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Volumn 23, Issue 7, 2007, Pages 901-902

DFprot: A webtool for predicting local chain deformability

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; COMPUTER INTERFACE; COMPUTER PROGRAM; INTERNET; MATHEMATICAL ANALYSIS; PREDICTION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; QUANTITATIVE ANALYSIS; STRUCTURE ANALYSIS; ALGORITHM; AMINO ACID SEQUENCE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER SIMULATION; ELASTICITY; METHODOLOGY; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; ULTRASTRUCTURE;

EID: 34248523175     PISSN: 13674803     EISSN: 13674811     Source Type: Journal    
DOI: 10.1093/bioinformatics/btm014     Document Type: Article
Times cited : (21)

References (23)
  • 1
    • 32344452680 scopus 로고    scopus 로고
    • Disseminating structural genomics data to the public: From a data dump to an animated story
    • Abagyan,R. et al. (2006) Disseminating structural genomics data to the public: From a data dump to an animated story. Trends Biochem. Sci., 31, 76-78.
    • (2006) Trends Biochem. Sci , vol.31 , pp. 76-78
    • Abagyan, R.1
  • 2
    • 14144256567 scopus 로고    scopus 로고
    • Normal modes for predicting protein motions: A comprehensive database assessment and associated Web tool
    • Alexandrov,V. et al. (2005) Normal modes for predicting protein motions: A comprehensive database assessment and associated Web tool. Protein Sci., 14, 633-643.
    • (2005) Protein Sci , vol.14 , pp. 633-643
    • Alexandrov, V.1
  • 3
    • 0030623823 scopus 로고    scopus 로고
    • Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential
    • Bahar,I. et al. (1997) Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential. Fold. Des. 2, 173-181.
    • (1997) Fold. Des , vol.2 , pp. 173-181
    • Bahar, I.1
  • 4
    • 25844431698 scopus 로고    scopus 로고
    • Coarse-grained normal mode analysis in structural biology
    • Bahar,I. and Rader,A.J. (2005) Coarse-grained normal mode analysis in structural biology. Curr. Opin. Struct. Biol., 15, 586-592.
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 586-592
    • Bahar, I.1    Rader, A.J.2
  • 5
    • 3242891875 scopus 로고    scopus 로고
    • MoViES: Molecular vibrations evaluation server for analysis of fluctuational dynamics of proteins and nucleic acids
    • Cao,Z.W. et al. (2004) MoViES: Molecular vibrations evaluation server for analysis of fluctuational dynamics of proteins and nucleic acids. Nucleic Acids Res., 32, W679-W685.
    • (2004) Nucleic Acids Res , vol.32
    • Cao, Z.W.1
  • 6
    • 21644473891 scopus 로고    scopus 로고
    • Representing receptor flexibility in ligand docking through relevant normal modes
    • Cavasotto,C.N. et al. (2005) Representing receptor flexibility in ligand docking through relevant normal modes. J. Am. Chem. Soc., 127, 9632-9640.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 9632-9640
    • Cavasotto, C.N.1
  • 7
    • 0037436340 scopus 로고    scopus 로고
    • Mega-Dalton biomolecular motion captured from electron microscopy reconstructions
    • Chacon,P. et al. (2003) Mega-Dalton biomolecular motion captured from electron microscopy reconstructions. J. Mol. Biol., 326 485-492.
    • (2003) J. Mol. Biol , vol.326 , pp. 485-492
    • Chacon, P.1
  • 8
    • 0032533790 scopus 로고    scopus 로고
    • Analysis of domain motions by approximate normal mode calculations
    • Hinsen,K. (1998) Analysis of domain motions by approximate normal mode calculations. Proteins, 33, 417-429.
    • (1998) Proteins , vol.33 , pp. 417-429
    • Hinsen, K.1
  • 9
    • 25444528449 scopus 로고    scopus 로고
    • WEBnm a web application for normal mode analyses of proteins
    • Hollup,S.M. et al. (2005) WEBnm" a web application for normal mode analyses of proteins. BMC Bioinformatics, 6, 52.
    • (2005) BMC Bioinformatics , vol.6 , pp. 52
    • Hollup, S.M.1
  • 10
    • 0035427398 scopus 로고    scopus 로고
    • Protein flexibility predictions using graph theory
    • Jacobs,D.J. et al. (2001) Protein flexibility predictions using graph theory. Proteins, 44, 150-165.
    • (2001) Proteins , vol.44 , pp. 150-165
    • Jacobs, D.J.1
  • 11
    • 0037666985 scopus 로고    scopus 로고
    • Conformational flexibility of pyruvate dehydrogenase complexes: A computational analysis by quantized elastic deformational model
    • Kong,Y. et al. (2003) Conformational flexibility of pyruvate dehydrogenase complexes: A computational analysis by quantized elastic deformational model. J. Mol. Biol., 330, 129-135.
