메뉴 건너뛰기




Volumn 38, Issue SUPPL. 2, 2010, Pages

PUDGE: A flexible, interactive server for protein structure prediction

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; COMPUTER INTERFACE; COMPUTER PREDICTION; COMPUTER PROGRAM; INFORMATION PROCESSING; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DATABASE; PROTEIN STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; WEB BROWSER; CHEMICAL STRUCTURE; CHEMISTRY; INTERNET; STRUCTURAL HOMOLOGY;

EID: 77954249072     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkq475     Document Type: Article
Times cited : (8)

References (22)
  • 1
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones,D.T. (1999) Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol., 292, 195-202.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 2
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: identification of signaling domains
    • Schultz,J., Milpetz,F., Bork,P. and Ponting,C.P. (1998) SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl Acad. Sci. USA, 95, 5857-5864.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 3
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • Dosztanyi,Z., Csizmok,V., Tompa,P. and Simon,I. (2005) IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics, 21, 3433-3434.
    • (2005) Bioinformatics , vol.21 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 4
    • 70350465128 scopus 로고    scopus 로고
    • Structural relationships among proteins with different global topologies and their implications for function annotation strategies
    • Petrey,D., Fischer,M. and Honig,B. (2009) Structural relationships among proteins with different global topologies and their implications for function annotation strategies. Proc. Natl Acad. Sci. USA, 106, 17377-17382.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 17377-17382
    • Petrey, D.1    Fischer, M.2    Honig, B.3
  • 8
    • 0344873345 scopus 로고    scopus 로고
    • On the role of structural information in remote homology detection and sequence alignment: new methods using hybrid sequence profiles
    • Tang,C.L., Xie,L., Koh,I.Y., Posy,S., Alexov,E. and Honig,B. (2003) On the role of structural information in remote homology detection and sequence alignment: new methods using hybrid sequence profiles. J. Mol. Biol., 334, 1043-1062.
    • (2003) J. Mol. Biol. , vol.334 , pp. 1043-1062
    • Tang, C.L.1    Xie, L.2    Koh, I.Y.3    Posy, S.4    Alexov, E.5    Honig, B.6
  • 9
    • 0035838974 scopus 로고    scopus 로고
    • Extending the accuracy limits of prediction for side-chain conformations
    • Xiang,Z. and Honig,B. (2001) Extending the accuracy limits of prediction for side-chain conformations. J. Mol. Biol., 311, 421-430.
    • (2001) J. Mol. Biol. , vol.311 , pp. 421-430
    • Xiang, Z.1    Honig, B.2
  • 10
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie,J.U., Luthy,R. and Eisenberg,D. (1991) A method to identify protein sequences that fold into a known three-dimensional structure. Science, 253, 164-170.
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 11
    • 0026610767 scopus 로고
    • Assessment of protein models with 3-dimensional profiles
    • Luthy,R., Bowie,J.U. and Eisenberg,D. (1992) Assessment of protein models with 3-dimensional profiles. Nature, 356, 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 12
    • 0036838311 scopus 로고    scopus 로고
    • Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction
    • Zhou,H. and Zhou,Y. (2002) Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction. Protein Sci., 11, 2714-2726.
    • (2002) Protein Sci. , vol.11 , pp. 2714-2726
    • Zhou, H.1    Zhou, Y.2
  • 16
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl,M.J. (1993) Recognition of errors in three-dimensional structures of proteins. Proteins, 17, 355-362.
    • (1993) Proteins , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 17
    • 70350495852 scopus 로고    scopus 로고
    • Structure elucidation and preliminary assessment of hydrolase activity of PqsE, the Pseudomonas quinolone signal (PQS) response protein
    • Yu,S., Jensen,V., Seeliger,J., Feldmann,I., Weber,S., Schleicher,E., Häussler,S. and Blankenfeldt,W. (2009) Structure elucidation and preliminary assessment of hydrolase activity of PqsE, the Pseudomonas quinolone signal (PQS) response protein. Biochemistry, 48, 10298-10307.
    • (2009) Biochemistry , vol.48 , pp. 10298-10307
    • Yu, S.1    Jensen, V.2    Seeliger, J.3    Feldmann, I.4    Weber, S.5    Schleicher, E.6    Häussler, S.7    Blankenfeldt, W.8
  • 18
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • Smith,T.F. and Waterman,M.S. (1981) Identification of common molecular subsequences. J. Mol. Biol., 147, 195-197.
    • (1981) J. Mol. Biol. , vol.147 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 19
    • 0027136282 scopus 로고
    • 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
  • 20
    • 0036310711 scopus 로고    scopus 로고
    • On the role of the crystal environment in determining protein side-chain conformations
    • Jacobson,M.P., Friesner,R.A., Xiang,Z. and Honig,B. (2002) On the role of the crystal environment in determining protein side-chain conformations. J. Mol. Biol., 320, 597-608.
    • (2002) J. Mol. Biol. , vol.320 , pp. 597-608
    • Jacobson, M.P.1    Friesner, R.A.2    Xiang, Z.3    Honig, B.4
  • 21
    • 0037188507 scopus 로고    scopus 로고
    • Evaluating conformational free energies: the colony energy and its application to the problem of loop prediction
    • Xiang,Z., Soto,C.S. and Honig,B. (2002) Evaluating conformational free energies: the colony energy and its application to the problem of loop prediction. Proc. Natl Acad. Sci. USA, 99, 7432-7437.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 7432-7437
    • Xiang, Z.1    Soto, C.S.2    Honig, B.3
  • 22
    • 0042511005 scopus 로고    scopus 로고
    • A graph-theory algorithm for rapid protein side-chain prediction
    • Canutescu,A.A., Shelenkov,A.A. and Dunbrack,R.L. Jr (2003) A graph-theory algorithm for rapid protein side-chain prediction. Protein Sci., 12, 2001-2014.
    • (2003) Protein Sci. , vol.12 , pp. 2001-2014
    • Canutescu, A.A.1    Shelenkov, A.A.2    Dunbrack R.L. Jr3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.