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Volumn 21, Issue 10, 2005, Pages 2539-2540

CoC: A database of universally conserved residues in protein folds

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CONSERVATISM OF CONSERVATISM; DATA ANALYSIS; PRIORITY JOURNAL; PROTEIN DATABASE; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; STATISTICAL ANALYSIS;

EID: 19544385993     PISSN: 13674803     EISSN: 13674811     Source Type: Journal    
DOI: 10.1093/bioinformatics/bti360     Document Type: Article
Times cited : (10)

References (10)
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  • 2
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    • Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism
    • Fersht,A.R. (2000) Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism. Proc. Natl Acad. Sci. USA, 97, 1525-1529.
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    • Fersht, A.R.1
  • 3
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    • Mapping the protein universe
    • Holm,L. and Sander,C. (1996) Mapping the protein universe. Science, 273, 595-603.
    • (1996) Science , vol.273 , pp. 595-603
    • Holm, L.1    Sander, C.2
  • 4
    • 0030334834 scopus 로고    scopus 로고
    • Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2
    • Lopez-Hernandez,E. and Serrano,L. (1996) Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2. Fold. Des., 1, 43-55.
    • (1996) Fold. Des. , vol.1 , pp. 43-55
    • Lopez-Hernandez, E.1    Serrano, L.2
  • 5
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt,E.A. and Bacon,D.J. (1997) Raster3D: photorealistic molecular graphics. Meth. Enzymol., 277, 505-524.
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    • Merritt, E.A.1    Bacon, D.J.2
  • 6
    • 0345062357 scopus 로고    scopus 로고
    • Universally conserved positions in protein folds; reading evolutionary, folding kinetics and function
    • Mirny,L.A. and Shakhnovich,E.I. (1999) Universally conserved positions in protein folds; reading evolutionary, folding kinetics and function. J. Mol. Biol., 291, 177-196.
    • (1999) J. Mol. Biol. , vol.291 , pp. 177-196
    • Mirny, L.A.1    Shakhnovich, E.I.2
  • 7
    • 0034984144 scopus 로고    scopus 로고
    • Protein folding theory: From lattice to all-atom models
    • Mirny,L. and Shakhnovich,E. (2001a) Protein folding theory: from lattice to all-atom models. Annu. Rev. Biophys. Biomol. Struct., 30, 361-396.
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 361-396
    • Mirny, L.1    Shakhnovich, E.2
  • 8
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    • Evolutionary conservation of the folding nucleus
    • Mirny,L. and Shakhnovich,E. (2001b) Evolutionary conservation of the folding nucleus. J. Mol. Biol., 308, 123-129.
    • (2001) J. Mol. Biol. , vol.308 , pp. 123-129
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  • 9
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    • (2004) J. Chem. Inf. Comput. Sci. , vol.44 , pp. 462-469
    • Murray-Rust, P.1
  • 10
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    • Database of homology-derived protein structures and the structural meaning of sequence alignment
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.