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Volumn 5, Issue 12, 2009, Pages

Defining an essence of structure determining residue contacts in proteins

Author keywords

[No Author keywords available]

Indexed keywords

SET THEORY; THREE DIMENSIONAL COMPUTER GRAPHICS;

EID: 74549198198     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1000584     Document Type: Article
Times cited : (37)

References (29)
  • 1
    • 43349102979 scopus 로고    scopus 로고
    • FT-COMAR: Fault tolerant three-dimensional structure reconstruction from protein contact maps
    • Vassura M, Margara L, Di Lena P, Medri F, Fariselli P, et al. (2008) FT-COMAR: fault tolerant three-dimensional structure reconstruction from protein contact maps. Bioinformatics 24: 1313-1315.
    • (2008) Bioinformatics , vol.24 , pp. 1313-1315
    • Vassura, M.1    Margara, L.2    Di Lena, P.3    Medri, F.4    Fariselli, P.5
  • 2
    • 0030627407 scopus 로고    scopus 로고
    • Recovery of protein structure from contact maps
    • Vendruscolo M, Kussell E, Domany E (1997) Recovery of protein structure from contact maps. Fold Des 2: 295-306.
    • (1997) Fold Des , vol.2 , pp. 295-306
    • Vendruscolo, M.1    Kussell, E.2    Domany, E.3
  • 3
    • 29444443942 scopus 로고    scopus 로고
    • Modelling the structure of latexin-carboxypeptidase A complex based on chemical cross-linking and molecular docking
    • Mouradov D, Craven A, Forwood JK, Flanagan JU, Garcia-Castellanos R, et al. (2006) Modelling the structure of latexin-carboxypeptidase A complex based on chemical cross-linking and molecular docking. Protein Eng Des Sel 19: 9-16.
    • (2006) Protein Eng Des Sel , vol.19 , pp. 9-16
    • Mouradov, D.1    Craven, A.2    Forwood, J.K.3    Flanagan, J.U.4    Garcia-Castellanos, R.5
  • 5
    • 38949171385 scopus 로고    scopus 로고
    • De novo high-resolution protein structure determination from sparse spin-labeling EPR data
    • Alexander N, Bortolus M, Al-Mestarihi A, McHaourab H, Meiler J (2008) De novo high-resolution protein structure determination from sparse spin-labeling EPR data. Structure 16: 181-195.
    • (2008) Structure , vol.16 , pp. 181-195
    • Alexander, N.1    Bortolus, M.2    Al-Mestarihi, A.3    McHaourab, H.4    Meiler, J.5
  • 6
    • 0034705128 scopus 로고    scopus 로고
    • High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry
    • Young MM, Tang N, Hempel JC, Oshiro CM, Taylor EW, et al. (2000) High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry. Proc Natl Acad Sci U S A 97: 5802-5806.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 5802-5806
    • Young, M.M.1    Tang, N.2    Hempel, J.C.3    Oshiro, C.M.4    Taylor, E.W.5
  • 7
    • 0029097099 scopus 로고
    • Global fold determination from a small number of distance restraints
    • Aszodi A, Gradwell MJ, Taylor WR (1995) Global fold determination from a small number of distance restraints. J Mol Biol 251: 308-326.
    • (1995) J Mol Biol , vol.251 , pp. 308-326
    • Aszodi, A.1    Gradwell, M.J.2    Taylor, W.R.3
  • 8
    • 0042010163 scopus 로고    scopus 로고
    • Discrete restraintbased protein modeling and the Calpha-trace problem
    • DePristo MA, De Bakker PI, Shetty RP, Blundell TL (2003) Discrete restraintbased protein modeling and the Calpha-trace problem. Protein Sci 12: 2032-2046.
    • (2003) Protein Sci , vol.12 , pp. 2032-2046
    • DePristo, M.A.1    De Bakker, P.I.2    Shetty, R.P.3    Blundell, T.L.4
  • 10
    • 51349158003 scopus 로고    scopus 로고
    • Generating properly weighted ensemble of conformations of proteins from sparse or indirect distance constraints
    • Lin M, Lu HM, Chen R, Liang J (2008) Generating properly weighted ensemble of conformations of proteins from sparse or indirect distance constraints. J Chem Phys 129: 094101.
    • (2008) J Chem Phys , vol.129 , pp. 094101
    • Lin, M.1    Lu, H.M.2    Chen, R.3    Liang, J.4
  • 11
    • 0031575423 scopus 로고    scopus 로고
    • MONSSTER: A method for folding globular proteins with a small number of distance restraints
    • Skolnick J, Kolinski A, Ortiz AR (1997) MONSSTER: a method for folding globular proteins with a small number of distance restraints. J Mol Biol 265: 217-241.
    • (1997) J Mol Biol , vol.265 , pp. 217-241
    • Skolnick, J.1    Kolinski, A.2    Ortiz, A.R.3
  • 12
    • 0027168790 scopus 로고
    • Global folding of proteins using a limited number of distance constraints
    • Smith-Brown MJ, Kominos D, Levy RM (1993) Global folding of proteins using a limited number of distance constraints. Protein Eng 6: 605-614.
    • (1993) Protein Eng , vol.6 , pp. 605-614
