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Volumn 67, Issue 2, 2007, Pages 400-417

PIER: Protein interface recognition for structural proteomics

Author keywords

Alignment independent interface prediction; Cell signaling and protein recognition; Protein protein interaction; Structural proteomics; Structure function annotation

Indexed keywords

ALGORITHM; ARTICLE; BINDING SITE; COMPUTER PREDICTION; CONTROLLED STUDY; GENETIC CONSERVATION; NONHUMAN; PRIORITY JOURNAL; PROCESS DEVELOPMENT; PROTEIN INTERFACE RECOGNITION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SENSITIVITY AND SPECIFICITY; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STATISTICAL ANALYSIS; STRUCTURAL PROTEOMICS; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

EID: 33947360625     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21233     Document Type: Article
Times cited : (104)

References (89)
  • 2
    • 0036601150 scopus 로고    scopus 로고
    • Computational methods for the prediction of protein interactions
    • Valencia A, Pazos F. Computational methods for the prediction of protein interactions. Curr Opin Struct Biol 2002;12:368-373.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 368-373
    • Valencia, A.1    Pazos, F.2
  • 3
    • 9244239761 scopus 로고    scopus 로고
    • A domain interaction map based on phylogenetic profiling
    • Pagel P, Wong P, Frishman D. A domain interaction map based on phylogenetic profiling. J Mol Biol 2004;344:1331-1346.
    • (2004) J Mol Biol , vol.344 , pp. 1331-1346
    • Pagel, P.1    Wong, P.2    Frishman, D.3
  • 5
    • 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
  • 6
    • 0038021436 scopus 로고    scopus 로고
    • Assessment of blind predictions of protein-protein interactions: Current status of docking methods
    • Méndez R, Leplae R, Maria LD, Wodak SJ. Assessment of blind predictions of protein-protein interactions: current status of docking methods. Proteins 2003;52:51-67.
    • (2003) Proteins , vol.52 , pp. 51-67
    • Méndez, R.1    Leplae, R.2    Maria, L.D.3    Wodak, S.J.4
  • 7
    • 0036468385 scopus 로고    scopus 로고
    • Prediction of protein-protein interactions by docking methods
    • Smith GR, Sternberg MJ. Prediction of protein-protein interactions by docking methods. Curr Opin Struct Biol 2002;12:28-35.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 28-35
    • Smith, G.R.1    Sternberg, M.J.2
  • 8
    • 1242270553 scopus 로고    scopus 로고
    • Protein-protein docking: Is the glass half-full or half-empty?
    • Vajda S, Camacho CJ. Protein-protein docking: is the glass half-full or half-empty? Trends Biotechnol 2004;22:110-116.
    • (2004) Trends Biotechnol , vol.22 , pp. 110-116
    • Vajda, S.1    Camacho, C.J.2
  • 9
    • 1842861590 scopus 로고    scopus 로고
    • Prediction of protein-protein interactions: The CAPRI experiment, its evaluation and implications
    • Wodak SJ, Méndez R. Prediction of protein-protein interactions: the CAPRI experiment, its evaluation and implications. Curr Opin Struct Biol 2004;14:242-249.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 242-249
    • Wodak, S.J.1    Méndez, R.2
  • 10
    • 0029913807 scopus 로고    scopus 로고
    • An evolutionary trace method defines binding surfaces common to protein families
    • Lichtarge O, Bourne HR, Cohen FE. An evolutionary trace method defines binding surfaces common to protein families. J Mol Biol 1996;257:342-358.
