메뉴 건너뛰기




Volumn 1-3, Issue , 2003, Pages 539-542

Principles of Kinase Regulation

Author keywords

[No Author keywords available]

Indexed keywords


EID: 57649240485     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012124546-7/50450-2     Document Type: Chapter
Times cited : (4)

References (32)
  • 1
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • T. Pawson and J.D. Scott (1997) Signaling through scaffold, anchoring, and adaptor proteins. Science 278 2075-2080.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 2
    • 0034989316 scopus 로고    scopus 로고
    • The protein kinase activity modulation sites: mechanisms for cellular regulation: targets for therapeutic intervention
    • R.A. Engh and D. Bossemeyer (2001) The protein kinase activity modulation sites: mechanisms for cellular regulation: targets for therapeutic intervention. Adv. Enzyme Regul. 41 121-149.
    • (2001) Adv. Enzyme Regul , vol.41 , pp. 121-149
    • Engh, R.A.1    Bossemeyer, D.2
  • 3
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • M. Huse and J. Kuriyan (2002) The conformational plasticity of protein kinases. Cell 109 275-282.
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 4
  • 5
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • S.R. Hubbard, L. Wei, L. Ellis and W.A. Hendrickson (1994) Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372 746-754.
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 6
    • 0033604499 scopus 로고    scopus 로고
    • Active site-directed protein regulation
    • B. Kobe and B.E. Kemp (1999) Active site-directed protein regulation. Nature 402 373-376.
    • (1999) Nature , vol.402 , pp. 373-376
    • Kobe, B.1    Kemp, B.E.2
  • 7
    • 73649152457 scopus 로고
    • Allosteric proteins and cellular control systems
    • J. Monod, J.P. Changeux and F. Jacob (1963) Allosteric proteins and cellular control systems. J. Mol. Biol. 6 306-329.
    • (1963) J. Mol. Biol , vol.6 , pp. 306-329
    • Monod, J.1    Changeux, J.P.2    Jacob, F.3
  • 8
    • 0025772230 scopus 로고
    • Intrasteric regulation of protein kinases and phosphatases
    • B.E. Kemp and R.B. Pearson (1991) Intrasteric regulation of protein kinases and phosphatases. Biochim. Biophys. Acta 1094 67-76.
    • (1991) Biochim. Biophys. Acta , vol.1094 , pp. 67-76
    • Kemp, B.E.1    Pearson, R.B.2
  • 9
  • 12
    • 0029871290 scopus 로고    scopus 로고
    • Structural basis for the auto-inhibition of calcium/calmodulin-dependent protein kinase I
    • J. Goldberg, A.C. Nairn and J. Kuriyan (1996) Structural basis for the auto-inhibition of calcium/calmodulin-dependent protein kinase I. Cell 84 875-887.
    • (1996) Cell , vol.84 , pp. 875-887
    • Goldberg, J.1    Nairn, A.C.2    Kuriyan, J.3
  • 13
    • 0034604338 scopus 로고    scopus 로고
    • Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch
    • M. Lei, W. Lu, W. Meng, M.C. Parrini, M.J. Eck, B.J. Mayer and S.C. Harrison (2000) Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch. Cell 102 387-397.
    • (2000) Cell , vol.102 , pp. 387-397
    • Lei, M.1    Lu, W.2    Meng, W.3    Parrini, M.C.4    Eck, M.J.5    Mayer, B.J.6    Harrison, S.C.7
  • 14
    • 0035875098 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition
    • R. Dajani, E. Fraser, S.M. Roe, N. Young, V. Good, T.C. Dale and L.H. Pearl (2001) Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition. Cell 105 721-732.
    • (2001) Cell , vol.105 , pp. 721-732
    • Dajani, R.1    Fraser, E.2    Roe, S.M.3    Young, N.4    Good, V.5    Dale, T.C.6    Pearl, L.H.7
  • 16
    • 0030766163 scopus 로고    scopus 로고
    • Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog
    • S.R. Hubbard (1997) Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J. 16 5572-5581.
    • (1997) EMBO J , vol.16 , pp. 5572-5581
    • Hubbard, S.R.1
  • 17
    • 0028157664 scopus 로고
