메뉴 건너뛰기




Volumn 77, Issue 1, 2009, Pages 14-25

Evolutionary conservation in multiple faces of protein interaction

Author keywords

Docking simulation; Evolutionary conservation; Multiple interfaces; Protein protein interaction

Indexed keywords

ARTICLE; MOLECULAR EVOLUTION; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN PROTEIN INTERACTION;

EID: 70349330141     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22410     Document Type: Article
Times cited : (59)

References (49)
  • 1
    • 33646182934 scopus 로고    scopus 로고
    • An integrated view of protein evolution
    • Pal C, Papp B, Lercher MJ. An integrated view of protein evolution. Nat Rev Genet 2006;7:337-348.
    • (2006) Nat Rev Genet , vol.7 , pp. 337-348
    • Pal, C.1    Papp, B.2    Lercher, M.J.3
  • 2
    • 0037177560 scopus 로고    scopus 로고
    • Evolutionary rate in the protein interaction network
    • DOI 10.1126/science.1068696
    • Fraser HB, Hirsh AE, Steinmetz LM, Scharfe C, Feldman MW. Evolutionary rate in the protein interaction network. Science 2002;296:750-752. (Pubitemid 34442006)
    • (2002) Science , vol.296 , Issue.5568 , pp. 750-752
    • Fraser, H.B.1    Hirsh, A.E.2    Steinmetz, L.M.3    Scharfe, C.4    Feldman, M.W.5
  • 3
    • 16844363315 scopus 로고    scopus 로고
    • Modularity and evolutionary constraint on proteins
    • Fraser HB. Modularity and evolutionary constraint on proteins. Nat Genet 2005;37:351-352.
    • (2005) Nat Genet , vol.37 , pp. 351-352
    • Fraser, H.B.1
  • 4
    • 0242284421 scopus 로고    scopus 로고
    • A simple dependence between protein evolution rate and the number of protein-protein interactions
    • Fraser HB, Wall DP, Hirsh AE. A simple dependence between protein evolution rate and the number of protein-protein interactions. BMC Evol Biol 2003;3:11.
    • (2003) BMC Evol Biol , vol.3 , pp. 11
    • Fraser, H.B.1    Wall, D.P.2    Hirsh, A.E.3
  • 5
    • 0035853028 scopus 로고    scopus 로고
    • Identification of protein oligomerization states by analysis of interface conservation
    • Elcock AH, McCammon JA. Identification of protein oligomerization states by analysis of interface conservation. Proc Natl Acad Sci USA 2001;98:2990-2994.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2990-2994
    • Elcock, A.H.1    McCammon, J.A.2
  • 6
    • 0035914476 scopus 로고    scopus 로고
    • Conservation helps to identify biologically relevant crystal contacts
    • Valdar WS, Thornton JM. Conservation helps to identify biologically relevant crystal contacts. J Mol Biol 2001;313:399-416.
    • (2001) J Mol Biol , vol.313 , pp. 399-416
    • Valdar, W.S.1    Thornton, J.M.2
  • 7
    • 33747150197 scopus 로고    scopus 로고
    • Protein binding site prediction using an empirical scoring function
    • DOI 10.1093/nar/gkl454
    • Liang S, Zhang C, Liu S, Zhou Y. Protein binding site prediction using an empirical scoring function. Nucleic Acids Res 2006;34:3698-3707. (Pubitemid 44400419)
    • (2006) Nucleic Acids Research , vol.34 , Issue.13 , pp. 3698-3707
    • Liang, S.1    Zhang, C.2    Liu, S.3    Zhou, Y.4
  • 8
    • 27644527039 scopus 로고    scopus 로고
    • Sequence variation in ligand binding sites in proteins
    • DOI 10.1186/1471-2105-6-240
    • Magliery TJ, Regan L. Sequence variation in ligand binding sites in proteins. BMC Bioinformatics 2005;6:240. (Pubitemid 41548715)
    • (2005) BMC Bioinformatics , vol.6 , pp. 240
    • Magliery, T.J.1    Regan, L.2
  • 9