    • (1996) J Mol Biol , vol.257 , pp. 342-358
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 11
    • 0036468670 scopus 로고    scopus 로고
    • Evolutionary predictions of binding surfaces and interactions
    • Lichtarge O, Sowa ME. Evolutionary predictions of binding surfaces and interactions. Curr Opin Struct Biol 2002;12:21-27.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 21-27
    • Lichtarge, O.1    Sowa, M.E.2
  • 12
    • 0035853280 scopus 로고    scopus 로고
    • Three-dimensional cluster analysis identifies interfaces and functional residue clusters in proteins
    • Landgraf R, Xenarios I, Eisenberg D. Three-dimensional cluster analysis identifies interfaces and functional residue clusters in proteins. J Mol Biol 2001;307:1487-1502.
    • (2001) J Mol Biol , vol.307 , pp. 1487-1502
    • Landgraf, R.1    Xenarios, I.2    Eisenberg, D.3
  • 13
    • 0035838976 scopus 로고    scopus 로고
    • Automated structure-based prediction of functional sites in proteins: Applications to assessing the validity of inheriting protein function from homology in genome annotation and to protein docking
    • Aloy P, Querol E, Aviles FX, Sternberg MJ. Automated structure-based prediction of functional sites in proteins: applications to assessing the validity of inheriting protein function from homology in genome annotation and to protein docking. J Mol Biol 2001;311:395-408.
    • (2001) J Mol Biol , vol.311 , pp. 395-408
    • Aloy, P.1    Querol, E.2    Aviles, F.X.3    Sternberg, M.J.4
  • 14
    • 0035896024 scopus 로고    scopus 로고
    • ConSurf: An algorithmic tool for the identification of functional regions in proteins by surface mapping of phylogenetic information
    • Armon A, Graur D, Ben-Tal N. ConSurf: an algorithmic tool for the identification of functional regions in proteins by surface mapping of phylogenetic information. J Mol Biol 2001;307:447-463.
    • (2001) J Mol Biol , vol.307 , pp. 447-463
    • Armon, A.1    Graur, D.2    Ben-Tal, N.3
  • 15
    • 2542445427 scopus 로고    scopus 로고
    • ConSurf: Identification of functional regions in proteins by surface-mapping of phylogenetic information
    • Glaser F, Pupko T, Paz I, Bell RE, Bechor-Shental D, Martz E, Ben-Tal N. ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information. Bioinformatics 2003;19:163-164.
    • (2003) Bioinformatics , vol.19 , pp. 163-164
    • Glaser, F.1    Pupko, T.2    Paz, I.3    Bell, R.E.4    Bechor-Shental, D.5    Martz, E.6    Ben-Tal, N.7
  • 16
    • 0002218484 scopus 로고    scopus 로고
    • Rate4Site: An algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues
    • Pupko T, Bell RE, Mayrose I, Glaser F, Ben-Tal N. Rate4Site: an algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues Bioinformatics 2002;18 (Suppl 1):71-77.
    • (2002) Bioinformatics , vol.18 , Issue.SUPPL. 1 , pp. 71-77
    • Pupko, T.1    Bell, R.E.2    Mayrose, I.3    Glaser, F.4    Ben-Tal, N.5
  • 17
    • 19544390737 scopus 로고    scopus 로고
    • REVCOM: A robust Bayesian method for evolutionary rate estimation
    • Bordner AJ, Abagyan R. REVCOM: a robust Bayesian method for evolutionary rate estimation. Bioinformatics 2005;21:2315-2321.
    • (2005) Bioinformatics , vol.21 , pp. 2315-2321
    • Bordner, A.J.1    Abagyan, R.2
  • 18
    • 1842526090 scopus 로고    scopus 로고
    • ProMate: A structure based prediction program to identify the location of protein-protein binding sites
    • Neuvirth H, Raz R, Schreiber G. ProMate: a structure based prediction program to identify the location of protein-protein binding sites. J Mol Biol 2004;338:181-199.
    • (2004) J Mol Biol , vol.338 , pp. 181-199
    • Neuvirth, H.1    Raz, R.2    Schreiber, G.3
  • 19
    • 23044487169 scopus 로고    scopus 로고
    • Statistical analysis and prediction of protein-protein interfaces
    • Bordner AJ, Abagyan R. Statistical analysis and prediction of protein-protein interfaces. Proteins 2005;60:353-366.
