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Volumn 32, Issue 12, 2014, Pages 1929-1935

Molecular mechanisms of activation in CDK2

Author keywords

activation; CDK2; conformational changes; molecular dynamics

Indexed keywords

CYCLIN DEPENDENT KINASE 2; CDK2 PROTEIN, HUMAN;

EID: 84906316802     PISSN: 07391102     EISSN: 15380254     Source Type: Journal    
DOI: 10.1080/07391102.2013.844080     Document Type: Article
Times cited : (13)

References (37)
  • 2
    • 4344606960 scopus 로고    scopus 로고
    • Multidimensional adaptive umbrella sampling: Applications to main chain and side chain peptide conformations
    • Bartels, C., & Karplus, M. (1997). Multidimensional adaptive umbrella sampling: Applications to main chain and side chain peptide conformations. Journal of Computational Chemistry, 18, 1450-1462.
    • (1997) Journal of Computational Chemistry , vol.18 , pp. 1450-1462
    • Bartels, C.1    Karplus, M.2
  • 6
    • 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. (1999). The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases. Nature Cell Biology, 1, 438-443.
    • (1999) Nature Cell Biology , vol.1 , pp. 438-443
    • Brown, N.R.1    Noble, M.E.2    Endicott, J.A.3    Johnson, L.N.4
  • 8
    • 0242353859 scopus 로고    scopus 로고
    • Molecular dynamics simulation of protein folding by essential dynamics sampling: Folding landscape of horse heart cytochrome c
    • Daidone, I., Amadei, A., Roccatano, D., & Di Nola, A. D. (2003). Molecular dynamics simulation of protein folding by essential dynamics sampling: Folding landscape of horse heart cytochrome c. Biophysical Journal, 85, 2865-2871.
    • (2003) Biophysical Journal , vol.85 , pp. 2865-2871
    • Daidone, I.1    Amadei, A.2    Roccatano, D.3    Di Nola, A.D.4
  • 9
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N [center-dot] log(N) method for Ewald sums in large systems
    • Darden, T., York, D., & Pedersen, L. (1993). Particle mesh Ewald: An N [center-dot] log(N) method for Ewald sums in large systems. Journal of Chemical Physics, 98, 10089- 10092.
    • (1993) Journal of Chemical Physics , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 11
    • 0000689085 scopus 로고
    • Predicting slow structural transitions in macromolecular systems: Conformational flooding
    • Grubmuller, H. (1995). Predicting slow structural transitions in macromolecular systems: Conformational flooding. Physical Review E, 52, 2893-2906.
    • (1995) Physical Review e , vol.52 , pp. 2893-2906
    • Grubmuller, H.1
  • 16
    • 84859961776 scopus 로고    scopus 로고
    • Alpha-C helix as a switch in the conformational transition of Src/CDK-like kinase domains
    • Huang, H., Zhao, R., Dickson, B. M., Skeel, R. D., & Post, C. B. (2012). Alpha-C helix as a switch in the conformational transition of Src/CDK-like kinase domains. The Journal of Physical Chemistry B, 116, 4465-4475.
    • (2012) The Journal of Physical Chemistry B , vol.116 , pp. 4465-4475
    • Huang, H.1    Zhao, R.2    Dickson, B.M.3    Skeel, R.D.4    Post, C.B.5
  • 17
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse, M., & Kuriyan, J. (2002). The conformational plasticity of protein kinases. Cell, 109, 275-282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 18
    • 0029029617 scopus 로고
    • Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
    • . Jeffrey, P., Russo, A., Polyak, K., Gibbs, E., Hurwitz, J., Massagué,J., & Pavletich, N. (1995). Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature, 376, 313-320.
    • (1995) Nature , vol.376 , pp. 313-320
    • Jeffrey, P.1    Russo, A.2    Polyak, K.3    Gibbs, E.4    Hurwitz, J.5    Massagué, J.6    Pavletich, N.7
  • 19
    • 67649726156 scopus 로고    scopus 로고
    • Protein kinase inhibitors: Contributions from structure to clinical compounds
    • Johnson, L. N. (2009). Protein kinase inhibitors: Contributions from structure to clinical compounds. Quarterly Reviews of Biophysics, 42, 1-40.
    • (2009) Quarterly Reviews of Biophysics , vol.42 , pp. 1-40
    • Johnson, L.N.1
  • 20
    • 79953308071 scopus 로고    scopus 로고
    • Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms
    • Jura, N., Zhang, X., Endres, N., & Seeliger, M. (2011). Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms. Molecular Cell, 42, 9-22.
    • (2011) Molecular Cell , vol.42 , pp. 9-22
    • Jura, N.1    Zhang, X.2    Endres, N.3    Seeliger, M.4
  • 21
    • 75349091799 scopus 로고    scopus 로고
    • Defining the conserved internal architecture of a protein kinase
