메뉴 건너뛰기




Volumn 21, Issue 8, 2014, Pages 779-789

Protein-protein interactions and prediction: A comprehensive overview

Author keywords

Binding sites; Interface features; Prediction; Protein complexes; Protein Protein interactions

Indexed keywords

MEMBRANE PROTEIN; PROTEIN P15; TRANSPORTER ASSOCIATED WITH ANTIGEN PROCESSING; UNCLASSIFIED DRUG;

EID: 84903701114     PISSN: 09298665     EISSN: 18755305     Source Type: Journal    
DOI: 10.2174/09298665113209990056     Document Type: Article
Times cited : (21)

References (144)
  • 1
    • 33846925964 scopus 로고    scopus 로고
    • The molecular architecture of protein-Protein binding sites
    • DOI 10.1016/j.sbi.2007.01.004, PII S0959440X0700005X, Foldinf and Binding / Protein-Nucleic Interactions
    • Reichmann, D.; Rahat, O.; Cohen, M.; Neuvirth, H.; Schreiber, G. The molecular architecture of protein-Protein binding sites. Curr. Opin. Struct. Biol., 2007, 17, 67-76. (Pubitemid 46240815)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.1 , pp. 67-76
    • Reichmann, D.1    Rahat, O.2    Cohen, M.3    Neuvirth, H.4    Schreiber, G.5
  • 2
    • 37249065351 scopus 로고    scopus 로고
    • The molecular sociology of the cell
    • DOI 10.1038/nature06523, PII NATURE06523
    • Robinson, C.V.; Sali, A.; Baumeister, W. The molecular sociology of the cell. Nature, 2007, 450, 973-82. (Pubitemid 350273627)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 973-982
    • Robinson, C.V.1    Sali, A.2    Baumeister, W.3
  • 3
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-Hanging fruit in drug discovery at protein-Protein interfaces
    • DOI 10.1038/nature06526, PII NATURE06526
    • Wells, J.A.; McClendon, C.L. Reaching for high-hanging fruit in drug discovery at protein-Protein interfaces. Nature, 2007, 450, 1001-9. (Pubitemid 350273630)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 4
    • 43149092276 scopus 로고    scopus 로고
    • Principles of protein-Protein interactions: What are the preferred ways for proteins to interact?
    • DOI 10.1021/cr040409x
    • Keskin, O.; Gursoy, A.; Ma, B.; Nussinov, R. Principles of proteinprotein interactions: what are the preferred ways for proteins to interact? Chem. Rev., 2008, 108, 1225-44. (Pubitemid 351638814)
    • (2008) Chemical Reviews , vol.108 , Issue.4 , pp. 1225-1244
    • Keskin, O.1    Gursoy, A.2    Ma, B.3    Nussinov, R.4
  • 5
    • 79551681222 scopus 로고    scopus 로고
    • Protein binding specificity versus promiscuity
    • Schreiber, G.; Keating, A.E. Protein binding specificity versus promiscuity. Curr. Opin. Struct. Biol., 2011, 21, 50-61.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 50-61
    • Schreiber, G.1    Keating, A.E.2
  • 6
    • 52649130704 scopus 로고    scopus 로고
    • Protein-Protein interaction and quaternary structure
    • Janin, J.; Bahadur, R.P.; Chakrabarti, P. Protein-Protein interaction and quaternary structure. Q Rev. Biophys., 2008, 41, 133-80.
    • (2008) Q Rev. Biophys. , vol.41 , pp. 133-180
    • Janin, J.1    Bahadur, R.P.2    Chakrabarti, P.3
  • 7
    • 84889817521 scopus 로고    scopus 로고
    • Insights from the structural analysis of protein heterodimer interfaces
    • Sowmya, G.; Anita, S.; Kangueane, P. Insights from the structural analysis of protein heterodimer interfaces. Bioinformation, 2011, 6, 137-43.
    • (2011) Bioinformation , vol.6 , pp. 137-143
    • Sowmya, G.1    Anita, S.2    Kangueane, P.3
  • 8
    • 0035212065 scopus 로고    scopus 로고
    • Is there a bias in proteome research?
    • DOI 10.1101/gr.206701
    • Mrowka, R.; Patzak, A.; Herzel, H. Is there a bias in proteome research? Genome Res., 2001, 11, 1971-3. (Pubitemid 33138792)
    • (2001) Genome Research , vol.11 , Issue.12 , pp. 1971-1973
    • Mrowka, R.1    Patzak, A.2    Herzel, H.3
  • 9
    • 0037161731 scopus 로고    scopus 로고
    • Comparative assessment of large-scale data sets of protein-Protein interactions
    • von Mering, C.; Krause, R.; Snel, B.; Cornell, M.; Oliver, S.G.; Fields, S.; Bork, P. Comparative assessment of large-scale data sets of protein-Protein interactions. Nature, 2002, 417, 399-403. (Pubitemid 34563526)
    • (2002) Nature , vol.417 , Issue.6887 , pp. 399-403
    • Von Mering, C.1    Krause, R.2    Snel, B.3    Cornell, M.4    Oliver, S.G.5    Fields, S.6    Bork, P.7
  • 10
    • 22344435988 scopus 로고    scopus 로고
    • Prediction of physical protein-Protein interactions
    • DOI 10.1088/1478-3975/2/2/S01
    • Szilagyi, A.; Grimm, V.; Arakaki, A.K.; Skolnick, J. Prediction of physical protein-Protein interactions. Phys. Biol., 2005, 2, S1-16. (Pubitemid 41001323)
    • (2005) Physical Biology , vol.2 , Issue.2
    • Szilagyi, A.1    Grimm, V.2    Arakaki, A.K.3    Skolnick, J.4
  • 11
    • 33644550021 scopus 로고    scopus 로고
    • Structural systems biology: Modelling protein interactions
    • Aloy, P.; Russell, R.B. Structural systems biology: modelling protein interactions. Nat. Rev. Mol. Cell Biol., 2006, 7, 188-97.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 188-197
    • Aloy, P.1    Russell, R.B.2
  • 13
    • 0036468385 scopus 로고    scopus 로고
    • Prediction of protein-Protein interactions by docking methods
    • DOI 10.1016/S0959-440X(02)00285-3
    • Smith, G.R.; Sternberg, M.J. Prediction of protein-Protein interactions by docking methods. Curr. Opin. Struct. Biol., 2002, 12, 28-35. (Pubitemid 34142717)
    • (2002) Current Opinion in Structural Biology , vol.12 , Issue.1 , pp. 28-35
    • Smith, G.R.1    Sternberg, M.J.E.2
  • 15
    • 0036468396 scopus 로고    scopus 로고
    • Protein-Protein association kinetics and protein docking
    • DOI 10.1016/S0959-440X(02)00286-5
    • Camacho, C.J.; Vajda, S. Protein-Protein association kinetics and protein docking. Curr. Opin. Struct. Biol., 2002, 12, 36-40. (Pubitemid 34142718)
    • (2002) Current Opinion in Structural Biology , vol.12 , Issue.1 , pp. 36-40
    • Camacho, C.J.1    Vajda, S.2
  • 16
    • 0036606483 scopus 로고    scopus 로고
    • Principles of docking: An overview of search algorithms and a guide to scoring functions
    • DOI 10.1002/prot.10115
    • 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, 409-43. (Pubitemid 34614722)
    • (2002) Proteins: Structure, Function and Genetics , vol.47 , Issue.4 , pp. 409-443
    • Halperin, I.1    Ma, B.2    Wolfson, H.3    Nussinov, R.4
  • 17
    • 0036180566 scopus 로고    scopus 로고
    • Electrostatics in protein-Protein docking
    • DOI 10.1110/ps.26002
    • Heifetz, A.; Katchalski-Katzir, E.; Eisenstein, M. Electrostatics in protein-Protein docking. Protein Sci., 2002, 11, 571-87. (Pubitemid 34171262)
    • (2002) Protein Science , vol.11 , Issue.3 , pp. 571-587
    • Heifetz, A.1    Katchalski-Katzir, E.2    Eisenstein, M.3
  • 19
    • 77952068704 scopus 로고    scopus 로고
    • Are scoring functions in proteinprotein docking ready to predict interactomes? Clues from a novel binding affinity benchmark
    • Kastritis, P.L.; Bonvin, A.M. Are scoring functions in proteinprotein docking ready to predict interactomes? Clues from a novel binding affinity benchmark. J. Proteome Res., 2010, 9, 2216-25.
