메뉴 건너뛰기




Volumn 22, Issue 6, 2015, Pages 689-703

Overcoming Chemical, Biological, and Computational Challenges in the Development of Inhibitors Targeting Protein-Protein Interactions

Author keywords

[No Author keywords available]

Indexed keywords

LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; MOLECULAR LIBRARY; PROTEIN; PROTEIN BINDING;

EID: 84934912798     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2015.04.019     Document Type: Review
Times cited : (125)

References (167)
  • 1
    • 80053367108 scopus 로고    scopus 로고
    • Probing the druggability of protein-protein interactions: Targeting the Notch1 receptor ankyrin domain using a fragment-based approach
    • N. Abdel-Rahman, A. Martinez-Arias, and T.L. Blundell Probing the druggability of protein-protein interactions: targeting the Notch1 receptor ankyrin domain using a fragment-based approach Biochem. Soc. Trans. 39 2011 1327 1333
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 1327-1333
    • Abdel-Rahman, N.1    Martinez-Arias, A.2    Blundell, T.L.3
  • 7
    • 84909587217 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing toward the reality
    • M.R. Arkin, Y. Tang, and J.A. Wells Small-molecule inhibitors of protein-protein interactions: progressing toward the reality Chem. Biol. 21 2014 1102 1114
    • (2014) Chem. Biol. , vol.21 , pp. 1102-1114
    • Arkin, M.R.1    Tang, Y.2    Wells, J.A.3
  • 8
    • 84875436143 scopus 로고    scopus 로고
    • Inhibition of [alpha]-helix-mediated protein-protein interactions using designed molecules
    • V. Azzarito, K. Long, N.S. Murphy, and A.J. Wilson Inhibition of [alpha]-helix-mediated protein-protein interactions using designed molecules Nat. Chem. 5 2013 161 173
    • (2013) Nat. Chem. , vol.5 , pp. 161-173
    • Azzarito, V.1    Long, K.2    Murphy, N.S.3    Wilson, A.J.4
  • 9
    • 77950571108 scopus 로고    scopus 로고
    • New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays
    • J.B. Baell, and G.A. Holloway New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays J. Med. Chem. 53 2010 2719 2740
    • (2010) J. Med. Chem. , vol.53 , pp. 2719-2740
    • Baell, J.B.1    Holloway, G.A.2
  • 10
    • 33746631391 scopus 로고    scopus 로고
    • Evolutionary and physiological importance of hub proteins
    • N.N. Batada, L.D. Hurst, and M. Tyers Evolutionary and physiological importance of hub proteins PLoS Comput. Biol. 2 2006 e88
    • (2006) PLoS Comput. Biol. , vol.2 , pp. e88
    • Batada, N.N.1    Hurst, L.D.2    Tyers, M.3
  • 11
    • 84859611714 scopus 로고    scopus 로고
    • Are protein force fields getting better? A systematic benchmark on 524 diverse NMR measurements
    • K.A. Beauchamp, Y.-S. Lin, R. Das, and V.S. Pande Are protein force fields getting better? A systematic benchmark on 524 diverse NMR measurements J. Chem. Theor. Comput. 8 2012 1409 1414
    • (2012) J. Chem. Theor. Comput. , vol.8 , pp. 1409-1414
    • Beauchamp, K.A.1    Lin, Y.-S.2    Das, R.3    Pande, V.S.4
  • 14
    • 84856776282 scopus 로고    scopus 로고
    • Thermodynamic analysis of water molecules at the surface of proteins and applications to binding site prediction and characterization
    • T. Beuming, Y. Che, R. Abel, B. Kim, V. Shanmugasundaram, and W. Sherman Thermodynamic analysis of water molecules at the surface of proteins and applications to binding site prediction and characterization Proteins 80 2012 871 883
    • (2012) Proteins , vol.80 , pp. 871-883
    • Beuming, T.1    Che, Y.2    Abel, R.3    Kim, B.4    Shanmugasundaram, V.5    Sherman, W.6
  • 15
    • 0032542374 scopus 로고    scopus 로고
    • Highly efficient synthesis of covalently cross-linked peptide helices by ring-closing metathesis
    • H.E. Blackwell, and R.H. Grubbs Highly efficient synthesis of covalently cross-linked peptide helices by ring-closing metathesis Angew. Chem. Int. Ed. Engl. 37 1998 3281 3284
    • (1998) Angew. Chem. Int. Ed. Engl. , vol.37 , pp. 3281-3284
    • Blackwell, H.E.1    Grubbs, R.H.2
  • 16
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • A.A. Bogan, and K.S. Thorn Anatomy of hot spots in protein interfaces J. Mol. Biol. 280 1998 1 9
    • (1998) J. Mol. Biol. , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 17
    • 78650486115 scopus 로고    scopus 로고
    • Comparing experimental and computational alanine scanning techniques for probing a prototypical protein-protein interaction
    • R.T. Bradshaw, B.H. Patel, E.W. Tate, R.J. Leatherbarrow, and I.R. Gould Comparing experimental and computational alanine scanning techniques for probing a prototypical protein-protein interaction Protein Eng. Des. Sel. 24 2011 197 207
    • (2011) Protein Eng. Des. Sel. , vol.24 , pp. 197-207
    • Bradshaw, R.T.1    Patel, B.H.2    Tate, E.W.3    Leatherbarrow, R.J.4    Gould, I.R.5
  • 20
    • 61449104961 scopus 로고    scopus 로고
    • Fragment-based identification of druggable 'hot spots' of proteins using Fourier domain correlation techniques
    • R. Brenke, D. Kozakov, G.-Y. Chuang, D. Beglov, D. Hall, M.R. Landon, C. Mattos, and S. Vajda Fragment-based identification of druggable 'hot spots' of proteins using Fourier domain correlation techniques Bioinformatics 25 2009 621 627
    • (2009) Bioinformatics , vol.25 , pp. 621-627
    • Brenke, R.1    Kozakov, D.2    Chuang, G.-Y.3    Beglov, D.4    Hall, D.5    Landon, M.R.6    Mattos, C.7    Vajda, S.8
  • 21
    • 33746076877 scopus 로고    scopus 로고
    • Effects of conformational dynamics on predicted protein druggability
    • S.P. Brown, and P.J. Hajduk Effects of conformational dynamics on predicted protein druggability ChemMedChem 1 2006 70 72
    • (2006) ChemMedChem , vol.1 , pp. 70-72
    • Brown, S.P.1    Hajduk, P.J.2
  • 22
    • 80052566586 scopus 로고    scopus 로고
    • Assessing helical protein interfaces for inhibitor design
    • B.N. Bullock, A.L. Jochim, and P.S. Arora Assessing helical protein interfaces for inhibitor design J. Am. Chem. Soc. 133 2011 14220 14223
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 14220-14223
    • Bullock, B.N.1    Jochim, A.L.2    Arora, P.S.3
  • 24
    • 24344484686 scopus 로고    scopus 로고
    • Prediction of interface residues in protein-protein complexes by a consensus neural network method: Test against NMR data
