메뉴 건너뛰기




Volumn 15, Issue 5, 2004, Pages 661-675

Regulation of protein kinases: Controlling activity through activation segment conformation

Author keywords

[No Author keywords available]

Indexed keywords

ABELSON KINASE; CHECKPOINT KINASE 2; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIN DEPENDENT KINASE 2; CYCLIN DEPENDENT KINASE 5; CYCLIN DEPENDENT KINASE 6; DEATH ASSOCIATED PROTEIN KINASE; EPIDERMAL GROWTH FACTOR RECEPTOR; FLT3 LIGAND; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN KINASE; PROTEIN KINASE B; PROTEIN KINASE LCK; PROTEIN TYROSINE KINASE; SCATTER FACTOR RECEPTOR; STEM CELL FACTOR; STRESS ACTIVATED PROTEIN KINASE; TRANSFORMING GROWTH FACTOR BETA RECEPTOR; VASCULOTROPIN RECEPTOR 2;

EID: 4444353636     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2004.08.024     Document Type: Review
Times cited : (891)

References (103)
  • 1
    • 0035413606 scopus 로고    scopus 로고
    • Kinetic and catalytic mechanisms of protein kinases
    • Adams J.A. Kinetic and catalytic mechanisms of protein kinases. Chem. Rev. 101:2001;2271-2290
    • (2001) Chem. Rev. , vol.101 , pp. 2271-2290
    • Adams, J.A.1
  • 2
    • 0037469146 scopus 로고    scopus 로고
    • Activation loop phosphorylation and catalysis in protein kinases: Is there functional evidence for the autoinhibitor model?
    • Adams J.A. Activation loop phosphorylation and catalysis in protein kinases. is there functional evidence for the autoinhibitor model? Biochemistry. 42:2003;601-607
    • (2003) Biochemistry , vol.42 , pp. 601-607
    • Adams, J.A.1
  • 3
    • 0033179621 scopus 로고    scopus 로고
    • APS, an adapter protein with a PH and SH2 domain, is a substrate for the insulin receptor kinase
    • Ahmed Z., Smith B.J., Kotani K., Wilden P., Pillay T.S. APS, an adapter protein with a PH and SH2 domain, is a substrate for the insulin receptor kinase. Biochem. J. 341:1999;665-668
    • (1999) Biochem. J. , vol.341 , pp. 665-668
    • Ahmed, Z.1    Smith, B.J.2    Kotani, K.3    Wilden, P.4    Pillay, T.S.5
  • 5
    • 0242330123 scopus 로고    scopus 로고
    • Structural basis of Aurora-A activation by TPX2 at the mitotic spindle
    • Bayliss R., Sardon T., Vernos I., Conti E. Structural basis of Aurora-A activation by TPX2 at the mitotic spindle. Mol. Cell. 12:2003;851-862
    • (2003) Mol. Cell , vol.12 , pp. 851-862
    • Bayliss, R.1    Sardon, T.2    Vernos, I.3    Conti, E.4
  • 6
    • 0033567706 scopus 로고    scopus 로고
    • The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation
    • Bellon S., Fitzgibbon M.J., Fox T., Hsiao H.M., Wilson K.P. The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation. Struct. Fold. Des. 7:1999;1057-1065
    • (1999) Struct. Fold. Des. , vol.7 , pp. 1057-1065
    • Bellon, S.1    Fitzgibbon, M.J.2    Fox, T.3    Hsiao, H.M.4    Wilson, K.P.5
  • 7
    • 0037102153 scopus 로고    scopus 로고
    • High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site
    • Biondi R.M., Komander D., Thomas C.C., Lizcano J.M., Deak M., Alessi D.R., van Aalten D.M.F. High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site. EMBO J. 21:2002;4219-4228
    • (2002) EMBO J. , vol.21 , pp. 4219-4228
    • Biondi, R.M.1    Komander, D.2    Thomas, C.C.3    Lizcano, J.M.4    Deak, M.5    Alessi, D.R.6    Van Aalten, D.M.F.7
  • 8
    • 0033224309 scopus 로고    scopus 로고
    • The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases
    • Brown N.R., Noble M.E., Endicott J.A., Johnson L.N. The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases. Nat. Cell Biol. 1:1999;438-443
