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Volumn 10, Issue 10, 2014, Pages

The SH2 Domain Regulates c-Abl Kinase Activation by a Cyclin-Like Mechanism and Remodulation of the Hinge Motion

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; COMPLEX NETWORKS; ENZYMES;

EID: 84908348822     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1003863     Document Type: Article
Times cited : (27)

References (54)
  • 1
    • 0025117392 scopus 로고
    • Induction of chronic myelogenous leukemia in mice by the P210bcr/abl gene of the Philadelphia chromosome
    • Daley GQ, van Etten RA, Baltimore D, (1990) Induction of chronic myelogenous leukemia in mice by the P210bcr/abl gene of the Philadelphia chromosome. Science 247: 824–830.
    • (1990) Science , vol.247 , pp. 824-830
    • Daley, G.Q.1    Van Etten, R.A.2    Baltimore, D.3
  • 2
    • 0000286732 scopus 로고
    • A Minute Chromosome In Human Chronic Granulocytic Leukemia
    • Nowell PC, Hungerford DA, (1960) A Minute Chromosome In Human Chronic Granulocytic Leukemia. Science 132: 1497 Available: http://www.sciencemag.org/content/132/3438/1488.extract.
    • (1960) Science , vol.132 , pp. 1497
    • Nowell, P.C.1    Hungerford, D.A.2
  • 3
    • 0015694748 scopus 로고
    • Letter: A new consistent chromosomal abnormality in chronic myelogenous leukaemia identified by quinacrine fluorescence and Giemsa staining
    • Rowley JD, (1973) Letter: A new consistent chromosomal abnormality in chronic myelogenous leukaemia identified by quinacrine fluorescence and Giemsa staining. Nature 243: 290–293.
    • (1973) Nature , vol.243 , pp. 290-293
    • Rowley, J.D.1
  • 4
    • 0347132269 scopus 로고    scopus 로고
    • Regulation of the c-Abl and Bcr–Abl Tyrosine Kinases
    • Hantschel O, Superti-Furga G, (2004) Regulation of the c-Abl and Bcr–Abl Tyrosine Kinases. Nat Rev Mol Cell Biol 5: 33–44 doi:10.1038/nrm1280
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 33-44
    • Hantschel, O.1    Superti-Furga, G.2
  • 5
    • 80054690374 scopus 로고    scopus 로고
    • Targeting the SH2-kinase interface in Bcr-Abl inhibits leukemogenesis
    • Grebien F, Hantschel O, Wojcik J, Kaupe I, Kovacic B, et al. (2011) Targeting the SH2-kinase interface in Bcr-Abl inhibits leukemogenesis. Cell 147: 306–319 doi:10.1016/j.cell.2011.08.046
    • (2011) Cell , vol.147 , pp. 306-319
    • Grebien, F.1    Hantschel, O.2    Wojcik, J.3    Kaupe, I.4    Kovacic, B.5
  • 6
    • 0031464009 scopus 로고    scopus 로고
    • The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src
    • Gonfloni S, Williams JC, Hattula K, Weijland A, Wierenga RK, et al. (1997) The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src. EMBO J 16: 7261–7271 doi:10.1093/emboj/16.24.7261
    • (1997) EMBO J , vol.16 , pp. 7261-7271
    • Gonfloni, S.1    Williams, J.C.2    Hattula, K.3    Weijland, A.4    Wierenga, R.K.5
  • 8
    • 0032769397 scopus 로고    scopus 로고
    • Leucine 255 of Src couples intramolecular interactions to inhibition of catalysis
    • Gonfloni S, Frischknecht F, Way M, Superti-Furga G, (1999) Leucine 255 of Src couples intramolecular interactions to inhibition of catalysis. Nat Struct Biol 6: 760–764 doi:10.1038/11537
    • (1999) Nat Struct Biol , vol.6 , pp. 760-764
    • Gonfloni, S.1    Frischknecht, F.2    Way, M.3    Superti-Furga, G.4
  • 9
    • 0029947186 scopus 로고    scopus 로고
    • Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr-Abl positive cells
    • Druker BJ, Tamura S, Buchdunger E, Ohno S, Segal GM, et al. (1996) Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr-Abl positive cells. Nat Med 2: 561–566.