    • H. Chen, and H.X. Zhou Prediction of interface residues in protein-protein complexes by a consensus neural network method: test against NMR data Proteins 61 2005 21 35
    • (2005) Proteins , vol.61 , pp. 21-35
    • Chen, H.1    Zhou, H.X.2
  • 26
    • 46849105028 scopus 로고    scopus 로고
    • Ensemble-based virtual screening reveals potential novel antiviral compounds for avian influenza neuraminidase
    • L.S. Cheng, R.E. Amaro, D. Xu, W.W. Li, P.W. Arzberger, and J.A. McCammon Ensemble-based virtual screening reveals potential novel antiviral compounds for avian influenza neuraminidase J. Med. Chem. 51 2008 3878 3894
    • (2008) J. Med. Chem. , vol.51 , pp. 3878-3894
    • Cheng, L.S.1    Amaro, R.E.2    Xu, D.3    Li, W.W.4    Arzberger, P.W.5    McCammon, J.A.6
  • 27
    • 84856397832 scopus 로고    scopus 로고
    • Fragment-based discovery of bromodomain inhibitors part 1: Inhibitor binding modes and implications for lead discovery
    • C.W. Chung, A.W. Dean, J.M. Woolven, and P. Bamborough Fragment-based discovery of bromodomain inhibitors part 1: inhibitor binding modes and implications for lead discovery J. Med. Chem. 55 2012 576 586
    • (2012) J. Med. Chem. , vol.55 , pp. 576-586
    • Chung, C.W.1    Dean, A.W.2    Woolven, J.M.3    Bamborough, P.4
  • 28
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • T. Clackson, and J.A. Wells A hot spot of binding energy in a hormone-receptor interface Science 267 1995 383 386
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 29
    • 77952546241 scopus 로고    scopus 로고
    • Drugging challenging targets using fragment-based approaches
    • A.G. Coyne, D.E. Scott, and C. Abell Drugging challenging targets using fragment-based approaches Curr. Opin. Chem. Biol. 14 2010 299 307
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 299-307
    • Coyne, A.G.1    Scott, D.E.2    Abell, C.3
  • 30
    • 77952541448 scopus 로고    scopus 로고
    • Disrupting protein-protein interactions with non-peptidic, small molecule α-helix mimetics
    • C.G. Cummings, and A.D. Hamilton Disrupting protein-protein interactions with non-peptidic, small molecule α-helix mimetics Curr. Opin. Chem. Biol. 14 2010 341 346
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 341-346
    • Cummings, C.G.1    Hamilton, A.D.2
  • 31
    • 34447271743 scopus 로고    scopus 로고
    • Exploring experimental sources of multiple protein conformations in structure-based drug design
    • K.L. Damm, and H.A. Carlson Exploring experimental sources of multiple protein conformations in structure-based drug design J. Am. Chem. Soc. 129 2007 8225 8235
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 8225-8235
    • Damm, K.L.1    Carlson, H.A.2
  • 33
    • 73349121291 scopus 로고    scopus 로고
    • Structure-based predictive models for allosteric hot spots
    • O.N. Demerdash, M.D. Daily, and J.C. Mitchell Structure-based predictive models for allosteric hot spots PLoS Comput. Biol. 5 2009 e1000531
    • (2009) PLoS Comput. Biol. , vol.5 , pp. e1000531
    • Demerdash, O.N.1    Daily, M.D.2    Mitchell, J.C.3
  • 34
    • 84923922070 scopus 로고    scopus 로고
    • NMR approaches in structure-based lead discovery: Recent developments and new frontiers for targeting multi-protein complexes
    • D.M. Dias, and A. Ciulli NMR approaches in structure-based lead discovery: recent developments and new frontiers for targeting multi-protein complexes Prog. Biophys. Mol. Biol. 116 2014 101 112
    • (2014) Prog. Biophys. Mol. Biol. , vol.116 , pp. 101-112
    • Dias, D.M.1    Ciulli, A.2
  • 35
    • 44949154279 scopus 로고    scopus 로고
    • Small molecular weight protein-protein interaction antagonists - An insurmountable challenge?
    • A. Dömling Small molecular weight protein-protein interaction antagonists - an insurmountable challenge? Curr. Opin. Chem. Biol. 12 2008 281 291
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 281-291
    • Dömling, A.1
  • 36
    • 84919774360 scopus 로고    scopus 로고
    • Targeting a dynamic protein-protein interaction: Fragment screening against the malaria myosin A motor complex
    • C.H. Douse, N. Vrielink, Z. Wenlin, E. Cota, and E.W. Tate Targeting a dynamic protein-protein interaction: fragment screening against the malaria myosin A motor complex ChemMedChem 10 2015 134 143
    • (2015) ChemMedChem , vol.10 , pp. 134-143
    • Douse, C.H.1    Vrielink, N.2    Wenlin, Z.3    Cota, E.4    Tate, E.W.5
  • 37
    • 79953703975 scopus 로고    scopus 로고
    • Fragment screening to predict druggability (ligandability) and lead discovery success
    • F.N. Edfeldt, R.H. Folmer, and A.L. Breeze Fragment screening to predict druggability (ligandability) and lead discovery success Drug Discov. Today 16 2011 284 287
    • (2011) Drug Discov. Today , vol.16 , pp. 284-287
    • Edfeldt, F.N.1    Folmer, R.H.2    Breeze, A.L.3
  • 38
    • 6244283606 scopus 로고    scopus 로고
    • Critical evaluation of search algorithms for automated molecular docking and database screening
    • T.J. Ewing, and I.D. Kuntz Critical evaluation of search algorithms for automated molecular docking and database screening J. Comput. Chem. 18 1997 1175 1189
    • (1997) J. Comput. Chem. , vol.18 , pp. 1175-1189
    • Ewing, T.J.1    Kuntz, I.D.2
  • 42
    • 1542390499 scopus 로고    scopus 로고
    • Identification of protein-protein interaction sites from docking energy landscapes
    • J. Fernandez-Recio, M. Totrov, and R. Abagyan Identification of protein-protein interaction sites from docking energy landscapes J. Mol. Biol. 335 2004 843 865
    • (2004) J. Mol. Biol. , vol.335 , pp. 843-865
    • Fernandez-Recio, J.1    Totrov, M.2    Abagyan, R.3
  • 46
    • 84863990355 scopus 로고    scopus 로고
    • Balancing target flexibility and target denaturation in computational fragment-based inhibitor discovery
    • T.J. Foster, A.D. MacKerell, and O. Guvench Balancing target flexibility and target denaturation in computational fragment-based inhibitor discovery J. Comput. Chem. 33 2012 1880 1891
    • (2012) J. Comput. Chem. , vol.33 , pp. 1880-1891
    • Foster, T.J.1    Mackerell, A.D.2    Guvench, O.3
  • 47
    • 0034710976 scopus 로고    scopus 로고
    • Can allosteric regulation be predicted from structure?
