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Volumn 60, Issue 2, 2005, Pages 269-274

Docking essential dynamics eigenstructures

Author keywords

CAPRI; Distance constraints; Eigenstructures; Eigenvector analysis; Essential dynamics; Hex; Polar Fourier correlation; Protein docking

Indexed keywords

ACCURACY; ALGORITHM; CONFERENCE PAPER; FOURIER TRANSFORMATION; MOLECULAR DYNAMICS; PREDICTION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; RIGIDITY;

EID: 21644460933     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20569     Document Type: Conference Paper
Times cited : (229)

References (23)
  • 1
    • 0036606483 scopus 로고    scopus 로고
    • Principles of docking: An overview of search algorithms and a guide to scoring functions
    • Halperin I, Ma B, Wolfson H, Nussinov R. Principles of docking: an overview of search algorithms and a guide to scoring functions. Proteins 2002;47:409-443.
    • (2002) Proteins , vol.47 , pp. 409-443
    • Halperin, I.1    Ma, B.2    Wolfson, H.3    Nussinov, R.4
  • 2
    • 0031565730 scopus 로고    scopus 로고
    • Modelling protein docking using shape complementarity, electrostatics and biochemical information
    • Gabb HA, Jackson RM, Sternberg MJE. Modelling protein docking using shape complementarity, electrostatics and biochemical information. J Mol Biol 1997;272:106-120.
    • (1997) J Mol Biol , vol.272 , pp. 106-120
    • Gabb, H.A.1    Jackson, R.M.2    Sternberg, M.J.E.3
  • 3
    • 0037230970 scopus 로고    scopus 로고
    • Implicit solvent models for flexible protein-protein docking by molecular dynamics simulation
    • Wang T, Wade RC. Implicit solvent models for flexible protein-protein docking by molecular dynamics simulation. Proteins 2003; 50:158-169.
    • (2003) Proteins , vol.50 , pp. 158-169
    • Wang, T.1    Wade, R.C.2
  • 4
    • 9944237833 scopus 로고    scopus 로고
    • Complementarity of structure ensembles in protein-protein docking
    • Grünberg R, Leckner J, Nilges M. Complementarity of structure ensembles in protein-protein docking. Structure 2004;12:2125-2136.
    • (2004) Structure , vol.12 , pp. 2125-2136
    • Grünberg, R.1    Leckner, J.2    Nilges, M.3
  • 5
    • 1542316339 scopus 로고    scopus 로고
    • Rapid protein-ligand docking using soft modes from molecular dynamics simulations to account for protein deformability: Binding of FK506 to FKBP
    • Zacharias M. Rapid protein-ligand docking using soft modes from molecular dynamics simulations to account for protein deformability: binding of FK506 to FKBP. Proteins 2004;54:759-767.
    • (2004) Proteins , vol.54 , pp. 759-767
    • Zacharias, M.1
  • 6
    • 0034193510 scopus 로고    scopus 로고
    • Protein docking using spherical polar Fourier correlations
    • Ritchie DW, Kemp GJL. Protein docking using spherical polar Fourier correlations. Proteins 2000;39:178-194.
    • (2000) Proteins , vol.39 , pp. 178-194
    • Ritchie, D.W.1    Kemp, G.J.L.2
  • 7
    • 0037683565 scopus 로고    scopus 로고
    • Evaluation of protein docking predictions using Hex 3.1 in CAPRI rounds 1 and 2
    • Ritchie DW. Evaluation of protein docking predictions using Hex 3.1 in CAPRI rounds 1 and 2. Proteins 2003;52:98-106.
    • (2003) Proteins , vol.52 , pp. 98-106
    • Ritchie, D.W.1
  • 10
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial constraints
    • Sali A, Blundell TL. Comparative protein modelling by satisfaction of spatial constraints. J Mol Biol 1993;234:779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 11
    • 0027286695 scopus 로고
    • A single EGF-like motif of laminin is responsible for high affinity nidogen binding