    • (1996) Nat Med , vol.2 , pp. 561-566
    • Druker, B.J.1    Tamura, S.2    Buchdunger, E.3    Ohno, S.4    Segal, G.M.5
  • 10
    • 63749113783 scopus 로고    scopus 로고
    • Tyrosine phosphorylation: thirty years and counting
    • Hunter T, (2009) Tyrosine phosphorylation: thirty years and counting. Curr Opin Cell Biol 21: 140–146 doi:10.1016/j.ceb.2009.01.028
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 140-146
    • Hunter, T.1
  • 11
    • 0031452274 scopus 로고    scopus 로고
    • Structures of Src-family tyrosine kinases
    • Sicheri F, Kuriyan J, (1997) Structures of Src-family tyrosine kinases. Curr Opin Struct Biol 7: 777–785 doi:10.1016/S0959-440X(97)80146-7
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 777-785
    • Sicheri, F.1    Kuriyan, J.2
  • 12
    • 0033001789 scopus 로고    scopus 로고
    • Crystal structures of c-Src reveal features of its autoinhibitory mechanism
    • Xu W, Doshi A, Lei M, Eck MJ, Harrison SC, (1999) Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Mol Cell 3: 629–638.
    • (1999) Mol Cell , vol.3 , pp. 629-638
    • Xu, W.1    Doshi, A.2    Lei, M.3    Eck, M.J.4    Harrison, S.C.5
  • 13
    • 0034072765 scopus 로고    scopus 로고
    • Crosstalk between the catalytic and regulatory domains allows bidirectional regulation of Src
    • Gonfloni S, Weijland A, Kretzschmar J, Superti-Furga G, (2000) Crosstalk between the catalytic and regulatory domains allows bidirectional regulation of Src. Nat Struct Biol 7: 281–286 doi:10.1038/74041
    • (2000) Nat Struct Biol , vol.7 , pp. 281-286
    • Gonfloni, S.1    Weijland, A.2    Kretzschmar, J.3    Superti-Furga, G.4
  • 14
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu W, Harrison SC, Eck MJ, (1997) Three-dimensional structure of the tyrosine kinase c-Src. Nature 385: 595–602 doi:10.1038/385595a0
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 15
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri F, Moarefi I, Kuriyan J, (1997) Crystal structure of the Src family tyrosine kinase Hck. Nature 385: 602–609 doi:10.1038/385602a0
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 16
    • 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
    • Young MA, Gonfloni S, Superti-Furga G, Roux B, Kuriyan J, (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
  • 17
    • 27644462900 scopus 로고    scopus 로고
    • The N-terminal end of the catalytic domain of SRC kinase Hck is a conformational switch implicated in long-range allosteric regulation
    • Banavali NK, Roux B, (2005) The N-terminal end of the catalytic domain of SRC kinase Hck is a conformational switch implicated in long-range allosteric regulation. Structure 13: 1715–1723 doi:10.1016/j.str.2005.09.005
    • (2005) Structure , vol.13 , pp. 1715-1723
    • Banavali, N.K.1    Roux, B.2
  • 18
    • 50249132542 scopus 로고    scopus 로고
    • Structural Coupling of SH2-Kinase Domains Links Fes and Abl Substrate Recognition and Kinase Activation
    • Filippakopoulos P, Kofler M, Hantschel O, Gish GD, Grebien F, et al. (2008) Structural Coupling of SH2-Kinase Domains Links Fes and Abl Substrate Recognition and Kinase Activation. Cell 134: 793–803 doi:10.1016/j.cell.2008.07.047
    • (2008) Cell , vol.134 , pp. 793-803
    • Filippakopoulos, P.1    Kofler, M.2    Hantschel, O.3    Gish, G.D.4    Grebien, F.5
  • 19
    • 70649096122 scopus 로고    scopus 로고