    • E. Freire Can allosteric regulation be predicted from structure? Proc. Natl. Acad. Sci. USA 97 2000 11680 11682
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11680-11682
    • Freire, E.1
  • 48
    • 33845594315 scopus 로고    scopus 로고
    • Protein-protein interactions as targets for small molecule drug discovery
    • D.C. Fry Protein-protein interactions as targets for small molecule drug discovery Biopolymers 84 2006 535 552
    • (2006) Biopolymers , vol.84 , pp. 535-552
    • Fry, D.C.1
  • 50
    • 58849145512 scopus 로고    scopus 로고
    • Predicting druggable binding sites at the protein-protein interface
    • J.C. Fuller, N.J. Burgoyne, and R.M. Jackson Predicting druggable binding sites at the protein-protein interface Drug Discov. Today 14 2009 155 161
    • (2009) Drug Discov. Today , vol.14 , pp. 155-161
    • Fuller, J.C.1    Burgoyne, N.J.2    Jackson, R.M.3
  • 51
    • 84880296641 scopus 로고    scopus 로고
    • Diversity-oriented synthesis as a tool for the discovery of novel biologically active small molecules
    • W.R. Galloway, A. Isidro-Llobet, and D.R. Spring Diversity-oriented synthesis as a tool for the discovery of novel biologically active small molecules Nat. Commun. 1 2010 80
    • (2010) Nat. Commun. , vol.1 , pp. 80
    • Galloway, W.R.1    Isidro-Llobet, A.2    Spring, D.R.3
  • 52
    • 84895548281 scopus 로고    scopus 로고
    • Automated NMR fragment based screening identified a novel interface blocker to the LARG/RhoA complex
    • J. Gao, R. Ma, W. Wang, N. Wang, R. Sasaki, D. Snyderman, J. Wu, and K. Ruan Automated NMR fragment based screening identified a novel interface blocker to the LARG/RhoA complex PLoS One 9 2014 e88098
    • (2014) PLoS One , vol.9 , pp. e88098
    • Gao, J.1    Ma, R.2    Wang, W.3    Wang, N.4    Sasaki, R.5    Snyderman, D.6    Wu, J.7    Ruan, K.8
  • 54
    • 79952171625 scopus 로고    scopus 로고
    • Probing the links between in vitro potency, ADMET and physicochemical parameters
    • M.P. Gleeson, A. Hersey, D. Montanari, and J. Overington Probing the links between in vitro potency, ADMET and physicochemical parameters Nat. Rev. Drug Discov. 10 2011 197 208
    • (2011) Nat. Rev. Drug Discov. , vol.10 , pp. 197-208
    • Gleeson, M.P.1    Hersey, A.2    Montanari, D.3    Overington, J.4
  • 55
    • 0043245780 scopus 로고    scopus 로고
    • Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes
    • H. Gohlke, C. Kiel, and D.A. Case Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes J. Mol. Biol. 330 2003 891 913
    • (2003) J. Mol. Biol. , vol.330 , pp. 891-913
    • Gohlke, H.1    Kiel, C.2    Case, D.A.3
  • 56
    • 84876316258 scopus 로고    scopus 로고
    • Stapled peptide to enter human testing, but affinity questions remain
    • Y. Grigoryev Stapled peptide to enter human testing, but affinity questions remain Nat. Med. 19 2013 120
    • (2013) Nat. Med. , vol.19 , pp. 120
    • Grigoryev, Y.1
  • 57
    • 38549092067 scopus 로고    scopus 로고
    • HotSprint: Database of computational hot spots in protein interfaces
    • E. Guney, N. Tuncbag, O. Keskin, and A. Gursoy HotSprint: database of computational hot spots in protein interfaces Nucleic Acids Res. 36 2008 D662 D666
    • (2008) Nucleic Acids Res. , vol.36 , pp. D662-D666
    • Guney, E.1    Tuncbag, N.2    Keskin, O.3    Gursoy, A.4
  • 59
    • 66249128230 scopus 로고    scopus 로고
    • Glucose promoiety enables glucose transporter mediated brain uptake of ketoprofen and indomethacin prodrugs in rats
    • M. Gynther, J. Ropponen, K. Laine, J. Leppanen, P. Haapakoski, L. Peura, T. Jarvinen, and J. Rautio Glucose promoiety enables glucose transporter mediated brain uptake of ketoprofen and indomethacin prodrugs in rats J. Med. Chem. 52 2009 3348 3353
    • (2009) J. Med. Chem. , vol.52 , pp. 3348-3353
    • Gynther, M.1    Ropponen, J.2    Laine, K.3    Leppanen, J.4    Haapakoski, P.5    Peura, L.6    Jarvinen, T.7    Rautio, J.8
  • 60
    • 84887096390 scopus 로고    scopus 로고
    • Combining solvent thermodynamic profiles with functionality maps of the Hsp90 binding site to predict the displacement of water molecules
    • M.K. Haider, and D.J. Huggins Combining solvent thermodynamic profiles with functionality maps of the Hsp90 binding site to predict the displacement of water molecules J. Chem. Inf. Model. 53 2013 2571 2586
    • (2013) J. Chem. Inf. Model. , vol.53 , pp. 2571-2586
    • Haider, M.K.1    Huggins, D.J.2
  • 61
    • 33845364148 scopus 로고    scopus 로고
    • Fragment-based drug design: How big is too big?
