메뉴 건너뛰기




Volumn 11, Issue 90, 2014, Pages

2P2IHUNTER: A tool for filtering orthosteric protein-protein interaction modulators via a dedicated support vector machine

Author keywords

Drug design; Filtering algorithm; Focused chemical library; Protein protein interactions; Small molecule inhibitors; Support vector machine

Indexed keywords

BIOASSAY; CHEMICAL COMPOUNDS; LIBRARIES; MOLECULES; PROTEINS; THROUGHPUT;

EID: 84889646329     PISSN: 17425689     EISSN: 17425662     Source Type: Journal    
DOI: 10.1098/rsif.2013.0860     Document Type: Article
Times cited : (37)

References (69)
  • 1
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for highhanging fruit in drug discovery at protein-protein interfaces
    • doi:10.1038/nature06526
    • Wells J, McClendon C. 2007 Reaching for highhanging fruit in drug discovery at protein-protein interfaces. Nature 450, 1001-1009. (doi:10.1038/nature06526)
    • (2007) Nature , vol.450 , pp. 1001-1009
    • Wells, J.1    McClendon, C.2
  • 2
    • 84866414275 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: How to mimic a protein partner
    • doi:10.2174/138161212802651634
    • Fry DC. 2012 Small-molecule inhibitors of protein-protein interactions: how to mimic a protein partner. Curr. Pharm. Des. 18, 4679-4684. (doi:10.2174/138161212802651634)
    • (2012) Curr. Pharm. Des. , vol.18 , pp. 4679-4684
    • Fry, D.C.1
  • 3
    • 84866978465 scopus 로고    scopus 로고
    • Searching for the Holy Grail; Protein-protein interaction analysis and modulation
    • doi:10.1038/embor.2012.137
    • Morelli X, Hupp T. 2012 Searching for the Holy Grail; protein-protein interaction analysis and modulation. EMBO Rep. 13, 877-879. (doi:10.1038/embor. 2012.137)
    • (2012) EMBO Rep. , vol.13 , pp. 877-879
    • Morelli, X.1    Hupp, T.2
  • 4
    • 84857712365 scopus 로고    scopus 로고
    • Protein-protein interaction inhibitors get into the groove
    • doi:10.1038/nrd3680
    • Mullard A. 2012 Protein-protein interaction inhibitors get into the groove. Nat. Rev. Drug Discov. 11, 173-175. (doi:10.1038/nrd3680)
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 173-175
    • Mullard, A.1
  • 5
    • 79960990847 scopus 로고    scopus 로고
    • Chemical and structural lessons from recent successes in protein-protein interaction inhibition (2P2I)
    • doi:10.1016/j.cbpa. 2011.05.024
    • Morelli X, Bourgeas R, Roche P. 2011 Chemical and structural lessons from recent successes in protein-protein interaction inhibition (2P2I). Curr. Opin. Chem. Biol. 15, 475-481. (doi:10.1016/j.cbpa. 2011.05.024)
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 475-481
    • Morelli, X.1    Bourgeas, R.2    Roche, P.3
  • 6
    • 84862868473 scopus 로고    scopus 로고
    • Small-molecule inhibitors of IL-2/IL-2R: Lessons learned and applied
    • doi:10.1007/82-2010-93
    • Wilson CG, Arkin MR. 2011 Small-molecule inhibitors of IL-2/IL-2R: lessons learned and applied. Curr. Top Microbiol. Immunol. 348, 25-59. (doi:10.1007/82-2010-93)
    • (2011) Curr. Top Microbiol. Immunol. , vol.348 , pp. 25-59
    • Wilson, C.G.1    Arkin, M.R.2
  • 7
    • 84866371810 scopus 로고    scopus 로고
    • P53 mdm2 inhibitors
    • doi:10.2174/138161212802651580
    • Khoury K, Dömling A. 2012 P53 mdm2 inhibitors. Curr. Pharm. Des. 18, 4668-4678. (doi:10.2174/138161212802651580)