    • 0346733329 scopus 로고    scopus 로고
    • Are protein-protein interfaces more conserved in sequence than the rest of the protein surface?
    • Caffrey DR, Somaroo S, Hughes JD, Mintseris J, Huang ES. Are protein-protein interfaces more conserved in sequence than the rest of the protein surface? Protein Sci 2004;13:190-202.
    • (2004) Protein Sci , vol.13 , pp. 190-202
    • Caffrey, D.R.1    Somaroo, S.2    Hughes, J.D.3    Mintseris, J.4    Huang, E.S.5
  • 11
    • 33748779553 scopus 로고    scopus 로고
    • Insights into Protein-Protein Interfaces using a Bayesian Network Prediction Method
    • DOI 10.1016/j.jmb.2006.07.028, PII S0022283606008965
    • Bradford JR, Needham CJ, Bulpitt AJ, Westhead DR. Insights into protein-protein interfaces using a Bayesian network prediction method. J Mol Biol 2006;362:365-386. (Pubitemid 44403921)
    • (2006) Journal of Molecular Biology , vol.362 , Issue.2 , pp. 365-386
    • Bradford, J.R.1    Needham, C.J.2    Bulpitt, A.J.3    Westhead, D.R.4
  • 12
    • 23044487169 scopus 로고    scopus 로고
    • Statistical analysis and prediction of protein-protein interfaces
    • DOI 10.1002/prot.20433
    • Bordner AJ, Abagyan R. Statistical analysis and prediction of protein-protein interfaces. Proteins 2005;60:353-366. (Pubitemid 41061632)
    • (2005) Proteins: Structure, Function and Genetics , vol.60 , Issue.3 , pp. 353-366
    • Bordner, A.J.1    Abagyan, R.2
  • 13
    • 17444372787 scopus 로고    scopus 로고
    • Improved prediction of protein-protein binding sites using a support vector machines approach
    • Bradford JR, Westhead DR. Improved prediction of protein-protein binding sites using a support vector machines approach. Bioinformatics 2005;21:1487-1494.
    • (2005) Bioinformatics , vol.21 , pp. 1487-1494
    • Bradford, J.R.1    Westhead, D.R.2
  • 15
    • 84860167598 scopus 로고    scopus 로고
    • http://www.rcsb.org/pdb/statistics/clusterStatistics.do.
  • 17
    • 84860146624 scopus 로고    scopus 로고
    • http://scop.berkeley.edu/.
  • 18
    • 33749337098 scopus 로고    scopus 로고
    • The many faces of protein-protein interactions: A compendium of interface geometry
    • DOI 10.1371/journal.pcbi.0020124
    • Kim WK, Henschel A, Winter C, Schroeder M. The many faces of protein-protein interactions: a compendium of interface geometry. PLoS Comput Biol 2006;2:e124. (Pubitemid 44495727)
    • (2006) PLoS Computational Biology , vol.2 , Issue.9 , pp. 1151-1164
    • Kim, W.K.1    Henschel, A.2    Winter, C.3    Schroeder, M.4
  • 21
    • 24344487344 scopus 로고    scopus 로고
    • Generation and analysis of a protein-protein interface data set with similar chemical and spatial patterns of interactions
    • DOI 10.1002/prot.20580
    • Mintz S, Shulman-Peleg A, Wolfson HJ, Nussinov R. Generation and analysis of a protein-protein interface data set with similar chemical and spatial patterns of interactions. Proteins 2005;61:6-20. (Pubitemid 41262913)
    • (2005) Proteins: Structure, Function and Genetics , vol.61 , Issue.1 , pp. 6-20
    • Mintz, S.1    Shulman-Peleg, A.2    Wolfson, H.J.3    Nussinov, R.4
  • 22
    • 84860183600 scopus 로고    scopus 로고
    • http://bioinfo3d.cs.tau.ac.il/Interfaces/Full-Dataset.
  • 24
    • 84860183599 scopus 로고    scopus 로고
    • http://au.expasy.org/sprot/.
  • 25
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterisation and functional significance of transient protein-protein interactions