    • P.J. Hajduk Fragment-based drug design: how big is too big? J. Med. Chem. 49 2006 6972 6976
    • (2006) J. Med. Chem. , vol.49 , pp. 6972-6976
    • Hajduk, P.J.1
  • 63
    • 65249117514 scopus 로고    scopus 로고
    • Identifying and characterizing binding sites and assessing druggability
    • T.A. Halgren Identifying and characterizing binding sites and assessing druggability J. Chem. Inf. Model. 49 2009 377 389
    • (2009) J. Chem. Inf. Model. , vol.49 , pp. 377-389
    • Halgren, T.A.1
  • 64
    • 84877278593 scopus 로고    scopus 로고
    • 2P2Ichem: Focused chemical libraries dedicated to orthosteric modulation of protein-protein interactions
    • V. Hamon, J.M. Brunel, S. Combes, M.J. Basse, P. Roche, and X. Morelli 2P2Ichem: focused chemical libraries dedicated to orthosteric modulation of protein-protein interactions Med. Chem. Commun. 4 2013 797 809
    • (2013) Med. Chem. Commun. , vol.4 , pp. 797-809
    • Hamon, V.1    Brunel, J.M.2    Combes, S.3    Basse, M.J.4    Roche, P.5    Morelli, X.6
  • 67
    • 84893018543 scopus 로고    scopus 로고
    • Protein-protein interactions as druggable targets: Recent technological advances
    • A.P. Higueruelo, H. Jubb, and T.L. Blundell Protein-protein interactions as druggable targets: recent technological advances Curr. Opin. Pharmacol. 13 2013 791 796
    • (2013) Curr. Opin. Pharmacol. , vol.13 , pp. 791-796
    • Higueruelo, A.P.1    Jubb, H.2    Blundell, T.L.3
  • 68
    • 84933500980 scopus 로고    scopus 로고
    • Selective targeting of the TPX2 site of importin-α using fragment-based ligand design
    • Published online April 20, 2015
    • R.S. Holvey, E. Valkov, D. Neal, M. Stewart, and C. Abell Selective targeting of the TPX2 site of importin-α using fragment-based ligand design ChemMedChem 2015 10.1002/cmdc.201500014 Published online April 20, 2015
    • (2015) ChemMedChem
    • Holvey, R.S.1    Valkov, E.2    Neal, D.3    Stewart, M.4    Abell, C.5
  • 69
    • 5044229321 scopus 로고    scopus 로고
    • The impact of systems approaches on biological problems in drug discovery
    • L. Hood, and R.M. Perlmutter The impact of systems approaches on biological problems in drug discovery Nat. Biotechnol. 22 2004 1215 1217
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1215-1217
    • Hood, L.1    Perlmutter, R.M.2
  • 70
    • 54249155522 scopus 로고    scopus 로고
    • Network pharmacology: The next paradigm in drug discovery
    • A.L. Hopkins Network pharmacology: the next paradigm in drug discovery Nat. Chem. Biol. 4 2008 682 690
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 682-690
    • Hopkins, A.L.1
  • 71
    • 1942453243 scopus 로고    scopus 로고
    • Ligand efficiency: A useful metric for lead selection
    • A.L. Hopkins, C.R. Groom, and A. Alex Ligand efficiency: a useful metric for lead selection Drug Discov. Today 9 2004 430 431
    • (2004) Drug Discov. Today , vol.9 , pp. 430-431
    • Hopkins, A.L.1    Groom, C.R.2    Alex, A.3
  • 73
    • 84880154439 scopus 로고    scopus 로고
    • Assessing the accuracy of inhomogeneous fluid solvation theory in predicting hydration free energies of simple solutes
    • D.J. Huggins, and M.C. Payne Assessing the accuracy of inhomogeneous fluid solvation theory in predicting hydration free energies of simple solutes J. Phys. Chem. B 117 2013 8232 8244
    • (2013) J. Phys. Chem. B , vol.117 , pp. 8232-8244
    • Huggins, D.J.1    Payne, M.C.2
  • 75
    • 79955637690 scopus 로고    scopus 로고
    • Rational methods for the selection of diverse screening compounds
    • D.J. Huggins, A.R. Venkitaraman, and D.R. Spring Rational methods for the selection of diverse screening compounds ACS Chem. Biol. 6 2011 208 217
    • (2011) ACS Chem. Biol. , vol.6 , pp. 208-217
    • Huggins, D.J.1    Venkitaraman, A.R.2    Spring, D.R.3
  • 77
    • 78149422216 scopus 로고    scopus 로고
    • Protein-protein docking tested in blind predictions: The CAPRI experiment
    • J. Janin Protein-protein docking tested in blind predictions: the CAPRI experiment Mol. Biosyst. 6 2010 2351 2362
    • (2010) Mol. Biosyst. , vol.6 , pp. 2351-2362
    • Janin, J.1
  • 78
    • 84875984520 scopus 로고    scopus 로고
    • Druggable protein interaction sites are more predisposed to surface pocket formation than the rest of the protein surface
    • D.K. Johnson, and J. Karanicolas Druggable protein interaction sites are more predisposed to surface pocket formation than the rest of the protein surface PLoS Comput. Biol. 9 2013 e1002951
    • (2013) PLoS Comput. Biol. , vol.9 , pp. e1002951
    • Johnson, D.K.1    Karanicolas, J.2
  • 79
    • 69949109727 scopus 로고    scopus 로고
    • Using the Golden Triangle to optimize clearance and oral absorption
    • T.W. Johnson, K.R. Dress, and M. Edwards Using the Golden Triangle to optimize clearance and oral absorption Bioorg. Med. Chem. Lett. 19 2009 5560 5564
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 5560-5564
    • Johnson, T.W.1    Dress, K.R.2    Edwards, M.3
  • 80
    • 0028854034 scopus 로고
    • Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation
    • G. Jones, P. Willett, and R.C. Glen Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation J. Mol. Biol. 245 1995 43 53
    • (1995) J. Mol. Biol. , vol.245 , pp. 43-53
    • Jones, G.1    Willett, P.2    Glen, R.C.3
  • 82
    • 3242887695 scopus 로고    scopus 로고
    • Protein structure prediction and analysis using the Robetta server
    • D.E. Kim, D. Chivian, and D. Baker Protein structure prediction and analysis using the Robetta server Nucleic Acids Res. 32 2004 W526 W531
    • (2004) Nucleic Acids Res. , vol.32 , pp. W526-W531
    • Kim, D.E.1    Chivian, D.2    Baker, D.3
  • 85
    • 74049122828 scopus 로고    scopus 로고
    • Cancer systems biology: A network modeling perspective
    • P.K. Kreeger, and D.A. Lauffenburger Cancer systems biology: a network modeling perspective Carcinogenesis 31 2010 2 8
    • (2010) Carcinogenesis , vol.31 , pp. 2-8
    • Kreeger, P.K.1    Lauffenburger, D.A.2
  • 86
    • 77954304081 scopus 로고    scopus 로고
    • DrugScorePPI webserver: Fast and accurate in silico alanine scanning for scoring protein-protein interactions
    • D.M. Krüger, and H. Gohlke DrugScorePPI webserver: fast and accurate in silico alanine scanning for scoring protein-protein interactions Nucleic Acids Res. 38 2010 W480 W486
    • (2010) Nucleic Acids Res. , vol.38 , pp. W480-W486
    • Krüger, D.M.1    Gohlke, H.2
  • 87
    • 84912572423 scopus 로고    scopus 로고
    • Which three-dimensional characteristics make efficient inhibitors of protein-protein interactions?