    • (2010) J. Proteome Res. , vol.9 , pp. 2216-2225
    • Kastritis, P.L.1    Bonvin, A.M.2
  • 21
    • 48749126860 scopus 로고    scopus 로고
    • Insights into protein flexibility: The relationship between normal modes and conformational change upon protein-Protein docking
    • Dobbins, S.E.; Lesk, V.I.; Sternberg, M.J. Insights into protein flexibility: The relationship between normal modes and conformational change upon protein-Protein docking. Proc. Natl. Acad. Sci. USA, 2008, 105, 10390-5.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 10390-10395
    • Dobbins, S.E.1    Lesk, V.I.2    Sternberg, M.J.3
  • 22
    • 33751423377 scopus 로고    scopus 로고
    • How different are structurally flexible and rigid binding sites? Sequence and structural features discriminating proteins that do and do not undergo conformational change upon ligand binding
    • DOI 10.1016/j.jmb.2006.09.062, PII S0022283606012861
    • Gunasekaran, K.; Nussinov, R. How different are structurally flexible and rigid binding sites? Sequence and structural features discriminating proteins that do and do not undergo conformational change upon ligand binding. J. Mol. Biol., 2007, 365, 257-73. (Pubitemid 44821204)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.1 , pp. 257-273
    • Gunasekaran, K.1    Nussinov, R.2
  • 23
    • 49049105131 scopus 로고    scopus 로고
    • Using protein binding site prediction to improve protein docking
    • Huang, B.; Schroeder, M. Using protein binding site prediction to improve protein docking. Gene, 2008, 422, 14-21.
    • (2008) Gene , vol.422 , pp. 14-21
    • Huang, B.1    Schroeder, M.2
  • 24
    • 66149136452 scopus 로고    scopus 로고
    • Shape complementarity of protein-Protein complexes at multiple resolutions
    • Zhang, Q.; Sanner, M.; Olson, A.J. Shape complementarity of protein-Protein complexes at multiple resolutions. Proteins, 2009, 75, 453-67.
    • (2009) Proteins , vol.75 , pp. 453-467
    • Zhang, Q.1    Sanner, M.2    Olson, A.J.3
  • 25
    • 0025123333 scopus 로고
    • The structure of protein-Protein recognition sites
    • Janin, J.; Chothia, C. The structure of protein-Protein recognition sites. J. Biol. Chem., 1990, 265, 16027-30.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 26
    • 0029109468 scopus 로고
    • Protein-Protein interactions: A review of protein dimer structures
    • Jones, S.; Thornton, J.M. Protein-Protein interactions: A review of protein dimer structures. Prog. Biophys. Mol. Biol., 1995, 63, 31-65.
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , pp. 31-65
    • Jones, S.1    Thornton, J.M.2
  • 29
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-Protein recognition sites
    • DOI 10.1006/jmbi.1998.2439
    • Lo Conte, L.; Chothia, C.; Janin, J. The atomic structure of proteinprotein recognition sites. J. Mol. Biol., 1999, 285, 2177-98. (Pubitemid 29078179)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.5 , pp. 2177-2198
    • Conte, L.L.1    Chothia, C.2    Janin, J.3
  • 31
    • 59549088662 scopus 로고    scopus 로고
    • ProtorP: A protein-Protein interaction analysis server
    • Reynolds, C.; Damerell, D.; Jones, S. ProtorP: A protein-Protein interaction analysis server. Bioinformatics, 2009, 25, 413-4.
    • (2009) Bioinformatics , vol.25 , pp. 413-414
    • Reynolds, C.1    Damerell, D.2    Jones, S.3
  • 35
    • 5044235050 scopus 로고    scopus 로고
    • Ten thousand interactions for the molecular biologist
    • DOI 10.1038/nbt1018
    • Aloy, P.; Russell, R. B. Ten thousand interactions for the molecular biologist. Nat Biotechnol, 2004, 22, 1317-21. (Pubitemid 39336787)
    • (2004) Nature Biotechnology , vol.22 , Issue.10 , pp. 1317-1321
    • Aloy, P.1    Russell, R.B.2
  • 36
    • 5044235050 scopus 로고    scopus 로고
    • Ten thousand interactions for the molecular biologist
    • DOI 10.1038/nbt1018
    • Aloy, P.; Russell, R. B. Ten thousand interactions for the molecular biologist. Nat. Biotechnol., 2004, 22, 1317-21. (Pubitemid 39336787)
    • (2004) Nature Biotechnology , vol.22 , Issue.10 , pp. 1317-1321
    • Aloy, P.1    Russell, R.B.2
  • 37
    • 33847744247 scopus 로고    scopus 로고
    • How complete are current yeast and human protein-Interaction networks?