    • (2003) J. Mol. Biol , vol.330 , pp. 129-135
    • Kong, Y.1
  • 12
    • 4043116913 scopus 로고    scopus 로고
    • Predictions of protein flexibility: First-order measures
    • Kovacs,J.A. et al. (2004) Predictions of protein flexibility: first-order measures. Proteins, 56, 661-668.
    • (2004) Proteins , vol.56 , pp. 661-668
    • Kovacs, J.A.1
  • 13
    • 33747858757 scopus 로고    scopus 로고
    • NOMAD-Ref: Visualization, deformation and refinement of macromolecular structures based on all-atom normal mode analysis
    • Lindahl,E. et al. (2006) NOMAD-Ref: Visualization, deformation and refinement of macromolecular structures based on all-atom normal mode analysis. Nucleic Acids Res., 34, W52-W56.
    • (2006) Nucleic Acids Res , vol.34
    • Lindahl, E.1
  • 14
    • 14844286108 scopus 로고    scopus 로고
    • Usefulness and limitations of normal mode analysis in modeling dynamics of biomolecular complexes
    • Ma,J. (2005) Usefulness and limitations of normal mode analysis in modeling dynamics of biomolecular complexes. Structure, 13, 373-380.
    • (2005) Structure , vol.13 , pp. 373-380
    • Ma, J.1
  • 15
    • 33646200456 scopus 로고    scopus 로고
    • Investigating the local flexibility of functional residues in hemoproteins
    • Sacquin-Mora,S. and Lavery,R. (2006) Investigating the local flexibility of functional residues in hemoproteins. Biophys. J., 90, 2706-2717.
    • (2006) Biophys. J , vol.90 , pp. 2706-2717
    • Sacquin-Mora, S.1    Lavery, R.2
  • 16
    • 33645019704 scopus 로고    scopus 로고
    • An enhanced elastic network model to represent the motions of domain-swapped proteins
    • Song,G. and Jernigan,R.L. (2006) An enhanced elastic network model to represent the motions of domain-swapped proteins. Proteins, 63 197-209.
    • (2006) Proteins , vol.63 , pp. 197-209
    • Song, G.1    Jernigan, R.L.2
  • 17
    • 3242875210 scopus 로고    scopus 로고
    • ElNemo: A normal mode web server for protein movement analysis and the generation of templates for molecular replacement
    • Suhre,K. and Sanejouand,Y.H. (2004) ElNemo: A normal mode web server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Res., 32, W610-W614.
    • (2004) Nucleic Acids Res , vol.32
    • Suhre, K.1    Sanejouand, Y.H.2
  • 18
    • 0035044995 scopus 로고    scopus 로고
    • Conformational change of proteins arising from normal mode calculations
    • Tama,F. and Sanejouand,Y.H. (2001) Conformational change of proteins arising from normal mode calculations. Protein Eng., 14, 1-6.
    • (2001) Protein Eng , vol.14 , pp. 1-6
    • Tama, F.1    Sanejouand, Y.H.2
  • 19
    • 0000197372 scopus 로고    scopus 로고
    • Large amplitude elastic motions in proteins from a single-parameter, atomic analysis
    • Tirion,M.M. (1996) Large amplitude elastic motions in proteins from a single-parameter, atomic analysis. Phys. Rev. Lett., 77, 1905-1908.
    • (1996) Phys. Rev. Lett , vol.77 , pp. 1905-1908
    • Tirion, M.M.1
  • 20
    • 4544280144 scopus 로고    scopus 로고
    • ProMode: A database of normal mode analyses on protein molecules with a full-atom model
    • Wako,H. et al. (2004) ProMode: A database of normal mode analyses on protein molecules with a full-atom model. Bioinformatics, 20 2035-2043.
    • (2004) Bioinformatics , vol.20 , pp. 2035-2043
    • Wako, H.1
  • 21
    • 20444429274 scopus 로고    scopus 로고
    • iGNM: A database of protein functional motions based on Gaussian Network Model
    • Yang,L.W. et al. (2005) iGNM: A database of protein functional motions based on Gaussian Network Model. Bioinformatics, 21, 2978-2987.
    • (2005) Bioinformatics , vol.21 , pp. 2978-2987
    • Yang, L.W.1
  • 22
    • 33646742004 scopus 로고    scopus 로고
    • Low-frequency normal modes that describe allosteric transitions in biological nanomachines are robust to sequence variations
    • Zheng,W. et al. (2006) Low-frequency normal modes that describe allosteric transitions in biological nanomachines are robust to sequence variations. Proc. Natl Acad. Sci. USA, 103, 7664-7669.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 7664-7669
    • Zheng, W.1
  • 23
    • 0345687171 scopus 로고    scopus 로고
    • A comparative study of motor-protein motions by using a simple elastic-network model
    • Zheng,W. and Doniach,S. (2003) A comparative study of motor-protein motions by using a simple elastic-network model. Proc. Natl Acad. Sci. USA, 100, 13253-13258.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 13253-13258
    • Zheng, W.1    Doniach, S.2


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