    • SH2 domains: modulators of nonreceptor tyrosine kinase activity
    • Filippakopoulos P, Müller S, Knapp S, (2009) SH2 domains: modulators of nonreceptor tyrosine kinase activity. Curr Opin Struct Biol 19: 643–649 doi:10.1016/j.sbi.2009.10.001
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 643-649
    • Filippakopoulos, P.1    Müller, S.2    Knapp, S.3
  • 20
    • 80053590126 scopus 로고    scopus 로고
    • Computational modeling of allosteric communication reveals organizing principles of mutation-induced signaling in ABL and EGFR kinases
    • Dixit A, Verkhivker GM, (2011) Computational modeling of allosteric communication reveals organizing principles of mutation-induced signaling in ABL and EGFR kinases. PLoS Comput Biol 7: e1002179 doi:10.1371/journal.pcbi.1002179
    • (2011) PLoS Comput Biol , vol.7 , pp. e1002179
    • Dixit, A.1    Verkhivker, G.M.2
  • 21
    • 0037169351 scopus 로고    scopus 로고
    • Autoinhibition of c-Abl
    • Pluk H, Dorey K, Superti-Furga G, (2002) Autoinhibition of c-Abl. Cell 108: 247–259 doi:10.1016/S0092-8674(02)00623-2
    • (2002) Cell , vol.108 , pp. 247-259
    • Pluk, H.1    Dorey, K.2    Superti-Furga, G.3
  • 22
    • 77956908206 scopus 로고    scopus 로고
    • BCR-ABL SH3-SH2 domain mutations in chronic myeloid leukemia patients on imatinib
    • Sherbenou DW, Hantschel O, Kaupe I, Willis S, Bumm T, et al. (2010) BCR-ABL SH3-SH2 domain mutations in chronic myeloid leukemia patients on imatinib. Blood 116: 3278–3285 doi:10.1182/blood-2008-10-183665
    • (2010) Blood , vol.116 , pp. 3278-3285
    • Sherbenou, D.W.1    Hantschel, O.2    Kaupe, I.3    Willis, S.4    Bumm, T.5
  • 23
    • 0344626926 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of c-Abl tyrosine kinase
    • Nagar B, Hantschel O, Young MA, Scheffzek K, Veach D, et al. (2003) Structural basis for the autoinhibition of c-Abl tyrosine kinase. Cell 112: 859–871.
    • (2003) Cell , vol.112 , pp. 859-871
    • Nagar, B.1    Hantschel, O.2    Young, M.A.3    Scheffzek, K.4    Veach, D.5
  • 24
    • 33644871166 scopus 로고    scopus 로고
    • Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase
    • Nagar B, Hantschel O, Seeliger M, Davies JM, Weis WI, et al. (2006) Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase. Mol Cell 21: 787–798 doi:10.1016/j.molcel.2006.01.035
    • (2006) Mol Cell , vol.21 , pp. 787-798
    • Nagar, B.1    Hantschel, O.2    Seeliger, M.3    Davies, J.M.4    Weis, W.I.5
  • 25
    • 84888104464 scopus 로고    scopus 로고
    • NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors
    • Skora L, Mestan J, Fabbro D, Jahnke W, Grzesiek S, (2013) NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors. Proc Natl Acad Sci USA 110: E4437–E4445 doi:10.1073/pnas.1314712110
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. E4437-E4445
    • Skora, L.1    Mestan, J.2    Fabbro, D.3    Jahnke, W.4    Grzesiek, S.5
  • 26
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of Protein KinasesControlling Activity through Activation Segment Conformation
    • Nolen B, Taylor S, Ghosh G, (2004) Regulation of Protein KinasesControlling Activity through Activation Segment Conformation. Mol Cell 15: 661–675 doi:10.1016/j.molcel.2004.08.024
    • (2004) Mol Cell , vol.15 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 28
    • 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
  • 29
    • 79551594605 scopus 로고    scopus 로고
