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Volumn 32, Issue DATABASE ISS., 2004, Pages

HOMSTRAD: Recent developments of the Homologous Protein Structure Alignment Database

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID;

EID: 0346494946     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (85)

References (20)
  • 1
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    • HOMSTRAD: A database of protein structure alignments for homologous families
    • Mizuguchi,K., Deane,C.M., Blundell,T.L. and Overington,J.P. (1998) HOMSTRAD: A database of protein structure alignments for homologous families. Protein Sci., 7, 2469-2471.
    • (1998) Protein Sci. , vol.7 , pp. 2469-2471
    • Mizuguchi, K.1    Deane, C.M.2    Blundell, T.L.3    Overington, J.P.4
  • 4
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi,J., Blundell,T.L. and Mizuguchi,K. (2001) FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J. Mol. Biol., 310, 243-257.
    • (2001) J. Mol. Biol. , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 6
    • 0034695422 scopus 로고    scopus 로고
    • The tertiary structure at 1.59 Å resolution and the proposed amino acid sequence of a family-11 xylanase from the thermophilic fungus Paecilomyces varioti bainier
    • Kumar,P.R., Eswaramoorthy,S., Vithayathil,P.J. and Viswamitra,M.A. (2000) The tertiary structure at 1.59 Å resolution and the proposed amino acid sequence of a family-11 xylanase from the thermophilic fungus Paecilomyces varioti bainier. J. Mol. Biol., 295, 581-593.
    • (2000) J. Mol. Biol. , vol.295 , pp. 581-593
    • Kumar, P.R.1    Eswaramoorthy, S.2    Vithayathil, P.J.3    Viswamitra, M.A.4
  • 7
    • 0033229863 scopus 로고    scopus 로고
    • Fix L, a haemoglobin that acts as an oxygen sensor: Signalling mechanism and structural basis of its homology with PAS domains
    • Perutz,M.F., Paoli,M. and Lesk,A.M. (1999) Fix L, a haemoglobin that acts as an oxygen sensor: signalling mechanism and structural basis of its homology with PAS domains. Chem. Biol., 6, R291-297.
    • (1999) Chem. Biol. , vol.6
    • Perutz, M.F.1    Paoli, M.2    Lesk, A.M.3
  • 8
    • 0027062943 scopus 로고
    • Environment-specific amino acid substitution tables: Tertiary templates and prediction of protein folds
    • Overington,J., Donnelly,D., Johnson,M.S., Sali,A. and Blundell,T.L. (1992) Environment-specific amino acid substitution tables: tertiary templates and prediction of protein folds. Protein Sci., 1, 216-226.
    • (1992) Protein Sci. , vol.1 , pp. 216-226
    • Overington, J.1    Donnelly, D.2    Johnson, M.S.3    Sali, A.4    Blundell, T.L.5
  • 9
    • 0032988850 scopus 로고    scopus 로고
    • BAliBASE: A benchmark alignment database for the evaluation of multiple alignment programs
    • Thompson,J.D., Plewniak,F. and Poch,O. (1999) BAliBASE: a benchmark alignment database for the evaluation of multiple alignment programs. Bioinformatics, 15, 87-88.
    • (1999) Bioinformatics , vol.15 , pp. 87-88
    • Thompson, J.D.1    Plewniak, F.2    Poch, O.3
  • 10
    • 0035222012 scopus 로고    scopus 로고
    • A new algorithm for the alignment of multiple protein structures using Monte Carlo optimization
    • Guda,C., Scheeff,E.D., Bourne,P.E. and Shindyalov,I.N. (2001) A new algorithm for the alignment of multiple protein structures using Monte Carlo optimization. Pac. Symp. Biocomput., 6, 275-286.
    • (2001) Pac. Symp. Biocomput. , vol.6 , pp. 275-286
    • Guda, C.1    Scheeff, E.D.2    Bourne, P.E.3    Shindyalov, I.N.4
  • 17
    • 0025317502 scopus 로고
    • Definition of general topological equivalence in protein structures. A procedure involving comparison of properties and relationships through simulated annealing and dynamic programming
    • Sali,A. and Blundell,T.L. (1990) Definition of general topological equivalence in protein structures. A procedure involving comparison of properties and relationships through simulated annealing and dynamic programming. J. Mol. Biol., 212, 403-428.
    • (1990) J. Mol. Biol. , vol.212 , pp. 403-428
    • Sali, A.1    Blundell, T.L.2
  • 18
    • 0034459679 scopus 로고    scopus 로고
    • Evolutionary trace analysis of TGF-beta and related growth factors: Implications for site-directed mutagenesis
    • Innis,C.A., Shi,J. and Blundell,T.L. (2000) Evolutionary trace analysis of TGF-beta and related growth factors: implications for site-directed mutagenesis. Protein Eng., 13, 839-847.
    • (2000) Protein Eng. , vol.13 , pp. 839-847
    • Innis, C.A.1    Shi, J.2    Blundell, T.L.3
  • 19
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson,J.D., Higgins,D.G. and Gibson,T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.