    • (1999) Nat. Cell Biol. , vol.1 , pp. 438-443
    • Brown, N.R.1    Noble, M.E.2    Endicott, J.A.3    Johnson, L.N.4
  • 9
    • 0030866897 scopus 로고    scopus 로고
    • Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
    • Canagarajah B.J., Khokhlatchev A., Cobb M.H., Goldsmith E.J. Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Cell. 90:1997;859-869
    • (1997) Cell , vol.90 , pp. 859-869
    • Canagarajah, B.J.1    Khokhlatchev, A.2    Cobb, M.H.3    Goldsmith, E.J.4
  • 13
    • 0029838105 scopus 로고    scopus 로고
    • Identification of the site in the Syk protein tyrosine kinase that binds the SH2 domain of Lck
    • Couture C., Deckert M., Williams S., Russo F.O., Altman A., Mustelin T. Identification of the site in the Syk protein tyrosine kinase that binds the SH2 domain of Lck. J. Biol. Chem. 271:1996;24294-24299
    • (1996) J. Biol. Chem. , vol.271 , pp. 24294-24299
    • Couture, C.1    Deckert, M.2    Williams, S.3    Russo, F.O.4    Altman, A.5    Mustelin, T.6
  • 14
    • 0028865669 scopus 로고
    • Kinetic analysis of cAMP-dependent protein kinase: Mutations at histidine 87 affect peptide binding and pH dependence
    • Cox S., Taylor S.S. Kinetic analysis of cAMP-dependent protein kinase. mutations at histidine 87 affect peptide binding and pH dependence Biochemistry. 34:1995;16203-16209
    • (1995) Biochemistry , vol.34 , pp. 16203-16209
    • Cox, S.1    Taylor, S.S.2
  • 15
    • 0035875098 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase kinase 3 beta: Structural basis for phosphate-primed substrate specificity and autoinhibition
    • Dajani R., Fraser E., Roe S.M., Young N., Good V., Dale T.C., Pearl L.H. Crystal structure of glycogen synthase kinase 3 beta. structural basis for phosphate-primed substrate specificity and autoinhibition Cell. 105:2001;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
    • 0037415737 scopus 로고    scopus 로고
    • Structural basis for recruitment of glycogen synthase kinase 3beta to the axin-APC scaffold complex
    • Dajani R., Fraser E., Roe S.M., Yeo M., Good V.M., Thompson V., Dale T.C., Pearl L.H. Structural basis for recruitment of glycogen synthase kinase 3beta to the axin-APC scaffold complex. EMBO J. 22:2003;494-501
    • (2003) EMBO J. , vol.22 , pp. 494-501
    • Dajani, R.1    Fraser, E.2    Roe, S.M.3    Yeo, M.4    Good, V.M.5    Thompson, V.6    Dale, T.C.7    Pearl, L.H.8
  • 18
    • 0035185571 scopus 로고    scopus 로고
    • Structure and autoregulation of the insulin-like growth factor 1 receptor kinase
    • Favelyukis S., Till J.H., Hubbard S.R., Miller W.T. Structure and autoregulation of the insulin-like growth factor 1 receptor kinase. Nat. Struct. Biol. 8:2001;1058-1063
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 1058-1063
    • Favelyukis, S.1    Till, J.H.2    Hubbard, S.R.3    Miller, W.T.4
  • 20
    • 0025739664 scopus 로고
    • Rational scanning mutagenesis of a protein kinase identifies functional regions involved in catalysis and substrate interactions
    • Gibbs C.S., Zoller M.J. Rational scanning mutagenesis of a protein kinase identifies functional regions involved in catalysis and substrate interactions. J. Biol. Chem. 266:1991;8923-8931
    • (1991) J. Biol. Chem. , vol.266 , pp. 8923-8931
    • Gibbs, C.S.1    Zoller, M.J.2
  • 21
    • 0029871290 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I
    • Goldberg J., Nairn A.C., Kuriyan J. Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I. Cell. 84:1996;875-887