    • Atomic structure of the MAP kinase ERK2 at 2.3 resolution
    • F. Zhang, A. Strand, D. Robbins, M.H. Cobb and E.J. Goldsmith (1994) Atomic structure of the MAP kinase ERK2 at 2.3 resolution. Nature 367 704-711.
    • (1994) Nature , vol.367 , pp. 704-711
    • Zhang, F.1    Strand, A.2    Robbins, D.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 18
    • 0030866897 scopus 로고    scopus 로고
    • Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
    • B.J. Canagarajah, A. Khokhlatchev, M.H. Cobb and E.J. Goldsmith (1997) Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Cell 90 859-869.
    • (1997) Cell , vol.90 , pp. 859-869
    • Canagarajah, B.J.1    Khokhlatchev, A.2    Cobb, M.H.3    Goldsmith, E.J.4
  • 19
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: structural basis for regulation
    • L.N. Johnson, M.E.M. Noble and D.J. Owen (1996) Active and inactive protein kinases: structural basis for regulation. Cell 85 149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.M.2    Owen, D.J.3
  • 23
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • F. Sicheri, I. Moarefi and J. Kuriyan (1997) Crystal structure of the Src family tyrosine kinase Hck. Nature 285 602-653.
    • (1997) Nature , vol.285 , pp. 602-653
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 24
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • W. Xu, S.C. Harrison and M.J. Eck (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
  • 26
    • 0032541623 scopus 로고    scopus 로고
    • Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a
    • A.A. Russo, L. Tong, J.O. Lee, P.D. Jeffrey and N.P. Pavletich (1998) Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a. Nature 395 237-243.
    • (1998) Nature , vol.395 , pp. 237-243
    • Russo, A.A.1    Tong, L.2    Lee, J.O.3    Jeffrey, P.D.4    Pavletich, N.P.5
  • 28
    • 0033575222 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase I in the absence of activation loop phosphorylation
    • S.S. Hook, B.E. Kemp and A.R. Means (1999) Peptide specificity determinants at P-7 and P-6 enhance the catalytic efficiency of Ca2+/calmodulin-dependent protein kinase I in the absence of activation loop phosphorylation. J. Biol. Chem. 274 20215-20222.
    • (1999) J. Biol. Chem , vol.274 , pp. 20215-20222
    • Hook, S.S.1    Kemp, B.E.2    Means, A.R.3
  • 29
    • 0033524943 scopus 로고    scopus 로고
    • Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12
    • M. Huse, Y.G. Chen, J. Massague and J. Kuriyan (1999) Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12. Cell 96 425-436.
    • (1999) Cell , vol.96 , pp. 425-436
    • Huse, M.1    Chen, Y.G.2    Massague, J.3    Kuriyan, J.4
  • 30
    • 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
    • M.A. Young, S. Gonfloni, G. Superti-Furga, B. Roux and J. Kuriyan (2001) Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation. Cell 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
  • 31
    • 0036306530 scopus 로고    scopus 로고
    • Evidence for an internal entropy contribution to phosphoryl transfer: a study of domain closure, backbone flexibility, and the catalytic cycle of cAMP-dependent protein kinase
    • F. Li, M. Gangal, C. Juliano, E. Gorfain, S.S. Taylor and D.A. Johnson (2002) Evidence for an internal entropy contribution to phosphoryl transfer: a study of domain closure, backbone flexibility, and the catalytic cycle of cAMP-dependent protein kinase. J. Mol. Biol. 315 459-469.
    • (2002) J. Mol. Biol , vol.315 , pp. 459-469
    • Li, F.1    Gangal, M.2    Juliano, C.3    Gorfain, E.4    Taylor, S.S.5    Johnson, D.A.6
  • 32
    • 0026319199 scopus 로고
    • Protein foldind and association: insights from the interfacial and thermodynamic properties of hydrocarbons
    • A. Nicholls, K.A. Sharp and B. Honig (1991) Protein foldind and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.