    • Protein kinases: evolution of dynamic regulatory proteins
    • Taylor SS, Kornev AP, (2011) Protein kinases: evolution of dynamic regulatory proteins. Trends Biochem Sci 36: 65–77 doi:10.1016/j.tibs.2010.09.006
    • (2011) Trends Biochem Sci , vol.36 , pp. 65-77
    • Taylor, S.S.1    Kornev, A.P.2
  • 30
    • 0141737107 scopus 로고    scopus 로고
    • Conformation of full-length Bruton tyrosine kinase (Btk) from synchrotron X-ray solution scattering
    • Márquez JA, Smith CIE, Petoukhov MV, Surdo Lo P, Mattsson PT, et al. (2003) Conformation of full-length Bruton tyrosine kinase (Btk) from synchrotron X-ray solution scattering. EMBO J 22: 4616–4624 doi:10.1093/emboj/cdg448
    • (2003) EMBO J , vol.22 , pp. 4616-4624
    • Márquez, J.A.1    Smith, C.I.E.2    Petoukhov, M.V.3    Surdo Lo, P.4    Mattsson, P.T.5
  • 31
    • 84874326369 scopus 로고    scopus 로고
    • Enhanced SH3/linker interaction overcomes Abl kinase activation by gatekeeper and myristic acid binding pocket mutations and increases sensitivity to small molecule inhibitors
    • Panjarian S, Iacob RE, Chen S, Wales TE, Engen JR, et al. (2013) Enhanced SH3/linker interaction overcomes Abl kinase activation by gatekeeper and myristic acid binding pocket mutations and increases sensitivity to small molecule inhibitors. J Biol Chem 288: 6116–6129 doi:10.1074/jbc.M112.431312
    • (2013) J Biol Chem , vol.288 , pp. 6116-6129
    • Panjarian, S.1    Iacob, R.E.2    Chen, S.3    Wales, T.E.4    Engen, J.R.5
  • 32
    • 58549114067 scopus 로고    scopus 로고
    • A conserved protonation-dependent switch controls drug binding in the Abl kinase
    • Shan Y, Seeliger MA, Eastwood MP, Frank F, Xu H, et al. (2009) A conserved protonation-dependent switch controls drug binding in the Abl kinase. Proc Natl Acad Sci USA 106: 139–144 doi:10.1073/pnas.0811223106
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 139-144
    • Shan, Y.1    Seeliger, M.A.2    Eastwood, M.P.3    Frank, F.4    Xu, H.5
  • 33
    • 70149098505 scopus 로고    scopus 로고
    • Coarse-grained modeling of allosteric regulation in protein receptors
    • Balabin IA, Yang W, Beratan DN, (2009) Coarse-grained modeling of allosteric regulation in protein receptors. Proc Natl Acad Sci USA 106: 14253–14258 doi:10.1073/pnas.0901811106
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14253-14258
    • Balabin, I.A.1    Yang, W.2    Beratan, D.N.3
  • 34
    • 33646755174 scopus 로고    scopus 로고
    • A Src-like inactive conformation in the abl tyrosine kinase domain
    • Levinson NM, Kuchment O, Shen K, Young MA, Koldobskiy M, et al. (2006) A Src-like inactive conformation in the abl tyrosine kinase domain. Plos Biol 4: e144 doi:10.1371/journal.pbio.0040144
    • (2006) Plos Biol , vol.4 , pp. e144
    • Levinson, N.M.1    Kuchment, O.2    Shen, K.3    Young, M.A.4    Koldobskiy, M.5
  • 35
    • 84860870716 scopus 로고    scopus 로고
    • Oncogenic mutations counteract intrinsic disorder in the EGFR kinase and promote receptor dimerization
    • Shan Y, Eastwood MP, Zhang X, Kim ET, Arkhipov A, et al. (2012) Oncogenic mutations counteract intrinsic disorder in the EGFR kinase and promote receptor dimerization. Cell 149: 860–870 doi:10.1016/j.cell.2012.02.063
    • (2012) Cell , vol.149 , pp. 860-870
    • Shan, Y.1    Eastwood, M.P.2    Zhang, X.3    Kim, E.T.4    Arkhipov, A.5
  • 36
    • 79959758717 scopus 로고    scopus 로고