    • Nooren IM, Thornton JM. Structural characterisation and functional significance of transient protein-protein interactions. J Mol Biol 2003;325:991-1018.
    • (2003) J Mol Biol , vol.325 , pp. 991-1018
    • Nooren, I.M.1    Thornton, J.M.2
  • 27
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • DOI 10.1093/nar/gkh340
    • Edgar RC. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 2004;32:1792-1797. (Pubitemid 38832724)
    • (2004) Nucleic Acids Research , vol.32 , Issue.5 , pp. 1792-1797
    • Edgar, R.C.1
  • 28
    • 4143051195 scopus 로고    scopus 로고
    • Comparison of site-specific rate-inference methods for protein sequences: Empirical Bayesian methods are superior
    • DOI 10.1093/molbev/msh194
    • Mayrose I, Graur D, Ben-Tal N, Pupko T. Comparison of site-specific rate-inference methods for protein sequences: empirical Bayesian methods are superior. Mol Biol Evol 2004;21:1781-1791. (Pubitemid 39096894)
    • (2004) Molecular Biology and Evolution , vol.21 , Issue.9 , pp. 1781-1791
    • Mayrose, I.1    Graur, D.2    Ben-Tal, N.3    Pupko, T.4
  • 29
    • 0002218484 scopus 로고    scopus 로고
    • Rate4Site: An algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues
    • Pupko T, Bell RE, Mayrose I, Glaser F, Ben-Tal N. Rate4Site: an algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues. Bioinformatics 2002;18 (Suppl 1):S71-S77. (Pubitemid 41185639)
    • (2002) Bioinformatics , vol.18 , Issue.SUPPL. 1
    • Pupko, T.1    Bell, R.E.2    Mayrose, I.3    Glaser, F.4    Ben-Tal, N.5
  • 32
    • 21644476468 scopus 로고    scopus 로고
    • PatchDock and SymmDock: Servers for rigid and symmetric docking
    • DOI 10.1093/nar/gki481
    • Schneidman-Duhovny D, Inbar Y, Nussinov R, Wolfson HJ. Patch-Dock and SymmDock: servers for rigid and symmetric docking. Nucleic Acids Res 2005;33(Web Server issue):W363-W367. (Pubitemid 44529944)
    • (2005) Nucleic Acids Research , vol.33 , Issue.WEB. SERV. ISS
    • Schneidman-Duhovny, D.1    Inbar, Y.2    Nussinov, R.3    Wolfson, H.J.4
  • 34
    • 0022332686 scopus 로고
    • Diversity in the germline antibody repertoire. Molecular evolution of the T15 V(H) gene family
    • Perlmutter RM, Berson B, Griffin JA, Hood L. Diversity in the germline antibody repertoire. Molecular evolution of the T15 VN gene family. J Exp Med 1985;162:1998-2016. (Pubitemid 16149691)
    • (1985) Journal of Experimental Medicine , vol.162 , Issue.6 , pp. 1998-2016
    • Perlmutter, R.M.1    Berson, B.2    Griffin, J.A.3    Hood, L.4
  • 36
    • 84860146633 scopus 로고    scopus 로고
    • http://www.pymol.org.
  • 38
    • 21644458102 scopus 로고    scopus 로고
    • Classification of protein complexes based on docking difficulty
    • DOI 10.1002/prot.20554
    • Vajda S. Classification of protein complexes based on docking difficulty. Proteins 2005;60:176-180. (Pubitemid 40934883)
    • (2005) Proteins: Structure, Function and Genetics , vol.60 , Issue.2 , pp. 176-180
    • Vajda, S.1
  • 39
    • 1242270553 scopus 로고    scopus 로고
    • Protein-protein docking: Is the glass half-full or half-empty?
    • Vajda S, Camacho CJ. Protein-protein docking: is the glass half-full or half-empty? Trends Biotechnol 2004;22:110-116.
    • (2004) Trends Biotechnol , vol.22 , pp. 110-116
    • Vajda, S.1    Camacho, C.J.2
  • 40
    • 13244277453 scopus 로고    scopus 로고
    • Physicochemical and residue conservation calculations to improve the ranking of protein-protein docking solutions
    • DOI 10.1110/ps.04941505