    • Hart, G. T.; Ramani, A. K.; Marcotte, E. M. How complete are current yeast and human protein-interaction networks? Genome Biol., 2006, 7, 120.
    • (2006) Genome Biol. , vol.7 , pp. 120
    • Hart, G.T.1    Ramani, A.K.2    Marcotte, E.M.3
  • 38
    • 78650274124 scopus 로고    scopus 로고
    • New insights into protein-Protein interaction data lead to increased estimates of the S. Cerevisiae interactome size
    • Sambourg, L.; Thierry-Mieg, N. New insights into protein-Protein interaction data lead to increased estimates of the S. cerevisiae interactome size. BMC Bioinformatics, 2010, 11, 605.
    • (2010) BMC Bioinformatics , vol.11 , pp. 605
    • Sambourg, L.1    Thierry-Mieg, N.2
  • 39
    • 13844277017 scopus 로고    scopus 로고
    • New methodologies for measuring protein interactions in vivo and in vitro
    • DOI 10.1016/j.sbi.2005.01.008
    • Piehler, J. New methodologies for measuring protein interactions in vivo and in vitro. Curr. Opin. Struct. Biol., 2005, 15, 4-14. (Pubitemid 40249503)
    • (2005) Current Opinion in Structural Biology , vol.15 , pp. 4-14
    • Piehler, J.1
  • 40
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-Protein interactions
    • DOI 10.1038/340245a0
    • Fields, S.; Song, O. A novel genetic system to detect proteinprotein interactions. Nature, 1989, 340, 245-6. (Pubitemid 19171591)
    • (1989) Nature , vol.340 , Issue.6230 , pp. 245-246
    • Fields, S.1    Song, O.-K.2
  • 41
    • 0027250250 scopus 로고
    • Mammalian ras interacts directly with the serine/threonine kinase Raf
    • DOI 10.1016/0092-8674(93)90307-C
    • Vojtek, A. B.; Hollenberg, S. M.; Cooper, J. A. Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell, 1993, 74, 205-14. (Pubitemid 23219891)
    • (1993) Cell , vol.74 , Issue.1 , pp. 205-214
    • Vojtek, A.B.1    Hollenberg, S.M.2    Cooper, J.A.3
  • 42
    • 0030624529 scopus 로고    scopus 로고
    • Alternative yeast two-Hybrid systems. The interaction trap and interaction mating
    • Golemis, E. A.; Khazak, V. Alternative yeast two-hybrid systems. The interaction trap and interaction mating. Methods Mol. Biol., 1997, 63, 197-218.
    • (1997) Methods Mol. Biol. , vol.63 , pp. 197-218
    • Golemis, E.A.1    Khazak, V.2
  • 43
    • 0030851629 scopus 로고    scopus 로고
    • Improved efficiency Sos recruitment system: Expression of the mammalian GAP reduces isolation of Ras GTPase false positives
    • DOI 10.1093/nar/25.16.3373
    • Aronheim, A. Improved efficiency sos recruitment system: expression of the mammalian GAP reduces isolation of Ras GTPase false positives. Nucleic Acids Res., 1997, 25, 3373-4. (Pubitemid 27338701)
    • (1997) Nucleic Acids Research , vol.25 , Issue.16 , pp. 3373-3374
    • Aronheim, A.1
  • 45
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial twohybrid system based on a reconstituted signal transduction pathway
    • Karimova, G.; Pidoux, J.; Ullmann, A.; Ladant, D. A bacterial twohybrid system based on a reconstituted signal transduction pathway. Proc. Natl. Acad. Sci. USA, 1998, 95, 5752-6.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 46
    • 0034691202 scopus 로고    scopus 로고
    • A bacterial two-Hybrid selection system for studying protein-DNA and protein-Protein interactions
    • Joung, J. K.; Ramm, E. I.; Pabo, C. O. A bacterial two-hybrid selection system for studying protein-DNA and protein-Protein interactions. Proc. Natl. Acad. Sci. USA, 2000, 97, 7382-7.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7382-7387
    • Joung, J.K.1    Ramm, E.I.2    Pabo, C.O.3
  • 48
    • 0037995710 scopus 로고    scopus 로고
    • Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis
    • DOI 10.1038/nbt816
    • Hu, C. D.; Kerppola, T. K. Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis. Nat. Biotechnol., 2003, 21, 539-45. (Pubitemid 36532019)
    • (2003) Nature Biotechnology , vol.21 , Issue.5 , pp. 539-545
    • Hu, C.-D.1    Kerppola, T.K.2
  • 50
    • 84855195456 scopus 로고    scopus 로고
    • Nanodisc-Based coimmunoprecipitation for mass spectrometric identification of membrane-Interacting proteins
    • O110 006775
    • Borch, J.; Roepstorff, P.; Moller-Jensen, J. Nanodisc-Based coimmunoprecipitation for mass spectrometric identification of membrane-interacting proteins. Mol. Cell Proteomics, 2011, 10, O110 006775.
    • (2011) Mol. Cell Proteomics , vol.10
    • Borch, J.1    Roepstorff, P.2    Moller-Jensen, J.3
  • 51
    • 77957254319 scopus 로고    scopus 로고
    • Identifying components of protein complexes in C. Elegans using co-Immunoprecipitation and mass spectrometry
    • Moresco, J. J.; Carvalho, P. C.; Yates, J. R., 3rd. Identifying components of protein complexes in C. elegans using co-immunoprecipitation and mass spectrometry. J. Proteomics, 2010, 73, 2198-204.
    • (2010) J. Proteomics , vol.73 , pp. 2198-2204
    • Moresco, J.J.1    Carvalho, P.C.2    Yates III, J.R.3
  • 52
    • 80755153605 scopus 로고    scopus 로고
    • Identification of proteins interacting with lactate dehydrogenase in claw muscle of the porcelain crab Petrolisthes cinctipes
    • Cayenne, A. P.; Gabert, B.; Stillman, J. H. Identification of proteins interacting with lactate dehydrogenase in claw muscle of the porcelain crab Petrolisthes cinctipes. Comp. Biochem. Physiol. Part D Genomics Proteomics, 2011, 6, 393-8.
    • (2011) Comp. Biochem. Physiol. Part D Genomics Proteomics , vol.6 , pp. 393-398
    • Cayenne, A.P.1    Gabert, B.2    Stillman, J.H.3
  • 53
    • 34047202181 scopus 로고    scopus 로고
    • Deciphering protein-Protein interactions. Part I. Experimental techniques and databases
    • Shoemaker, B. A.; Panchenko, A. R. Deciphering protein-Protein interactions. Part I. Experimental techniques and databases. PLoS Comput. Biol., 2007, 3, e42.