    • (2012) Curr. Pharm. Des. , vol.18 , pp. 4668-4678
    • Khoury, K.1    Dömling, A.2
  • 8
    • 84884603669 scopus 로고    scopus 로고
    • Inhibitors of difficult protein-protein interactions identified by high-throughput screening of multiprotein complexes
    • doi:10.1021/cb400356m
    • Cesa LC, Patury S, Komiyama T, Ahmad A, Zuiderweg ER, Gestwicki JE. 2013 Inhibitors of difficult protein-protein interactions identified by high-throughput screening of multiprotein complexes. ACS Chem. Biol. 8, 1988-1997 (doi:10.1021/cb400356m)
    • (2013) ACS Chem. Biol. , vol.8 , pp. 1988-1997
    • Cesa, L.C.1    Patury, S.2    Komiyama, T.3    Ahmad, A.4    Zuiderweg, E.R.5    Gestwicki, J.E.6
  • 9
    • 67649841614 scopus 로고    scopus 로고
    • The road less traveled: Modulating signal transduction enzymes by inhibiting their protein-protein interactions
    • doi:10.1016/j.cbpa.2009.05.125
    • Arkin MR, Whitty A. 2009 The road less traveled: modulating signal transduction enzymes by inhibiting their protein-protein interactions. Curr. Opin. Chem. Biol. 13, 284-290. (doi:10.1016/j.cbpa.2009.05.125)
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 284-290
    • Arkin, M.R.1    Whitty, A.2
  • 10
    • 84875436143 scopus 로고    scopus 로고
    • Inhibition of a-helix-mediated protein-protein interactions using designed molecules
    • doi:10.1038/nchem.1568
    • Azzarito V, Long K, Murphy NS, Wilson AJ. 2013 Inhibition of a-helix-mediated protein-protein interactions using designed molecules. Nat. Chem. 5, 161-173. (doi:10.1038/nchem.1568)
    • (2013) Nat. Chem. , vol.5 , pp. 161-173
    • Azzarito, V.1    Long, K.2    Murphy, N.S.3    Wilson, A.J.4
  • 11
    • 33645827371 scopus 로고    scopus 로고
    • Targeting protein-protein interactions by rational design: Mimicry of protein surfaces
    • doi:10.1098/rsif.2006.0115
    • Fletcher S, Hamilton AD. 2006 Targeting protein-protein interactions by rational design: mimicry of protein surfaces. J. R. Soc. Interface 3, 215-233. (doi:10.1098/rsif.2006.0115)
    • (2006) J. R. Soc. Interface , vol.3 , pp. 215-233
    • Fletcher, S.1    Hamilton, A.D.2
  • 12
    • 15444379315 scopus 로고
    • Structural and functional epitopes in the growth hormone receptor complex
    • doi:10.1038/nbt0795-647
    • Wells JA. 1995 Structural and functional epitopes in the growth hormone receptor complex. Nat. Biotechnol. 13, 647-651. (doi:10.1038/nbt0795-647)
    • (1995) Nat. Biotechnol. , vol.13 , pp. 647-651
    • Wells, J.A.1
  • 13
    • 57649138736 scopus 로고    scopus 로고
    • Small molecule protein-protein interaction inhibitors as CNS therapeutic agents: Current progress and future hurdles
    • doi:10.1038/npp.2008.151
    • Blazer LL, Neubig RR. 2009 Small molecule protein-protein interaction inhibitors as CNS therapeutic agents: current progress and future hurdles. Neuropsychopharmacology 34, 126-141. (doi:10.1038/npp.2008.151)
    • (2009) Neuropsychopharmacology , vol.34 , pp. 126-141
    • Blazer, L.L.1    Neubig, R.R.2
  • 15
    • 79961002098 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions
    • eds L Vassilev, D Fry. New Jersey: Springer
    • Fry D. 2011 Small-molecule inhibitors of protein-protein interactions. In Nutley (eds L Vassilev, D Fry), pp. 184. New Jersey: Springer.
