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Volumn 26, Issue 23, 2010, Pages 2986-2987

FILTREST3D: Discrimination of structural models using restraints from experimental data

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BIOLOGY; CHEMICAL STRUCTURE; COMPUTER PROGRAM; CONFORMATION; METHODOLOGY; PROTEIN CONFORMATION;

EID: 78449278402     PISSN: 13674803     EISSN: 14602059     Source Type: Journal    
DOI: 10.1093/bioinformatics/btq582     Document Type: Article
Times cited : (15)

References (11)
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  • 3
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    • Furnham,N. et al. (2006) Knowledge-based real-space explorations for low-resolution structure determination. Structure, 14, 1313-1320.
    • (2006) Structure , vol.14 , pp. 1313-1320
    • Furnham, N.1
  • 4
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    • THUMP from archaeal tRNA:m22G10 methyltransferase, a genuine autonomously folding domain
    • Gabant,G. et al. (2006) THUMP from archaeal tRNA:m22G10 methyltransferase, a genuine autonomously folding domain. Nucleic Acids Res., 34, 2483-2494.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 2483-2494
    • Gabant, G.1
  • 5
    • 23444458450 scopus 로고    scopus 로고
    • Analysis of the quaternary structure of the MutL C-terminal domain
    • Kosinski,J. et al. (2005) Analysis of the quaternary structure of the MutL C-terminal domain. J. Mol. Biol., 351, 895-909.
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    • Kosinski, J.1
  • 6
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    • Geometric analysis of cross-linkability for protein fold discrimination
    • Potluri,S. et al. (2004) Geometric analysis of cross-linkability for protein fold discrimination. Pac. Symp. Biocomput., 9, 447-458.
    • (2004) Pac. Symp. Biocomput. , vol.9 , pp. 447-458
    • Potluri, S.1
  • 7
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    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali,A. and Blundell,T.L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol., 234, 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 8
    • 0034710671 scopus 로고    scopus 로고
    • A deeply knotted protein structure and how it might fold
    • Taylor,W.R. (2000) A deeply knotted protein structure and how it might fold. Nature, 406, 916-919.
    • (2000) Nature , vol.406 , pp. 916-919
    • Taylor, W.R.1
  • 9
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    • Protein docking for low-resolution structures
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    • Aknowledge-based potential function predicts the specificity and relative binding energy of RNA-binding proteins
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.