메뉴 건너뛰기




Volumn 24, Issue 3, 2008, Pages 426-427

A note on difficult structure alignment problems

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; COMPUTER PROGRAM; INTERNET; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; STRUCTURAL BIOINFORMATICS; STRUCTURAL HOMOLOGY; STRUCTURE ANALYSIS; TOPMATCH;

EID: 38849092210     PISSN: 13674803     EISSN: 14602059     Source Type: Journal    
DOI: 10.1093/bioinformatics/btm622     Document Type: Article
Times cited : (109)

References (9)
  • 1
    • 38549153238 scopus 로고    scopus 로고
    • Data growth and its impact on the SCOP database: New developments
    • doi:10.1093/nar/ gkm993
    • Andreeva,A. et al. (2007) Data growth and its impact on the SCOP database: New developments. Nucleic Acids Res., doi:10.1093/nar/ gkm993.
    • (2007) Nucleic Acids Res
    • Andreeva, A.1
  • 2
    • 0033954256 scopus 로고    scopus 로고
    • The Protein Data Bank
    • Berman,H.M. et al. (2000) The Protein Data Bank. Nucleic Acids Res., 28, 235-242.
    • (2000) Nucleic Acids Res , vol.28 , pp. 235-242
    • Berman, H.M.1
  • 3
    • 0030334647 scopus 로고    scopus 로고
    • Optimum superimposition of protein structures: Ambiguities and implications
    • Feng,Z.K. and Sippl,M.I. (1996) Optimum superimposition of protein structures: Ambiguities and implications. Fold. Des., 1, 123-132.
    • (1996) Fold. Des , vol.1 , pp. 123-132
    • Feng, Z.K.1    Sippl, M.I.2
  • 4
    • 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
  • 5
    • 13444279981 scopus 로고    scopus 로고
    • Comprehensive evaluation of protein structure alignment methods: Scoring by geometric measures
    • Kolodny,R. et al. (2005) Comprehensive evaluation of protein structure alignment methods: Scoring by geometric measures. J. Mol. Biol., 346, 1173-1188.
    • (2005) J. Mol. Biol , vol.346 , pp. 1173-1188
    • Kolodny, R.1
  • 6
    • 0033835533 scopus 로고    scopus 로고
    • Structure-derived substitution matrices for alignment of distantly related sequepoes
    • Prlic,A. et al. (2000) Structure-derived substitution matrices for alignment of distantly related sequepoes. Protein Eng., 13, 545-550.
    • (2000) Protein Eng , vol.13 , pp. 545-550
    • Prlic, A.1
  • 7
    • 0035755109 scopus 로고    scopus 로고
    • Assessment of the CASP4 Fold Recognition Category
    • Sippl,M.J. et al. (2001) Assessment of the CASP4 Fold Recognition Category. Proteins, 45, 55-67.
    • (2001) Proteins , vol.45 , pp. 55-67
    • Sippl, M.J.1
  • 8
    • 34547589581 scopus 로고    scopus 로고
    • QSCOP-BLAST-fast retrieval of quantified structural information for protein sequences of unknown structure
    • Web Server issue, W411-W415
    • Suhrer,S.J. et al. (2007a) QSCOP-BLAST-fast retrieval of quantified structural information for protein sequences of unknown structure. Nucleic Acids Res., 35 (Web Server issue), W411-W415.
    • (2007) Nucleic Acids Res , vol.35
    • Suhrer, S.J.1
  • 9
    • 33847249065 scopus 로고    scopus 로고
    • QSCOP-SCOP quantified by structural relationships
    • Suhrer,S.J. et al. (2007b) QSCOP-SCOP quantified by structural relationships. Bioinformatics, 23, 513-514.
    • (2007) Bioinformatics , vol.23 , pp. 513-514
    • Suhrer, S.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.