    • (2005) Proteins , vol.60 , pp. 353-366
    • Bordner, A.J.1    Abagyan, R.2
  • 20
    • 17444372787 scopus 로고    scopus 로고
    • Improved prediction of protein-protein binding sites using a support vector machines approach
    • Bradford JR, Westhead DR. Improved prediction of protein-protein binding sites using a support vector machines approach. Bioinformatics 2005;21:1487-1494.
    • (2005) Bioinformatics , vol.21 , pp. 1487-1494
    • Bradford, J.R.1    Westhead, D.R.2
  • 21
    • 1842765629 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction sites using support vector machines
    • Koike A, Takagi T. Prediction of protein-protein interaction sites using support vector machines. Protein Eng Des Sel 2004;17:165-173.
    • (2004) Protein Eng Des Sel , vol.17 , pp. 165-173
    • Koike, A.1    Takagi, T.2
  • 23
    • 0036122073 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction sites in heterocomplexes with neural networks
    • Fariselli P, Pazos F, Valencia A, Casadio R. Prediction of protein-protein interaction sites in heterocomplexes with neural networks. Eur J Biochem 2002;269:1356-1361.
    • (2002) Eur J Biochem , vol.269 , pp. 1356-1361
    • Fariselli, P.1    Pazos, F.2    Valencia, A.3    Casadio, R.4
  • 24
    • 0035914476 scopus 로고    scopus 로고
    • Conservation helps to identify biologically relevant crystal contacts
    • Valdar WS, Thornton JM. Conservation helps to identify biologically relevant crystal contacts. J Mol Biol 2001;313:399-416.
    • (2001) J Mol Biol , vol.313 , pp. 399-416
    • Valdar, W.S.1    Thornton, J.M.2
  • 25
    • 0035882570 scopus 로고    scopus 로고
    • Prediction of protein interaction sites from sequence profile and residue neighbor list
    • Zhou HX, Shan Y. Prediction of protein interaction sites from sequence profile and residue neighbor list. Proteins 2001;44:336-343.
    • (2001) Proteins , vol.44 , pp. 336-343
    • Zhou, H.X.1    Shan, Y.2
  • 26
    • 2942553723 scopus 로고    scopus 로고
    • Protein-protein interactions; coupling of structurally conserved residues and of hot spots across interfaces. Implications for docking
    • Halperin I, Wolfson H, Nussinov R. Protein-protein interactions; coupling of structurally conserved residues and of hot spots across interfaces. Implications for docking. Structure (Camb) 2004;12:1027-1038.
    • (2004) Structure (Camb) , vol.12 , pp. 1027-1038
    • Halperin, I.1    Wolfson, H.2    Nussinov, R.3
  • 27
    • 0037609791 scopus 로고    scopus 로고
    • Protein-protein interactions: Structurally conserved residues distinguish between binding sites and exposed protein surfaces
    • Ma B, Elkayam T, Wolfson H, Nussinov R. Protein-protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfaces. Proc Natl Acad Sci USA 2003;100:5772-5777.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5772-5777
    • Ma, B.1    Elkayam, T.2    Wolfson, H.3    Nussinov, R.4
  • 28
    • 0037265213 scopus 로고    scopus 로고
    • Prediction of protein-protein interactions from evolutionary information
    • Valencia A, Pazos F. Prediction of protein-protein interactions from evolutionary information. Methods Biochem Anal 2003;44:411-426.