    • (2011) Nutley , pp. 184
    • Fry, D.1
  • 16
    • 84859023900 scopus 로고    scopus 로고
    • Small-molecule inhibitor starting points learned from protein-protein interaction inhibitor structure
    • doi:10.1093/bioinformatics/btr717
    • Koes DR, Camacho CJ. 2011 Small-molecule inhibitor starting points learned from protein-protein interaction inhibitor structure. Bioinformatics 28, 784-791. (doi:10.1093/bioinformatics/btr717)
    • (2011) Bioinformatics , vol.28 , pp. 784-791
    • Koes, D.R.1    Camacho, C.J.2
  • 17
    • 84862856894 scopus 로고    scopus 로고
    • Small-molecule inhibitors of the p53-MDM2 interaction
    • doi:10.1007/82-2010-110
    • Vu BT, Vassilev L. 2011 Small-molecule inhibitors of the p53-MDM2 interaction. Curr. Top. Microbiol. Immunol. 348, 151-172. (doi:10.1007/82-2010- 110)
    • (2011) Curr. Top. Microbiol. Immunol. , vol.348 , pp. 151-172
    • Vu, B.T.1    Vassilev, L.2
  • 18
    • 79551599947 scopus 로고    scopus 로고
    • ABT-263, a Bcl-2 inhibitor, enhances the susceptibility of lung adenocarcinoma cells treated with Src inhibitors to anoikis
    • doi:10.3892/or.2010.1123
    • Sakuma Y, Tsunezumi J, Nakamura Y, Yoshihara M, Matsukuma S, Koizume S, Miyagi Y. 2011 ABT-263, a Bcl-2 inhibitor, enhances the susceptibility of lung adenocarcinoma cells treated with Src inhibitors to anoikis. Oncol. Rep. 25, 661-667. (doi:10.3892/or.2010.1123)
    • (2011) Oncol. Rep. , vol.25 , pp. 661-667
    • Sakuma, Y.1    Tsunezumi, J.2    Nakamura, Y.3    Yoshihara, M.4    Matsukuma, S.5    Koizume, S.6    Miyagi, Y.7
  • 19
    • 84893018543 scopus 로고    scopus 로고
    • Protein-protein interactions as druggable targets: Recent technological advances
    • doi:10.1016/j.coph.2013.05.009
    • Higueruelo AP, Jubb H, Blundell TL. 2013 Protein-protein interactions as druggable targets: recent technological advances. Curr. Opin. Pharmacol. 13, 791-796. (doi:10.1016/j.coph.2013.05.009)
    • (2013) Curr. Opin. Pharmacol. , vol.13 , pp. 791-796
    • Higueruelo, A.P.1    Jubb, H.2    Blundell, T.L.3
  • 20
    • 84885920636 scopus 로고    scopus 로고
    • TIMBAL v2: Update of a database holding small molecules modulating protein-protein interactions
    • bat039. (doi:10.1093/database/bat039)
    • Higueruelo AP, Jubb H, Blundell TL. 2013 TIMBAL v2: update of a database holding small molecules modulating protein-protein interactions. Database 2013, bat039. (doi:10.1093/database/bat039)
    • (2013) Database , vol.2013
    • Higueruelo, A.P.1    Jubb, H.2    Blundell, T.L.3
  • 21
    • 58849145512 scopus 로고    scopus 로고
    • Predicting druggable binding sites at the protein-protein interface
    • doi:10.1016/j.drudis.2008.10.009
    • Fuller JC, Burgoyne NJ, Jackson RM. 2009 Predicting druggable binding sites at the protein-protein interface. Drug Discov. Today 14, 155-161. (doi:10.1016/j.drudis.2008.10.009)
    • (2009) Drug Discov. Today , vol.14 , pp. 155-161
    • Fuller, J.C.1    Burgoyne, N.J.2    Jackson, R.M.3
  • 22
    • 70349739403 scopus 로고    scopus 로고
    • Assessing the druggability of protein-protein interactions by a supervised machine-learning method
    • doi:10.1186/1471-2105-10-263
    • Sugaya N, Ikeda K. 2009 Assessing the druggability of protein-protein interactions by a supervised machine-learning method. BMC Bioinform. 10, 263. (doi:10.1186/1471-2105-10-263)
    • (2009) BMC Bioinform. , vol.10 , pp. 263
    • Sugaya, N.1    Ikeda, K.2
  • 23
    • 77949743743 scopus 로고    scopus 로고
    • Atomic analysis of protein-protein interfaces with known inhibitors: The 2P2I database
    • e9598. (doi:10.1371/journal.pone.0009598)
    • Bourgeas R, Basse M-J, Morelli X, Roche P. 2010 Atomic analysis of protein-protein interfaces with known inhibitors: the 2P2I database. PLoS ONE 5, e9598. (doi:10.1371/journal.pone.0009598)