    • Mayer U, Nischt R, Poschl E, Mann K, Fukuda K, Gerl M, Yamada Y, Timpl R. A single EGF-like motif of laminin is responsible for high affinity nidogen binding. EMBO J 1993;12:1879-1885.
    • (1993) EMBO J , vol.12 , pp. 1879-1885
    • Mayer, U.1    Nischt, R.2    Poschl, E.3    Mann, K.4    Fukuda, K.5    Gerl, M.6    Yamada, Y.7    Timpl, R.8
  • 12
    • 0034711422 scopus 로고    scopus 로고
    • Crystal structure of a cohesin module from Clostridium cellulolyticum: Implications for dockerin recognition
    • Spinelli S, Fiérobe H-P, Belaïch A, Belaïch J-P, Henrissat B, Cambillou C. Crystal structure of a cohesin module from Clostridium cellulolyticum: implications for dockerin recognition. J Mol Biol 2000;304:189-200.
    • (2000) J Mol Biol , vol.304 , pp. 189-200
    • Spinelli, S.1    Fiérobe, H.-P.2    Belaïch, A.3    Belaïch, J.-P.4    Henrissat, B.5    Cambillou, C.6
  • 13
    • 0035970297 scopus 로고    scopus 로고
    • Solution of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain
    • Lytle B, Volkman BF, Westler WM, Heckman MP, Wu JHD. Solution of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain. J Mol Biol 2001;307:745-753.
    • (2001) J Mol Biol , vol.307 , pp. 745-753
    • Lytle, B.1    Volkman, B.F.2    Westler, W.M.3    Heckman, M.P.4    Wu, J.H.D.5
  • 14
    • 0036315557 scopus 로고    scopus 로고
    • Structure of the immunodominant surface antigen from the Toxoplasma gondii SRS superfamily
    • He X-L, Grigg ME, Boothroyd JC, Garcia KC. Structure of the immunodominant surface antigen from the Toxoplasma gondii SRS superfamily. Nat Struct Biol 2002;9:606-611.
    • (2002) Nat Struct Biol , vol.9 , pp. 606-611
    • He, X.-L.1    Grigg, M.E.2    Boothroyd, J.C.3    Garcia, K.C.4
  • 15
    • 0032416318 scopus 로고    scopus 로고
    • Myosin phosphatase: Subunits and interactions
    • Hartshorne DJ. Myosin phosphatase: subunits and interactions. Acta Physiol Scand 1998;164:483-493.
    • (1998) Acta Physiol Scand , vol.164 , pp. 483-493
    • Hartshorne, D.J.1
  • 16
    • 0030977268 scopus 로고    scopus 로고
    • Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1
    • Egloff M-P, Johnson DF, Moorhead G, Cohen PTW, Cohen P, Barford D. Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1. EMBO J 1997;16:1876-1887.
    • (1997) EMBO J , vol.16 , pp. 1876-1887
    • Egloff, M.-P.1    Johnson, D.F.2    Moorhead, G.3    Cohen, P.T.W.4    Cohen, P.5    Barford, D.6
  • 18
    • 21644469377 scopus 로고    scopus 로고
    • Assessment of CAPRI predictions in Rounds 3-5 shows progress in docking procedures
    • Méndez R, Leplae R, Lensink MF, Wodak SJ. Assessment of CAPRI predictions in Rounds 3-5 shows progress in docking procedures. Proteins 2005;60:150-169.
    • (2005) Proteins , vol.60 , pp. 150-169
    • Méndez, R.1    Leplae, R.2    Lensink, M.F.3    Wodak, S.J.4
  • 20
  • 22
    • 0041858013 scopus 로고    scopus 로고
    • Complex between nidogen and laminin fragments reveals a paradigmatic β-propeller interface
    • Takagi J, Yang Y, Liu J-H, Wang J-H, Springer TA. Complex between nidogen and laminin fragments reveals a paradigmatic β-propeller interface. Nature 2004;424:969-974.
    • (2004) Nature , vol.424 , pp. 969-974
    • Takagi, J.1    Yang, Y.2    Liu, J.-H.3    Wang, J.-H.4    Springer, T.A.5
  • 23
    • 17644378441 scopus 로고    scopus 로고
    • Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes
    • Graille M, Zhao C-Z, Receveur-Bréchot V, Collinet B, Declerck N, van Tilbeurgh H. Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes. J Biol Chem 2005;280: 14780-14789.
    • (2005) J Biol Chem , vol.280 , pp. 14780-14789
    • Graille, M.1    Zhao, C.-Z.2    Receveur-Bréchot, V.3    Collinet, B.4    Declerck, N.5    Van Tilbeurgh, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.