    • (2003) Methods Biochem Anal , vol.44 , pp. 411-426
    • Valencia, A.1    Pazos, F.2
  • 29
    • 0037197902 scopus 로고    scopus 로고
    • Interrogating protein interaction networks through structural biology
    • Aloy P, Russell RB. Interrogating protein interaction networks through structural biology. Proc Natl Acad Sci USA 2002;99:5896-5901.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5896-5901
    • Aloy, P.1    Russell, R.B.2
  • 30
    • 0042010066 scopus 로고    scopus 로고
    • Asymmetric mutation rates at enzyme-inhibitor interfaces: Implications for the protein-protein docking problem
    • Bradford JR, Westhead DR. Asymmetric mutation rates at enzyme-inhibitor interfaces: implications for the protein-protein docking problem. Protein Sci 2003;12:2099-2103.
    • (2003) Protein Sci , vol.12 , pp. 2099-2103
    • Bradford, J.R.1    Westhead, D.R.2
  • 31
    • 0346733329 scopus 로고    scopus 로고
    • Are protein-protein interfaces more conserved in sequence than the rest of the protein surface?
    • Caffrey DR, Somaroo S, Hughes JD, Mintseris J, Huang ES. Are protein-protein interfaces more conserved in sequence than the rest of the protein surface? Protein Sci 2004;13:190-202.
    • (2004) Protein Sci , vol.13 , pp. 190-202
    • Caffrey, D.R.1    Somaroo, S.2    Hughes, J.D.3    Mintseris, J.4    Huang, E.S.5
  • 32
    • 23344451687 scopus 로고    scopus 로고
    • Structure, function, and evolution of transient and obligate protein-protein interactions
    • Mintseris J, Weng Z. Structure, function, and evolution of transient and obligate protein-protein interactions. Proc Natl Acad Sci USA 2005;102:10930-10935.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 10930-10935
    • Mintseris, J.1    Weng, Z.2
  • 33
    • 0029790856 scopus 로고    scopus 로고
    • Pitfalls of protein sequence analysis
    • Rost B, Valencia A. Pitfalls of protein sequence analysis. Curr Opin Biotechnol 1996;7:457-461.
    • (1996) Curr Opin Biotechnol , vol.7 , pp. 457-461
    • Rost, B.1    Valencia, A.2
  • 34
    • 0035815113 scopus 로고    scopus 로고
    • Evolution of function in protein superfamilies, from a structural perspective
    • Todd AE, Orengo CA, Thornton JM. Evolution of function in protein superfamilies, from a structural perspective. J Mol Biol 2001;307:1113-1143.
    • (2001) J Mol Biol , vol.307 , pp. 1113-1143
    • Todd, A.E.1    Orengo, C.A.2    Thornton, J.M.3
  • 35
    • 0029587166 scopus 로고
    • A method to predict functional residues in proteins
    • Casari G, Sander C, Valencia A. A method to predict functional residues in proteins. Nat Struct Biol 1995;2:171-178.
    • (1995) Nat Struct Biol , vol.2 , pp. 171-178
    • Casari, G.1    Sander, C.2    Valencia, A.3
  • 36
    • 0037470597 scopus 로고    scopus 로고
    • Automatic methods for predicting functionally important residues
    • Mesa AdS, Pazos F, Valencia A. Automatic methods for predicting functionally important residues. J Mol Biol 2003;326:1289-1302.
    • (2003) J Mol Biol , vol.326 , pp. 1289-1302
    • Mesa, A.S.1    Pazos, F.2    Valencia, A.3
  • 37
    • 0036681416 scopus 로고    scopus 로고
    • Scoring residue conservation
    • Valdar WS. Scoring residue conservation. Proteins 2002;48:227-241.
    • (2002) Proteins , vol.48 , pp. 227-241
    • Valdar, W.S.1
  • 38
    • 1042275583 scopus 로고    scopus 로고
    • A dissection of specific and non-specific protein-protein interfaces
    • Bahadur RP, Chakrabarti P, Rodier F, Janin J. A dissection of specific and non-specific protein-protein interfaces. J Mol Biol 2004;336:943-955.
