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Volumn 30, Issue 22, 2014, Pages 3189-3196

Quantitative method for the assignment of hinge and shear mechanism in protein domain movements

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTER PROGRAM; MOTION; PROTEIN TERTIARY STRUCTURE; ROTATION; STATISTICAL MODEL;

EID: 84911453369     PISSN: 13674803     EISSN: 14602059     Source Type: Journal    
DOI: 10.1093/bioinformatics/btu506     Document Type: Article
Times cited : (43)

References (23)
  • 1
    • 0028114231 scopus 로고
    • Structure at 2.8Åresolution of F1-ATPase from bovine heart-mitochondria
    • Abrahams, J.P. et al. (1994) Structure at 2.8Åresolution of F1-ATPase from bovine heart-mitochondria. Nature, 370, 621-628.
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1
  • 2
    • 79953905577 scopus 로고    scopus 로고
    • Classification and annotation of the relationship between protein structural change and ligand binding
    • Amemiya, T. et al. (2011) Classification and annotation of the relationship between protein structural change and ligand binding. J. Mol. Biol., 408, 568-584.
    • (2011) J. Mol. Biol. , vol.408 , pp. 568-584
    • Amemiya, T.1
  • 3
    • 0021314461 scopus 로고
    • Structural and functional aspects of domain motions in proteins
    • Bennet, W.S. and Huber, R. (1984) Structural and functional aspects of domain motions in proteins. Crit. Rev. Biochem., 15, 291-384.
    • (1984) Crit. Rev. Biochem. , vol.15 , pp. 291-384
    • Bennet, W.S.1    Huber, R.2
  • 4
    • 0028204771 scopus 로고
    • Domain swapping: Entangling alliances between proteins
    • Bennett, M.J. et al. (1994) Domain swapping: entangling alliances between proteins. Proc. Natl Acad. Sci. USA, 91, 3127-3131.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 3127-3131
    • Bennett, M.J.1
  • 5
    • 0033954256 scopus 로고    scopus 로고
    • The protein data bank
    • Berman, H.M. et al. (2000) The protein data bank. Nucleic Acids Res., 28, 235-242.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 235-242
    • Berman, H.M.1
  • 6
    • 37849035176 scopus 로고    scopus 로고
    • What is the relationship between the global structures of apo and holo proteins?
    • Brylinski, M. and Skolnick, J. (2008) What is the relationship between the global structures of apo and holo proteins? Proteins, 70, 363-377.
    • (2008) Proteins , vol.70 , pp. 363-377
    • Brylinski, M.1    Skolnick, J.2
  • 8
    • 43049121679 scopus 로고    scopus 로고
    • Efficient approximate leave-one-out crossvalidation for kernel logistic regression
    • Cawley, G.C. and Talbot, N.L.C. (2008) Efficient approximate leave-one-out crossvalidation for kernel logistic regression. Mach. Learn., 71, 243-264.
    • (2008) Mach. Learn. , vol.71 , pp. 243-264
    • Cawley, G.C.1    Talbot, N.L.C.2
  • 10
    • 0000758915 scopus 로고
    • Note sur les propri-et-es g-en-erales du systeme de deux corps semblables entreux et plac-es dune maniere quelconque dans lespace; Et sur le d-eplacement fini ou infiniment petit dun corps solide libre
    • Chasles, M. (1830) Note sur les propri-et-es g-en-erales du systeme de deux corps semblables entreux et plac-es dune maniere quelconque dans lespace; et sur le d-eplacement fini ou infiniment petit dun corps solide libre. Bull. Sci. Math., 14, 321-326.
    • (1830) Bull. Sci. Math. , vol.14 , pp. 321-326
    • Chasles, M.1
  • 11
    • 0019880506 scopus 로고
    • Structure of a triclinic ternary complex of horse liver alcohol- dehydrogenase at 2.9 a resolution
    • Eklund, H. et al. (1981) Structure of a triclinic ternary complex of horse liver alcohol- dehydrogenase at 2.9 a resolution. J. Mol. Biol., 146, 561-587.
    • (1981) J. Mol. Biol. , vol.146 , pp. 561-587
    • Eklund, H.1
  • 12
    • 0032530836 scopus 로고    scopus 로고
    • A database of macromolecular motions
    • Gerstein, M. and Krebs, W. (1998) A database of macromolecular motions. Nucleic Acids Res., 26, 4280-4290.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4280-4290
    • Gerstein, M.1    Krebs, W.2
  • 13
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • Gerstein, M. et al. (1994) Structural mechanisms for domain movements in proteins. Biochemistry, 33, 6739-6749.
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1
  • 14
    • 0032769661 scopus 로고    scopus 로고
    • Structural principles governing domain motions in proteins
    • Hayward, S. (1999) Structural principles governing domain motions in proteins. Proteins, 36, 425-435.
    • (1999) Proteins , vol.36 , pp. 425-435
    • Hayward, S.1
  • 15
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme
    • Hayward, S. and Berendsen, H.J.C. (1998) Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme. Proteins, 30, 144-154.
    • (1998) Proteins , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.C.2
  • 16
    • 0036888353 scopus 로고    scopus 로고
    • Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50
    • Hayward, S. and Lee, R.A. (2002) Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50. J. Mol. Graph. Model., 21, 181-183.
    • (2002) J. Mol. Graph. Model. , vol.21 , pp. 181-183
    • Hayward, S.1    Lee, R.A.2
  • 17
    • 20844448232 scopus 로고    scopus 로고
    • A comprehensive and non-redundant database of protein domain movements
    • Qi, G. et al. (2005) A comprehensive and non-redundant database of protein domain movements. Bioinformatics, 21, 2832-2838.
    • (2005) Bioinformatics , vol.21 , pp. 2832-2838
    • Qi, G.1
  • 18
    • 65349173946 scopus 로고    scopus 로고
    • Database of ligand-induced domain movements in enzymes
    • Qi, G.Y. and Hayward, S. (2009) Database of ligand-induced domain movements in enzymes. BMC Struct. Biol., 9, 13.
    • (2009) BMC Struct. Biol. , vol.9 , pp. 13
    • Qi, G.Y.1    Hayward, S.2
  • 19
    • 0000453761 scopus 로고
    • Domain motions in proteins
    • Schulz, G.E. (1991) Domain motions in proteins. Curr. Opin. Struct. Biol., 1, 883-888.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 883-888
    • Schulz, G.E.1
  • 20
    • 0035659482 scopus 로고    scopus 로고
    • Interdomain interactions in hinge-bending transitions
    • Sinha, N. et al. (2001) Interdomain interactions in hinge-bending transitions. Structure, 9, 1165-1181.
    • (2001) Structure , vol.9 , pp. 1165-1181
    • Sinha, N.1
  • 21
    • 84894175025 scopus 로고    scopus 로고
    • Classification of domain movements in proteins using dynamic contact graphs
    • Taylor, D. et al. (2013) Classification of domain movements in proteins using dynamic contact graphs. PloS One, 8, e81224.
    • (2013) PloS One , vol.8 , pp. e81224
    • Taylor, D.1
  • 22
    • 0037666888 scopus 로고    scopus 로고
    • Implications of protein flexibility for drug discovery
    • Teague, S.J. (2003) Implications of protein flexibility for drug discovery. Nat. Rev., 527, 527-541.
    • (2003) Nat. Rev. , vol.527 , pp. 527-541
    • Teague, S.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.