    • (2007) PLoS Comput. Biol. , vol.3
    • Shoemaker, B.A.1    Panchenko, A.R.2
  • 54
    • 65549157572 scopus 로고    scopus 로고
    • A survey of available tools and web servers for analysis of proteinprotein interactions and interfaces
    • Tuncbag, N.; Kar, G.; Keskin, O.; Gursoy, A.; Nussinov, R. A survey of available tools and web servers for analysis of proteinprotein interactions and interfaces. Brief Bioinform., 2009, 10, 217-32.
    • (2009) Brief Bioinform. , vol.10 , pp. 217-232
    • Tuncbag, N.1    Kar, G.2    Keskin, O.3    Gursoy, A.4    Nussinov, R.5
  • 55
    • 0036088133 scopus 로고    scopus 로고
    • DIP, the Database of Interacting Proteins: A research tool for studying cellular networks of protein interactions
    • Xenarios, I.; Salwinski, L.; Duan, X. J.; Higney, P.; Kim, S. M.; Eisenberg, D. DIP, the Database of Interacting Proteins: A research tool for studying cellular networks of protein interactions. Nucleic Acids Res., 2002, 30, 303-5. (Pubitemid 34679570)
    • (2002) Nucleic Acids Research , vol.30 , Issue.1 , pp. 303-305
    • Xenarios, I.1    Salwinski, L.2    Duan, X.J.3    Higney, P.4    Kim, S.-M.5    Eisenberg, D.6
  • 56
    • 0036463402 scopus 로고    scopus 로고
    • Describing biological protein interactions in terms of protein states and state transitions: The LiveDIP database
    • Duan, X. J.; Xenarios, I.; Eisenberg, D. Describing biological protein interactions in terms of protein states and state transitions: The LiveDIP database. Mol. Cell Proteomics, 2002, 1, 104-16.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 104-116
    • Duan, X.J.1    Xenarios, I.2    Eisenberg, D.3
  • 58
    • 0033930882 scopus 로고    scopus 로고
    • BIND -A data specification for storing and describing biomolecular interactions, molecular complexes and pathways
    • Bader, G. D.; Hogue, C. W. BIND-A data specification for storing and describing biomolecular interactions, molecular complexes and pathways. Bioinformatics, 2000, 16, 465-77. (Pubitemid 30487967)
    • (2000) Bioinformatics , vol.16 , Issue.5 , pp. 465-477
    • Bader, G.D.1    Hogue, C.W.V.2
  • 60
    • 79955667824 scopus 로고    scopus 로고
    • The Biomolecular Interaction Network Database in PSI-MI 2.5
    • (Oxford)
    • Isserlin, R.; El-Badrawi, R. A.; Bader, G. D. The Biomolecular Interaction Network Database in PSI-MI 2.5. Database (Oxford), 2011, 2011, baq037.
    • (2011) Database , vol.2011
    • Isserlin, R.1    El-Badrawi, R.A.2    Bader, G.D.3
  • 66
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-Protein interactions
    • DOI 10.1093/emboj/cdg359
    • Nooren, I. M.; Thornton, J. M. Diversity of protein-Protein interactions. EMBO J., 2003, 22, 3486-92. (Pubitemid 36898326)
    • (2003) EMBO Journal , vol.22 , Issue.14 , pp. 3486-3492
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 68
  • 69
    • 0031565729 scopus 로고    scopus 로고
    • Analysis of protein-Protein interaction sites using surface patches
    • DOI 10.1006/jmbi.1997.1234
    • Jones, S.; Thornton, J. M. Analysis of protein-Protein interaction sites using surface patches. J. Mol. Biol., 1997, 272, 121-32. (Pubitemid 27395542)
    • (1997) Journal of Molecular Biology , vol.272 , Issue.1 , pp. 121-132
    • Jones, S.1    Thornton, J.M.2
  • 71
    • 79956221510 scopus 로고    scopus 로고
    • On the role of electrostatics in protein-Protein interactions
    • Zhang, Z.; Witham, S.; Alexov, E. On the role of electrostatics in protein-Protein interactions. Phys. Biol., 2011, 8, 035001.
    • (2011) Phys. Biol. , vol.8 , pp. 035001
    • Zhang, Z.1    Witham, S.2    Alexov, E.3
  • 72
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterisation and functional significance of transient protein-Protein interactions
    • DOI 10.1016/S0022-2836(02)01281-0
    • Nooren, I. M.; Thornton, J. M. Structural characterisation and functional significance of transient protein-Protein interactions. J. Mol. Biol., 2003, 325, 991-1018. (Pubitemid 36263408)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.5 , pp. 991-1018
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 73
    • 85067775899 scopus 로고    scopus 로고
    • Predicting permanent and transient protein-Protein interfaces
    • La, D.; Kong, M.; Hoffman, W.; Choi, Y. I.; Kihara, D. Predicting permanent and transient protein-Protein interfaces. Proteins, 2012.
    • (2012) Proteins
    • La, D.1    Kong, M.2    Hoffman, W.3    Choi, Y.I.4    Kihara, D.5
  • 74
    • 0037229456 scopus 로고    scopus 로고
    • Analysing six types of protein-Protein interfaces
    • DOI 10.1016/S0022-2836(02)01223-8
    • Ofran, Y.; Rost, B. Analysing six types of protein-Protein interfaces. J. Mol. Biol., 2003, 325, 377-87. (Pubitemid 36062695)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.2 , pp. 377-387
    • Ofran, Y.1    Rost, B.2
  • 76
    • 77957771797 scopus 로고    scopus 로고
    • Transient protein-Protein interactions: Structural, functional, and network properties
    • Perkins, J. R.; Diboun, I.; Dessailly, B. H.; Lees, J. G.; Orengo, C. Transient protein-Protein interactions: Structural, functional, and network properties. Structure, 2010, 18, 1233-43.
    • (2010) Structure , vol.18 , pp. 1233-1243
    • Perkins, J.R.1    Diboun, I.2    Dessailly, B.H.3    Lees, J.G.4    Orengo, C.5
  • 77
    • 77957944014 scopus 로고    scopus 로고
    • Protein-Protein docking benchmark version 4.0
    • Hwang, H.; Vreven, T.; Janin, J.; Weng, Z. Protein-Protein docking benchmark version 4.0. Proteins, 2010, 78, 3111-4.