    • (1996) Cell , vol.84 , pp. 875-887
    • Goldberg, J.1    Nairn, A.C.2    Kuriyan, J.3
  • 24
    • 0036428762 scopus 로고    scopus 로고
    • Phosphorylation driven motions in the COOH-terminal Src kinase, CSK, revealed through enhanced hydrogen-deuterium exchange and mass spectrometry (DXMS)
    • Hamuro Y., Wong L., Shaffer J., Kim J.S., Stranz D.D., Jennings P.A., Woods V.L. Jr., Adams J.A. Phosphorylation driven motions in the COOH-terminal Src kinase, CSK, revealed through enhanced hydrogen-deuterium exchange and mass spectrometry (DXMS). J. Mol. Biol. 323:2002;871-881
    • (2002) J. Mol. Biol. , vol.323 , pp. 871-881
    • Hamuro, Y.1    Wong, L.2    Shaffer, J.3    Kim, J.S.4    Stranz, D.D.5    Jennings, P.A.6    Woods Jr., V.L.7    Adams, J.A.8
  • 26
    • 0035969987 scopus 로고    scopus 로고
    • Changes in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange
    • Hoofnagle A.N., Resing K.A., Goldsmith E.J., Ahn N.G. Changes in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange. Proc. Natl. Acad. Sci. USA. 98:2001;956-961
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 956-961
    • Hoofnagle, A.N.1    Resing, K.A.2    Goldsmith, E.J.3    Ahn, N.G.4
  • 27
    • 0346688715 scopus 로고    scopus 로고
    • Phosphorylation-dependent changes in structure and dynamics in ERK2 detected by SDSL and EPR
    • Hoofnagle A.N., Stoner J.W., Lee T., Eaton S.S., Ahn N.G. Phosphorylation-dependent changes in structure and dynamics in ERK2 detected by SDSL and EPR. Biophys. J. 86:2004;395-403
    • (2004) Biophys. J. , vol.86 , pp. 395-403
    • Hoofnagle, A.N.1    Stoner, J.W.2    Lee, T.3    Eaton, S.S.4    Ahn, N.G.5
  • 28
    • 0346156078 scopus 로고    scopus 로고
    • Structural basis for recruitment of the adaptor protein APS to the activated insulin receptor
    • Hu J., Liu J., Ghirlando R., Saltiel A.R., Hubbard S.R. Structural basis for recruitment of the adaptor protein APS to the activated insulin receptor. Mol. Cell. 12:2003;1379-1389
    • (2003) Mol. Cell , vol.12 , pp. 1379-1389
    • Hu, J.1    Liu, J.2    Ghirlando, R.3    Saltiel, A.R.4    Hubbard, S.R.5
  • 30
    • 0030766163 scopus 로고    scopus 로고
    • Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog
    • Hubbard S.R. Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J. 16:1997;5572-5581
    • (1997) EMBO J. , vol.16 , pp. 5572-5581
    • Hubbard, S.R.1
  • 31
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • Hubbard S.R., Wei L., Ellis L., Hendrickson W.A. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature. 372:1994;746-754
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 32
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M., Kuriyan J. The conformational plasticity of protein kinases. Cell. 109:2002;275-282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 33
    • 0033524943 scopus 로고    scopus 로고
    • Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12
    • Huse M., Chen Y.G., Massague J., Kuriyan J. Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12. Cell. 96:1999;425-436
    • (1999) Cell , vol.96 , pp. 425-436
    • Huse, M.1    Chen, Y.G.2    Massague, J.3    Kuriyan, J.4
  • 35
    • 0032560489 scopus 로고    scopus 로고
    • The Eleventh Datta Lecture. The structural basis for substrate recognition and control by protein kinases
    • Johnson L.N., Lowe E.D., Noble M.E., Owen D.J. The Eleventh Datta Lecture. The structural basis for substrate recognition and control by protein kinases. FEBS Lett. 430:1998;1-11
