메뉴 건너뛰기




Volumn 64, Issue 2-3, 1995, Pages 145-166

Protein-protein recognition

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BETA LACTAMASE; BETA LACTAMASE INHIBITOR PROTEIN, STREPTOMYCES; BETA-LACTAMASE-INHIBITOR PROTEIN, STREPTOMYCES; ENZYME INHIBITOR; PROTEIN;

EID: 0029421048     PISSN: 00796107     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0079-6107(96)00001-6     Document Type: Review
Times cited : (105)

References (100)
  • 5
    • 0028168537 scopus 로고
    • Rethinking “shape space”: evidence from simulated docking suggests that steric shape complementarity is not limiting for antibody-antigen recognition and idiotypic interactions
    • (1994) J. Theor. Biol. , vol.169 , pp. 391-402
    • Carneiro1    Stewart2
  • 10
    • 0016352763 scopus 로고
    • Hydrophobic bonding and accessible surface area in proteins
    • (1974) Nature , vol.248 , pp. 338-339
    • Chothia1
  • 11
    • 0016708122 scopus 로고
    • Principles of protein-protein recognition
    • (1975) Nature , vol.256 , pp. 705-708
    • Chothia1    Janin2
  • 12
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly1
  • 15
    • 0026924836 scopus 로고
    • Shape distribution of protein topography
    • (1992) Biopolymers , vol.32 , pp. 1215-1236
    • Connolly1
  • 19
    • 0027551946 scopus 로고
    • Approximation and characterization of molecular surfaces
    • (1993) Biopolymers , vol.33 , pp. 219-229
    • Duncan1    Olson2
  • 22
    • 0027049805 scopus 로고
    • The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α-helices: crystal structure of a the protein-DNA complex
    • (1992) Cell , vol.71 , pp. 1223-1237
    • Ellenberger1    Brandl2    Struhl3    Harrison4
  • 26
    • 0025135112 scopus 로고
    • Automated docking of substrates to proteins by simulated annealing
    • (1990) Proteins , vol.8 , pp. 195-202
    • Goodsell1    Olson2
  • 30
    • 0028280409 scopus 로고
    • Isothermal titration calorimetric study of the association of hen egg lysozyme and the anti-lysozyme antibody HyHEL5
    • (1994) Biochemistry , vol.33 , pp. 3584-3590
    • Hibbitts1    Gill2    Wilson3
  • 31
    • 0027087369 scopus 로고
    • Calculation of the free energy of association for protein complexes
    • (1992) Protein Sci. , vol.1 , pp. 169-181
    • Horton1    Lewis2
  • 32
    • 0029019869 scopus 로고
    • A continuum model for protein-protein interactions: application to the docking problem
    • (1995) J. Mol. Biol. , vol.250 , pp. 258-275
    • Jackson1    Sternberg2
  • 33
    • 0021908041 scopus 로고
    • A reaction pathway for the quaternary structure change in hemoglobin
    • (1985) Biopolymers , vol.24 , pp. 509-526
    • Janin1    Wodak2
  • 36
    • 0028853544 scopus 로고
    • Principles of protein-protein recognition from structure to thermodynamics
    • (1995) Biochimie , vol.77 , pp. 497-505
    • Janin1
  • 38
    • 0026310932 scopus 로고
    • “Soft Docking”: matching of molecular surface cubes
    • (1991) J. Mol. Biol. , vol.219 , pp. 79-102
    • Jiang1    Kim2
  • 41
    • 0027483012 scopus 로고
    • Co-crystal structure of TBP recognizing the minor groove of a TATA element
    • (1993) Nature , vol.365 , pp. 520-527
    • Kim1    Nikolov2    Burley3
  • 43
    • 0028181137 scopus 로고
    • Monte Carlo docking of protein-DNA complexes: incorporation of DNA flexibility and exprerimental data
    • (1994) Protein Eng. , vol.7 , pp. 761-767
    • Knegtel1    Boelens2    Kaptein3
  • 47
    • 0028158936 scopus 로고
    • Ligand docking to proteins with discrete side-chain flexibility
    • (1994) J. Mol. Biol. , vol.2357 , pp. 345-356
    • Leach1
  • 49
    • 0022105876 scopus 로고
    • Molecular recognition. I. Automatic identification of topograpic surface features
    • (1985) Biopolymers , vol.24 , pp. 1613-1627
    • Lee1    Rose2
  • 53
    • 0025360593 scopus 로고
    • Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: hydration effect
    • (1990) J. Mol. Biol. , vol.213 , pp. 375-384
    • Makhatadze1    Privalov2
  • 63
    • 0029089732 scopus 로고
    • Molecular surface complementarity at protein-protein interfaces: the critical role played by surface normals at well placed, sparse, points in docking
    • (1995) J. Mol. Biol. , vol.252 , pp. 263-273
    • Norel1    Lin2    Wolfson3    Nussinov4
  • 64
    • 0024362070 scopus 로고
    • On the attribution of binding energy in the antigen-antibody complexes McPC603, D1.3 and HyHEL-5
    • (1989) Biochemistry , vol.28 , pp. 4735-4748
    • Novotny1    Bruccoleri2    Saul3
  • 69
    • 0001971367 scopus 로고
    • The nature of the intermolecular forces operative in biological processes
    • (1940) Science , vol.92 , pp. 77-79
    • Pauling1    Delbrück2
  • 72
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study
    • (1974) J. Mol. Biol. , vol.86 , pp. 665-684
    • Privalov1    Khechinashvili2
  • 74
    • 0026076664 scopus 로고
    • Extracting hydrophobic free energies from experimental data: relationship to protein folding and theoretical models
    • (1991) Biochemistry , vol.30 , pp. 9686-9697
    • Sharp1    Nicholls2    Friedman3    Honig4
  • 82
    • 0026684671 scopus 로고
    • Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding form the removal of non-polar and polar surface from water
    • (1992) Biochemistry , vol.31 , pp. 3947-3955
    • Spolar1    Livingstone2    Record3
  • 83
    • 0028174101 scopus 로고
    • Protein side-chain conformational entropy derived from fusion data-comparison with other empirical scales
    • (1994) Protein Eng. , vol.7 , pp. 149-155
    • Sternberg1    Chickos2
  • 88
    • 0014718113 scopus 로고
    • Protein denaturation. Part C. Theoretical models for the mechanism of denaturation
    • (1970) Adv. Protein Chem. , vol.24 , pp. 1-95
    • Tanford1
  • 90
    • 0028227795 scopus 로고
    • N9 Neuraminidase complexes with antibodies NC41 and CN10: empirical free energy calculations capture specificity trends observed with mutant binding data
    • (1994) Biochemistry , vol.33 , pp. 7986-7997
    • Tulip1    Harley2    Webster3    Novotny4
  • 93
    • 0028984540 scopus 로고
    • Protein docking for low-resolution structures
    • (1995) Protein Eng. , vol.8 , pp. 371-377
    • Vakser1
  • 94
    • 0028881193 scopus 로고
    • Empirical free energy calculations of ligand-protein crystallographic complexes. I. Knowledge-based ligand-protein interaction potentials applied to the prediction of human immunodeficiency virus 1 protease binding affinity
    • (1995) Protein Eng. , vol.8 , pp. 677-691
    • Verkhivker1    Appelt2    Freer3    Villafranca4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.