    • Understanding the Impact of the P-loop Conformation on Kinase Selectivity
    • Guimarães CRW, Rai BK, Munchhof MJ, Liu S, Wang J, et al. (2011) Understanding the Impact of the P-loop Conformation on Kinase Selectivity. J Chem Inf Model 51: 1199–1204 doi:10.1021/ci200153c
    • (2011) J Chem Inf Model , vol.51 , pp. 1199-1204
    • Guimarães, C.R.W.1    Rai, B.K.2    Munchhof, M.J.3    Liu, S.4    Wang, J.5
  • 37
    • 84876902448 scopus 로고    scopus 로고
    • Transitions to catalytically inactive conformations in EGFR kinase
    • Shan Y, Arkhipov A, Kim ET, Pan AC, Shaw DE, (2013) Transitions to catalytically inactive conformations in EGFR kinase. Proc Natl Acad Sci USA 110: 7270–7275 doi:10.1073/pnas.1220843110
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 7270-7275
    • Shan, Y.1    Arkhipov, A.2    Kim, E.T.3    Pan, A.C.4    Shaw, D.E.5
  • 38
    • 0035413606 scopus 로고    scopus 로고
    • Kinetic and catalytic mechanisms of protein kinases
    • Adams JA, (2001) Kinetic and catalytic mechanisms of protein kinases. Chem Rev 101: 2271–2290.
    • (2001) Chem Rev , vol.101 , pp. 2271-2290
    • Adams, J.A.1
  • 39
    • 84856694630 scopus 로고    scopus 로고
    • The Different Flexibility of c-Src and c-Abl Kinases Regulates the Accessibility of a Druggable Inactive Conformation
    • Lovera S, Sutto L, Boubeva R, Scapozza L, Dölker N, et al. (2012) The Different Flexibility of c-Src and c-Abl Kinases Regulates the Accessibility of a Druggable Inactive Conformation. J Am Chem Soc 134: 2496–2499 doi:10.1021/ja210751t
    • (2012) J Am Chem Soc , vol.134 , pp. 2496-2499
    • Lovera, S.1    Sutto, L.2    Boubeva, R.3    Scapozza, L.4    Dölker, N.5
  • 40
    • 53549104402 scopus 로고    scopus 로고
    • Activation of tyrosine kinases by mutation of the gatekeeper threonine
    • Azam M, Seeliger MA, Gray NS, Kuriyan J, Daley GQ, (2008) Activation of tyrosine kinases by mutation of the gatekeeper threonine. Nat Struct Mol Biol 15: 1109–1118 doi:10.1038/nsmb.1486
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1109-1118
    • Azam, M.1    Seeliger, M.A.2    Gray, N.S.3    Kuriyan, J.4    Daley, G.Q.5
  • 41
    • 79953308071 scopus 로고    scopus 로고
    • Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms
    • Jura N, Zhang X, Endres NF, Seeliger MA, Schindler T, et al. (2011) Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms. Mol Cell 42: 9–22 doi:10.1016/j.molcel.2011.03.004
    • (2011) Mol Cell , vol.42 , pp. 9-22
    • Jura, N.1    Zhang, X.2    Endres, N.F.3    Seeliger, M.A.4    Schindler, T.5
  • 42
    • 83455244845 scopus 로고    scopus 로고
    • A Hybrid All-Atom Structure-Based Model for Protein Folding and Large Scale Conformational Transitions
    • Sutto L, Mereu I, Gervasio FL, (2011) A Hybrid All-Atom Structure-Based Model for Protein Folding and Large Scale Conformational Transitions. J Chem Theory Comput 7: 4208–4217 doi:10.1021/ct200547m
    • (2011) J Chem Theory Comput , vol.7 , pp. 4208-4217
    • Sutto, L.1    Mereu, I.2    Gervasio, F.L.3
  • 43
    • 0035909107 scopus 로고    scopus 로고
    • Nucleotide release and associated conformational changes regulate function in the COOH-terminal Src kinase, Csk
    • Shaffer J, Sun G, Adams JA, (2001) Nucleotide release and associated conformational changes regulate function in the COOH-terminal Src kinase, Csk. Biochemistry 40: 11149–11155.