    • (1998) FEBS Lett. , vol.430 , pp. 1-11
    • Johnson, L.N.1    Lowe, E.D.2    Noble, M.E.3    Owen, D.J.4
  • 36
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson L.N., Noble M.E., Owen D.J. Active and inactive protein kinases. structural basis for regulation Cell. 85:1996;149-158
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.2    Owen, D.J.3
  • 39
    • 0033555270 scopus 로고    scopus 로고
    • Structure of the protein tyrosine kinase domain of C-terminal Src kinase (CSK) in complex with staurosporine
    • Lamers M.B., Antson A.A., Hubbard R.E., Scott R.K., Williams D.H. Structure of the protein tyrosine kinase domain of C-terminal Src kinase (CSK) in complex with staurosporine. J. Mol. Biol. 285:1999;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
  • 40
    • 0034604338 scopus 로고    scopus 로고
    • Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch
    • Lei M., Lu W., Meng W., Parrini M.C., Eck M.J., Mayer B.J., Harrison S.C. Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch. Cell. 102:2000;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
  • 41
    • 0035964253 scopus 로고    scopus 로고
    • Electrostatic environment surrounding the activation loop phosphotyrosine in the oncoprotein v-Fps
    • Leon B.C., Tsigelny I., Adams J.A. Electrostatic environment surrounding the activation loop phosphotyrosine in the oncoprotein v-Fps. Biochemistry. 40:2001;10078-10086
    • (2001) Biochemistry , vol.40 , pp. 10078-10086
    • Leon, B.C.1    Tsigelny, I.2    Adams, J.A.3
  • 42
    • 0037417767 scopus 로고    scopus 로고
    • MAP kinases and CDKs: Kinetic basis for catalytic activation
    • Lew J. MAP kinases and CDKs. kinetic basis for catalytic activation Biochemistry. 42:2003;849-856
    • (2003) Biochemistry , vol.42 , pp. 849-856
    • Lew, J.1
  • 43
    • 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
    • Li F., Gangal M., Juliano C., Gorfain E., Taylor S.S., Johnson D.A. 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. 315:2002;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
  • 44
    • 0038267169 scopus 로고    scopus 로고
    • Functions of the activation loop in Csk protein-tyrosine kinase
    • Lin X., Lee S., Sun G. Functions of the activation loop in Csk protein-tyrosine kinase. J. Biol. Chem. 278:2003;24072-24077
    • (2003) J. Biol. Chem. , vol.278 , pp. 24072-24077
    • Lin, X.1    Lee, S.2    Sun, G.3
  • 45
    • 0037799206 scopus 로고    scopus 로고
    • Keeping G proteins at bay: A complex between G protein-coupled receptor kinase 2 and Gbetagamma
    • Lodowski D.T., Pitcher J.A., Capel W.D., Lefkowitz R.J., Tesmer J.J. Keeping G proteins at bay. a complex between G protein-coupled receptor kinase 2 and Gbetagamma Science. 300:2003;1256-1262
    • (2003) Science , vol.300 , pp. 1256-1262
    • Lodowski, D.T.1    Pitcher, J.A.2    Capel, W.D.3    Lefkowitz, R.J.4    Tesmer, J.J.5
  • 46
    • 0029963896 scopus 로고    scopus 로고
    • Three-dimensional structure of mammalian casein kinase I: Molecular basis for phosphate recognition
    • Longenecker K.L., Roach P.J., Hurley T.D. Three-dimensional structure of mammalian casein kinase I. molecular basis for phosphate recognition J. Mol. Biol. 257:1996;618-631
    • (1996) J. Mol. Biol. , vol.257 , pp. 618-631
    • Longenecker, K.L.1    Roach, P.J.2    Hurley, T.D.3
  • 47
    • 0030812650 scopus 로고    scopus 로고
    • The crystal structure of a phosphorylase kinase peptide substrate complex: Kinase substrate recognition
