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Volumn 31, Issue 7, 2014, Pages 1787-1792

Why human disease-associated residues appear as the wild-type in other species: Genome-scale structural evidence for the compensation hypothesis

Author keywords

disease mutation; epistasis; evolution; intramolecular interaction; protein stability

Indexed keywords

AMINO ACID; PROTEIN;

EID: 84903742512     PISSN: 07374038     EISSN: 15371719     Source Type: Journal    
DOI: 10.1093/molbev/msu130     Document Type: Article
Times cited : (21)

References (28)
  • 3
    • 37549024654 scopus 로고    scopus 로고
    • The protein data bank: A historical perspective
    • Berman HM. 2008. The Protein Data Bank: A historical perspective. Acta Crystallogr A. 64:88-95.
    • (2008) Acta Crystallogr A. , vol.64 , pp. 88-95
    • Berman, H.M.1
  • 5
    • 66149185556 scopus 로고    scopus 로고
    • Compensatory mutations are repeatable and clustered within proteins
    • Davis BH, Poon AF, Whitlock MC. 2009. Compensatory mutations are repeatable and clustered within proteins. Proc Biol Sci. 276: 1823-1827.
    • (2009) Proc Biol Sci. , vol.276 , pp. 1823-1827
    • Davis, B.H.1    Poon, A.F.2    Whitlock, M.C.3
  • 6
    • 0000228203 scopus 로고
    • A model of evolutionary change in proteins
    • DathoffMO, editor. Atlas of protein sequence and structure. Silver Spring (MD)
    • Dayhoff MO, Schwartz R, Orcutt BC. 1978. A model of evolutionary change in proteins. In: DathoffMO, editor. Atlas of protein sequence and structure. Silver Spring (MD): National Biomedical Research Foundation. p. 345-352.
    • (1978) National Biomedical Research Foundation. , pp. 345-352
    • Dayhoff, M.O.1    Schwartz, R.2    Orcutt, B.C.3
  • 8
    • 33751541671 scopus 로고    scopus 로고
    • Characterization of compensated mutations in terms of structural and physico-chemical properties
    • DOI 10.1016/j.jmb.2006.09.053, PII S0022283606012770
    • Ferrer-Costa C, Orozco M, de la Cruz X. 2007. Characterization of compensated mutations in terms of structural and physico-chemical properties. J Mol Biol. 365:249-256. (Pubitemid 44830033)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.1 , pp. 249-256
    • Ferrer-Costa, C.1    Orozco, M.2    Cruz, X.D.L.3
  • 9
    • 0345293158 scopus 로고    scopus 로고
    • Why are some human disease-Associated mutations fixed in mice?
    • Gao L, Zhang J. 2003. Why are some human disease-Associated mutations fixed in mice? Trends Genet. 19:678-681.
    • (2003) Trends Genet. , vol.19 , pp. 678-681
    • Gao, L.1    Zhang, J.2
  • 10
    • 0036291145 scopus 로고    scopus 로고
    • Predicting changes in the stability of proteins and protein complexes: A study of more than 10000 mutations
    • Guerois R, Nielsen JE, Serrano L 2002. Predicting changes in the stability of proteins and protein complexes: A study of more than 10000 mutations. J Mol Biol. 320:369-387.
    • (2002) J Mol Biol. , vol.320 , pp. 369-387
    • Guerois, R.1    Nielsen, J.E.2    Serrano, L.3
  • 11
    • 79551470095 scopus 로고    scopus 로고
    • Role of conformational sampling in computing mutation-induced changes in protein structure and stability
    • Kellogg EH, Leaver-Fay A, Baker D. 2011. Role of conformational sampling in computing mutation-induced changes in protein structure and stability. Proteins 79:830-838.
    • (2011) Proteins , vol.79 , pp. 830-838
    • Kellogg, E.H.1    Leaver-Fay, A.2    Baker, D.3
  • 12