    • (2004) J Mol Biol , vol.336 , pp. 943-955
    • Bahadur, R.P.1    Chakrabarti, P.2    Rodier, F.3    Janin, J.4
  • 39
    • 0031565729 scopus 로고    scopus 로고
    • Analysis of protein-protein interaction sites using surface patches
    • Jones S, Thornton JM. Analysis of protein-protein interaction sites using surface patches. J Mol Biol 1997;272:121-132.
    • (1997) J Mol Biol , vol.272 , pp. 121-132
    • Jones, S.1    Thornton, J.M.2
  • 40
  • 41
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Conte LL, Chothia C, Janin J. The atomic structure of protein-protein recognition sites. J Mol Biol 1999;285:2177-2198.
    • (1999) J Mol Biol , vol.285 , pp. 2177-2198
    • Conte, L.L.1    Chothia, C.2    Janin, J.3
  • 42
    • 0030580057 scopus 로고    scopus 로고
    • Antibody-antigen interactions: Contact analysis and binding site topography
    • MacCallum RM, Martin AC, Thornton JM. Antibody-antigen interactions: contact analysis and binding site topography. J Mol Biol 1996;262:732-745.
    • (1996) J Mol Biol , vol.262 , pp. 732-745
    • MacCallum, R.M.1    Martin, A.C.2    Thornton, J.M.3
  • 43
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterisation and functional significance of transient protein-protein interactions
    • Nooren IM, Thornton JM. Structural characterisation and functional significance of transient protein-protein interactions. J Mol Biol 2003;325:991-1018.
    • (2003) J Mol Biol , vol.325 , pp. 991-1018
    • Nooren, I.M.1    Thornton, J.M.2
  • 44
    • 0037229456 scopus 로고    scopus 로고
    • Analysing six types of protein-protein interfaces
    • Ofran Y, Rost B. Analysing six types of protein-protein interfaces. J Mol Biol 2003;325:377-387.
    • (2003) J Mol Biol , vol.325 , pp. 377-387
    • Ofran, Y.1    Rost, B.2
  • 46
    • 1842405464 scopus 로고    scopus 로고
    • Studies of protein-protein interfaces: A statistical analysis of the hydrophobic effect
    • Tsai CJ, Lin SL, Wolfson HJ, Nussinov R. Studies of protein-protein interfaces: a statistical analysis of the hydrophobic effect. Protein Sci 1997;6:53-64.
    • (1997) Protein Sci , vol.6 , pp. 53-64
    • Tsai, C.J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 47
    • 0028332007 scopus 로고
    • A role for surface hydrophobicity in protein-protein recognition
    • Young L, Jernigan RL, Covell DG. A role for surface hydrophobicity in protein-protein recognition. Protein Sci 1994;3:717-729.
    • (1994) Protein Sci , vol.3 , pp. 717-729
    • Young, L.1    Jernigan, R.L.2    Covell, D.G.3
  • 48
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S, Thornton JM. Principles of protein-protein interactions. Proc Natl Acad Sci USA 1996;93:13-20.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 49
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-protein interactions
    • Nooren IM, Thornton JM. Diversity of protein-protein interactions. EMBO J 2003;22:3486-3492.
    • (2003) EMBO J , vol.22 , pp. 3486-3492
    • Nooren, I.M.1    Thornton, J.M.2
  • 50
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan AA, Thorn KS. Anatomy of hot spots in protein interfaces. J Mol Biol 1998;280:1-9.
    • (1998) J Mol Biol , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 51
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T, Wells JA. A hot spot of binding energy in a hormone-receptor interface. Science 1995;267:383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 53
    • 0031565725 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction sites using patch analysis
    • Jones S, Thornton JM. Prediction of protein-protein interaction sites using patch analysis. J Mol Biol 1997;272:133-143.
