메뉴 건너뛰기




Volumn 21, Issue 10, 2013, Pages 1735-1742

High-resolution comparative modeling with RosettaCM

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CHEMICAL STRUCTURE; COMPARATIVE STUDY; CONTROLLED STUDY; ENERGY; HYDROGEN BOND; METHODOLOGY; MOLECULAR MODEL; PRIORITY JOURNAL; ROSETTACM; SEQUENCE ALIGNMENT;

EID: 84885431817     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2013.08.005     Document Type: Article
Times cited : (881)

References (26)
  • 3
    • 50649095790 scopus 로고    scopus 로고
    • Macromolecular modeling with rosetta
    • R. Das, and D. Baker Macromolecular modeling with rosetta Annu. Rev. Biochem. 77 2008 363 382
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 363-382
    • Das, R.1    Baker, D.2
  • 7
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch, and C. Sander Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22 1983 2577 2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 10
    • 67650439454 scopus 로고    scopus 로고
    • Boosting protein threading accuracy
    • J. Peng, and J. Xu Boosting protein threading accuracy Res. Comput. Mol. Biol. 5541 2009 31 45
    • (2009) Res. Comput. Mol. Biol. , vol.5541 , pp. 31-45
    • Peng, J.1    Xu, J.2
  • 14
    • 84856489442 scopus 로고    scopus 로고
    • HHblits: Lightning-fast iterative protein sequence searching by HMM-HMM alignment
    • M. Remmert, A. Biegert, A. Hauser, and J. Söding HHblits: lightning-fast iterative protein sequence searching by HMM-HMM alignment Nat. Methods 9 2012 173 175
    • (2012) Nat. Methods , vol.9 , pp. 173-175
    • Remmert, M.1    Biegert, A.2    Hauser, A.3    Söding, J.4
  • 16
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • A. Sali, and T.L. Blundell Comparative protein modelling by satisfaction of spatial restraints J. Mol. Biol. 234 1993 779 815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 17
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • J. Söding, A. Biegert, and A.N. Lupas The HHpred interactive server for protein homology detection and structure prediction Nucleic Acids Res. 33 Web Server issue 2005 W244 W248
    • (2005) Nucleic Acids Res. , vol.33 , Issue.WEB SERVER ISSUE
    • Söding, J.1    Biegert, A.2    Lupas, A.N.3
  • 18
    • 79960078022 scopus 로고    scopus 로고
    • Incorporation of evolutionary information into Rosetta comparative modeling
    • J. Thompson, and D. Baker Incorporation of evolutionary information into Rosetta comparative modeling Proteins 79 2011 2380 2388
    • (2011) Proteins , vol.79 , pp. 2380-2388
    • Thompson, J.1    Baker, D.2
  • 19
    • 0035703311 scopus 로고    scopus 로고
    • Analysis and assessment of comparative modeling predictions in CASP4
    • A. Tramontano, R. Leplae, and V. Morea Analysis and assessment of comparative modeling predictions in CASP4 Proteins Suppl 5 2001 22 38
    • (2001) Proteins , Issue.SUPPL. 5 , pp. 22-38
    • Tramontano, A.1    Leplae, R.2    Morea, V.3
  • 21
    • 0037188507 scopus 로고    scopus 로고
    • Evaluating conformational free energies: The colony energy and its application to the problem of loop prediction
    • Z. Xiang, C.S. Soto, and B. Honig Evaluating conformational free energies: the colony energy and its application to the problem of loop prediction Proc. Natl. Acad. Sci. USA 99 2002 7432 7437
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7432-7437
    • Xiang, Z.1    Soto, C.S.2    Honig, B.3
  • 22
    • 80855147432 scopus 로고    scopus 로고
    • Automated protein structure modeling in CASP9 by I-TASSER pipeline combined with QUARK-based ab initio folding and FG-MD-based structure refinement
    • D. Xu, J. Zhang, A. Roy, and Y. Zhang Automated protein structure modeling in CASP9 by I-TASSER pipeline combined with QUARK-based ab initio folding and FG-MD-based structure refinement Proteins 79 Suppl 10 2011 147 160
    • (2011) Proteins , vol.79 , Issue.SUPPL. 10 , pp. 147-160
    • Xu, D.1    Zhang, J.2    Roy, A.3    Zhang, Y.4
  • 23
    • 0042622381 scopus 로고    scopus 로고
    • LGA: A method for finding 3D similarities in protein structures
    • A. Zemla LGA: a method for finding 3D similarities in protein structures Nucleic Acids Res. 31 2003 3370 3374
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3370-3374
    • Zemla, A.1
  • 24
    • 0032605828 scopus 로고    scopus 로고
    • Processing and analysis of CASP3 protein structure predictions
    • A. Zemla, C. Venclovas, J. Moult, and K. Fidelis Processing and analysis of CASP3 protein structure predictions Proteins Suppl 3 1999 22 29
    • (1999) Proteins , Issue.SUPPL. 3 , pp. 22-29
    • Zemla, A.1    Venclovas, C.2    Moult, J.3    Fidelis, K.4
  • 25
    • 2542631929 scopus 로고    scopus 로고
    • Single-body residue-level knowledge-based energy score combined with sequence-profile and secondary structure information for fold recognition
    • H. Zhou, and Y. Zhou Single-body residue-level knowledge-based energy score combined with sequence-profile and secondary structure information for fold recognition Proteins 55 2004 1005 1013
    • (2004) Proteins , vol.55 , pp. 1005-1013
    • Zhou, H.1    Zhou, Y.2
  • 26
    • 34247619229 scopus 로고    scopus 로고
    • DDOMAIN: Dividing structures into domains using a normalized domain-domain interaction profile
    • H. Zhou, B. Xue, and Y. Zhou DDOMAIN: dividing structures into domains using a normalized domain-domain interaction profile Protein Sci. 16 2007 947 955
    • (2007) Protein Sci. , vol.16 , pp. 947-955
    • Zhou, H.1    Xue, B.2    Zhou, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.