    • 77952706843 scopus 로고    scopus 로고
    • Performance of protein stability predictors
    • Khan S, Vihinen M. 2010. Performance of protein stability predictors. Hum Mutat. 31:675-684.
    • (2010) Hum Mutat. , vol.31 , pp. 675-684
    • Khan, S.1    Vihinen, M.2
  • 14
    • 9444269272 scopus 로고    scopus 로고
    • Compensated deleterious mutations in insect ganomes
    • DOI 10.1126/science.1100522
    • Kulathinal RJ, Bettencourt BR, Hartl DL. 2004. Compensated deleterious mutations in insect genomes. Science 306:1553-1554. (Pubitemid 39564950)
    • (2004) Science , vol.306 , Issue.5701 , pp. 1553-1554
    • Kulathinal, R.J.1    Bettencourt, B.R.2    Hartl, D.L.3
  • 17
    • 0024792699 scopus 로고
    • Genetic analysis of protein stability and function
    • Pakula AA, Sauer RT. 1989. Genetic analysis of protein stability and function. Annu Rev Genet. 23:289-310. (Pubitemid 20033405)
    • (1989) Annual Review of Genetics , vol.23 , pp. 289-310
    • Pakula, A.A.1    Sauer, R.T.2
  • 18
    • 21044440015 scopus 로고    scopus 로고
    • The coupon collector and the suppressor mutation: Estimating the number of compensatory mutations by maximum likelihood
    • DOI 10.1534/genetics.104.037259
    • Poon A, Davis BH, Chao L. 2005. The coupon collector and the suppressor mutation: Estimating the number of compensatory mutations by maximum likelihood. Genetics 170:1323-1332. (Pubitemid 41105485)
    • (2005) Genetics , vol.170 , Issue.3 , pp. 1323-1332
    • Poon, A.1    Davis, B.H.2    Chao, L.3
  • 22
    • 84868133037 scopus 로고    scopus 로고
    • Assessing predictors of changes in protein stability upon mutation using self-consistency
    • Thiltgen G, Goldstein RA. 2012. Assessing predictors of changes in protein stability upon mutation using self-consistency. PLoS One 7: E46084.
    • (2012) PLoS One , vol.7
    • Thiltgen, G.1    Goldstein, R.A.2
  • 23
    • 70349901079 scopus 로고    scopus 로고
    • Stability effects of mutations and protein evolvability
    • Tokuriki N, Tawfik DS. 2009. Stability effects of mutations and protein evolvability. Curr Opin Struct Biol. 19:596-604.
    • (2009) Curr Opin Struct Biol. , vol.19 , pp. 596-604
    • Tokuriki, N.1    Tawfik, D.S.2
  • 24
    • 78651319979 scopus 로고    scopus 로고
    • Ongoing and future developments at the Universal Protein Resource
    • UniProt Consortium.
    • UniProt Consortium. 2011. Ongoing and future developments at the Universal Protein Resource. Nucleic Acids Res. 39:D214-D219.
    • (2011) Nucleic Acids Res. , vol.39
  • 27
    • 25144523127 scopus 로고    scopus 로고
    • Loss of protein structure stability as a major causative factor in monogenic disease
    • DOI 10.1016/j.jmb.2005.08.020, PII S0022283605009575
    • Yue P, Li Z, Moult J. 2005. Loss of protein structure stability as a major causative factor in monogenic disease. J Mol Biol. 353:459-473. (Pubitemid 41356624)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.2 , pp. 459-473
    • Yue, P.1    Li, Z.2    Moult, J.3
  • 28
    • 0033921902 scopus 로고    scopus 로고
    • Rates of conservative and radical nonsynonymous nucleotide substitutions in mammalian nuclear genes
    • Zhang J. 2000. Rates of conservative and radical nonsynonymous nucleotide substitutions in mammalian nuclear genes. J Mol Evol. 50: 56-68. (Pubitemid 30430003).
    • (2000) Journal of Molecular Evolution , vol.50 , Issue.1 , pp. 56-68
    • Zhang, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.