    • (2010) Proteins , vol.78 , pp. 3111-3114
    • Hwang, H.1    Vreven, T.2    Janin, J.3    Weng, Z.4
  • 78
    • 84859738249 scopus 로고    scopus 로고
    • Roles of residues in the interface of transient protein-Protein complexes before complexation
    • Swapna, L. S.; Bhaskara, R. M.; Sharma, J.; Srinivasan, N. Roles of residues in the interface of transient protein-Protein complexes before complexation. Sci. Rep., 2012, 2, 334.
    • (2012) Sci. Rep. , vol.2 , pp. 334
    • Swapna, L.S.1    Bhaskara, R.M.2    Sharma, J.3    Srinivasan, N.4
  • 79
    • 0034060520 scopus 로고    scopus 로고
    • Protein domain interfaces: Characterization and comparison with oligomeric protein interfaces
    • Jones, S.; Marin, A.; Thornton, J. M. Protein domain interfaces: Characterization and comparison with oligomeric protein interfaces. Protein Eng., 2000, 13, 77-82. (Pubitemid 30151037)
    • (2000) Protein Engineering , vol.13 , Issue.2 , pp. 77-82
    • Jones, S.1    Marin, A.2    Thornton, J.M.3
  • 80
    • 64849109745 scopus 로고    scopus 로고
    • Prediction of protein-Protein interaction types using association rule based classification
    • Park, S. H.; Reyes, J. A.; Gilbert, D. R.; Kim, J. W.; Kim, S. Prediction of protein-Protein interaction types using association rule based classification. BMC Bioinformatics, 2009, 10, 36.
    • (2009) BMC Bioinformatics , vol.10 , pp. 36
    • Park, S.H.1    Reyes, J.A.2    Gilbert, D.R.3    Kim, J.W.4    Kim, S.5
  • 81
    • 0016708122 scopus 로고
    • Principles of protein-Protein recognition
    • Chothia, C.; Janin, J. Principles of protein-Protein recognition. Nature, 1975, 256, 705-8.
    • (1975) Nature , vol.256 , pp. 705-708
    • Chothia, C.1    Janin, J.2
  • 82
    • 0023193446 scopus 로고
    • The accessible surface area and stability of oligomeric proteins
    • DOI 10.1038/328834a0
    • Miller, S.; Lesk, A. M.; Janin, J.; Chothia, C. The accessible surface area and stability of oligomeric proteins. Nature, 1987, 328, 834-6. (Pubitemid 17125965)
    • (1987) Nature , vol.328 , Issue.6133 , pp. 834-836
    • Miller, S.1    Lesk, A.M.2    Janin, J.3    Chothia, C.4
  • 83
    • 1842405464 scopus 로고    scopus 로고
    • Studies of protein-Protein interfaces: A statistical analysis of the hydrophobic effect
    • Tsai, C. J.; Lin, S. L.; Wolfson, H. J.; Nussinov, R. Studies of protein-protein interfaces: A statistical analysis of the hydrophobic effect. Protein Sci., 1997, 6, 53-64. (Pubitemid 27045243)
    • (1997) Protein Science , vol.6 , Issue.1 , pp. 53-64
    • Tsai, C.-J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 84
    • 33746276951 scopus 로고    scopus 로고
    • ProFace: A server for the analysis of the physicochemical features of protein-Protein interfaces
    • Saha, R. P.; Bahadur, R. P.; Pal, A.; Mandal, S.; Chakrabarti, P. ProFace: A server for the analysis of the physicochemical features of protein-Protein interfaces. BMC Struct. Biol., 2006, 6, 11.
    • (2006) BMC Struct. Biol. , vol.6 , pp. 11
    • Saha, R.P.1    Bahadur, R.P.2    Pal, A.3    Mandal, S.4    Chakrabarti, P.5
  • 85
    • 0346733329 scopus 로고    scopus 로고
    • Are protein-Protein interfaces more conserved in sequence than the rest of the protein surface?
    • DOI 10.1110/ps.03323604
    • Caffrey, D. R.; Somaroo, S.; Hughes, J. D.; Mintseris, J.; Huang, E. S. Are protein-Protein interfaces more conserved in sequence than the rest of the protein surface? Protein Sci., 2004, 13, 190-202. (Pubitemid 38021153)
    • (2004) Protein Science , vol.13 , Issue.1 , pp. 190-202
    • Caffrey, D.R.1    Somaroo, S.2    Hughes, J.D.3    Mintseris, J.4    Huang, E.S.5
  • 88
    • 33846662784 scopus 로고    scopus 로고
    • ISIS: Interaction sites identified from sequence
    • DOI 10.1093/bioinformatics/btl303
    • Ofran, Y.; Rost, B. ISIS: interaction sites identified from sequence. Bioinformatics, 2007, 23, e13-6. (Pubitemid 46189629)
    • (2007) Bioinformatics , vol.23 , Issue.2
    • Ofran, Y.1    Rost, B.2
  • 89
    • 0031450506 scopus 로고    scopus 로고
    • Hydrogen bonds and salt bridges across protein-Protein interfaces
    • Xu, D.; Tsai, C. J.; Nussinov, R. Hydrogen bonds and salt bridges across protein-Protein interfaces. Protein Eng., 1997, 10, 999-1012. (Pubitemid 28004646)
    • (1997) Protein Engineering , vol.10 , Issue.9 , pp. 999-1012
    • Xu, D.1    Tsai, C.-J.2    Nussinov, R.3
  • 90
    • 2942741128 scopus 로고    scopus 로고
    • Structure-Based method for analyzing protein-Protein interfaces
    • DOI 10.1007/s00894-003-0168-3
    • Gao, Y.; Wang, R.; Lai, L. Structure-Based method for analyzing protein-Protein interfaces. J. Mol. Model., 2004, 10, 44-54. (Pubitemid 38787175)
    • (2004) Journal of Molecular Modeling , vol.10 , Issue.1 , pp. 44-54
    • Gao, Y.1    Wang, R.2    Lai, L.3
  • 92
    • 77952686736 scopus 로고    scopus 로고
    • Conserved residue clusters at proteinprotein interfaces and their use in binding site identification
    • Guharoy, M.; Chakrabarti, P. Conserved residue clusters at proteinprotein interfaces and their use in binding site identification. BMC Bioinformatics, 2010, 11, 286.