    • Lowe E.D., Noble M.E., Skamnaki V.T., Oikonomakos N.G., Owen D.J., Johnson L.N. The crystal structure of a phosphorylase kinase peptide substrate complex. kinase substrate recognition EMBO J. 16:1997;6646-6658
    • (1997) EMBO J. , vol.16 , pp. 6646-6658
    • Lowe, E.D.1    Noble, M.E.2    Skamnaki, V.T.3    Oikonomakos, N.G.4    Owen, D.J.5    Johnson, L.N.6
  • 50
    • 0035798646 scopus 로고    scopus 로고
    • Crystal structure of Bruton's tyrosine kinase domain suggests a novel pathway for activation and provides insights into the molecular basis of X-linked agammaglobulinemia
    • Mao C., Zhou M., Uckun F.M. Crystal structure of Bruton's tyrosine kinase domain suggests a novel pathway for activation and provides insights into the molecular basis of X-linked agammaglobulinemia. J. Biol. Chem. 276:2001;41435-41443
    • (2001) J. Biol. Chem. , vol.276 , pp. 41435-41443
    • Mao, C.1    Zhou, M.2    Uckun, F.M.3
  • 53
    • 0037020266 scopus 로고    scopus 로고
    • Structure of mitogen-activated protein kinase-activated protein (MAPKAP) kinase 2 suggests a bifunctional switch that couples kinase activation with nuclear export
    • Meng W., Swenson L.L., Fitzgibbon M.J., Hayakawa K., Ter Haar E., Behrens A.E., Fulghum J.R., Lippke J.A. Structure of mitogen-activated protein kinase-activated protein (MAPKAP) kinase 2 suggests a bifunctional switch that couples kinase activation with nuclear export. J. Biol. Chem. 277:2002;37401-37405
    • (2002) J. Biol. Chem. , vol.277 , pp. 37401-37405
    • Meng, W.1    Swenson, L.L.2    Fitzgibbon, M.J.3    Hayakawa, K.4    Ter Haar, E.5    Behrens, A.E.6    Fulghum, J.R.7    Lippke, J.A.8
  • 54
    • 0030598848 scopus 로고    scopus 로고
    • Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism
    • Mohammadi M., Schlessinger J., Hubbard S.R. Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism. Cell. 86:1996;577-587
    • (1996) Cell , vol.86 , pp. 577-587
    • Mohammadi, M.1    Schlessinger, J.2    Hubbard, S.R.3
  • 57
    • 0037518278 scopus 로고    scopus 로고
    • Structural basis for peptide binding in protein kinase A. Role of glutamic acid. 203(and tyrosine 204 in the peptide-positioning loop
    • Moore M.J., Adams J.A., Taylor S.S. Structural basis for peptide binding in protein kinase A. Role of glutamic acid. 203(and tyrosine 204 in the peptide-positioning loop. J. Biol. Chem. 278):2003;10613-10618
    • (2003) J. Biol. Chem. , vol.278 , pp. 10613-10618
    • Moore, M.J.1    Adams, J.A.2    Taylor, S.S.3
  • 58
    • 0028271690 scopus 로고
    • Protein kinase regulation: Insights from crystal structure analysis
    • Morgan D.O., De Bondt H.L. Protein kinase regulation. insights from crystal structure analysis Curr. Opin. Cell Biol. 6:1994;239-246
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 239-246
    • Morgan, D.O.1    De Bondt, H.L.2
  • 61
    • 0032079650 scopus 로고    scopus 로고
    • Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 a resolution
    • Niefind K., Guerra B., Pinna L.A., Issinger O.G., Schomburg D. Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution. EMBO J. 17:1998;2451-2462
    • (1998) EMBO J. , vol.17 , pp. 2451-2462
    • Niefind, K.1    Guerra, B.2    Pinna, L.A.3    Issinger, O.G.4    Schomburg, D.5
  • 64
    • 0042527480 scopus 로고    scopus 로고
    • Nucleotide-induced conformational changes in the Saccharomyces cerevisiae SR protein kinase, Sky1p, revealed by X-ray crystallography