    • (1997) J Mol Biol , vol.272 , pp. 133-143
    • Jones, S.1    Thornton, J.M.2
  • 54
    • 0034049350 scopus 로고    scopus 로고
    • Kinetics of desolvation-mediated protein-protein binding
    • Camacho CJ, Kimura SR, DeLisi C, Vajda S. Kinetics of desolvation-mediated protein-protein binding. Biophys J 2000;78:1094-1105.
    • (2000) Biophys J , vol.78 , pp. 1094-1105
    • Camacho, C.J.1    Kimura, S.R.2    DeLisi, C.3    Vajda, S.4
  • 56
    • 10844235653 scopus 로고    scopus 로고
    • Optimal docking area: A new method for predicting protein-protein interaction sites
    • Fernandez-Recio J, Totrov M, Skorodumov C, Abagyan R. Optimal docking area: a new method for predicting protein-protein interaction sites. Proteins 2005;58:134-143.
    • (2005) Proteins , vol.58 , pp. 134-143
    • Fernandez-Recio, J.1    Totrov, M.2    Skorodumov, C.3    Abagyan, R.4
  • 57
    • 1942422617 scopus 로고    scopus 로고
    • Pattern recognition strategies for molecular surfaces. III. Binding site prediction with a neural network
    • Keil M, Exner TE, Brickmann J. Pattern recognition strategies for molecular surfaces. III. Binding site prediction with a neural network. J Comput Chem 2004;25:779-789.
    • (2004) J Comput Chem , vol.25 , pp. 779-789
    • Keil, M.1    Exner, T.E.2    Brickmann, J.3
  • 58
    • 11144325691 scopus 로고
    • Partial least squares regression: A tutorial
    • Geladi P, Kowalski B. Partial least squares regression: a tutorial. Anal Chim Acta 1986;185:1-17.
    • (1986) Anal Chim Acta , vol.185 , pp. 1-17
    • Geladi, P.1    Kowalski, B.2
  • 60
    • 0015866154 scopus 로고
    • Environment and exposure to solvent of protein atoms: Lysozyme and insulin
    • Shrake A, Rupley JA. Environment and exposure to solvent of protein atoms: lysozyme and insulin. J Mol Biol 1973;79:351-357.
    • (1973) J Mol Biol , vol.79 , pp. 351-357
    • Shrake, A.1    Rupley, J.A.2
  • 61
    • 84986522918 scopus 로고
    • ICM: A new method for structure modeling and design: applications to docking and structure prediction from the distorted native conformation
    • Abagyan RA, Totrov MM, Kuznetsov DA. ICM: a new method for structure modeling and design: applications to docking and structure prediction from the distorted native conformation. J Comput Chem 1994;15:488-506.
    • (1994) J Comput Chem , vol.15 , pp. 488-506
    • Abagyan, R.A.1    Totrov, M.M.2    Kuznetsov, D.A.3
  • 65
    • 0031576355 scopus 로고    scopus 로고
    • Do aligned sequences share the same fold?
    • Abagyan RA, Batalov S. Do aligned sequences share the same fold? J Mol Biol 1997;273:355-368.
    • (1997) J Mol Biol , vol.273 , pp. 355-368
    • Abagyan, R.A.1    Batalov, S.2
  • 66
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • Needleman SB, Wunsch CD. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol 1970;48:443-453.
    • (1970) J Mol Biol , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 67
    • 0026656815 scopus 로고
    • Exhaustive matching of the entire protein sequence database
    • Gonnet GH, Cohen MA, Benner SA. Exhaustive matching of the entire protein sequence database. Science 1992;256:1443-1445.
    • (1992) Science , vol.256 , pp. 1443-1445
    • Gonnet, G.H.1    Cohen, M.A.2    Benner, S.A.3
  • 68
    • 33947367995 scopus 로고    scopus 로고
    • Abagyan R. ICM Manual v. 3.1. 2005.
    • Abagyan R. ICM Manual v. 3.1. 2005.