    • (2010) PLoS ONE , vol.5
    • Bourgeas, R.1    Basse, M.-J.2    Morelli, X.3    Roche, P.4
  • 24
    • 79953060278 scopus 로고    scopus 로고
    • Context-based identification of protein-protein interfaces and 'hot-spot' residues
    • doi:10.1016/j.chembiol.2011.01.005
    • Geppert T, Hoy B, Wessler S, Schneider G. 2011 Context-based identification of protein-protein interfaces and 'hot-spot' residues. Chem. Biol. 18, 344-353. (doi:10.1016/j.chembiol.2011.01.005)
    • (2011) Chem. Biol. , vol.18 , pp. 344-353
    • Geppert, T.1    Hoy, B.2    Wessler, S.3    Schneider, G.4
  • 25
    • 81855166104 scopus 로고    scopus 로고
    • Druggability assessment of protein-protein interfaces
    • doi:10.4155/fmc.11.156
    • Wanner J, Fry DC, Peng Z, Roberts J. 2011 Druggability assessment of protein-protein interfaces. Future Med. Chem. 3, 2021-2038. (doi:10.4155/fmc.11. 156)
    • (2011) Future Med. Chem. , vol.3 , pp. 2021-2038
    • Wanner, J.1    Fry, D.C.2    Peng, Z.3    Roberts, J.4
  • 26
    • 79651474672 scopus 로고    scopus 로고
    • Dr. PIAS: An integrative system for assessing the druggability of protein-protein interactions
    • doi:10.1186/1471-2105-12-50
    • Sugaya N, Furuya T. 2011 Dr. PIAS: an integrative system for assessing the druggability of protein-protein interactions. BMC Bioinform. 12, 50. (doi:10.1186/1471-2105-12-50)
    • (2011) BMC Bioinform. , vol.12 , Issue.50
    • Sugaya, N.1    Furuya, T.2
  • 27
    • 80051966197 scopus 로고    scopus 로고
    • Structural conservation of druggable hot spots in protein-protein interfaces
    • doi:10.1073/pnas.1101835108
    • Kozakov D et al. 2011 Structural conservation of druggable hot spots in protein-protein interfaces. Proc. Natl Acad. Sci. USA 108, 13 528-13 533. (doi:10.1073/pnas.1101835108)
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 13528-13533
    • Kozakov, D.1
  • 28
    • 84864451527 scopus 로고    scopus 로고
    • PocketQuery: Protein-protein interaction inhibitor starting points from protein-protein interaction structure
    • doi:10.1093/nar/gks336
    • Koes DR, Camacho CJ. 2012 PocketQuery: protein-protein interaction inhibitor starting points from protein-protein interaction structure. Nucleic Acids Res. 40, W387-W392. (doi:10.1093/nar/gks336)
    • (2012) Nucleic Acids Res , vol.40
    • Koes, D.R.1    Camacho, C.J.2
  • 29
    • 84866309070 scopus 로고    scopus 로고
    • Modulating protein-protein interactions: From structural determinants of binding to druggability prediction to application
    • doi:10.2174/138161212802651553
    • Metz A, Ciglia E, Gohlke H. 2012 Modulating protein-protein interactions: from structural determinants of binding to druggability prediction to application. Curr. Pharm. Des. 18, 4630-4647. (doi:10.2174/138161212802651553)
    • (2012) Curr. Pharm. Des. , vol.18 , pp. 4630-4647
    • Metz, A.1    Ciglia, E.2    Gohlke, H.3
  • 30
    • 84855812283 scopus 로고    scopus 로고
    • Modulating protein-protein interactions with small molecules: The importance of binding hotspots
    • doi:10.1016/j.jmb.2011.12.026
    • Thangudu RR, Bryant SH, Panchenko AR, Madej T. 2012 Modulating protein-protein interactions with small molecules: the importance of binding hotspots. J. Mol. Biol. 415, 443-453. (doi:10.1016/j.jmb.2011.12.026)
    • (2012) J. Mol. Biol. , vol.415 , pp. 443-453
    • Thangudu, R.R.1    Bryant, S.H.2    Panchenko, A.R.3    Madej, T.4
  • 31
    • 84866388293 scopus 로고    scopus 로고
    • Druggability of dynamic protein-protein interfaces
    • doi:10.2174/138161212802651652
    • Ulucan O, Eyrisch S, Helms V. 2012 Druggability of dynamic protein-protein interfaces. Curr. Pharm. Des. 18, 4599-4606. (doi:10.2174/138161 212802651652)
    • (2012) Curr. Pharm. Des. , vol.18 , pp. 4599-4606
