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Volumn 52, Issue 1, 2003, Pages 41-46

Prediction of the unknown: Inspiring experience with the CAPRI experiment

Author keywords

Blind predictions; Clusters; Conserved surface patches; Protein protein interactions; Weighted docking

Indexed keywords

ACCURACY; ARTICLE; BINDING SITE; COMPLEX FORMATION; EXPERIMENT; GEOMETRY; MOLECULAR MODEL; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; SEQUENCE ANALYSIS;

EID: 0037849892     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10392     Document Type: Article
Times cited : (15)

References (33)
  • 1
    • 0026572775 scopus 로고
    • Molecular surface recognition: Determination of geometric fit between proteins and their ligands by correlation techniques
    • Katchalski-Katzir E, Shariv I, Eisenstein M, Friesem AA, Aflalo C, Vakser IA. Molecular surface recognition: determination of geometric fit between proteins and their ligands by correlation techniques. Proc Natl Acad Sci USA 1992;89:2195-2199.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2195-2199
    • Katchalski-Katzir, E.1    Shariv, I.2    Eisenstein, M.3    Friesem, A.A.4    Aflalo, C.5    Vakser, I.A.6
  • 2
    • 0031566966 scopus 로고    scopus 로고
    • Modeling supra-molecular helices: Extension of the molecular surface recognition algorithm and application to the protein coat of the tobacco mosaic virus
    • Eisenstein M, Shariv I, Koren G, Friesem AA, Katchalski-Katzir E. Modeling supra-molecular helices: extension of the molecular surface recognition algorithm and application to the protein coat of the tobacco mosaic virus. J Mol Biol 1997;266:135-143.
    • (1997) J Mol Biol , vol.266 , pp. 135-143
    • Eisenstein, M.1    Shariv, I.2    Koren, G.3    Friesem, A.A.4    Katchalski-Katzir, E.5
  • 4
    • 0038187616 scopus 로고    scopus 로고
    • Weighted geometric docking: Incorporating external information in the rotation-translation scan
    • Ben-Zeev E, Eisenstein M. Weighted geometric docking: incorporating external information in the rotation-translation scan. Proteins 2003;52:24-27.
    • (2003) Proteins , vol.52 , pp. 24-27
    • Ben-Zeev, E.1    Eisenstein, M.2
  • 5
    • 0032568649 scopus 로고    scopus 로고
    • A unified statistical framework for sequence comparison and structure comparison
    • Levitt M, Gerstein M. A unified statistical framework for sequence comparison and structure comparison. Proc Natl Acad Sci USA 1998;95:5913-5920.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5913-5920
    • Levitt, M.1    Gerstein, M.2
  • 6
    • 0034701013 scopus 로고    scopus 로고
    • Crystal structure of adenosine 5′-phosphosulfate kinase from Penicillium chrysogenum
    • MacRae IJ, Segel IH, Fisher AJ. Crystal structure of adenosine 5′-phosphosulfate kinase from Penicillium chrysogenum. Biochemistry 2000;39:1613-1621.
    • (2000) Biochemistry , vol.39 , pp. 1613-1621
    • MacRae, I.J.1    Segel, I.H.2    Fisher, A.J.3
  • 8
    • 0034656949 scopus 로고    scopus 로고
    • Side-chain flexibility in proteins upon ligand binding
    • Najmanovich R, Kuttner J, Sobolev V, Edelman M. Side-chain flexibility in proteins upon ligand binding. Proteins 2000;39:261-268.
    • (2000) Proteins , vol.39 , pp. 261-268
    • Najmanovich, R.1    Kuttner, J.2    Sobolev, V.3    Edelman, M.4
  • 10
    • 0026799307 scopus 로고
    • Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: Analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography
    • Sauter NK, Hanson JE, Glick GD, Brown JH, Crowther RL, Park SJ, Skehel, JJ, Wiley DC. Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography. Biochemistry 1992;31:9609-9621.
    • (1992) Biochemistry , vol.31 , pp. 9609-9621
    • Sauter, N.K.1    Hanson, J.E.2    Glick, G.D.3    Brown, J.H.4    Crowther, R.L.5    Park, S.J.6    Skehel, J.J.7    Wiley, D.C.8
  • 11
    • 0030668602 scopus 로고    scopus 로고
    • Comparison of the rotavirus gene 6 from different species by sequence analysis and localization of subgroup-specific epitopes using site-directed mutagenesis
    • Tang B, Gilbert JM, Matsui SM, Greenberg HB. Comparison of the rotavirus gene 6 from different species by sequence analysis and localization of subgroup-specific epitopes using site-directed mutagenesis. Virology 1997;237:89-96.
    • (1997) Virology , vol.237 , pp. 89-96
    • Tang, B.1    Gilbert, J.M.2    Matsui, S.M.3    Greenberg, H.B.4
  • 13
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley DC, Skehel JJ. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu Rev Biochem 1987;56:365-394.
    • (1987) Annu Rev Biochem , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 14
    • 0021927922 scopus 로고
    • Antigenic determinants of influenza virus hemagglutinin. XI. Conformational changes detected by monoclonal antibodies
