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Volumn 15, Issue 6, 1999, Pages 480-500

A comparison of sequence and structure protein domain families as a basis for structural genomics

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; FUNGAL PROTEIN; MEMBRANE PROTEIN;

EID: 0032787618     PISSN: 13674803     EISSN: 13674811     Source Type: Journal    
DOI: 10.1093/bioinformatics/15.6.480     Document Type: Article
Times cited : (49)

References (29)
  • 1
    • 0003698705 scopus 로고
    • Data Commission of the international union of crystallography
    • Allen, F.H., Bergerhoff, G. and Sievers, R. (eds), Data Commission of the International Union of Crystallography, Bonn/Cambridge/Chester
    • Abola, E., Bernstein, F.C., Bryant, S.H., Koetzle, T.F. and Weng, J. (1987) Data Commission of the international union of crystallography. In Allen, F.H., Bergerhoff, G. and Sievers, R. (eds), Data-bases-Information Content, Software Systems, Scientific Applications, Protein Data Bank. Data Commission of the International Union of Crystallography, Bonn/Cambridge/Chester, pp. 107-132.
    • (1987) Data-bases-Information Content, Software Systems, Scientific Applications, Protein Data Bank , pp. 107-132
    • Abola, E.1    Bernstein, F.C.2    Bryant, S.H.3    Koetzle, T.F.4    Weng, J.5
  • 2
    • 0029916911 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence data bank and its new supplement TREMBL
    • Bairoch, A. and Apweiler, R. (1996) The SWISS-PROT protein sequence data bank and its new supplement TREMBL. Nucleic Acids Res., 24, 17-21.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 17-21
    • Bairoch, A.1    Apweiler, R.2
  • 9
    • 0031000180 scopus 로고    scopus 로고
    • The first genome from the third domain of life
    • Clayton, R.A., White, O., Ketchum, K.A. and Venter, J.C. (1997) The first genome from the third domain of life. Nature, 387, 459-462.
    • (1997) Nature , vol.387 , pp. 459-462
    • Clayton, R.A.1    White, O.2    Ketchum, K.A.3    Venter, J.C.4
  • 10
    • 0031696078 scopus 로고    scopus 로고
    • New insights into microtubule structure and function from the atomic model of tubulin
    • Downing, K.H. and Nogales, E. (1998) New insights into microtubule structure and function from the atomic model of tubulin. Eur. Biophys. J., 27, 431-436.
    • (1998) Eur. Biophys. J. , vol.27 , pp. 431-436
    • Downing, K.H.1    Nogales, E.2
  • 12
    • 0025753142 scopus 로고
    • Similarity of the three-dimensional structures of actin and the atpase fragment of a 70-kda heat shock cognate protein
    • Flaherty, K., McKay, D., Kabsch, W. and Holmes, K. (1991) Similarity of the three-dimensional structures of actin and the atpase fragment of a 70-kda heat shock cognate protein. Proc. Natl Acad. Sci. USA, 88, 5041-5045.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 5041-5045
    • Flaherty, K.1    McKay, D.2    Kabsch, W.3    Holmes, K.4
  • 13
    • 0030764671 scopus 로고    scopus 로고
    • Protein structural classes in five complete genomes
    • Frishman, D. and Mewes, H.W. (1997) Protein structural classes in five complete genomes. Nature Struct. Biol., 4, 626-628.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 626-628
    • Frishman, D.1    Mewes, H.W.2
  • 15
    • 0029785147 scopus 로고    scopus 로고
    • 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
  • 16
    • 0030765455 scopus 로고    scopus 로고
    • Dali/FSSP classification of three-dimensional protein folds
    • Holm, L. and Sander, C. (1997) Dali/FSSP classification of three-dimensional protein folds. Nucleic Acids Res., 25, 231-234.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 231-234
    • Holm, L.1    Sander, C.2