    • (2010) BMC Bioinformatics , vol.11 , pp. 286
    • Guharoy, M.1    Chakrabarti, P.2
  • 94
    • 80054029788 scopus 로고    scopus 로고
    • Sequence and structural features of binding site residues in proteinprotein complexes: Comparison with protein-Nucleic acid complexes
    • Gromiha, M. M.; Saranya, N.; Selvaraj, S.; Jayaram, B.; Fukui, K. Sequence and structural features of binding site residues in proteinprotein complexes: Comparison with protein-nucleic acid complexes. Proteome Sci., 2011, 9 Suppl 1, S13.
    • (2011) Proteome Sci. , vol.9 , Issue.SUPPL.1
    • Gromiha, M.M.1    Saranya, N.2    Selvaraj, S.3    Jayaram, B.4    Fukui, K.5
  • 95
    • 84871967106 scopus 로고    scopus 로고
    • Interactome3D: Adding structural details to protein networks
    • Mosca, R.; Ceol, A.; Aloy, P. Interactome3D: Adding structural details to protein networks. Nat. Methods, 2012, 10, 47-53.
    • (2012) Nat. Methods , vol.10 , pp. 47-53
    • Mosca, R.1    Ceol, A.2    Aloy, P.3
  • 96
    • 18744382508 scopus 로고    scopus 로고
    • PIBASE: A comprehensive database of structurally defined protein interfaces
    • DOI 10.1093/bioinformatics/bti277
    • Davis, F. P.; Sali, A. PIBASE: A comprehensive database of structurally defined protein interfaces. Bioinformatics, 2005, 21, 1901-7. (Pubitemid 40668025)
    • (2005) Bioinformatics , vol.21 , Issue.9 , pp. 1901-1907
    • Davis, F.P.1    Sali, A.2
  • 97
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A. G.; Brenner, S. E.; Hubbard, T.; Chothia, C. SCOP: A structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol., 1995, 247, 536-40.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 98
    • 85027934053 scopus 로고    scopus 로고
    • The CATH database
    • Knudsen, M.; Wiuf, C. The CATH database. Hum. Genomics, 2010, 4, 207-12.
    • (2010) Hum. Genomics , vol.4 , pp. 207-212
    • Knudsen, M.1    Wiuf, C.2
  • 99
    • 33644876493 scopus 로고    scopus 로고
    • SCOPPI: A structural classification of protein-Protein interfaces
    • Winter, C.; Henschel, A.; Kim, W. K.; Schroeder, M. SCOPPI: A structural classification of protein-Protein interfaces. Nucleic Acids Res., 2006, 34, D310-4.
    • (2006) Nucleic Acids Res. , vol.34
    • Winter, C.1    Henschel, A.2    Kim, W.K.3    Schroeder, M.4
  • 100
    • 13444257903 scopus 로고    scopus 로고
    • 3did: Interacting protein domains of known three-Dimensional structure
    • DOI 10.1093/nar/gki037
    • Stein, A.; Russell, R. B.; Aloy, P. 3did: interacting protein domains of known three-Dimensional structure. Nucleic Acids Res., 2005, 33, D413-7. (Pubitemid 40207906)
    • (2005) Nucleic Acids Research , vol.33 , Issue.DATA. ISSUE
    • Stein, A.1    Russell, R.B.2    Aloy, P.3
  • 102
    • 0035175679 scopus 로고    scopus 로고
    • PDBsum: Summaries and analyses of PDB structures
    • Laskowski, R. A. PDBsum: Summaries and analyses of PDB structures. Nucleic Acids Res., 2001, 29, 221-2. (Pubitemid 32054453)
    • (2001) Nucleic Acids Research , vol.29 , Issue.1 , pp. 221-222
    • Laskowski, R.A.1
  • 107
    • 33846077881 scopus 로고    scopus 로고
    • PROTCOM: Searchable database of protein complexes enhanced with domain-Domain structures
    • DOI 10.1093/nar/gkl768
    • Kundrotas, P. J.; Alexov, E. PROTCOM: Searchable database of protein complexes enhanced with domain-Domain structures. Nucleic Acids Res., 2007, 35, D575-9. (Pubitemid 46056273)
    • (2007) Nucleic Acids Research , vol.35 , Issue.SUPPL.1
    • Kundrotas, P.J.1    Alexov, E.2
  • 108
    • 33646553913 scopus 로고    scopus 로고
    • SCOWLP: A web-Based database for detailed characterization and visualization of protein interfaces
    • Teyra, J.; Doms, A.; Schroeder, M.; Pisabarro, M. T. SCOWLP: A web-Based database for detailed characterization and visualization of protein interfaces. BMC Bioinformatics, 2006, 7, 104.
    • (2006) BMC Bioinformatics , vol.7 , pp. 104
    • Teyra, J.1    Doms, A.2    Schroeder, M.3    Pisabarro, M.T.4
  • 109
    • 0037250158 scopus 로고    scopus 로고
    • InterPreTS: Protein Interaction Prediction through Tertiary Structure
    • DOI 10.1093/bioinformatics/19.1.161
    • Aloy, P.; Russell, R. B. InterPreTS: protein interaction prediction through tertiary structure. Bioinformatics, 2003, 19, 161-2. (Pubitemid 36150198)
    • (2003) Bioinformatics , vol.19 , Issue.1 , pp. 161-162
    • Aloy, P.1    Russell, R.B.2
  • 111
    • 33846200437 scopus 로고    scopus 로고
    • Prediction-Based fingerprints of proteinprotein interactions
    • Porollo, A.; Meller, J. Prediction-Based fingerprints of proteinprotein interactions. Proteins, 2007, 66, 630-45.
