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Volumn 1804, Issue 3, 2010, Pages 429-432

Insights into protein kinase regulation and inhibition by large scale structural comparison

Author keywords

Atypical kinase; Kinase regulation; Protein kinase; Structure based drug design; X ray crystallography

Indexed keywords

IMATINIB; PROTEIN KINASE; PROTEIN KINASE INHIBITOR;

EID: 75349102353     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.10.013     Document Type: Review
Times cited : (42)

References (38)
  • 3
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases-the major drug targets of the twenty-first century?
    • Cohen P. Protein kinases-the major drug targets of the twenty-first century?. Nat. Rev. Drug Discov. 1 (2002) 309-315
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 309-315
    • Cohen, P.1
  • 4
    • 20444383859 scopus 로고    scopus 로고
    • Protein phosphorylation in signaling-50 years and counting
    • Pawson T., and Scott J.D. Protein phosphorylation in signaling-50 years and counting. Trends Biochem. Sci. 30 (2005) 286-290
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 286-290
    • Pawson, T.1    Scott, J.D.2
  • 6
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • Zhang J., Yang P.L., and Gray N.S. Targeting cancer with small molecule kinase inhibitors. Nat. Rev. Cancer 9 (2009) 28-39
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 7
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases; controlling activity through activation segment conformation
    • Nolen B., Taylor S., and Ghosh G. Regulation of protein kinases; controlling activity through activation segment conformation. Mol. Cell 15 (2004) 661-675
    • (2004) Mol. Cell , vol.15 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 8
    • 33845197964 scopus 로고    scopus 로고
    • Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism
    • Kornev A.P., Haste N.M., Taylor S.S., and Eyck L.F. Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 17783-17788
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 17783-17788
    • Kornev, A.P.1    Haste, N.M.2    Taylor, S.S.3    Eyck, L.F.4
  • 9
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: structural basis for regulation
    • Johnson L.N., Noble M.E., and 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
  • 10
    • 40949151046 scopus 로고    scopus 로고
    • Doing more than just the structure-structural genomics in kinase drug discovery
    • Marsden B.D., and Knapp S. Doing more than just the structure-structural genomics in kinase drug discovery. Curr. Opin. Chem. Biol. 12 (2008) 40-45
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 40-45
    • Marsden, B.D.1    Knapp, S.2
  • 11
    • 33645018289 scopus 로고    scopus 로고
    • Protein kinase resource: an integrated environment for phosphorylation research
    • Niedner R.H., Buzko O.V., Haste N.M., Taylor A., Gribskov M., and Taylor S.S. Protein kinase resource: an integrated environment for phosphorylation research. Proteins 63 (2006) 78-86
    • (2006) Proteins , vol.63 , pp. 78-86
    • Niedner, R.H.1    Buzko, O.V.2    Haste, N.M.3    Taylor, A.4    Gribskov, M.5    Taylor, S.S.6
  • 14
    • 34547154729 scopus 로고    scopus 로고
    • Activation segment exchange: a common mechanism of kinase autophosphorylation?
    • Oliver A.W., Knapp S., and Pearl L.H. Activation segment exchange: a common mechanism of kinase autophosphorylation?. Trends Biochem. Sci. 32 (2007) 351-356
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 351-356
    • Oliver, A.W.1    Knapp, S.2    Pearl, L.H.3
  • 19
    • 58149204174 scopus 로고    scopus 로고
    • Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site
    • Scheeff E.D., Eswaran J., Bunkoczi G., Knapp S., and Manning G. Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site. Structure 17 (2009) 128-138
    • (2009) Structure , vol.17 , pp. 128-138
    • Scheeff, E.D.1    Eswaran, J.2    Bunkoczi, G.3    Knapp, S.4    Manning, G.5
  • 21
    • 33745298429 scopus 로고    scopus 로고
    • Rational design of inhibitors that bind to inactive kinase conformations
    • Liu Y., and Gray N.S. Rational design of inhibitors that bind to inactive kinase conformations. Nat. Chem. Biol. 2 (2006) 358-364
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 358-364
    • Liu, Y.1    Gray, N.S.2
  • 27
    • 0034924175 scopus 로고    scopus 로고
    • Haspin-like proteins: a new family of evolutionarily conserved putative eukaryotic protein kinases
    • Higgins J.M. Haspin-like proteins: a new family of evolutionarily conserved putative eukaryotic protein kinases. Protein Sci. 10 (2001) 1677-1684
    • (2001) Protein Sci. , vol.10 , pp. 1677-1684
    • Higgins, J.M.1
  • 28
    • 13844252061 scopus 로고    scopus 로고
    • The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment
    • Dai J., Sultan S., Taylor S.S., and Higgins J.M. The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment. Genes Dev. 19 (2005) 472-488
    • (2005) Genes Dev. , vol.19 , pp. 472-488
    • Dai, J.1    Sultan, S.2    Taylor, S.S.3    Higgins, J.M.4
  • 29
    • 25144516018 scopus 로고    scopus 로고
    • Haspin: a mitotic histone kinase required for metaphase chromosome alignment
    • Dai J., and Higgins J.M. Haspin: a mitotic histone kinase required for metaphase chromosome alignment. Cell Cycle 4 (2005) 665-668
    • (2005) Cell Cycle , vol.4 , pp. 665-668
    • Dai, J.1    Higgins, J.M.2
  • 30
    • 33750428233 scopus 로고    scopus 로고
    • Regulation of mitotic chromosome cohesion by Haspin and Aurora B
    • Dai J., Sullivan B.A., and Higgins J.M. Regulation of mitotic chromosome cohesion by Haspin and Aurora B. Dev. Cell 11 (2006) 741-750
    • (2006) Dev. Cell , vol.11 , pp. 741-750
    • Dai, J.1    Sullivan, B.A.2    Higgins, J.M.3
  • 31
    • 38549168381 scopus 로고    scopus 로고
    • Centromeric Aurora-B activation requires TD-60, microtubules, and substrate priming phosphorylation
    • Rosasco-Nitcher S.E., Lan W., Khorasanizadeh S., and Stukenberg P.T. Centromeric Aurora-B activation requires TD-60, microtubules, and substrate priming phosphorylation. Science 319 (2008) 469-472
    • (2008) Science , vol.319 , pp. 469-472
    • Rosasco-Nitcher, S.E.1    Lan, W.2    Khorasanizadeh, S.3    Stukenberg, P.T.4
  • 35
    • 34247350792 scopus 로고    scopus 로고
    • Insights for the development of specific kinase inhibitors by targeted structural genomics
    • Fedorov O., Sundstrom M., Marsden B., and Knapp S. Insights for the development of specific kinase inhibitors by targeted structural genomics. Drug Discov. Today 12 (2007) 365-372
    • (2007) Drug Discov. Today , vol.12 , pp. 365-372
    • Fedorov, O.1    Sundstrom, M.2    Marsden, B.3    Knapp, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.