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Volumn 2003-January, Issue , 2003, Pages 161-170

Database support for 3D-protein data set analysis

Author keywords

Amino acids; Association rules; Bioinformatics; Data analysis; Database systems; Genomics; Proteins; Relational databases; Spatial databases; Yarn

Indexed keywords

AMINO ACIDS; ASSOCIATION RULES; BIOINFORMATICS; DATA REDUCTION; DATABASE SYSTEMS; MANAGEMENT INFORMATION SYSTEMS; PROTEINS; YARN;

EID: 33750845464     PISSN: 10993371     EISSN: None     Source Type: Conference Proceeding    
DOI: 10.1109/SSDM.2003.1214977     Document Type: Conference Paper
Times cited : (4)

References (14)
  • 3
    • 0031576989 scopus 로고    scopus 로고
    • Homology modeling with a backbone-dependent rotamer library
    • M. Bower, F. Cohen, and R. Dunbrack. Homology modeling with a backbone-dependent rotamer library. J. Mol. Biol., 267:1268-1282, 1997.
    • (1997) J. Mol. Biol. , vol.267 , pp. 1268-1282
    • Bower, M.1    Cohen, F.2    Dunbrack, R.3
  • 4
    • 0014885326 scopus 로고
    • Studies on the conformation of amino acids. Xi. Analysis of the observed side group conformations in proteins
    • R. Chandrasekaran and G. Ramachandran. Studies on the conformation of amino acids. xi. analysis of the observed side group conformations in proteins. Int. J. Pept. Prot. Res., 2:223-233, 1970.
    • (1970) Int. J. Pept. Prot. Res. , vol.2 , pp. 223-233
    • Chandrasekaran, R.1    Ramachandran, G.2
  • 5
    • 1842326139 scopus 로고    scopus 로고
    • Bayesian statistical analysis of protein side-chain rotamer preferences
    • R. Dunbrack and F. Cohen. Bayesian statistical analysis of protein side-chain rotamer preferences. Protein Sci., 6:1661-1681, 1997.
    • (1997) Protein Sci. , vol.6 , pp. 1661-1681
    • Dunbrack, R.1    Cohen, F.2
  • 8
    • 0020685129 scopus 로고
    • Structure and refinement of penicillo-pepsin at 1.8 a resolution
    • M. James and A. Sielecki. Structure and refinement of penicillo-pepsin at 1.8 a resolution. J. Mol. Biol., 125:299-361, 1983.
    • (1983) J. Mol. Biol. , vol.125 , pp. 299-361
    • James, M.1    Sielecki, A.2
  • 9
    • 0030000912 scopus 로고    scopus 로고
    • Improving the quality of nmr and crystallographic protein structures by means of conformational database potential derived from structure databases
    • J. Kuszewski, A. Gronenborn, and G. Clore. Improving the quality of nmr and crystallographic protein structures by means of conformational database potential derived from structure databases. Protein Sci., 5:1067-1080, 1996.
    • (1996) Protein Sci. , vol.5 , pp. 1067-1080
    • Kuszewski, J.1    Gronenborn, A.2    Clore, G.3
  • 11
    • 0023521842 scopus 로고
    • Analysis of the relationship between side-chain conformation and secondary structure in globular proteins
    • M. MCGregor, S. Islam, and M. Sternberg. Analysis of the relationship between side-chain conformation and secondary structure in globular proteins. J. Mol. Biol., 198:295-310, 1987.
    • (1987) J. Mol. Biol. , vol.198 , pp. 295-310
    • MCGregor, M.1    Islam, S.2    Sternberg, M.3
  • 14
    • 57749091666 scopus 로고    scopus 로고
    • Ffs - An i/o-efficient algorithm for mining frequent sequences
    • Knowledge Discovery and Data Mining - PAKDD 2001, 5th Pacific-Asia Conference, Hong Kong, China, April 16-18, 2001, Proceedings, Springer
    • M. Zhang, B. Kao, C. L. Yip, and D. W.-L. Cheung. Ffs - an i/o-efficient algorithm for mining frequent sequences. In Knowledge Discovery and Data Mining - PAKDD 2001, 5th Pacific-Asia Conference, Hong Kong, China, April 16-18, 2001, Proceedings, volume 2035 of Lecture Notes in Computer Science, pages 294-305. Springer, 2001.
    • (2001) Lecture Notes in Computer Science , vol.2035 , pp. 294-305
    • Zhang, M.1    Kao, B.2    Yip, C.L.3    Cheung, D.W.-L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.