    • (2007) Proteins , vol.66 , pp. 630-645
    • Porollo, A.1    Meller, J.2
  • 112
    • 24344484686 scopus 로고    scopus 로고
    • Prediction of interface residues in protein-Protein complexes by a consensus neural network method: Test against NMR data
    • DOI 10.1002/prot.20514
    • Chen, H.; Zhou, H. X. Prediction of interface residues in proteinprotein complexes by a consensus neural network method: Test against NMR data. Proteins, 2005, 61, 21-35. (Pubitemid 41262914)
    • (2005) Proteins: Structure, Function and Genetics , vol.61 , Issue.1 , pp. 21-35
    • Chen, H.1    Zhou, H.-X.2
  • 113
    • 34548751368 scopus 로고    scopus 로고
    • Meta-PPISP: A meta web server for protein-Protein interaction site prediction
    • DOI 10.1093/bioinformatics/btm434
    • Qin, S.; Zhou, H. X. meta-PPISP: A meta web server for proteinprotein interaction site prediction. Bioinformatics, 2007, 23, 3386-7. (Pubitemid 350238893)
    • (2007) Bioinformatics , vol.23 , Issue.24 , pp. 3386-3387
    • Qin, S.1    Zhou, H.-X.2
  • 114
    • 34547597799 scopus 로고    scopus 로고
    • PI2PE: Protein interface/interior prediction engine
    • Tjong, H.; Qin, S.; Zhou, H. X. PI2PE: protein interface/interior prediction engine. Nucleic Acids Res., 2007, 35, W357-62.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 357-362
    • Tjong, H.1    Qin, S.2    Zhou, H.X.3
  • 116
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-Ligand interactions
    • Wallace, A. C.; Laskowski, R. A.; Thornton, J. M. LIGPLOT: A program to generate schematic diagrams of protein-Ligand interactions. Protein Eng., 1995, 8, 127-34.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 118
    • 17444372787 scopus 로고    scopus 로고
    • Improved prediction of protein-Protein binding sites using a support vector machines approach
    • DOI 10.1093/bioinformatics/bti242
    • Bradford, J. R.; Westhead, D. R. Improved prediction of proteinprotein binding sites using a support vector machines approach. Bioinformatics, 2005, 21, 1487-94. (Pubitemid 40542704)
    • (2005) Bioinformatics , vol.21 , Issue.8 , pp. 1487-1494
    • Bradford, J.R.1    Westhead, D.R.2
  • 119
    • 38649087636 scopus 로고    scopus 로고
    • Spatial chemical conservation of hot spot interactions in proteinprotein complexes
    • Shulman-Peleg, A.; Shatsky, M.; Nussinov, R.; Wolfson, H. J. Spatial chemical conservation of hot spot interactions in proteinprotein complexes. BMC Biol., 2007, 5, 43.
    • (2007) BMC Biol. , vol.5 , pp. 43
    • Shulman-Peleg, A.1    Shatsky, M.2    Nussinov, R.3    Wolfson, H.J.4
  • 120
    • 33646044395 scopus 로고    scopus 로고
    • WHISCY: What information does surface conservation yield? Application to datadriven docking
    • de Vries, S. J.; van Dijk, A. D.; Bonvin, A. M. WHISCY: what information does surface conservation yield? Application to datadriven docking. Proteins, 2006, 63, 479-89.
    • (2006) Proteins , vol.63 , pp. 479-489
    • De Vries, S.J.1    Van Dijk, A.D.2    Bonvin, A.M.3
  • 121
    • 33846052595 scopus 로고    scopus 로고
    • SNAPPI-DB: A database and API of structures, iNterfaces and Alignments for Protein-Protein Interactions
    • DOI 10.1093/nar/gkl836
    • Jefferson, E. R.; Walsh, T. P.; Roberts, T. J.; Barton, G. J. SNAPPI-DB: A database and API of Structures, iNterfaces and Alignments for Protein-Protein Interactions. Nucleic Acids Res., 2007, 35, D580-9. (Pubitemid 46056274)
    • (2007) Nucleic Acids Research , vol.35 , Issue.SUPPL.1
    • Jefferson, E.R.1    Walsh, T.P.2    Roberts, T.J.3    Barton, G.J.4
  • 122
  • 123
    • 84858175431 scopus 로고    scopus 로고
    • Predicting protein-Protein interface residues using local surface structural similarity
    • Jordan, R. A.; El-Manzalawy, Y.; Dobbs, D.; Honavar, V. Predicting protein-Protein interface residues using local surface structural similarity. BMC Bioinformatics, 2012, 13, 41.
    • (2012) BMC Bioinformatics , vol.13 , pp. 41
    • Jordan, R.A.1    El-Manzalawy, Y.2    Dobbs, D.3    Honavar, V.4
  • 124
    • 84870318670 scopus 로고    scopus 로고
    • Wiki-Pi: A web-Server of annotated human protein-Protein interactions to aid in discovery of protein function
    • Orii, N.; Ganapathiraju, M. K. Wiki-Pi: A web-server of annotated human protein-Protein interactions to aid in discovery of protein function. PLoS One, 2012, 7, e49029.
    • (2012) PLoS One , vol.7
    • Orii, N.1    Ganapathiraju, M.K.2
  • 125
    • 0035066602 scopus 로고    scopus 로고
    • ASEdb: A database of alanine mutations and their effects on the free energy of binding in protein interactions
    • Thorn, K. S.; Bogan, A. A. ASEdb: A database of alanine mutations and their effects on the free energy of binding in protein interactions. Bioinformatics, 2001, 17, 284-5. (Pubitemid 32288219)
    • (2001) Bioinformatics , vol.17 , Issue.3 , pp. 284-285
    • Thorn, K.S.1    Bogan, A.A.2
  • 127
    • 48449100887 scopus 로고    scopus 로고
    • KFC Server: Interactive forecasting of protein interaction hot spots
    • Darnell, S. J.; LeGault, L.; Mitchell, J. C. KFC Server: interactive forecasting of protein interaction hot spots. Nucleic Acids Res., 2008, 36, W265-9.
    • (2008) Nucleic Acids Res. , vol.36
    • Darnell, S.J.1    Legault, L.2    Mitchell, J.C.3
  • 128
    • 38549092067 scopus 로고    scopus 로고
    • HotSprint: Database of computational hot spots in protein interfaces
    • DOI 10.1093/nar/gkm813
    • Guney, E.; Tuncbag, N.; Keskin, O.; Gursoy, A. HotSprint: database of computational hot spots in protein interfaces. Nucleic Acids Res., 2008, 36, D662-6. (Pubitemid 351149803)
    • (2008) Nucleic Acids Research , vol.36 , Issue.SUPPL.1
    • Guney, E.1    Tuncbag, N.2    Keskin, O.3    Gursoy, A.4
  • 129
    • 77954294794 scopus 로고    scopus 로고
    • HotPoint: Hot spot prediction server for protein interfaces
    • Tuncbag, N.; Keskin, O.; Gursoy, A. HotPoint: Hot spot prediction server for protein interfaces. Nucleic Acids Res., 2010, 38, W402-6.
    • (2010) Nucleic Acids Res. , vol.38
    • Tuncbag, N.1    Keskin, O.2    Gursoy, A.3
  • 130
    • 77950651626 scopus 로고    scopus 로고
    • APIS: Accurate prediction of hot spots in protein interfaces by combining protrusion index with solvent accessibility
    • Xia, J. F.; Zhao, X. M.; Song, J.; Huang, D. S. APIS: Accurate prediction of hot spots in protein interfaces by combining protrusion index with solvent accessibility. BMC Bioinformatics, 2010, 11, 174.