    • M.A. Kuenemann, L.M. Bourbon, C.M. Labbe, B.O. Villoutreix, and O. Sperandio Which three-dimensional characteristics make efficient inhibitors of protein-protein interactions? J. Chem. Inf. Model. 54 2014 3067 3079
    • (2014) J. Chem. Inf. Model. , vol.54 , pp. 3067-3079
    • Kuenemann, M.A.1    Bourbon, L.M.2    Labbe, C.M.3    Villoutreix, B.O.4    Sperandio, O.5
  • 88
    • 84884587933 scopus 로고    scopus 로고
    • IPPI-DB: A manually curated and interactive database of small non-peptide inhibitors of protein-protein interactions
    • C.M. Labbé, G. Laconde, M.A. Kuenemann, B.O. Villoutreix, and O. Sperandio iPPI-DB: A manually curated and interactive database of small non-peptide inhibitors of protein-protein interactions Drug Discov. Today 18 2013 958 968
    • (2013) Drug Discov. Today , vol.18 , pp. 958-968
    • Labbé, C.M.1    Laconde, G.2    Kuenemann, M.A.3    Villoutreix, B.O.4    Sperandio, O.5
  • 89
    • 33947658802 scopus 로고    scopus 로고
    • Identification of hot spots within druggable binding regions by computational solvent mapping of proteins
    • M.R. Landon, D.R. Lancia, J. Yu, S.C. Thiel, and S. Vajda Identification of hot spots within druggable binding regions by computational solvent mapping of proteins J. Med. Chem. 50 2007 1231 1240
    • (2007) J. Med. Chem. , vol.50 , pp. 1231-1240
    • Landon, M.R.1    Lancia, D.R.2    Yu, J.3    Thiel, S.C.4    Vajda, S.5
  • 93
    • 37749004225 scopus 로고    scopus 로고
    • Protein therapeutics: A summary and pharmacological classification
    • B. Leader, Q.J. Baca, and D.E. Golan Protein therapeutics: a summary and pharmacological classification Nat. Rev. Drug Discov. 7 2008 21 39
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 21-39
    • Leader, B.1    Baca, Q.J.2    Golan, D.E.3
  • 94
    • 79851497821 scopus 로고    scopus 로고
    • Novel pyrrolopyrimidine-based alpha-helix mimetics: Cell-permeable inhibitors of protein-protein interactions
    • J.H. Lee, Q. Zhang, S. Jo, S.C. Chai, M. Oh, W. Im, H. Lu, and H.S. Lim Novel pyrrolopyrimidine-based alpha-helix mimetics: cell-permeable inhibitors of protein-protein interactions J. Am. Chem. Soc. 133 2011 676 679
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 676-679
    • Lee, J.H.1    Zhang, Q.2    Jo, S.3    Chai, S.C.4    Oh, M.5    Im, W.6    Lu, H.7    Lim, H.S.8
  • 95
    • 35748934487 scopus 로고    scopus 로고
    • The influence of drug-like concepts on decision-making in medicinal chemistry
    • P.D. Leeson, and B. Springthorpe The influence of drug-like concepts on decision-making in medicinal chemistry Nat. Rev. Drug Discov. 6 2007 881 890
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 881-890
    • Leeson, P.D.1    Springthorpe, B.2
  • 96
    • 78651402672 scopus 로고    scopus 로고
    • Full protein flexibility is essential for proper hot-spot mapping
    • K.W. Lexa, and H.A. Carlson Full protein flexibility is essential for proper hot-spot mapping J. Am. Chem. Soc. 133 2010 200 202
    • (2010) J. Am. Chem. Soc. , vol.133 , pp. 200-202
    • Lexa, K.W.1    Carlson, H.A.2
  • 97
    • 84874413947 scopus 로고    scopus 로고
    • Improving protocols for protein mapping through proper comparison to crystallography data
    • K.W. Lexa, and H.A. Carlson Improving protocols for protein mapping through proper comparison to crystallography data J. Chem. Inf. Model. 53 2013 391 402
    • (2013) J. Chem. Inf. Model. , vol.53 , pp. 391-402
    • Lexa, K.W.1    Carlson, H.A.2
  • 98
    • 33644527925 scopus 로고    scopus 로고
    • Thermodynamics of buried water clusters at a protein-ligand binding interface
    • Z. Li, and T. Lazaridis Thermodynamics of buried water clusters at a protein-ligand binding interface J. Phys. Chem. B 110 2006 1464 1475
    • (2006) J. Phys. Chem. B , vol.110 , pp. 1464-1475
    • Li, Z.1    Lazaridis, T.2
  • 100
    • 33846108633 scopus 로고    scopus 로고
    • BindingDB: A web-accessible database of experimentally determined protein-ligand binding affinities
    • T. Liu, Y. Lin, X. Wen, R.N. Jorissen, and M.K. Gilson BindingDB: a web-accessible database of experimentally determined protein-ligand binding affinities Nucleic Acids Res. 35 2007 D198 D201
    • (2007) Nucleic Acids Res. , vol.35 , pp. D198-D201
    • Liu, T.1    Lin, Y.2    Wen, X.3    Jorissen, R.N.4    Gilson, M.K.5
  • 101
    • 84923369622 scopus 로고    scopus 로고
    • Inhibition of CDC25B phosphatase through disruption of protein-protein interaction
    • G. Lund, S. Dudkin, D. Borkin, W. Ni, J. Grembecka, and T. Cierpicki Inhibition of CDC25B phosphatase through disruption of protein-protein interaction ACS Chem. Biol. 10 2015 390 394
    • (2015) ACS Chem. Biol. , vol.10 , pp. 390-394
    • Lund, G.1    Dudkin, S.2    Borkin, D.3    Ni, W.4    Grembecka, J.5    Cierpicki, T.6
  • 102
    • 64349122942 scopus 로고    scopus 로고
    • Diversity-oriented synthesis of a cytisine-inspired pyridone library leading to the discovery of novel inhibitors of Bcl-2
    • L.A. Marcaurelle, C. Johannes, D. Yohannes, B.P. Tillotson, and D. Mann Diversity-oriented synthesis of a cytisine-inspired pyridone library leading to the discovery of novel inhibitors of Bcl-2 Bioorg. Med. Chem. Lett. 19 2009 2500 2503
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 2500-2503
    • Marcaurelle, L.A.1    Johannes, C.2    Yohannes, D.3    Tillotson, B.P.4    Mann, D.5
  • 106
    • 84857291408 scopus 로고    scopus 로고
    • Hot spots and transient pockets: Predicting the determinants of small-molecule binding to a protein-protein interface
    • A. Metz, C. Pfleger, H. Kopitz, S. Pfeiffer-Marek, K.H. Baringhaus, and H. Gohlke Hot spots and transient pockets: predicting the determinants of small-molecule binding to a protein-protein interface J. Chem. Inf. Model. 52 2012 120 133
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 120-133
