopus 로고
    • Principles of CDK regulation
    • Morgan, D. O. Principles of CDK regulation. Nature 374, 131-134 (1995).
    • (1995) Nature , vol.374 , pp. 131-134
    • Morgan, D.O.1
  • 11
    • 0031253655 scopus 로고    scopus 로고
    • Protein kinase inhibition by staurosporine revealed in details of the molecular interaction with CDK2
    • Lawrie, A. M. et al. Protein kinase inhibition by staurosporine revealed in details of the molecular interaction with CDK2. Nature Struct. Biol. 4, 796-801 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 796-801
    • Lawrie, A.M.1
  • 12
    • 0030670394 scopus 로고    scopus 로고
    • Design and implementation of an efficient synthetic approach to furanosylated indolocarbazoles: Total synthesis of (+)- and (-)-K252a
    • Wood, J. L., Stoltz, B. M., Dietrich, H. J., Pflum, D. A. & Petsch, D. T. Design and implementation of an efficient synthetic approach to furanosylated indolocarbazoles: total synthesis of (+)- and (-)-K252a. J. Am. Chem. Soc. 119, 9641-9651 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 9641-9651
    • Wood, J.L.1    Stoltz, B.M.2    Dietrich, H.J.3    Pflum, D.A.4    Petsch, D.T.5
  • 13
    • 0033200390 scopus 로고    scopus 로고
    • Structural basis for selective inhibition of Src family kinases by PPI
    • Liu, Y. et al. Structural basis for selective inhibition of Src family kinases by PPI. Chem. Biol. 6, 671-678 (1999).
    • (1999) Chem. Biol. , vol.6 , pp. 671-678
    • Liu, Y.1
  • 14
    • 0031026008 scopus 로고    scopus 로고
    • The protein kinases of budding yeast: Six score and more
    • Hunter, T. & Plowman, G. D. The protein kinases of budding yeast: six score and more. Trends Biochem. Sci. 22, 18-22 (1997).
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 18-22
    • Hunter, T.1    Plowman, G.D.2
  • 15
    • 0028104106 scopus 로고
    • Yeast homolog of mammalian mitogen-activated protein kinase, Fus3/Dac2 kinase, is required both for cell fusion and for G1 arrest of the cell cycle and morphological changes by the cdc37 mutation
    • Fujimura, H. A. Yeast homolog of mammalian mitogen-activated protein kinase, Fus3/Dac2 kinase, is required both for cell fusion and for G1 arrest of the cell cycle and morphological changes by the cdc37 mutation. J. Cell. Sci. 107, 2617-2622 (1994).
    • (1994) J. Cell. Sci. , vol.107 , pp. 2617-2622
    • Fujimura, H.A.1
  • 16
    • 0017373258 scopus 로고
    • Temperature-sensitive loss of sexual agglutinability in Saccharomyces cerevisiae
    • Doi, S. & Yoshimura, M. Temperature-sensitive loss of sexual agglutinability in Saccharomyces cerevisiae. Arch. Microbiol. 114, 287-288 (1977).
    • (1977) Arch. Microbiol. , vol.114 , pp. 287-288
    • Doi, S.1    Yoshimura, M.2
  • 17
    • 0031737085 scopus 로고    scopus 로고
    • Regulation of Cdc28 cyclin-dependent protein kinase activity during the cell cycle of the yeast Saccharomyces cerevisiae
    • Mendenhall, M. D. & Hodge, A. E. Regulation of Cdc28 cyclin-dependent protein kinase activity during the cell cycle of the yeast Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 62, 1191-1243 (1998).
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1191-1243
    • Mendenhall, M.D.1    Hodge, A.E.2
  • 19
    • 0025753515 scopus 로고
    • The role of CDC28 and cyclins during mitosis in the budding yeast S. cerevisiae
    • Surana, U. et al. The role of CDC28 and cyclins during mitosis in the budding yeast S. cerevisiae. Cell 65, 145-161 (1991).
    • (1991) Cell , vol.65 , pp. 145-161
    • Surana, U.1
  • 20
    • 0029918062 scopus 로고    scopus 로고
    • Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1
    • Bourne, Y. et al. Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1. Cell 84, 863-874 (1996).
    • (1996) Cell , vol.84 , pp. 863-874
    • Bourne, Y.1
  • 22
    • 0028559010 scopus 로고
    • Cell cycle control by a complex of the cyclin HCS26 (PCL1) and the kinase PHO85
    • Espinoza, F. H., Ogas, J., Herskowitz, J. & Morgan, D. O. Cell cycle control by a complex of the cyclin HCS26 (PCL1) and the kinase PHO85. Science 266, 1388-1391 (1994).
    • (1994) Science , vol.266 , pp. 1388-1391
    • Espinoza, F.H.1    Ogas, J.2    Herskowitz, J.3    Morgan, D.O.4
  • 23
    • 0031742022 scopus 로고    scopus 로고
    • Comprehensive identification of cell cycle-regulated genes of the yeast Saccharomyces cerevisiae by microarray hybridization
    • Spellman, P. T. et al. Comprehensive identification of cell cycle-regulated genes of the yeast Saccharomyces cerevisiae by microarray hybridization. Mol. Biol. Cell 9, 3273-3297 (1998).
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3273-3297
    • Spellman, P.T.1
  • 24
    • 0027058054 scopus 로고
    • Characterization of four B-type cyclin genes of the budding yeast Saccharomyces cerevisiae
    • Fitch, I. et al. Characterization of four B-type cyclin genes of the budding yeast Saccharomyces cerevisiae. Mol. Biol. Cell 3, 805-818 (1992).
    • (1992) Mol. Biol. Cell , vol.3 , pp. 805-818
    • Fitch, I.1
  • 25
    • 0030249292 scopus 로고    scopus 로고
    • A quantitative model for the cdc2 control of S phase and mitosis in fission yeast
    • Stern, B. & Nurse, P. A quantitative model for the cdc2 control of S phase and mitosis in fission yeast. Trends Genet. 12, 345-350 (1996).
    • (1996) Trends Genet. , vol.12 , pp. 345-350
    • Stern, B.1    Nurse, P.2
  • 26
    • 0033974108 scopus 로고    scopus 로고
    • Cdc37 promotes the stability of protein kinases Cdc28 and Cak1
    • Farrell, A. & Morgan, D. O. Cdc37 promotes the stability of protein kinases Cdc28 and Cak1. Mol. Cell. Biol. 20, 749-754 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 749-754
    • Farrell, A.1    Morgan, D.O.2
  • 28
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S. & Hieter, P. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27 (1989).
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 29
    • 0033063429 scopus 로고    scopus 로고
    • Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor
    • Schindler, T. et al. Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor. Mol. Cell 3, 639-648 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 639-648
    • Schindler, T.1
  • 30
    • 0033106222 scopus 로고    scopus 로고
    • The conserved protein kinase Ipl1 regulates microtubule binding to kinetochores in budding yeast
    • Biggins, S. et al. The conserved protein kinase Ipl1 regulates microtubule binding to kinetochores in budding yeast. Genes Dev. 13, 532-544 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 532-544
    • Biggins, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.