    • Nolen B., Ngo J., Chakrabarti S., Vu D., Adams J.A., Ghosh G. Nucleotide-induced conformational changes in the Saccharomyces cerevisiae SR protein kinase, Sky1p, revealed by X-ray crystallography. Biochemistry. 42:2003;9575-9585
    • (2003) Biochemistry , vol.42 , pp. 9575-9585
    • Nolen, B.1    Ngo, J.2    Chakrabarti, S.3    Vu, D.4    Adams, J.A.5    Ghosh, G.6
  • 67
    • 0029644732 scopus 로고
    • Two structures of the catalytic domain of phosphorylase kinase: An active protein kinase complexed with substrate analogue and product
    • Owen D.J., Noble M.E., Garman E.F., Papageorgiou A.C., Johnson L.N. Two structures of the catalytic domain of phosphorylase kinase. an active protein kinase complexed with substrate analogue and product Structure. 3:1995;467-482
    • (1995) Structure , vol.3 , pp. 467-482
    • Owen, D.J.1    Noble, M.E.2    Garman, E.F.3    Papageorgiou, A.C.4    Johnson, L.N.5
  • 68
    • 0034793734 scopus 로고    scopus 로고
    • Crystal structure of bisphosphorylated IGF-1 receptor kinase: Insight into domain movements upon kinase activation
    • Pautsch A., Zoephel A., Ahorn H., Spevak W., Hauptmann R., Nar H. Crystal structure of bisphosphorylated IGF-1 receptor kinase. insight into domain movements upon kinase activation Structure (Camb). 9:2001;955-965
    • (2001) Structure (Camb) , vol.9 , pp. 955-965
    • Pautsch, A.1    Zoephel, A.2    Ahorn, H.3    Spevak, W.4    Hauptmann, R.5    Nar, H.6
  • 69
    • 0030581751 scopus 로고    scopus 로고
    • How do protein kinases recognize their substrates?
    • Pinna L.A., Ruzzene M. How do protein kinases recognize their substrates? Biochim. Biophys. Acta. 1314:1996;191-225
    • (1996) Biochim. Biophys. Acta , vol.1314 , pp. 191-225
    • Pinna, L.A.1    Ruzzene, M.2
  • 70
    • 0035798540 scopus 로고    scopus 로고
    • The complete pathway for catalytic activation of the mitogen-activated protein kinase, ERK2
    • Prowse C.N., Deal M.S., Lew J. The complete pathway for catalytic activation of the mitogen-activated protein kinase, ERK2. J. Biol. Chem. 276:2001;40817-40823
    • (2001) J. Biol. Chem. , vol.276 , pp. 40817-40823
    • Prowse, C.N.1    Deal, M.S.2    Lew, J.3
  • 71
    • 0026321413 scopus 로고
    • Multisite and hierarchal protein phosphorylation
    • Roach P.J. Multisite and hierarchal protein phosphorylation. J. Biol. Chem. 266:1991;14139-14142
    • (1991) J. Biol. Chem. , vol.266 , pp. 14139-14142
    • Roach, P.J.1
  • 72
    • 0029767016 scopus 로고    scopus 로고
    • Structural basis of cyclin-dependent kinase activation by phosphorylation
    • Russo A.A., Jeffrey P.D., Pavletich N.P. Structural basis of cyclin-dependent kinase activation by phosphorylation. Nat. Struct. Biol. 3:1996;696-700
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 696-700
    • Russo, A.A.1    Jeffrey, P.D.2    Pavletich, N.P.3
  • 73
    • 0242268455 scopus 로고    scopus 로고
    • Crystal structure of the tyrosine kinase domain of the hepatocyte growth factor receptor c-Met and its complex with the microbial alkaloid K-252a
    • Schiering N., Knapp S., Marconi M., Flocco M.M., Cui J., Perego R., Rusconi L., Cristiani C. Crystal structure of the tyrosine kinase domain of the hepatocyte growth factor receptor c-Met and its complex with the microbial alkaloid K-252a. Proc. Natl. Acad. Sci. USA. 100:2003;12654-12659
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12654-12659
    • Schiering, N.1    Knapp, S.2    Marconi, M.3    Flocco, M.M.4    Cui, J.5    Perego, R.6    Rusconi, L.7    Cristiani, C.8
  • 74
    • 0036176979 scopus 로고    scopus 로고