    • Ulucan, O.1    Eyrisch, S.2    Helms, V.3
  • 32
    • 84875984520 scopus 로고    scopus 로고
    • Druggable protein interaction sites are more predisposed to surface pocket formation than the rest of the protein surface
    • e1002951. (doi:10.1371/journal.pcbi.1002951)
    • Johnson DK, Karanicolas J. 2013 Druggable protein interaction sites are more predisposed to surface pocket formation than the rest of the protein surface. PLoS Comput. Biol. 9, e1002951. (doi:10.1371/journal.pcbi.1002951)
    • (2013) PLoS Comput. Biol. , vol.9
    • Johnson, D.K.1    Karanicolas, J.2
  • 33
    • 84957099788 scopus 로고    scopus 로고
    • Druggability of protein-protein interactions
    • (ed. G. Zinzalla). London, UK: Future Science Ltd. (doi:10.4155/ 9781909453463)
    • Hamon V, Morelli X. 2013 Druggability of protein-protein interactions. In Understanding and exploiting protein-protein interactions as drug targets (ed. G. Zinzalla), pp. 18-31. London, UK: Future Science Ltd. (doi:10.4155/ 9781909453463)
    • (2013) Understanding and Exploiting Protein-protein Interactions As Drug Targets , pp. 18-31
    • Hamon, V.1    Morelli, X.2
  • 34
    • 29144483936 scopus 로고    scopus 로고
    • Predicting protein druggability
    • doi:10.1016/S1359-6446(05)03624-X
    • Hajduk PJ, Huth JR, Tse C. 2005 Predicting protein druggability. Drug Discov. Today 10, 1675-1682. (doi:10.1016/S1359-6446(05)03624-X)
    • (2005) Drug Discov. Today , vol.10 , pp. 1675-1682
    • Hajduk, P.J.1    Huth, J.R.2    Tse, C.3
  • 35
    • 79953703975 scopus 로고    scopus 로고
    • Fragment screening to predict druggability (ligandability) and lead discovery success
    • doi:10.1016/j.drudis.2011.02.002
    • Edfeldt FN, Folmer RH, Breeze AL. 2011 Fragment screening to predict druggability (ligandability) and lead discovery success. Drug Discov. Today 16, 284-287. (doi:10.1016/j.drudis.2011.02.002)
    • (2011) Drug Discov. Today , vol.16 , pp. 284-287
    • Edfeldt, F.N.1    Folmer, R.H.2    Breeze, A.L.3
  • 36
    • 84858131639 scopus 로고    scopus 로고
    • Targeting protein-protein interactions and fragment-based drug discovery
    • Valkov E, Sharpe T, Marsh M, Greive S, Hyvönen M. 2012 Targeting protein-protein interactions and fragment-based drug discovery. Top. Curr. Chem. 317, 145-179.
    • (2012) Top. Curr. Chem. , vol.317 , pp. 145-179
    • Valkov, E.1    Sharpe, T.2    Marsh, M.3    Greive, S.4    Hyvönen, M.5
  • 37
    • 84870810902 scopus 로고    scopus 로고
    • Biophysical and computational fragment-based approaches to targeting protein-protein interactions: Applications in structure-guided drug discovery
    • doi:10.1017/S0033583512000108
    • Winter A, Higueruelo AP, Marsh M, Sigurdardottir A, Pitt WR, Blundell TL. 2012 Biophysical and computational fragment-based approaches to targeting protein-protein interactions: applications in structure-guided drug discovery. Q. Rev. Biophys. 45, 1-44. (doi:10.1017/S0033583512000108)
    • (2012) Q. Rev. Biophys. , vol.45 , pp. 1-44
    • Winter, A.1    Higueruelo, A.P.2    Marsh, M.3    Sigurdardottir, A.4    Pitt, W.R.5    Blundell, T.L.6
  • 40
    • 84874713456 scopus 로고    scopus 로고
    • Expanding medicinal chemistry space
    • doi:10.1016/j.drudis.2012.10.008
    • Barker A, Kettle JG, Nowak T, Pease JE. 2013 Expanding medicinal chemistry space. Drug Discov. Today 18, 298-304. (doi:10.1016/j.drudis.2012.10. 008)
    • (2013) Drug Discov. Today , vol.18 , pp. 298-304
    • Barker, A.1    Kettle, J.G.2    Nowak, T.3    Pease, J.E.4
  • 41
    • 84877059094 scopus 로고    scopus 로고
    • Design of libraries targeting protein-protein interfaces
    • doi:10.1002/cmdc.201200540
    • Fry D et al. 2013 Design of libraries targeting protein-protein interfaces. ChemMedChem 8, 726-732. (doi:10.1002/cmdc.201200540)