    • (2010) BMC Bioinformatics , vol.11 , pp. 174
    • Xia, J.F.1    Zhao, X.M.2    Song, J.3    Huang, D.S.4
  • 131
    • 77951273638 scopus 로고    scopus 로고
    • PCRPi: Presaging Critical Residues in Protein interfaces, a new computational tool to chart hot spots in protein interfaces
    • Assi, S. A.; Tanaka, T.; Rabbitts, T. H.; Fernandez-Fuentes, N. PCRPi: Presaging Critical Residues in Protein interfaces, a new computational tool to chart hot spots in protein interfaces. Nucleic Acids Res., 2010, 38, e86.
    • (2010) Nucleic Acids Res. , vol.38
    • Assi, S.A.1    Tanaka, T.2    Rabbitts, T.H.3    Fernandez-Fuentes, N.4
  • 132
    • 84861036418 scopus 로고    scopus 로고
    • HotRegion: A database of predicted hot spot clusters
    • Cukuroglu, E.; Gursoy, A.; Keskin, O. HotRegion: A database of predicted hot spot clusters. Nucleic Acids Res., 2012, 40, D829-33.
    • (2012) Nucleic Acids Res. , vol.40
    • Cukuroglu, E.1    Gursoy, A.2    Keskin, O.3
  • 133
    • 79959269001 scopus 로고    scopus 로고
    • DBAC: A simple prediction method for protein binding hot spots based on burial levels and deeply buried atomic contacts
    • Li, Z.; Wong, L.; Li, J. DBAC: A simple prediction method for protein binding hot spots based on burial levels and deeply buried atomic contacts. BMC Syst. Biol., 2011, 5 Suppl 1, S5.
    • (2011) BMC Syst. Biol. , vol.5 , Issue.SUPPL.1
    • Li, Z.1    Wong, L.2    Li, J.3
  • 134
    • 84863243858 scopus 로고    scopus 로고
    • Computational prediction of protein hot spot residues
    • Morrow, J. K.; Zhang, S. Computational prediction of protein hot spot residues. Curr. Pharm. Des., 2012, 18, 1255-65.
    • (2012) Curr. Pharm. Des. , vol.18 , pp. 1255-1265
    • Morrow, J.K.1    Zhang, S.2
  • 136
    • 13244262600 scopus 로고    scopus 로고
    • Assessing predictions of protein-Protein interaction: The CAPRI experiment
    • DOI 10.1110/ps.041081905
    • Janin, J. Assessing predictions of protein-Protein interaction: The CAPRI experiment. Protein Sci., 2005, 14, 278-83. (Pubitemid 40194579)
    • (2005) Protein Science , vol.14 , Issue.2 , pp. 278-283
    • Janin, J.1
  • 138
    • 0009845923 scopus 로고
    • Role of subunit interfaces in the allosteric mechanism of hemoglobin
    • Chothia, C.; Wodak, S.; Janin, J. Role of subunit interfaces in the allosteric mechanism of hemoglobin. Proc. Natl. Acad. Sci. USA, 1976, 73, 3793-7.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 3793-3797
    • Chothia, C.1    Wodak, S.2    Janin, J.3
  • 139
    • 0030877077 scopus 로고    scopus 로고
    • Extent and nature of contacts between protein molecules in crystal lattices and between subunits of protein oligomers
    • DOI 10.1002/(SICI) 1097-0134 (199708)28:4<494:: AID-PROT4> 3.0.CO;2-A
    • Dasgupta, S.; Iyer, G. H.; Bryant, S. H.; Lawrence, C. E.; Bell, J. A. Extent and nature of contacts between protein molecules in crystal lattices and between subunits of protein oligomers. Proteins, 1997, 28, 494-514. (Pubitemid 27328566)
    • (1997) Proteins: Structure, Function and Genetics , vol.28 , Issue.4 , pp. 494-514
    • Dasgupta, S.1    Iyer, G.H.2    Bryant, S.H.3    Lawrence, C.E.4    Bell, J.A.5
  • 140
    • 0030997363 scopus 로고    scopus 로고
    • Hydrophobic patches on protein subunit interfaces: Characteristics and prediction
    • DOI 10.1002/(SICI)1097-0134(199707)28:3<333::AID-PROT4>3.0.CO;2-D
    • Lijnzaad, P.; Argos, P. Hydrophobic patches on protein subunit interfaces: Characteristics and prediction. Proteins, 1997, 28, 333-43. (Pubitemid 27280338)
    • (1997) Proteins: Structure, Function and Genetics , vol.28 , Issue.3 , pp. 333-343
    • Lijnzaad, P.1    Argos, P.2
  • 141
    • 0036093538 scopus 로고    scopus 로고
    • Analysis of homodimeric protein interfaces by graph-spectral methods
    • Brinda, K. V.; Kannan, N.; Vishveshwara, S. Analysis of homodimeric protein interfaces by graph-spectral methods. Protein Eng., 2002, 15, 265-77. (Pubitemid 34532765)
    • (2002) Protein Engineering , vol.15 , Issue.4 , pp. 265-277
    • Brinda, K.V.1    Kannan, N.2    Vishveshwara, S.3
  • 142
    • 1042275583 scopus 로고    scopus 로고
    • A dissection of specific and non-Specific protein-Protein interfaces
    • Bahadur, R. P.; Chakrabarti, P.; Rodier, F.; Janin, J. A dissection of specific and non-specific protein-Protein interfaces. J. Mol. Biol., 2004, 336, 943-55.
    • (2004) J. Mol. Biol. , vol.336 , pp. 943-955
    • Bahadur, R.P.1    Chakrabarti, P.2    Rodier, F.3    Janin, J.4
  • 143
    • 72949113228 scopus 로고    scopus 로고
    • Energy based approach for understanding the recognition mechanism in protein-Protein complexes
    • Gromiha, M. M.; Yokota, K.; Fukui, K. Energy based approach for understanding the recognition mechanism in protein-Protein complexes. Mol. Biosyst., 2009, 5, 1779-86.
    • (2009) Mol. Biosyst. , vol.5 , pp. 1779-1786
    • Gromiha, M.M.1    Yokota, K.2    Fukui, K.3
  • 144
    • 84878306995 scopus 로고    scopus 로고
    • Protein-Protein interactions: General trends in the relationship between binding affinity and interfacial buried surface area
    • Chen, J.; Sawyer, N.; Regan, L. Protein-Protein interactions: General trends in the relationship between binding affinity and interfacial buried surface area. Protein Sci., 2013, 22, 510-5
    • (2013) Protein Sci. , vol.22 , pp. 510-515
    • Chen, J.1    Sawyer, N.2    Regan, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.