    • Kornev, A. P., & Taylor, S. S. (2010). Defining the conserved internal architecture of a protein kinase. Biochimica et Biophysica Acta, 1804, 440-444.
    • (2010) Biochimica et Biophysica Acta , vol.1804 , pp. 440-444
    • Kornev, A.P.1    Taylor, S.S.2
  • 22
    • 48149084621 scopus 로고    scopus 로고
    • The atomistic mechanism of conformational transition in adenylate kinase: A TEE-REX molecular dynamics study
    • Kubitzki, M. B., & de Groot, B. L. (2008). The atomistic mechanism of conformational transition in adenylate kinase: A TEE-REX molecular dynamics study. Structure, 16, 1175-1182.
    • (2008) Structure , vol.16 , pp. 1175-1182
    • Kubitzki, M.B.1    De Groot, B.L.2
  • 25
    • 41849107614 scopus 로고    scopus 로고
    • Single Molecule conformational dynamics of adenylate kinase: Energy Landscape, structural correlations, and transition state ensembles
    • Lu, Q., & Wang, J. (2008). Single Molecule conformational dynamics of adenylate kinase: Energy Landscape, structural correlations, and transition state ensembles. Journal of the American Chemical Society, 130, 4772-4783.
    • (2008) Journal of the American Chemical Society , vol.130 , pp. 4772-4783
    • Lu, Q.1    Wang, J.2
  • 26
    • 0036682301 scopus 로고    scopus 로고
    • Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571)
    • Nagar, B., Bornmann, W. G., Pellicena, P., Schindler, T., Veach, D. R., Miller, W. T., ⋯ Kuriyan, J. (2002). Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI- 571). Cancer Research, 62, 4236-4243.
    • (2002) Cancer Research , vol.62 , pp. 4236-4243
    • Nagar, B.1    Bornmann, W.G.2    Pellicena, P.3    Schindler, T.4    Veach, D.R.5    Miller, W.T.6    Kuriyan, J.7
  • 29
    • 0033574614 scopus 로고    scopus 로고
    • Mechanisms of cyclin-dependent kinase regulation: Structures of Cdks, their cyclin activators, and Cip and INK4 inhibitors
    • Pavletich, N. P. (1999). Mechanisms of cyclin-dependent kinase regulation: Structures of Cdks, their cyclin activators, and Cip and INK4 inhibitors. Journal of Molecular Biology, 287, 821-828.
    • (1999) Journal of Molecular Biology , vol.287 , pp. 821-828
    • Pavletich, N.P.1
  • 30
    • 0029665852 scopus 로고    scopus 로고
    • Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin ACdk2 complex
    • Russo, A. A., Jeffrey, P. D., Patten, A. K., Massagué, J., & Pavletich, N. P. (1996). Crystal structure of the p27Kip1 cyclin-dependent- kinase inhibitor bound to the cyclin ACdk2 complex. Nature, 382, 325-331.
    • (1996) Nature , vol.382 , pp. 325-331
    • Russo, A.A.1    Jeffrey, P.D.2    Patten, A.K.3    Massagué, J.4    Pavletich, N.P.5
  • 32
    • 0035265679 scopus 로고    scopus 로고
    • Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2
    • Song, H., Hanlon, N., Brown, N. R., Noble, M. E., Johnson, L. N., & Barford, D. (2001). Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2. Molecular Cell, 7, 615-626.
    • (2001) Molecular Cell , vol.7 , pp. 615-626
    • Song, H.1    Hanlon, N.2    Brown, N.R.3    Noble, M.E.4    Johnson, L.N.5    Barford, D.6
  • 33
    • 1242338103 scopus 로고    scopus 로고
    • Conformational sampling for the impatient
    • Tai, K. (2004). Conformational sampling for the impatient. Biophysical Chemistry, 107, 213-220.
    • (2004) Biophysical Chemistry , vol.107 , pp. 213-220
    • Tai, K.1
  • 34
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?
    • Wang, J., Cieplak, P., & Kollmann, P. A. (2000). How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? Journal of Computational Chemistry, 21, 1049-1074.
    • (2000) Journal of Computational Chemistry , vol.21 , pp. 1049-1074
    • Wang, J.1    Cieplak, P.2    Kollmann, P.A.3
  • 36
    • 62649161772 scopus 로고    scopus 로고
    • Mapping the conformational transition in Src activation by cumulating the information from multiple molecular dynamics trajectories
    • Yang, S., Banavali, N., & Roux, B. (2009). Mapping the conformational transition in Src activation by cumulating the information from multiple molecular dynamics trajectories. Proceedings of National Academic of Sciences USA, 106, 1-6.
    • (2009) Proceedings of National Academic of Sciences USA , vol.106 , pp. 1-6
    • Yang, S.1    Banavali, N.2    Roux, B.3
  • 37
    • 41849097740 scopus 로고    scopus 로고
    • Src kinase conformational activation: Thermodynamics, pathways, and mechanisms
    • Yang, S., & Roux, B. (2008). Src kinase conformational activation: Thermodynamics, pathways, and mechanisms. PLoS Computational Biology, 4, e1000047.
    • (2008) PLoS Computational Biology , vol.4
    • Yang, S.1    Roux, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.