    • (2013) ChemMedChem , vol.8 , pp. 726-732
    • Fry, D.1
  • 42
    • 79956140184 scopus 로고    scopus 로고
    • Getting pharmaceutical R&D back on target
    • doi:10.1038/nchembio.581
    • Bunnage ME. 2011 Getting pharmaceutical R&D back on target. Nat. Chem. Biol. 7, 335-339. (doi:10.1038/nchembio.581)
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 335-339
    • Bunnage, M.E.1
  • 43
  • 44
    • 70349756972 scopus 로고    scopus 로고
    • Atomic interactions and profile of small molecules disrupting protein-protein interfaces: The TIMBAL database
    • doi:10.1111/j.1747-0285.2009.00889.x
    • Higueruelo AP, Schreyer A, Bickerton GRJ, Pitt WR, Groom CR, Blundell TL. 2009 Atomic interactions and profile of small molecules disrupting protein-protein interfaces: the TIMBAL database. Chem. Biol. Drug Des. 74, 457-467. (doi:10.1111/j.1747-0285.2009.00889.x)
    • (2009) Chem. Biol. Drug Des. , vol.74 , pp. 457-467
    • Higueruelo, A.P.1    Schreyer, A.2    Grj, B.3    Pitt, W.R.4    Groom, C.R.5    Blundell, T.L.6
  • 45
    • 34648833340 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction inhibitors by chemoinformatics and machine learning methods
    • doi:10.1021/jm070533j
    • Neugebauer A, Hartmann RW, Klein CD. 2007 Prediction of protein-protein interaction inhibitors by chemoinformatics and machine learning methods. J. Med. Chem. 50, 4665-4668. (doi:10.1021/jm070533j)
    • (2007) J. Med. Chem. , vol.50 , pp. 4665-4668
    • Neugebauer, A.1    Hartmann, R.W.2    Klein, C.D.3
  • 46
    • 77950839899 scopus 로고    scopus 로고
    • Designing focused chemical libraries enriched in protein-protein interaction inhibitors using machine-learning methods
    • e1000695. (doi:10.1371/journal.pcbi.1000695)
    • Reynes C et al. 2010 Designing focused chemical libraries enriched in protein-protein interaction inhibitors using machine-learning methods. PLoS Comput. Biol. 6, e1000695. (doi:10.1371/journal.pcbi.1000695)
    • (2010) PLoS Comput. Biol. , vol.6
    • Reynes, C.1
  • 47
    • 77649233664 scopus 로고    scopus 로고
    • Rationalizing the chemical space of protein-protein interaction inhibitors
    • doi:10.1016/j.drudis.2009.11.007
    • Sperandio O, Reynès C, Camproux A, Villoutreix B. 2010 Rationalizing the chemical space of protein-protein interaction inhibitors. Drug Discov. Today 15, 220-229. (doi:10.1016/j.drudis.2009.11.007)
    • (2010) Drug Discov. Today , vol.15 , pp. 220-229
    • Sperandio, O.1    Reynès, C.2    Camproux, A.3    Villoutreix, B.4
  • 48
    • 84866306870 scopus 로고    scopus 로고
    • A leap into the chemical space of protein-protein interaction inhibitors
    • doi:10.2174/138161212802651571
    • Villoutreix BO, Labbé CM, Lagorce D, Laconde G, Sperandio O. 2012 A leap into the chemical space of protein-protein interaction inhibitors. Curr. Pharm. Des. 18, 4648-4667. (doi:10.2174/138161212802651571)
    • (2012) Curr. Pharm. Des. , vol.18 , pp. 4648-4667
    • Villoutreix, B.O.1    Labbé, C.M.2    Lagorce, D.3    Laconde, G.4    Sperandio, O.5
  • 49
    • 84884587933 scopus 로고    scopus 로고
    • IPPI-DB: A manually curated and interactive database of small non-peptide inhibitors of protein-protein interactions
    • doi:10.1016/j.drudis.2013.05.003
    • Labbé CM, Laconde G, Kuenemann MA, Villoutreix BO, Sperandio O. 2013 iPPI-DB: a manually curated and interactive database of small non-peptide inhibitors of protein-protein interactions. Drug Discov. Today 18, 958-968. (doi:10.1016/j.drudis.2013.05.003)
    • (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
  • 50
    • 79951960238 scopus 로고    scopus 로고
    • Small-molecule protein-protein interaction inhibitors: Therapeutic potential in light of molecular size, chemical space, and ligand binding efficiency considerations