    • (2001) Biochemistry , vol.40 , pp. 11149-11155
    • Shaffer, J.1    Sun, G.2    Adams, J.A.3
  • 45
    • 0029029617 scopus 로고
    • Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
    • Jeffrey PD, Russo AA, Polyak K, Gibbs E, Hurwitz J, et al. (1995) Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature 376: 313–320 doi:10.1038/376313a0
    • (1995) Nature , vol.376 , pp. 313-320
    • Jeffrey, P.D.1    Russo, A.A.2    Polyak, K.3    Gibbs, E.4    Hurwitz, J.5
  • 46
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • Zhang X, Gureasko J, Shen K, Cole PA, Kuriyan J, (2006) An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 125: 1137–1149 doi:10.1016/j.cell.2006.05.013
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 47
    • 75749146563 scopus 로고    scopus 로고
    • Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors
    • Zhang J, Adrián FJ, Jahnke W, Cowan-Jacob SW, Li AG, et al. (2010) Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors. Nature 463: 501–506 doi:10.1038/nature08675
    • (2010) Nature , vol.463 , pp. 501-506
    • Zhang, J.1    Adrián, F.J.2    Jahnke, W.3    Cowan-Jacob, S.W.4    Li, A.G.5
  • 48
    • 84876266689 scopus 로고    scopus 로고
    • Allostery in disease and in drug discovery
    • Nussinov R, Tsai C-J, (2013) Allostery in disease and in drug discovery. Cell 153: 293–305 doi:10.1016/j.cell.2013.03.034
    • (2013) Cell , vol.153 , pp. 293-305
    • Nussinov, R.1    Tsai, C.-J.2
  • 50
    • 79959720287 scopus 로고    scopus 로고
    • How robust are protein folding simulations with respect to force field parameterization?
    • Piana S, Lindorff-Larsen K, Shaw DE, (2011) How robust are protein folding simulations with respect to force field parameterization? Biophys J 100: L47–L49 doi:10.1016/j.bpj.2011.03.051
    • (2011) Biophys J , vol.100 , pp. L47-L49
    • Piana, S.1    Lindorff-Larsen, K.2    Shaw, D.E.3
  • 51
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
    • Hess B, Kutzner C, Van Der Spoel D, Lindahl E, (2008) GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation. J Chem Theory Comput 4: 435–447 doi:10.1021/ct700301q
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 52
    • 33750040264 scopus 로고    scopus 로고
    • Free-energy landscape for beta hairpin folding from combined parallel tempering and metadynamics
    • Bussi G, Gervasio FL, Laio A, Parrinello M, (2006) Free-energy landscape for beta hairpin folding from combined parallel tempering and metadynamics. J Am Chem Soc 128: 13435–13441 doi:10.1021/ja062463w
    • (2006) J Am Chem Soc , vol.128 , pp. 13435-13441
    • Bussi, G.1    Gervasio, F.L.2    Laio, A.3    Parrinello, M.4
  • 53
    • 79955574923 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System. DeLano Scientific
    • DeLano WL (2008) The PyMOL Molecular Graphics System. DeLano Scientific, Palo Alto, California, USA.
    • (2008)
    • Delano, W.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.