  • 18
    • 0031547967 scopus 로고    scopus 로고
    • Global self-organization of all known protein sequences reveals inherent biological signatures
    • Linial, M., Linial, N., Tishby, N. and Yona, G. (1997) Global self-organization of all known protein sequences reveals inherent biological signatures. J. Mol. Biol., 268, 539-556.
    • (1997) J. Mol. Biol. , vol.268 , pp. 539-556
    • Linial, M.1    Linial, N.2    Tishby, N.3    Yona, G.4
  • 19
    • 0000925139 scopus 로고
    • Calculation of the structures of collagen models role of interchain interactions in determining the triple-helical coiled-coil conformation. I
    • Miller, M.H. and Scheraga, H.A. (1976) Calculation of the structures of collagen models role of interchain interactions in determining the triple-helical coiled-coil conformation. I. J. Polym. Sci., 54, 171.
    • (1976) J. Polym. Sci. , vol.54 , pp. 171
    • Miller, M.H.1    Scheraga, H.A.2
  • 20
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A.G., Brenner, S.E., Hubbard, T. and Chothia, C. (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol. Biol., 247, 536-540.
    • (1995) J Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 22
    • 0023989064 scopus 로고
    • Improved tools for biological sequence analysis
    • Pearson, W.R. and Lipman, D.J. (1988) Improved tools for biological sequence analysis. Proc. Natl Acad. Sci. USA, 85, 2444-2448.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 23
    • 0028218683 scopus 로고
    • Modular arrangement of proteins as inferred from analysis of homology
    • Sonnhammer, E.L. and Kahn, D. (1994) Modular arrangement of proteins as inferred from analysis of homology. Protein Sci., 3, 482-492.
    • (1994) Protein Sci. , vol.3 , pp. 482-492
    • Sonnhammer, E.L.1    Kahn, D.2
  • 24
    • 0030925920 scopus 로고    scopus 로고
    • Pfam: A comprehensive database of protein domain families based on seed alignments
    • Sonnhammer, E.L., Eddy, S.R. and Durbin, R. (1997) Pfam: a comprehensive database of protein domain families based on seed alignments. Proteins. Structure Function and Genetics, 28, 405-420.
    • (1997) Proteins. Structure Function and Genetics , vol.28 , pp. 405-420
    • Sonnhammer, E.L.1    Eddy, S.R.2    Durbin, R.3
  • 25
  • 27
    • 0030111235 scopus 로고    scopus 로고
    • Metabolism and evolution of Haemophilus influenzae deduced from a whole-genome comparison with Escherichia coli
    • Tatusov, R.L., Mushegian, A.R., Bork, P., Brown, N.P., Hayes, W.S., Borodovsky, M. and Rudd, K.E. (1996) Metabolism and evolution of Haemophilus influenzae deduced from a whole-genome comparison with Escherichia coli. Curr. Biol., 6, 279-291.
    • (1996) Curr. Biol. , vol.6 , pp. 279-291
    • Tatusov, R.L.1    Mushegian, A.R.2    Bork, P.3    Brown, N.P.4    Hayes, W.S.5    Borodovsky, M.6    Rudd, K.E.7
  • 28
    • 0028501914 scopus 로고
    • Non-globular domains in protein sequences: Automated segmentation using complexity measures
    • Wootton, J.C. (1994) Non-globular domains in protein sequences: automated segmentation using complexity measures. Comput Chem., 18, 268-285.
    • (1994) Comput Chem. , vol.18 , pp. 268-285
    • Wootton, J.C.1
  • 29
    • 0029933832 scopus 로고    scopus 로고
    • Motif identification neural design for rapid and sensitive protein family search
    • Wu, C.H., Zhao, S., Chen, H.L., Lo, C.J. and McLarty, J. (1996) Motif identification neural design for rapid and sensitive protein family search. Comput. Applic. Biosci., 12, 109-118.
    • (1996) Comput. Applic. Biosci. , vol.12 , pp. 109-118
    • Wu, C.H.1    Zhao, S.2    Chen, H.L.3    Lo, C.J.4    McLarty, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.