    • Duan Y, Reddy BV, Kaznessis YN. Physicochemical and residue conservation calculations to improve the ranking of protein-protein docking solutions. Protein Sci 2005;14:316-328. (Pubitemid 40194583)
    • (2005) Protein Science , vol.14 , Issue.2 , pp. 316-328
    • Duan, Y.1    Reddy, B.V.B.2    Kaznessis, Y.N.3
  • 41
    • 33750029942 scopus 로고    scopus 로고
    • csc: Predicting ligand binding sites using the Connolly surface and degree of conservation
    • DOI 10.1186/1472-6807-6-19
    • Huang B, Schroeder M. LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation. BMC Struct Biol 2006;6:19. (Pubitemid 44570436)
    • (2006) BMC Structural Biology , vol.6 , pp. 19
    • Huang, B.1    Schroeder, M.2
  • 42
    • 0031297461 scopus 로고    scopus 로고
    • Specific versus non-specific contacts in protein crystals
    • Janin J. Specific versus non-specific contacts in protein crystals. Nat Struct Biol 1997;4:973-974.
    • (1997) Nat Struct Biol , vol.4 , pp. 973-974
    • Janin, J.1
  • 43
    • 0032169688 scopus 로고    scopus 로고
    • PQS: A protein quaternary structure file server
    • DOI 10.1016/S0968-0004(98)01253-5, PII S0968000498012535
    • Henrick K, Thornton JM. PQS: a protein quaternary structure file server. Trends Biochem Sci 1998;23:358-361. (Pubitemid 28461869)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.9 , pp. 358-361
    • Henrick, K.1    Thornton, J.M.2
  • 44
    • 0034308172 scopus 로고    scopus 로고
    • Discriminating between homodimeric and monomeric proteins in the crystalline state
    • DOI 10.1002/1097-0134(20001001)41:1<47::AID-PROT80>3.0.CO;2-8
    • Ponstingl H, Henrick K, Thornton JM. Discriminating between homodimeric and monomeric proteins in the crystalline state. Proteins 2000;41:47-57. (Pubitemid 30666912)
    • (2000) Proteins: Structure, Function and Genetics , vol.41 , Issue.1 , pp. 47-57
    • Ponstingl, H.1    Henrick, K.2    Thornton, J.M.3
  • 45
    • 0036443972 scopus 로고    scopus 로고
    • The constraints protein-protein interactions place on sequence divergence
    • Teichmann SA. The constraints protein-protein interactions place on sequence divergence. J Mol Biol 2002;324:399-407.
    • (2002) J Mol Biol , vol.324 , pp. 399-407
    • Teichmann, S.A.1
  • 46
    • 33645961330 scopus 로고    scopus 로고
    • Flexible protein-protein docking
    • Bonvin AM. Flexible protein-protein docking. Curr Opin Struct Biol 2006;16:194-200.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 194-200
    • Bonvin, A.M.1
  • 48
    • 48449094112 scopus 로고    scopus 로고
    • Conformer selection and induced fit in flexible backbone protein-protein docking using computational and NMR ensembles
    • Chaudhury S, Gray JJ. Conformer selection and induced fit in flexible backbone protein-protein docking using computational and NMR ensembles. J Mol Biol 2008;381:1068-1087.
    • (2008) J Mol Biol , vol.381 , pp. 1068-1087
    • Chaudhury, S.1    Gray, J.J.2
  • 49
    • 51649094321 scopus 로고    scopus 로고
    • Built-in loops allow versatility in domain-domain interactions: Lessons from self-interacting domains
    • Akiva E, Itzhaki Z, Margalit H. Built-in loops allow versatility in domain-domain interactions: lessons from self-interacting domains. Proc Natl Acad Sci USA 2008;105:13292-13297.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 13292-13297
    • Akiva, E.1    Itzhaki, Z.2    Margalit, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.