    • Structural basis for CDK6 activation by a virus-encoded cyclin
    • Schulze-Gahmen U., Kim S.H. Structural basis for CDK6 activation by a virus-encoded cyclin. Nat. Struct. Biol. 9:2002;177-181
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 177-181
    • Schulze-Gahmen, U.1    Kim, S.H.2
  • 75
    • 0029850471 scopus 로고    scopus 로고
    • High-resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP: Bound waters and natural ligand as guides for inhibitor design
    • Schulze-Gahmen U., De Bondt H.L., Kim S.H. High-resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP. bound waters and natural ligand as guides for inhibitor design J. Med. Chem. 39:1996;4540-4546
    • (1996) J. Med. Chem. , vol.39 , pp. 4540-4546
    • Schulze-Gahmen, U.1    De Bondt, H.L.2    Kim, S.H.3
  • 76
    • 0033554425 scopus 로고    scopus 로고
    • Detection of conformational changes along the kinetic pathway of protein kinase a using a catalytic trapping technique
    • Shaffer J., Adams J.A. Detection of conformational changes along the kinetic pathway of protein kinase A using a catalytic trapping technique. Biochemistry. 38:1999;12072-12079
    • (1999) Biochemistry , vol.38 , pp. 12072-12079
    • Shaffer, J.1    Adams, J.A.2
  • 78
    • 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. 385:1997;602-609
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 81
    • 0141599428 scopus 로고    scopus 로고
    • Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor
    • Stamos J., Sliwkowski M.X., Eigenbrot C. Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor. J. Biol. Chem. 277:2002;46265-46272
    • (2002) J. Biol. Chem. , vol.277 , pp. 46265-46272
    • Stamos, J.1    Sliwkowski, M.X.2    Eigenbrot, C.3
  • 83
    • 0028773477 scopus 로고
    • Three protein kinase structures define a common motif
    • Taylor S.S., Radzio-Andzelm E. Three protein kinase structures define a common motif. Structure. 2:1994;345-355
    • (1994) Structure , vol.2 , pp. 345-355
    • Taylor, S.S.1    Radzio-Andzelm, E.2
  • 85
    • 0034810794 scopus 로고    scopus 로고
    • Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression
    • Tereshko V., Teplova M., Brunzelle J., Watterson D.M., Egli M. Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression. Nat. Struct. Biol. 8:2001;899-907
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 899-907
    • Tereshko, V.1    Teplova, M.2    Brunzelle, J.3    Watterson, D.M.4    Egli, M.5
  • 92
    • 0035816678 scopus 로고    scopus 로고
    • Involvement of the activation loop of ERK in the detachment from cytosolic anchoring
    • Wolf I., Rubinfeld H., Yoon S., Marmor G., Hanoch T., Seger R. Involvement of the activation loop of ERK in the detachment from cytosolic anchoring. J. Biol. Chem. 276:2001;24490-24497
    • (2001) J. Biol. Chem. , vol.276 , pp. 24490-24497
    • Wolf, I.1    Rubinfeld, H.2    Yoon, S.3    Marmor, G.4    Hanoch, T.5    Seger, R.6
  • 93
    • 0035929146 scopus 로고    scopus 로고
    • Structural basis for autoinhibition of the Ephb2 receptor tyrosine kinase by the unphosphorylated juxtamembrane region
    • Wybenga-Groot L.E., Baskin B., Ong S.H., Tong J., Pawson T., Sicheri F. Structural basis for autoinhibition of the Ephb2 receptor tyrosine kinase by the unphosphorylated juxtamembrane region. Cell. 106:2001;745-757
    • (2001) Cell , vol.106 , pp. 745-757
    • Wybenga-Groot, L.E.1    Baskin, B.2    Ong, S.H.3    Tong, J.4    Pawson, T.5    Sicheri, F.6
  • 95
    • 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. 385:1997;595-602