    • Smith-Brown, M.J.1    Kominos, D.2    Levy, R.M.3
  • 13
    • 49049098242 scopus 로고    scopus 로고
    • A stochastic method for the reconstruction of protein structures from one-dimensional structural profiles
    • Wolff K, Vendruscolo M, Porto M (2008) A stochastic method for the reconstruction of protein structures from one-dimensional structural profiles. Gene 422: 47-51.
    • (2008) Gene , vol.422 , pp. 47-51
    • Wolff, K.1    Vendruscolo, M.2    Porto, M.3
  • 16
    • 34547237581 scopus 로고    scopus 로고
    • Fidelity of the protein structure reconstruction from inter-residue proximity constraints
    • Chen Y, Ding F, Dokholyan NV (2007) Fidelity of the protein structure reconstruction from inter-residue proximity constraints. J Phys Chem B 111: 7432-7438.
    • (2007) J Phys Chem B , vol.111 , pp. 7432-7438
    • Chen, Y.1    Ding, F.2    Dokholyan, N.V.3
  • 17
    • 3142558004 scopus 로고    scopus 로고
    • Reconstruction of protein structures from a vectorial representation
    • Porto M, Bastolla U, Roman HE, Vendruscolo M (2004) Reconstruction of protein structures from a vectorial representation. Phys Rev Lett 92: 218101.
    • (2004) Phys Rev Lett , vol.92 , pp. 218101
    • Porto, M.1    Bastolla, U.2    Roman, H.E.3    Vendruscolo, M.4
  • 18
    • 34547909602 scopus 로고    scopus 로고
    • Assortative mixing in Protein Contact Networks and protein folding kinetics
    • Bagler G, Sinha S (2007) Assortative mixing in Protein Contact Networks and protein folding kinetics. Bioinformatics 23: 1760-1767.
    • (2007) Bioinformatics , vol.23 , pp. 1760-1767
    • Bagler, G.1    Sinha, S.2
  • 19
    • 1842464687 scopus 로고    scopus 로고
    • Inter-residue interactions in protein folding and stability
    • Gromiha MM, Selvaraj S (2004) Inter-residue interactions in protein folding and stability. Prog Biophys Mol Biol 86: 235-277.
    • (2004) Prog Biophys Mol Biol , vol.86 , pp. 235-277
    • Gromiha, M.M.1    Selvaraj, S.2
  • 20
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • Baker D (2000) A surprising simplicity to protein folding. Nature 405: 39-42.
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 21
    • 0036073603 scopus 로고    scopus 로고
    • Contact order and ab initio protein structure prediction
    • Bonneau R, Ruczinski I, Tsai J, Baker D (2002) Contact order and ab initio protein structure prediction. Protein Sci 11: 1937-1944.
    • (2002) Protein Sci , vol.11 , pp. 1937-1944
    • Bonneau, R.1    Ruczinski, I.2    Tsai, J.3    Baker, D.4
  • 23
    • 34547177765 scopus 로고    scopus 로고
    • Structural characterization of deformed crystals by analysis of common atomic neighborhood
    • Tsusuki H, Branicio PS, Rino JP (2007) Structural characterization of deformed crystals by analysis of common atomic neighborhood Computer Physics Communications. 518-523.
    • (2007) Computer Physics Communications , pp. 518-523
    • Tsusuki, H.1    Branicio, P.S.2    Rino, J.P.3
  • 24
    • 33845983675 scopus 로고    scopus 로고
    • Relative tolerance of mesostable and thermostable protein homologs to extensive mutation
    • Besenmatter W, Kast P, Hilvert D (2007) Relative tolerance of mesostable and thermostable protein homologs to extensive mutation. Proteins 66: 500-506.
    • (2007) Proteins , vol.66 , pp. 500-506
    • Besenmatter, W.1    Kast, P.2    Hilvert, D.3
  • 25
    • 58149165033 scopus 로고    scopus 로고
    • Relative tolerance of an enzymatic molten globule and its thermostable counterpart to point mutation
    • Woycechowsky KJ, Choutko A, Vamvaca K, Hilvert D (2008) Relative tolerance of an enzymatic molten globule and its thermostable counterpart to point mutation. Biochemistry 47: 13489-13496.
    • (2008) Biochemistry , vol.47 , pp. 13489-13496
    • Woycechowsky, K.J.1    Choutko, A.2    Vamvaca, K.3    Hilvert, D.4
  • 26
    • 34447537179 scopus 로고    scopus 로고
    • Evolution favors protein mutational robustness in sufficiently large populations
    • Bloom JD, Lu Z, Chen D, Raval A, Venturelli OS, et al. (2007) Evolution favors protein mutational robustness in sufficiently large populations. BMC Biol 5: 29.
    • (2007) BMC Biol , vol.5 , pp. 29
    • Bloom, J.D.1    Lu, Z.2    Chen, D.3    Raval, A.4    Venturelli, O.S.5
  • 27
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 247: 536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 28
    • 74549152093 scopus 로고    scopus 로고
    • Ponder JW (2004) Software Tools for Molecular Design, User's Guide for Version 4.2.
    • Ponder JW (2004) Software Tools for Molecular Design, User's Guide for Version 4.2.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.