    • doi:10.1002/iub.383
    • Buchwald P. 2010 Small-molecule protein-protein interaction inhibitors: therapeutic potential in light of molecular size, chemical space, and ligand binding efficiency considerations. IUBMB Life 62, 724-731. (doi:10.1002/iub.383)
    • (2010) IUBMB Life , vol.62 , pp. 724-731
    • Buchwald, P.1
  • 51
    • 84876546810 scopus 로고    scopus 로고
    • 2P2Idb: A structural database dedicated to orthosteric modulation of protein-protein interactions
    • doi:10.1093/nar/gks1002
    • Basse MJ, Betzi S, Bourgeas R, Bouzidi S, Chetrit B, Hamon V, Morelli X, Roche P. 2013 2P2Idb: a structural database dedicated to orthosteric modulation of protein-protein interactions. Nucleic Acids Res. 41, D824-D827. (doi:10.1093/nar/gks1002)
    • (2013) Nucleic Acids Res , vol.41
    • Basse, M.J.1    Betzi, S.2    Bourgeas, R.3    Bouzidi, S.4    Chetrit, B.5    Hamon, V.6    Morelli, X.7    Roche, P.8
  • 52
    • 58149305794 scopus 로고    scopus 로고
    • An empirical framework for binary interactome mapping
    • doi:10.1038/nmeth.1280
    • Venkatesan K et al. 2009 An empirical framework for binary interactome mapping. Nat. Methods 6, 83-90. (doi:10.1038/nmeth.1280)
    • (2009) Nat. Methods , vol.6 , pp. 83-90
    • Venkatesan, K.1
  • 54
    • 75849133755 scopus 로고    scopus 로고
    • A novel method for mining highly imbalanced high-throughput screening data in PubChem
    • doi:10.1093/bioinformatics/btp589
    • Li Q, Wang Y, Bryant SH. 2009 A novel method for mining highly imbalanced high-throughput screening data in PubChem. Bioinformatics 25, 3310-3316. (doi:10.1093/bioinformatics/btp589)
    • (2009) Bioinformatics , vol.25 , pp. 3310-3316
    • Li, Q.1    Wang, Y.2    Bryant, S.H.3
  • 55
    • 84877278593 scopus 로고    scopus 로고
    • 2P2Ichem: Focused chemical libraries dedicated to orthosteric modulation of protein-protein interactions
    • doi:10.1039/c3md00018d
    • Hamon V, Brunel JM, Combes S, Basse MJ, Roche P, Morelli X. 2013 2P2Ichem: focused chemical libraries dedicated to orthosteric modulation of protein-protein interactions. MedChemComm 4, 797-809. (doi:10.1039/c3md00018d)
    • (2013) MedChemComm , 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
  • 56
    • 33750067690 scopus 로고    scopus 로고
    • Discovery of novel inhibitors of the ZipA/FtsZ complex by NMR fragment screening coupled with structure-based design
    • doi:10.1016/j.bmc.2006.07.050
    • Tsao DHH et al. 2006 Discovery of novel inhibitors of the ZipA/FtsZ complex by NMR fragment screening coupled with structure-based design. Bioorg. Med. Chem. 14, 7953-7961. (doi:10.1016/j.bmc.2006.07.050)
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 7953-7961
    • Dhh, T.1
  • 57
    • 84862271587 scopus 로고    scopus 로고
    • New class of HIV-1 integrase (IN) inhibitors with a dual mode of action
    • doi:10.1074/jbc.M112.347534
    • Tsiang M et al. 2012 New class of HIV-1 integrase (IN) inhibitors with a dual mode of action. J. Biol. Chem. 287, 21 189-21 203. (doi:10.1074/jbc.M112. 347534)
    • (2012) J. Biol. Chem. , vol.287 , pp. 21189-21203
    • Tsiang, M.1
  • 58
    • 77952553431 scopus 로고    scopus 로고
    • Rational design of smallmolecule inhibitors of the LEDGF/p75-integrase interaction and HIV replication
    • doi:10.1038/nchembio.370
    • Christ F et al. 2010 Rational design of smallmolecule inhibitors of the LEDGF/p75-integrase interaction and HIV replication. Nat. Chem. Biol. 6, 442-448. (doi:10.1038/nchembio.370)
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 442-448
    • Christ, F.1
  • 59
    • 57049144228 scopus 로고    scopus 로고
    • Designing Smac-mimetics as antagonists of XIAP, cIAP1, and cIAP2
    • doi:10.1016/j.bbrc.2008.10.139