    • Jackson DC, Nestorowicz A. Antigenic determinants of influenza virus hemagglutinin. XI. Conformational changes detected by monoclonal antibodies. Virology 1985;145:72-83.
    • (1985) Virology , vol.145 , pp. 72-83
    • Jackson, D.C.1    Nestorowicz, A.2
  • 15
    • 0030593488 scopus 로고    scopus 로고
    • Carbohydrate and protein-based inhibitors of porcine pancreatic alpha-amylase: Structure analysis and comparison of their binding characteristics
    • Machius M, Vertesy L, Huber R, Wiegand G. Carbohydrate and protein-based inhibitors of porcine pancreatic alpha-amylase: structure analysis and comparison of their binding characteristics. J Mol Biol 1996;260:409-421.
    • (1996) J Mol Biol , vol.260 , pp. 409-421
    • Machius, M.1    Vertesy, L.2    Huber, R.3    Wiegand, G.4
  • 16
    • 0030589635 scopus 로고    scopus 로고
    • Substrate mimicry in the active center of a mammalian alpha-amylase: Structural analysis of an enzyme-inhibitor complex
    • Bompard-Gilles C, Rousseau P, Rouge P, Payan F. Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complex. Structure 1996;4:1441-1452.
    • (1996) Structure , vol.4 , pp. 1441-1452
    • Bompard-Gilles, C.1    Rousseau, P.2    Rouge, P.3    Payan, F.4
  • 17
    • 0033561250 scopus 로고    scopus 로고
    • A single-domain antibody fragment in complex with RNase A: Non-canonical loop structures and nanomolar affinity using two CDR loops
    • Decanniere K, Desmyter A, Lauwereys M, Ghahroudi MA, Muyldermans S, Wyns L. A single-domain antibody fragment in complex with RNase A: non-canonical loop structures and nanomolar affinity using two CDR loops. Struct Fold Des 1999;7:361-370.
    • (1999) Struct Fold Des , vol.7 , pp. 361-370
    • Decanniere, K.1    Desmyter, A.2    Lauwereys, M.3    Ghahroudi, M.A.4    Muyldermans, S.5    Wyns, L.6
  • 18
    • 0035854724 scopus 로고    scopus 로고
    • Antigen specificity and high affinity binding provided by one single loop of a camel single-domain antibody
    • Desmyter A, Decanniere K, Muyldermans S, Wyns L. Antigen specificity and high affinity binding provided by one single loop of a camel single-domain antibody. J Biol Chem 2001;276:26285-26290.
    • (2001) J Biol Chem , vol.276 , pp. 26285-26290
    • Desmyter, A.1    Decanniere, K.2    Muyldermans, S.3    Wyns, L.4
  • 21
    • 0034329441 scopus 로고    scopus 로고
    • Structure of a covalently stabilized complex of a human alphabeta T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1
    • Hennecke J, Carfi A, Wiley DC. Structure of a covalently stabilized complex of a human alphabeta T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1. EMBO J 2000;19:5611-5624.
    • (2000) EMBO J , vol.19 , pp. 5611-5624
    • Hennecke, J.1    Carfi, A.2    Wiley, D.C.3
  • 23
    • 0033521685 scopus 로고    scopus 로고
    • Structural basis for the recognition of superantigen streptococcal pyrogenic exotoxin A (SpeA1) by MHC class II molecules and T-cell receptors
    • Papageorgiou AC, Collins CM, Gutman DM, Kline JB, O'Brien SM, Tranter HS, Acharya KR. Structural basis for the recognition of superantigen streptococcal pyrogenic exotoxin A (SpeA1) by MHC class II molecules and T-cell receptors. EMBO J 1999;18:9-21.
    • (1999) EMBO J , vol.18 , pp. 9-21
    • Papageorgiou, A.C.1    Collins, C.M.2    Gutman, D.M.3    Kline, J.B.4    O'Brien, S.M.5    Tranter, H.S.6    Acharya, K.R.7
  • 25
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 27
    • 0028774703 scopus 로고
    • Refined structures of the active Ser83→Cys and impaired Ser46→Asp histidine-containing phosphocarrier proteins
    • Liao DI, Herzberg O. Refined structures of the active Ser83→Cys and impaired Ser46→Asp histidine-containing phosphocarrier proteins. Structure 1994;2:1203-1216.
    • (1994) Structure , vol.2 , pp. 1203-1216
    • Liao, D.I.1    Herzberg, O.2
  • 30
    • 0037189507 scopus 로고    scopus 로고
    • Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology
    • Desmyter A, Spinelli S, Payan F, Lauwereys M, Wyns L, Muyldermans S, Cambillau C. Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology. J Biol Chem 2002;277:23645-23650.
    • (2002) J Biol Chem , vol.277 , pp. 23645-23650
    • Desmyter, A.1    Spinelli, S.2    Payan, F.3    Lauwereys, M.4    Wyns, L.5    Muyldermans, S.6    Cambillau, C.7
  • 32
    • 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
  • 33
    • 0038185195 scopus 로고    scopus 로고
    • Effect of local shape modifications of molecular surfaces on rigid-body protein-protein docking
    • in press
    • Heifetz A, Eisenstein M. Effect of local shape modifications of molecular surfaces on rigid-body protein-protein docking. Protein Engineering 2003:16 (in press).
    • (2003) Protein Engineering , pp. 16
    • Heifetz, A.1    Eisenstein, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.