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 96
    • 16144364951 scopus 로고    scopus 로고
    • Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation
    • Yamaguchi H., Hendrickson W.A. Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation. Nature. 384:1996;484-489
    • (1996) Nature , vol.384 , pp. 484-489
    • Yamaguchi, H.1    Hendrickson, W.A.2
  • 97
    • 18744373865 scopus 로고    scopus 로고
    • Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP
    • a
    • Yang J., Cron P., Good V.M., Thompson V., Hemmings B.A., Barford D. Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP. Nat. Struct. Biol. 9:2002;940-944. a
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 940-944
    • Yang, J.1    Cron, P.2    Good, V.M.3    Thompson, V.4    Hemmings, B.A.5    Barford, D.6
  • 98
    • 0036295728 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation
    • b
    • Yang J., Cron P., Thompson V., Good V.M., Hess D., Hemmings B.A., Barford D. Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation. Mol. Cell. 9:2002;1227-1240. b
    • (2002) Mol. Cell , vol.9 , pp. 1227-1240
    • Yang, J.1    Cron, P.2    Thompson, V.3    Good, V.M.4    Hess, D.5    Hemmings, B.A.6    Barford, D.7
  • 99
    • 0037337317 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases
    • Young T.A., Delagoutte B., Endrizzi J.A., Falick A.M., Alber T. Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases. Nat. Struct. Biol. 10:2003;168-174
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 168-174
    • Young, T.A.1    Delagoutte, B.2    Endrizzi, J.A.3    Falick, A.M.4    Alber, T.5
  • 100
    • 0034675919 scopus 로고    scopus 로고
    • Activation of B-Raf kinase requires phosphorylation of the conserved residues Thr598 and Ser601
    • Zhang B.H., Guan K.L. Activation of B-Raf kinase requires phosphorylation of the conserved residues Thr598 and Ser601. EMBO J. 19:2000;5429-5439
    • (2000) EMBO J. , vol.19 , pp. 5429-5439
    • Zhang, B.H.1    Guan, K.L.2
  • 101
    • 0028157664 scopus 로고
    • Atomic structure of the MAP kinase ERK2 at 2.3 a resolution
    • Zhang F., Strand A., Robbins D., Cobb M.H., Goldsmith E.J. Atomic structure of the MAP kinase ERK2 at 2.3 A resolution. Nature. 367:1994;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
  • 102
    • 0027408171 scopus 로고
    • Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor
    • a
    • Zheng J., Knighton D.R., ten Eyck L.F., Karlsson R., Xuong N., Taylor S.S., Sowadski J.M. Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor. Biochemistry. 32:1993;2154-2161. a
    • (1993) Biochemistry , vol.32 , pp. 2154-2161
    • Zheng, J.1    Knighton, D.R.2    Ten Eyck, L.F.3    Karlsson, R.4    Xuong, N.5    Taylor, S.S.6    Sowadski, J.M.7
  • 103
    • 0000127673 scopus 로고
    • 2.2-Angstrom refined crystal structure of the catalytic subunit of cAMP-dependent Protein Kinase complexed with MnATP and a peptide inhibitor
    • b
    • Zheng J., Trafny E.A., Knighton D.K., Xuong N., Taylor S., Ten Eyck L., Sowadski J. 2.2-Angstrom refined crystal structure of the catalytic subunit of cAMP-dependent Protein Kinase complexed with MnATP and a peptide inhibitor. Acta Crystallogr. D Biol. Crystallogr. 49:1993;362-365. b
    • (1993) Acta Crystallogr. D Biol. Crystallogr. , vol.49 , pp. 362-365
    • Zheng, J.1    Trafny, E.A.2    Knighton, D.K.3    Xuong, N.4    Taylor, S.5    Ten Eyck, L.6    Sowadski, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.