    • Metz, A.1    Pfleger, C.2    Kopitz, H.3    Pfeiffer-Marek, S.4    Baringhaus, K.H.5    Gohlke, H.6
  • 107
    • 70249091154 scopus 로고    scopus 로고
    • Transmembrane structures of amyloid precursor protein dimer predicted by replica-exchange molecular dynamics simulations
    • N. Miyashita, J.E. Straub, D. Thirumalai, and Y. Sugita Transmembrane structures of amyloid precursor protein dimer predicted by replica-exchange molecular dynamics simulations J. Am. Chem. Soc. 131 2009 3438 3439
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 3438-3439
    • Miyashita, N.1    Straub, J.E.2    Thirumalai, D.3    Sugita, Y.4
  • 109
    • 84856315533 scopus 로고    scopus 로고
    • Structural insights of the MLF1/14-3-3 interaction
    • M. Molzan, M. Weyand, R. Rose, and C. Ottmann Structural insights of the MLF1/14-3-3 interaction FEBS J. 279 2012 563 571
    • (2012) FEBS J. , vol.279 , pp. 563-571
    • Molzan, M.1    Weyand, M.2    Rose, R.3    Ottmann, C.4
  • 110
    • 68949207961 scopus 로고    scopus 로고
    • Structural and biophysical characterization of XIAP BIR3 G306E mutant: Insights in protein dynamics and application for fragment-based drug design
    • C.D. Moore, H. Wu, B. Bolanos, S. Bergqvist, A. Brooun, T. Pauly, and D. Nowlin Structural and biophysical characterization of XIAP BIR3 G306E mutant: insights in protein dynamics and application for fragment-based drug design Chem. Biol. Drug Des. 74 2009 212 223
    • (2009) Chem. Biol. Drug Des. , vol.74 , pp. 212-223
    • Moore, C.D.1    Wu, H.2    Bolanos, B.3    Bergqvist, S.4    Brooun, A.5    Pauly, T.6    Nowlin, D.7
  • 111
    • 33847650393 scopus 로고    scopus 로고
    • Computational alanine scanning mutagenesis - An improved methodological approach
    • I.S. Moreira, P.A. Fernandes, and M.J. Ramos Computational alanine scanning mutagenesis - an improved methodological approach J. Comput. Chem. 28 2007 644 654
    • (2007) J. Comput. Chem. , vol.28 , pp. 644-654
    • Moreira, I.S.1    Fernandes, P.A.2    Ramos, M.J.3
  • 112
    • 79960990847 scopus 로고    scopus 로고
    • Chemical and structural lessons from recent successes in protein-protein interaction inhibition (2P2I)
    • X. Morelli, R. Bourgeas, and P. Roche Chemical and structural lessons from recent successes in protein-protein interaction inhibition (2P2I) Curr. Opin. Chem. Biol. 15 2011 475 481
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 475-481
    • Morelli, X.1    Bourgeas, R.2    Roche, P.3
  • 114
    • 84857712365 scopus 로고    scopus 로고
    • Protein-protein interaction inhibitors get into the groove
    • A. Mullard Protein-protein interaction inhibitors get into the groove Nat. Rev. Drug Discov. 11 2012 173 175
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 173-175
    • Mullard, A.1
  • 115
    • 84876931578 scopus 로고    scopus 로고
    • Solid-phase methodology for synthesis of O-alkylated aromatic oligoamide inhibitors of α-helix-mediated protein-protein interactions
    • N.S. Murphy, P. Prabhakaran, V. Azzarito, J.P. Plante, M.J. Hardie, C.A. Kilner, S.L. Warriner, and A.J. Wilson Solid-phase methodology for synthesis of O-alkylated aromatic oligoamide inhibitors of α-helix-mediated protein-protein interactions Chem-Eur J. 19 2013 5546 5550
    • (2013) Chem-Eur J. , vol.19 , pp. 5546-5550
    • Murphy, N.S.1    Prabhakaran, P.2    Azzarito, V.3    Plante, J.P.4    Hardie, M.J.5    Kilner, C.A.6    Warriner, S.L.7    Wilson, A.J.8
  • 116
    • 34848854803 scopus 로고    scopus 로고
    • Statistical analysis of physical-chemical properties and prediction of protein-protein interfaces
    • S.S. Negi, and W. Braun Statistical analysis of physical-chemical properties and prediction of protein-protein interfaces J. Mol. Model. 13 2007 1157 1167
    • (2007) J. Mol. Model. , vol.13 , pp. 1157-1167
    • Negi, S.S.1    Braun, W.2
  • 117
    • 34648833340 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction inhibitors by chemoinformatics and machine learning methods
    • A. Neugebauer, R.W. Hartmann, and C.D. Klein Prediction of protein-protein interaction inhibitors by chemoinformatics and machine learning methods J. Med. Chem. 50 2007 4665 4668
    • (2007) J. Med. Chem. , vol.50 , pp. 4665-4668
    • Neugebauer, A.1    Hartmann, R.W.2    Klein, C.D.3
  • 118
    • 0017625882 scopus 로고
    • 3H] vinblastine in tumor and host tissues of Nb rats bearing a transplantable lymphoma which is highly sensitive to the alkaloid
    • 3H] vinblastine in tumor and host tissues of Nb rats bearing a transplantable lymphoma which is highly sensitive to the alkaloid Cancer Res. 37 1977 1455 1460
    • (1977) Cancer Res. , vol.37 , pp. 1455-1460
    • Noble, R.L.1    Gout, P.W.2    Wijcik, L.L.3    Hebden, H.F.4    Beer, C.T.5
  • 122
    • 84864235498 scopus 로고    scopus 로고
    • Design, synthesis, and biological and structural evaluations of novel HIV-1 protease inhibitors to combat drug resistance
    • M.K. Parai, D.J. Huggins, H. Cao, M.N.L. Nalam, A. Ali, C.A. Schiffer, B. Tidor, and T.M. Rana Design, synthesis, and biological and structural evaluations of novel HIV-1 protease inhibitors to combat drug resistance J. Med. Chem. 55 2012 6328 6341
    • (2012) J. Med. Chem. , vol.55 , pp. 6328-6341
    • Parai, M.K.1    Huggins, D.J.2    Cao, H.3    Nalam, M.N.L.4    Ali, A.5    Schiffer, C.A.6    Tidor, B.7    Rana, T.M.8
  • 124
    • 84927919934 scopus 로고    scopus 로고
    • Biophysical methods for identifying fragment-based inhibitors of protein-protein interactions
    • S.J. Pfaff, M.S. Chimenti, M.J. Kelly, and M.R. Arkin Biophysical methods for identifying fragment-based inhibitors of protein-protein interactions Methods Mol. Biol. 1278 2015 587 613
    • (2015) Methods Mol. Biol. , vol.1278 , pp. 587-613
    • Pfaff, S.J.1    Chimenti, M.S.2    Kelly, M.J.3    Arkin, M.R.4
  • 125
    • 33748135657 scopus 로고    scopus 로고