    • Cossu F et al. 2009 Designing Smac-mimetics as antagonists of XIAP, cIAP1, and cIAP2. Biochem. Biophys. Res. Commun. 378, 162-167. (doi:10.1016/j.bbrc.2008.10.139)
    • (2009) Biochem. Biophys. Res. Commun. , vol.378 , pp. 162-167
    • Cossu, F.1
  • 60
    • 75549087817 scopus 로고    scopus 로고
    • An overview of the PubChem BioAssay resource
    • doi:10.1093/nar/gkp965
    • Wang Y et al. 2010 An overview of the PubChem BioAssay resource. Nucleic Acids Res. 38, D255-D266. (doi:10.1093/nar/gkp965)
    • (2010) Nucleic Acids Res , vol.38
    • Wang, Y.1
  • 61
    • 78649386109 scopus 로고    scopus 로고
    • Exploiting PubChem for virtual screening
    • doi:10.1517/17460441.2010.524924
    • Xie XQ. 2010 Exploiting PubChem for virtual screening. Expert Opin. Drug Discov. 5, 1205-1220. (doi:10.1517/17460441.2010.524924)
    • (2010) Expert Opin. Drug Discov. , vol.5 , pp. 1205-1220
    • Xie, X.Q.1
  • 62
    • 80054970242 scopus 로고    scopus 로고
    • New and unusual scaffolds in medicinal chemistry
    • doi:10.1039/c1cs15119c
    • Marson CM. 2011 New and unusual scaffolds in medicinal chemistry. Chem. Soc. Rev. 40, 5514-5533. (doi:10.1039/c1cs15119c)
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 5514-5533
    • Marson, C.M.1
  • 63
    • 77958549006 scopus 로고    scopus 로고
    • Large-scale protein interactome mapping: Strategies and opportunities
    • doi:10.1586/epr.10.30
    • Lievens S, Eyckerman S, Lemmens I, Tavernier J. 2010 Large-scale protein interactome mapping: strategies and opportunities. Expert Rev. Proteomics 7, 679-690. (doi:10.1586/epr.10.30)
    • (2010) Expert Rev. Proteomics , vol.7 , pp. 679-690
    • Lievens, S.1    Eyckerman, S.2    Lemmens, I.3    Tavernier, J.4
  • 64
    • 84889654459 scopus 로고    scopus 로고
    • Cambridge, UK: HTStec
    • HTStec. 2012 Future Directions of HTS Trends. Cambridge, UK: HTStec. See http://www.htstec.com/.
    • (2012) Future Directions of HTS Trends
  • 65
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • doi:10.1016/S0169-409X(00)00129-0
    • Lipinski C, Lombardo F, Dominy B, Feeney P. 2001 Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Deliv. Rev. 46, 3-26. (doi:10.1016/S0169-409X(00)00129-0)
    • (2001) Adv. Drug Deliv. Rev. , vol.46 , pp. 3-26
    • Lipinski, C.1    Lombardo, F.2    Dominy, B.3    Feeney, P.4
  • 66
    • 0037030653 scopus 로고    scopus 로고
    • Molecular properties that influence the oral bioavailability of drug candidates
    • doi:10.1021/jm020017n
    • Veber DF, Johnson SR, Cheng HY, Smith BR, Ward KW, Kopple KD. 2002 Molecular properties that influence the oral bioavailability of drug candidates. J. Med. Chem. 45, 2615-2623. (doi:10.1021/jm020017n)
    • (2002) J. Med. Chem. , vol.45 , pp. 2615-2623
    • Veber, D.F.1    Johnson, S.R.2    Cheng, H.Y.3    Smith, B.R.4    Ward, K.W.5    Kopple, K.D.6
  • 67
    • 15744363581 scopus 로고    scopus 로고
    • Metric validation and the receptor-relevant subspace concept
    • doi:10.1021/ci980137x
    • Pearlman RS, Smith KM. 1999 Metric validation and the receptor-relevant subspace concept. J. Chem. Info. Comput. Sci. 39, 28-35. (doi:10.1021/ci980137x)
    • (1999) J. Chem. Info. Comput. Sci. , vol.39 , pp. 28-35
    • Pearlman, R.S.1    Smith, K.M.2
  • 68
    • 34249753618 scopus 로고
    • Support-vector networks
    • doi:10.1007/BF00994018
    • Cortes C, Vapnik V. 1995 Support-vector networks. Mach. Learn. 20, 273-297. (doi:10.1007/BF00994018)
    • (1995) Mach. Learn. , vol.20 , pp. 273-297
    • Cortes, C.1    Vapnik, V.2
  • 69
    • 46749110034 scopus 로고    scopus 로고
    • FactoMineR: An R package for multivariate analysis
    • Josse J. 2008 FactoMineR: an R package for multivariate analysis. J. Stat. Softw. 25, 1-18.
    • (2008) J. Stat. Softw. , vol.25 , pp. 1-18
    • Josse, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.