  • 69
    • 0037093645 scopus 로고    scopus 로고
    • Dissecting protein-protein recognition sites
    • Chakrabarti P, Janin J. Dissecting protein-protein recognition sites. Proteins 2002;47:334-343.
    • (2002) Proteins , vol.47 , pp. 334-343
    • Chakrabarti, P.1    Janin, J.2
  • 70
    • 0035342450 scopus 로고    scopus 로고
    • Residue frequencies and pairing preferences at protein-protein interfaces
    • Glaser F, Steinberg DM, Vakser IA, Ben-Tal N. Residue frequencies and pairing preferences at protein-protein interfaces. Proteins 2001;43:89-102.
    • (2001) Proteins , vol.43 , pp. 89-102
    • Glaser, F.1    Steinberg, D.M.2    Vakser, I.A.3    Ben-Tal, N.4
  • 71
    • 0035053587 scopus 로고    scopus 로고
    • Assessing the role of tryptophan residues in the binding site
    • Samanta U, Chakrabarti P. Assessing the role of tryptophan residues in the binding site. Protein Eng 2001;14:7-15.
    • (2001) Protein Eng , vol.14 , pp. 7-15
    • Samanta, U.1    Chakrabarti, P.2
  • 72
    • 0035841343 scopus 로고    scopus 로고
    • Characterization of aromatic-thiol π-type hydrogen bonding and phenylalanine-cysteine side chain interactions through ab initio calculations and protein database analyses
    • Duan G, Smith VHJ, Weaver DF. Characterization of aromatic-thiol π-type hydrogen bonding and phenylalanine-cysteine side chain interactions through ab initio calculations and protein database analyses. Mol Phys 2001;99:1689-1699.
    • (2001) Mol Phys , vol.99 , pp. 1689-1699
    • Duan, G.1    Smith, V.H.J.2    Weaver, D.F.3
  • 73
    • 0034846083 scopus 로고    scopus 로고
    • Non-hydrogen bond interactions involving the methionine sulfur atom
    • Pal D, Chakrabarti P. Non-hydrogen bond interactions involving the methionine sulfur atom. J Biomol Struct Dyn 2001;19:115-128.
    • (2001) J Biomol Struct Dyn , vol.19 , pp. 115-128
    • Pal, D.1    Chakrabarti, P.2
  • 74
    • 0242299201 scopus 로고    scopus 로고
    • Dissecting subunit interfaces in homodimeric proteins
    • Bahadur RP, Chakrabarti P, Rodier F, Janin J. Dissecting subunit interfaces in homodimeric proteins. Proteins 2003;53:708-719.
    • (2003) Proteins , vol.53 , pp. 708-719
    • Bahadur, R.P.1    Chakrabarti, P.2    Rodier, F.3    Janin, J.4
  • 75
    • 0031552370 scopus 로고    scopus 로고
    • Determination of atomic desolvation energies from the structures of crystallized proteins
    • Zhang C, Vasmatzis G, Cornette JL, DeLisi C. Determination of atomic desolvation energies from the structures of crystallized proteins. J Mol Biol 1997;267:707-726.
    • (1997) J Mol Biol , vol.267 , pp. 707-726
    • Zhang, C.1    Vasmatzis, G.2    Cornette, J.L.3    DeLisi, C.4
  • 76
    • 0029918062 scopus 로고    scopus 로고
    • Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1
    • Bourne Y, Watson MH, Hickey MJ, Holmes W, Rocque W, Reed SI, Tainer JA. Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1. Cell 1996;84:863-874.
    • (1996) Cell , vol.84 , pp. 863-874
    • Bourne, Y.1    Watson, M.H.2    Hickey, M.J.3    Holmes, W.4    Rocque, W.5    Reed, S.I.6    Tainer, J.A.7
  • 77
    • 0029767016 scopus 로고    scopus 로고
    • Structural basis of cyclin-dependent kinase activation by phosphorylation
    • Russo AA, Jeffrey PD, Pavletich NP. Structural basis of cyclin-dependent kinase activation by phosphorylation. Nat Struct Biol 1996;3:696-700.