    • PIPE: A protein-protein interaction prediction engine based on the re-occurring short polypeptide sequences between known interacting protein pairs
    • S. Pitre, F. Dehne, A. Chan, J. Cheetham, A. Duong, A. Emili, M. Gebbia, J. Greenblatt, M. Jessulat, and N. Krogan PIPE: a protein-protein interaction prediction engine based on the re-occurring short polypeptide sequences between known interacting protein pairs BMC Bioinformatics 7 2006 365
    • (2006) BMC Bioinformatics , vol.7 , pp. 365
    • Pitre, S.1    Dehne, F.2    Chan, A.3    Cheetham, J.4    Duong, A.5    Emili, A.6    Gebbia, M.7    Greenblatt, J.8    Jessulat, M.9    Krogan, N.10
  • 126
    • 84855347756 scopus 로고    scopus 로고
    • Interfacial inhibitors: Targeting macromolecular complexes
    • Y. Pommier, and C. Marchand Interfacial inhibitors: targeting macromolecular complexes Nat. Rev. Drug Discov. 11 2012 25 36
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 25-36
    • Pommier, Y.1    Marchand, C.2
  • 127
    • 79955425362 scopus 로고    scopus 로고
    • Reproducing crystal binding modes of ligand functional groups using Site-Identification by Ligand Competitive Saturation (SILCS) simulations
    • E.P. Raman, W. Yu, O. Guvench, and A.D. MacKerell Jr. Reproducing crystal binding modes of ligand functional groups using Site-Identification by Ligand Competitive Saturation (SILCS) simulations J. Chem. Inf. Model. 51 2011 877 896
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 877-896
    • Raman, E.P.1    Yu, W.2    Guvench, O.3    Mackerell, Jr.A.D.4
  • 130
    • 81555209041 scopus 로고    scopus 로고
    • Calculation of relative free energies for ligand-protein binding, solvation, and conformational transitions using the GROMOS software
    • S. Riniker, C.D. Christ, H.S. Hansen, P.H. Hünenberger, C. Oostenbrink, D. Steiner, and W.F. van Gunsteren Calculation of relative free energies for ligand-protein binding, solvation, and conformational transitions using the GROMOS software J. Phys. Chem. B 115 2011 13570 13577
    • (2011) J. Phys. Chem. B , vol.115 , pp. 13570-13577
    • Riniker, S.1    Christ, C.D.2    Hansen, H.S.3    Hünenberger, P.H.4    Oostenbrink, C.5    Steiner, D.6    Van Gunsteren, W.F.7
  • 131
    • 78650352933 scopus 로고    scopus 로고
    • Quo vadis, virtual screening? A comprehensive survey of prospective applications
    • P. Ripphausen, B. Nisius, L. Peltason, and J. Bajorath Quo vadis, virtual screening? A comprehensive survey of prospective applications J. Med. Chem. 53 2010 8461 8467
    • (2010) J. Med. Chem. , vol.53 , pp. 8461-8467
    • Ripphausen, P.1    Nisius, B.2    Peltason, L.3    Bajorath, J.4
  • 132
    • 0035159540 scopus 로고    scopus 로고
    • A peptide needle in a signaling haystack
    • P.D. Roepe A peptide needle in a signaling haystack Nat. Genet. 27 2001 6 7
    • (2001) Nat. Genet. , vol.27 , pp. 6-7
    • Roepe, P.D.1
  • 134
    • 34548394483 scopus 로고    scopus 로고
    • Human protein-protein interaction networks and the value for drug discovery
    • H. Ruffner, A. Bauer, and T. Bouwmeester Human protein-protein interaction networks and the value for drug discovery Drug Discov. Today 12 2007 709 716
    • (2007) Drug Discov. Today , vol.12 , pp. 709-716
    • Ruffner, H.1    Bauer, A.2    Bouwmeester, T.3
  • 137
  • 139
    • 34547693013 scopus 로고    scopus 로고
    • Probabilistic prediction and ranking of human protein-protein interactions
    • M.S. Scott, and G.J. Barton Probabilistic prediction and ranking of human protein-protein interactions BMC Bioinformatics 8 2007 239
    • (2007) BMC Bioinformatics , vol.8 , pp. 239
    • Scott, M.S.1    Barton, G.J.2
  • 142
    • 78649523910 scopus 로고    scopus 로고
    • Drug-like density: A method of quantifying the "bindability" of a protein target based on a very large set of pockets and drug-like ligands from the Protein Data Bank
    • R.P. Sheridan, V.N. Maiorov, M.K. Holloway, W.D. Cornell, and Y.-D. Gao Drug-like density: a method of quantifying the "bindability" of a protein target based on a very large set of pockets and drug-like ligands from the Protein Data Bank J. Chem. Inf. Model. 50 2010 2029 2040
    • (2010) J. Chem. Inf. Model. , vol.50 , pp. 2029-2040
    • Sheridan, R.P.1    Maiorov, V.N.2    Holloway, M.K.3    Cornell, W.D.4    Gao, Y.-D.5
  • 143
    • 84926390889 scopus 로고    scopus 로고
    • Using ligand-mapping simulations to design a ligand selectively targeting a cryptic surface pocket of polo-like kinase 1
    • Y.S. Tan, P. ͆ledź, S. Lang, C.J. Stubbs, D.R. Spring, C. Abell, and R.B. Best Using ligand-mapping simulations to design a ligand selectively targeting a cryptic surface pocket of polo-like kinase 1 Angew. Chem. Int. Ed. Engl. 124 2012 10225 10228
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.124 , pp. 10225-10228
    • Tan, Y.S.1    ͆ledź, P.2    Lang, S.3    Stubbs, C.J.4    Spring, D.R.5    Abell, C.6    Best, R.B.7
  • 145
    • 0035066602 scopus 로고    scopus 로고
    • ASEdb: A database of alanine mutations and their effects on the free energy of binding in protein interactions
    • K.S. Thorn, and A.A. Bogan ASEdb: a database of alanine mutations and their effects on the free energy of binding in protein interactions Bioinformatics 17 2001 284 285
    • (2001) Bioinformatics , vol.17 , pp. 284-285
    • Thorn, K.S.1    Bogan, A.A.2
  • 146
    • 41949132916 scopus 로고    scopus 로고
    • Flexible ligand docking to multiple receptor conformations: A practical alternative
    • M. Totrov, and R. Abagyan Flexible ligand docking to multiple receptor conformations: a practical alternative Curr. Opin. Struct. Biol. 18 2008 178 184
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 178-184
    • Totrov, M.1    Abagyan, R.2
  • 148
    • 66349094681 scopus 로고    scopus 로고
    • Identification of computational hot spots in protein interfaces: Combining solvent accessibility and inter-residue potentials improves the accuracy
