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Volumn 26, Issue 19, 2010, Pages 2466-2467

SPRINT: Side-chain prediction inference toolbox for multistate protein design

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; PROTEIN;

EID: 77957233448     PISSN: 13674803     EISSN: 14602059     Source Type: Journal    
DOI: 10.1093/bioinformatics/btq445     Document Type: Article
Times cited : (10)

References (13)
  • 1
    • 31944435091 scopus 로고    scopus 로고
    • Computational design of a single amino acid sequence that can switch between two distinct protein folds
    • Ambroggio,X.I. and Kuhlman,B. (2006) Computational design of a single amino acid sequence that can switch between two distinct protein folds. J. Am. Chem. Soc., 128, 1154-1161.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 1154-1161
    • Ambroggio, X.I.1    Kuhlman, B.2
  • 2
    • 0027160197 scopus 로고
    • Backbone-dependent rotamer library for proteins application to side-chain prediction
    • Dunbrack,R.L. and Karplus,M. (1993) Backbone-dependent rotamer library for proteins application to side-chain prediction. J. Mol. Biol., 230, 543-574.
    • (1993) J. Mol. Biol. , vol.230 , pp. 543-574
    • Dunbrack, R.L.1    Karplus, M.2
  • 3
    • 74549136698 scopus 로고    scopus 로고
    • Tradeoff between stability and multispecificity in the design of promiscuous proteins
    • Fromer,M. and Shifman,J.M. (2009) Tradeoff between stability and multispecificity in the design of promiscuous proteins. PLoS Comput. Biol., 5, e1000627.
    • (2009) PLoS Comput. Biol. , vol.5
    • Fromer, M.1    Shifman, J.M.2
  • 4
    • 46249085661 scopus 로고    scopus 로고
    • Acomputational framework to empower probabilistic protein design
    • Fromer,M. andYanover,C. (2008)Acomputational framework to empower probabilistic protein design. Bioinformatics, 24, i214-i222.
    • (2008) Bioinformatics , vol.24 , pp. 1214-1222
    • Fromer, M.1    Yanover, C.2
  • 5
    • 63549137183 scopus 로고    scopus 로고
    • Accurate prediction for atomic-level protein design and its application in diversifying the near-optimal sequence space
    • Fromer,M. and Yanover,C. (2009) Accurate prediction for atomic-level protein design and its application in diversifying the near-optimal sequence space. Proteins Struct. Funct. Bioinform., 75, 682-705.
    • (2009) Proteins Struct. Funct. Bioinform. , vol.75 , pp. 682-705
    • Fromer, M.1    Yanover, C.2
  • 6
    • 77949894732 scopus 로고    scopus 로고
    • Design of multispecific protein sequences using probabilistic graphical modeling
    • Fromer,M. et al. (2010) Design of multispecific protein sequences using probabilistic graphical modeling. Proteins Struct. Funct. Bioinform., 78, 530-547.
    • (2010) Proteins Struct. Funct. Bioinform. , vol.78 , pp. 530-547
    • Fromer, M.1
  • 7
    • 0033178329 scopus 로고    scopus 로고
    • Energy functions for protein design
    • Gordon,D.B. et al. (1999) Energy functions for protein design. Curr. Opin. Struc. Biol., 9, 509-513.
    • (1999) Curr. Opin. Struc. Biol. , vol.9 , pp. 509-513
    • Gordon, D.B.1
  • 8
    • 0037217406 scopus 로고    scopus 로고
    • Automated design of specificity in molecular recognition
    • Havranek,J.J. and Harbury,P.B. (2003) Automated design of specificity in molecular recognition. Nat. Struct. Mol. Biol., 10, 45-52.
    • (2003) Nat. Struct. Mol. Biol. , vol.10 , pp. 45-52
    • Havranek, J.J.1    Harbury, P.B.2
  • 9
    • 77957230613 scopus 로고    scopus 로고
    • Available at, (last accessed date August 25, 2010)
    • Jaimovich,A. et al. (2010) FastInf. Available at http://jmlr.csail.mit.edu/papers/v11/jaimovich10a.html (last accessed date August 25, 2010).
    • (2010) FastInf
    • Jaimovich, A.1
  • 10
    • 0345306764 scopus 로고    scopus 로고
    • Design of a novel globular protein fold with atomic-level accuracy
    • Kuhlman,B. et al. (2003) Design of a novel globular protein fold with atomic-level accuracy. Science, 302, 1364-1368.
    • (2003) Science , vol.302 , pp. 1364-1368
    • Kuhlman, B.1
  • 11
    • 0031717560 scopus 로고    scopus 로고
    • Exploring the conformational space of protein side chains using dead-end elimination and the A* algorithm
    • Leach,A.R. and Lemon,A.P. (1998) Exploring the conformational space of protein side chains using dead-end elimination and the A* algorithm. Proteins Struct. Funct. Genet., 33, 227-239.
    • (1998) Proteins Struct. Funct. Genet. , vol.33 , pp. 227-239
    • Leach, A.R.1    Lemon, A.P.2
  • 12
    • 74549207309 scopus 로고    scopus 로고
    • Assessing computational methods for predicting protein stability upon mutation: good on average but not in the details
    • Potapov,V. et al. (2009)Assessing computational methods for predicting protein stability upon mutation: good on average but not in the details. Protein Eng. Des. Sel., 22, 553-560.
    • (2009) Protein Eng. Des. Sel. , vol.22 , pp. 553-560
    • Potapov, V.1
  • 13
    • 34547957588 scopus 로고    scopus 로고
    • Dead-end elimination for multistate protein design
    • Yanover,C. et al. (2007) Dead-end elimination for multistate protein design. J. Comput. Chem., 28, 2122-2129
    • (2007) J. Comput. Chem. , vol.28 , pp. 2122-2129
    • Yanover, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.