    • (1996) Nat Struct Biol , vol.3 , pp. 696-700
    • Russo, A.A.1    Jeffrey, P.D.2    Pavletich, N.P.3
  • 78
    • 0025998314 scopus 로고
    • Multiple murine α 1-protease inhibitor genes show unusual evolutionary divergence
    • Borriello F, Krauter KS. Multiple murine α 1-protease inhibitor genes show unusual evolutionary divergence. Proc Natl Acad Sci USA 1991;88:9417-9421.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9417-9421
    • Borriello, F.1    Krauter, K.S.2
  • 79
    • 0024382970 scopus 로고
    • Functional evolutionary divergence of proteolytic enzymes and their inhibitors
    • Creighton TE, Darby NJ. Functional evolutionary divergence of proteolytic enzymes and their inhibitors. Trends Biochem Sci 1989;14:319-324.
    • (1989) Trends Biochem Sci , vol.14 , pp. 319-324
    • Creighton, T.E.1    Darby, N.J.2
  • 80
    • 0028140075 scopus 로고
    • Evolution of murine α 1-proteinase inhibitors: Gene amplification and reactive center divergence
    • Rheaume C, Goodwin RL, Latimer JJ, Baumann H, Berger FG. Evolution of murine α 1-proteinase inhibitors: gene amplification and reactive center divergence. J Mol Evol 1994;38:121-131.
    • (1994) J Mol Evol , vol.38 , pp. 121-131
    • Rheaume, C.1    Goodwin, R.L.2    Latimer, J.J.3    Baumann, H.4    Berger, F.G.5
  • 81
    • 0030063088 scopus 로고    scopus 로고
    • Patterns of divergence during evolution of α 1-proteinase inhibitors in mammals
    • Goodwin RL, Baumann H, Berger FG. Patterns of divergence during evolution of α 1-proteinase inhibitors in mammals. Mol Biol Evol 1996;13:346-358.
    • (1996) Mol Biol Evol , vol.13 , pp. 346-358
    • Goodwin, R.L.1    Baumann, H.2    Berger, F.G.3
  • 82
    • 0023188637 scopus 로고
    • Accelerated evolution in the reactive centre regions of serine protease inhibitors
    • Hill RE, Hastie ND. Accelerated evolution in the reactive centre regions of serine protease inhibitors. Nature 1987;326:96-99.
    • (1987) Nature , vol.326 , pp. 96-99
    • Hill, R.E.1    Hastie, N.D.2
  • 83
    • 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
  • 84
    • 0032169688 scopus 로고    scopus 로고
    • PQS: A protein quaternary structure file server
    • Henrick K, Thornton JM. PQS: a protein quaternary structure file server. Trends Biochem Sci 1998;23:358-361.
    • (1998) Trends Biochem Sci , vol.23 , pp. 358-361
    • Henrick, K.1    Thornton, J.M.2
  • 85
    • 0034308172 scopus 로고    scopus 로고
    • Discriminating between homodimeric and monomeric proteins in the crystalline state
    • Ponstingl H, Henrick K, Thornton JM. Discriminating between homodimeric and monomeric proteins in the crystalline state. Proteins 2000;41:47-57.
    • (2000) Proteins , vol.41 , pp. 47-57
    • Ponstingl, H.1    Henrick, K.2    Thornton, J.M.3
  • 86
    • 0031787909 scopus 로고    scopus 로고
    • Aminoacyl tRNA synthetases as targets for new anti-infectives
    • Schimmel P, Tao J, Hill J. Aminoacyl tRNA synthetases as targets for new anti-infectives. FASEB J 1998;12:1599-1609.
    • (1998) FASEB J , vol.12 , pp. 1599-1609
    • Schimmel, P.1    Tao, J.2    Hill, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.