    • N. Tuncbag, A. Gursoy, and O. Keskin Identification of computational hot spots in protein interfaces: combining solvent accessibility and inter-residue potentials improves the accuracy Bioinformatics 25 2009 1513 1520
    • (2009) Bioinformatics , vol.25 , pp. 1513-1520
    • Tuncbag, N.1    Gursoy, A.2    Keskin, O.3
  • 149
    • 77954294794 scopus 로고    scopus 로고
    • HotPoint: Hot spot prediction server for protein interfaces
    • N. Tuncbag, O. Keskin, and A. Gursoy HotPoint: hot spot prediction server for protein interfaces Nucleic Acids Res. 38 2010 W402 W406
    • (2010) Nucleic Acids Res. , vol.38 , pp. W402-W406
    • Tuncbag, N.1    Keskin, O.2    Gursoy, A.3
  • 150
    • 84857790849 scopus 로고    scopus 로고
    • Fast and accurate modeling of protein-protein interactions by combining template-interface-based docking with flexible refinement
    • N. Tuncbag, O. Keskin, R. Nussinov, and A. Gursoy Fast and accurate modeling of protein-protein interactions by combining template-interface-based docking with flexible refinement Proteins 80 2012 1239 1249
    • (2012) Proteins , vol.80 , pp. 1239-1249
    • Tuncbag, N.1    Keskin, O.2    Nussinov, R.3    Gursoy, A.4
  • 151
    • 84858131639 scopus 로고    scopus 로고
    • Targeting protein-protein interactions and fragment-based drug discovery
    • E. Valkov, T. Sharpe, M. Marsh, S. Greive, and M. Hyvonen Targeting protein-protein interactions and fragment-based drug discovery Top. Curr. Chem. 317 2012 145 179
    • (2012) Top. Curr. Chem. , vol.317 , pp. 145-179
    • Valkov, E.1    Sharpe, T.2    Marsh, M.3    Greive, S.4    Hyvonen, M.5
  • 152
    • 84868026890 scopus 로고    scopus 로고
    • Dissecting fragment-based lead discovery at the von Hippel-Lindau protein:hypoxia inducible factor 1alpha protein-protein interface
    • I. Van Molle, A. Thomann, D.L. Buckley, E.C. So, S. Lang, C.M. Crews, and A. Ciulli Dissecting fragment-based lead discovery at the von Hippel-Lindau protein:hypoxia inducible factor 1alpha protein-protein interface Chem. Biol. 19 2012 1300 1312
    • (2012) Chem. Biol. , vol.19 , pp. 1300-1312
    • Van Molle, I.1    Thomann, A.2    Buckley, D.L.3    So, E.C.4    Lang, S.5    Crews, C.M.6    Ciulli, A.7
  • 155
    • 84901681947 scopus 로고    scopus 로고
    • Hydrocarbon-stapled peptides: Principles, practice, and progress
    • L.D. Walensky, and G.H. Bird Hydrocarbon-stapled peptides: principles, practice, and progress J. Med. Chem. 57 2014 6275 6288
    • (2014) J. Med. Chem. , vol.57 , pp. 6275-6288
    • Walensky, L.D.1    Bird, G.H.2
  • 156
    • 84873642828 scopus 로고    scopus 로고
    • Modeling local structural rearrangements using FEP/REST: Application to relative binding affinity predictions of CDK2 inhibitors
    • L. Wang, Y. Deng, J.L. Knight, Y. Wu, B. Kim, W. Sherman, J.C. Shelley, T. Lin, and R. Abel Modeling local structural rearrangements using FEP/REST: application to relative binding affinity predictions of CDK2 inhibitors J. Chem. Theor. Comput. 9 2013 1282 1293
    • (2013) J. Chem. Theor. Comput. , vol.9 , pp. 1282-1293
    • Wang, L.1    Deng, Y.2    Knight, J.L.3    Wu, Y.4    Kim, B.5    Sherman, W.6    Shelley, J.C.7    Lin, T.8    Abel, R.9
  • 157
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • J.A. Wells, and C.L. McClendon Reaching for high-hanging fruit in drug discovery at protein-protein interfaces Nature 450 2007 1001 1009
    • (2007) Nature , vol.450 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 158
    • 84867511957 scopus 로고    scopus 로고
    • Comprehensive peptidomimetic libraries targeting protein-protein interactions
    • L.R. Whitby, and D.L. Boger Comprehensive peptidomimetic libraries targeting protein-protein interactions Acc. Chem. Res. 45 2012 1698 1709
    • (2012) Acc. Chem. Res. , vol.45 , pp. 1698-1709
    • Whitby, L.R.1    Boger, D.L.2
  • 159
    • 84886290829 scopus 로고    scopus 로고
    • Probing structural adaptivity at PPI interfaces with small molecules
    • C.G. Wilson, and M.R. Arkin Probing structural adaptivity at PPI interfaces with small molecules Drug Discov. Today 10 2013 e501 e508
    • (2013) Drug Discov. Today , vol.10 , pp. e501-e508
    • Wilson, C.G.1    Arkin, M.R.2
  • 160
    • 84870810902 scopus 로고    scopus 로고
    • Biophysical and computational fragment-based approaches to targeting protein-protein interactions: Applications in structure-guided drug discovery
    • A. Winter, A.P. Higueruelo, M. Marsh, A. Sigurdardottir, W.R. Pitt, and T.L. Blundell Biophysical and computational fragment-based approaches to targeting protein-protein interactions: applications in structure-guided drug discovery Q. Rev. Biophys. 45 2012 383 426
    • (2012) Q. Rev. Biophys. , vol.45 , pp. 383-426
    • Winter, A.1    Higueruelo, A.P.2    Marsh, M.3    Sigurdardottir, A.4    Pitt, W.R.5    Blundell, T.L.6
  • 164
    • 84865494461 scopus 로고    scopus 로고
    • Relationship between hot spot residues and ligand binding hot spots in protein-protein interfaces
    • B.S. Zerbe, D.R. Hall, S. Vajda, A. Whitty, and D. Kozakov Relationship between hot spot residues and ligand binding hot spots in protein-protein interfaces J. Chem. Inf. Model. 52 2012 2236 2244
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 2236-2244
    • Zerbe, B.S.1    Hall, D.R.2    Vajda, S.3    Whitty, A.4    Kozakov, D.5
  • 167
    • 76149109071 scopus 로고    scopus 로고
    • Targeting protein-protein interactions for therapeutic intervention: A challenge for the future
    • G. Zinzalla, and D.E. Thurston Targeting protein-protein interactions for therapeutic intervention: a challenge for the future Future Med. Chem. 1 2009 65 93
    • (2009) Future Med. Chem. , vol.1 , pp. 65-93
    • Zinzalla, G.1    Thurston, D.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.