메뉴 건너뛰기




Volumn 29, Issue 19, 2013, Pages 2512-2514

CoDNaS: A database of conformational diversity in the native state of proteins

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND; PROTEIN;

EID: 84897366399     PISSN: 13674803     EISSN: 14602059     Source Type: Journal    
DOI: 10.1093/bioinformatics/btt405     Document Type: Article
Times cited : (28)

References (22)
  • 1
    • 0025183708 scopus 로고
    • Basic local alignment search tool
    • Altschul,S.F. et al. (1990) Basic local alignment search tool. J. Mol. Biol., 215, 403-410.
    • (1990) J. Mol. Biol. , vol.215 , pp. 403-410
    • Altschul, S.F.1
  • 2
    • 0034069495 scopus 로고    scopus 로고
    • Gene ontology: Tool for the unification of biology
    • Ashburner,M. et al. (2000) Gene ontology: tool for the unification of biology. The Gene Ontology Consortium. Nat. Genet., 25, 25-29.
    • (2000) The Gene Ontology Consortium. Nat. Genet. , vol.25 , pp. 25-29
    • Ashburner, M.1
  • 3
    • 0033954256 scopus 로고    scopus 로고
    • The protein data bank
    • Berman,H.M. (2000) The protein data bank. Nucleic Acids Res., 28, 235-242.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 235-242
    • Berman, H.M.1
  • 4
    • 33746652529 scopus 로고    scopus 로고
    • Relation between native ensembles and experimental structures of proteins
    • Best,R.B. et al. (2006) Relation between native ensembles and experimental structures of proteins. Proc. Natl Acad. Sci. USA, 103, 10901-10906.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 10901-10906
    • Best, R.B.1
  • 5
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • Boehr,D.D. et al. (2010) The role of dynamic conformational ensembles in biomolecular recognition. Nat. Chem. Biol., 5, 789-796.
    • (2010) Nat. Chem. Biol. , vol.5 , pp. 789-796
    • Boehr, D.D.1
  • 6
    • 84865129593 scopus 로고    scopus 로고
    • MobiDB: A comprehensive database of intrinsic protein disorder annotations
    • Di Domenico,T. et al. (2012) MobiDB: a comprehensive database of intrinsic protein disorder annotations. Bioinformatics, 28, 2080-2081.
    • (2012) Bioinformatics , vol.28 , pp. 2080-2081
    • Di Domenico, T.1
  • 7
    • 33846033844 scopus 로고    scopus 로고
    • The CATH domain structure database: New protocols and classification levels give a more comprehensive resource for exploring evolution
    • Greene,L.H. et al. (2007) The CATH domain structure database: new protocols and classification levels give a more comprehensive resource for exploring evolution. Nucleic Acids Res., 35, D291-D297.
    • (2007) Nucleic Acids Res. , vol.35
    • Greene, L.H.1
  • 8
    • 66449084442 scopus 로고    scopus 로고
    • Infrastructure for the life sciences: Design and implementation of the UniProt website
    • Jain,E. et al. (2009) Infrastructure for the life sciences: design and implementation of the UniProt website. BMC Bioinformatics, 10, 136.
    • (2009) BMC Bioinformatics , vol.10 , pp. 136
    • Jain, E.1
  • 9
    • 84868020188 scopus 로고    scopus 로고
    • On the effect of protein conformation diversity in discriminating among neutral and disease related single amino acid substitutions
    • Juritz,E. et al. (2012) On the effect of protein conformation diversity in discriminating among neutral and disease related single amino acid substitutions. BMC Genomics, 13 (Suppl. 4), S5.
    • (2012) BMC Genomics , vol.13 , Issue.SUPPL. 4
    • Juritz, E.1
  • 10
    • 84871839239 scopus 로고    scopus 로고
    • Protein conformational diversity modulates sequence divergence
    • Juritz,E. et al. (2013) Protein conformational diversity modulates sequence divergence. Mol. Biol. Evol., 30, 79-87.
    • (2013) Mol. Biol. Evol. , vol.30 , pp. 79-87
    • Juritz, E.1
  • 11
    • 78651327630 scopus 로고    scopus 로고
    • PCDB: A database of protein conformational diversity
    • Juritz,E.I. et al. (2011) PCDB: a database of protein conformational diversity. Nucleic Acids Res., 39, D475-D479.
    • (2011) Nucleic Acids Res. , vol.39
    • Juritz, E.I.1
  • 12
    • 11444249446 scopus 로고    scopus 로고
    • Computational assignment of the EC numbers for genomicscale analysis of enzymatic reactions
    • Kotera,M. et al. (2004) Computational assignment of the EC numbers for genomicscale analysis of enzymatic reactions. J. Am. Chem. Soc., 126, 16487-16498.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 16487-16498
    • Kotera, M.1
  • 13
    • 0033970020 scopus 로고    scopus 로고
    • Folding and binding cascades: Dynamic landscapes and population shifts
    • Kumar,S. et al. (2000) Folding and binding cascades: dynamic landscapes and population shifts. Protein Sci., 9, 10-19.
    • (2000) Protein Sci. , vol.9 , pp. 10-19
    • Kumar, S.1
  • 14
    • 84879327937 scopus 로고    scopus 로고
    • Exploiting conformational ensembles in modeling protein-protein interactions on the proteome scale
    • Kuzu,G. et al. (2013) Exploiting conformational ensembles in modeling protein-protein interactions on the proteome scale. J. Proteome Res., 12, 2641-2653.
    • (2013) J. Proteome Res. , vol.12 , pp. 2641-2653
    • Kuzu, G.1
  • 15
    • 0000009443 scopus 로고
    • Rapid comparison of protein structures
    • McLachlan,A.D. (1982) Rapid comparison of protein structures. Acta Crystallogr. A, 38, 871-873.
    • (1982) Acta Crystallogr. A , vol.38 , pp. 871-873
    • McLachlan, A.D.1
  • 16
    • 84856078561 scopus 로고    scopus 로고
    • Protein dynamics and conformational selection in bidirectional signal transduction
    • Nussinov,R. and Ma,B. (2012) Protein dynamics and conformational selection in bidirectional signal transduction. BMC Biol., 10, 2.
    • (2012) BMC Biol. , vol.10 , pp. 2
    • Nussinov, R.1    Ma, B.2
  • 17
    • 0036839162 scopus 로고    scopus 로고
    • MAMMOTH (matching molecular models obtained from theory): An automated method for model comparison
    • Ortiz,A.R. et al. (2002) MAMMOTH (matching molecular models obtained from theory): an automated method for model comparison. Protein Sci., 11, 2606-2621.
    • (2002) Protein Sci. , vol.11 , pp. 2606-2621
    • Ortiz, A.R.1
  • 18
    • 84864000092 scopus 로고    scopus 로고
    • Generation of receptor structural ensembles for virtual screening using binding site shape analysis and clustering
    • Osguthorpe,D.J. et al. (2012) Generation of receptor structural ensembles for virtual screening using binding site shape analysis and clustering. Chem Biol Drug Des., 80, 182-193.
    • (2012) Chem Biol Drug Des. , vol.80 , pp. 182-193
    • Osguthorpe, D.J.1
  • 19
    • 84872145488 scopus 로고    scopus 로고
    • Molecular dynamics simulations provide atomistic insight into hydrogen exchange mass spectrometry experiments
    • Petruk,A.A. et al. (2013) Molecular dynamics simulations provide atomistic insight into hydrogen exchange mass spectrometry experiments. J. Chem. Theory Comput., 9, 658-669.
    • (2013) J. Chem. Theory Comput. , vol.9 , pp. 658-669
    • Petruk, A.A.1
  • 20
    • 0033056708 scopus 로고    scopus 로고
    • Folding funnels, binding funnels, and protein function
    • Tsai,C.J. et al. (1999) Folding funnels, binding funnels, and protein function. Protein Sci., 8, 1181-1190.
    • (1999) Protein Sci. , vol.8 , pp. 1181-1190
    • Tsai, C.J.1
  • 21
    • 13444288174 scopus 로고    scopus 로고
    • E-MSD: An integrated data resource for bioinformatics
    • Velankar,S. et al. (2005) E-MSD: an integrated data resource for bioinformatics. Nucleic Acids Res., 33, D262-D265.
    • (2005) Nucleic Acids Res. , vol.33
    • Velankar, S.1
  • 22
    • 10344232638 scopus 로고    scopus 로고
    • Scoring function for automated assessment of protein structure template quality
    • Zhang,Y. and Skolnick,J. (2004) Scoring function for automated assessment of protein structure template quality. Proteins, 57, 702-710.
    • (2004) Proteins , vol.57 , pp. 702-710
    • Zhang, Y.1    Skolnick, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.