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Volumn 15, Issue 5-6, 2010, Pages 220-229

Rationalizing the chemical space of protein-protein interaction inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

4 [4 (4' CHLORO 2 BIPHENYLYLMETHYL) 1 PIPERAZINYL] N [4 [3 DIMETHYLAMINO 1 (PHENYLTHIOMETHYL)PROPYLAMINO] 3 NITROBENZENESULFONYL]BENZAMIDE; 4 [4 [2 (4 CHLOROPHENYL) 5,5 DIMETHYL 1 CYCLOHEXEN 1 YLMETHYL] 1 PIPERAZINYL] N [4 [3 MORPHOLINO 1 (PHENYLTHIOMETHYL)PROPYLAMINO] 3 (TRIFLUOROMETHYLSULFONYL)BENZENESULFONYL]BENZAMIDE; BCL2 RELATED PROTEIN A1; BENZODIAZEPINEDIONE; BH3 PROTEIN; EPHRIN A4; G PROTEIN COUPLED RECEPTOR; METHIONINE; NERVE GROWTH FACTOR; NUTLIN 3; PHENYLALANINE; PHOSPHOTRANSFERASE INHIBITOR; PROTEIN BAK; PROTEIN BCL XL; PROTEIN BID; PROTEIN INHIBITOR; PROTEIN MDM2; PROTEIN P53; PROTEIN P75; PROTEINASE INHIBITOR; SP 4206; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG;

EID: 77649233664     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.drudis.2009.11.007     Document Type: Review
Times cited : (178)

References (40)
  • 1
    • 44349113144 scopus 로고    scopus 로고
    • Estimating the size of the human interactome
    • Stumpf M.P., et al. Estimating the size of the human interactome. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 6959-6964
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 6959-6964
    • Stumpf, M.P.1
  • 2
    • 50249154886 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions
    • Berg T. Small-molecule inhibitors of protein-protein interactions. Curr. Opin. Drug Discov. Dev. 11 (2008) 666-674
    • (2008) Curr. Opin. Drug Discov. Dev. , vol.11 , pp. 666-674
    • Berg, T.1
  • 3
    • 47349109056 scopus 로고    scopus 로고
    • Drug-like inhibitors of protein-protein interactions: a structural examination of effective protein mimicry
    • Fry D.C. Drug-like inhibitors of protein-protein interactions: a structural examination of effective protein mimicry. Curr. Protein Pept. Sci. 9 (2008) 240-247
    • (2008) Curr. Protein Pept. Sci. , vol.9 , pp. 240-247
    • Fry, D.C.1
  • 4
    • 41949126415 scopus 로고    scopus 로고
    • In silico-in vitro screening of protein-protein interactions: towards the next generation of therapeutics
    • Villoutreix B.O., et al. In silico-in vitro screening of protein-protein interactions: towards the next generation of therapeutics. Curr. Pharm. Biotechnol. 9 (2008) 103-122
    • (2008) Curr. Pharm. Biotechnol. , vol.9 , pp. 103-122
    • Villoutreix, B.O.1
  • 5
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • Wells J.A., and McClendon C.L. 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
  • 6
    • 33646567148 scopus 로고    scopus 로고
    • Between a rock and a hard place?
    • Whitty A., and Kumaravel G. Between a rock and a hard place?. Nat. Chem. Biol. 2 (2006) 112-118
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 112-118
    • Whitty, A.1    Kumaravel, G.2
  • 7
    • 58849145512 scopus 로고    scopus 로고
    • Predicting druggable binding sites at the protein-protein interface
    • Fuller J.C., et al. 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
  • 8
    • 67649841614 scopus 로고    scopus 로고
    • The road less traveled: modulating signal transduction enzymes by inhibiting their protein-protein interactions
    • Arkin M.R., and Whitty A. The road less traveled: modulating signal transduction enzymes by inhibiting their protein-protein interactions. Curr. Opin. Chem. Biol. 13 (2009) 284-290
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 284-290
    • Arkin, M.R.1    Whitty, A.2
  • 9
    • 11144323163 scopus 로고    scopus 로고
    • Virtual screening of chemical libraries
    • Shoichet B.K. Virtual screening of chemical libraries. Nature 432 (2004) 862-865
    • (2004) Nature , vol.432 , pp. 862-865
    • Shoichet, B.K.1
  • 10
    • 33750610998 scopus 로고    scopus 로고
    • Drugs targeting protein-protein interactions
    • Chene P. Drugs targeting protein-protein interactions. ChemMedChem 1 (2006) 400-411
    • (2006) ChemMedChem , vol.1 , pp. 400-411
    • Chene, P.1
  • 11
    • 34547583152 scopus 로고    scopus 로고
    • Transient pockets on protein surfaces involved in protein-protein interaction
    • Eyrisch S., and Helms V. Transient pockets on protein surfaces involved in protein-protein interaction. J. Med. Chem. 50 (2007) 3457-3464
    • (2007) J. Med. Chem. , vol.50 , pp. 3457-3464
    • Eyrisch, S.1    Helms, V.2
  • 12
    • 20444376940 scopus 로고    scopus 로고
    • Protein-protein interactions and cancer: small molecules going in for the kill
    • Arkin M. Protein-protein interactions and cancer: small molecules going in for the kill. Curr. Opin. Chem. Biol. 9 (2005) 317-324
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 317-324
    • Arkin, M.1
  • 13
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T., and Wells J.A. 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
  • 14
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte L., et al. The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285 (1999) 2177-2198
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Lo Conte, L.1
  • 15
    • 34447286664 scopus 로고    scopus 로고
    • Trp/Met/Phe hot spots in protein-protein interactions: potential targets in drug design
    • Ma B., and Nussinov R. Trp/Met/Phe hot spots in protein-protein interactions: potential targets in drug design. Curr. Top. Med. Chem. 7 (2007) 999-1005
    • (2007) Curr. Top. Med. Chem. , vol.7 , pp. 999-1005
    • Ma, B.1    Nussinov, R.2
  • 16
    • 33846925964 scopus 로고    scopus 로고
    • The molecular architecture of protein-protein binding sites
    • Reichmann D., et al. The molecular architecture of protein-protein binding sites. Curr. Opin. Struct. Biol. 17 (2007) 67-76
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 67-76
    • Reichmann, D.1
  • 17
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: progressing towards the dream
    • Arkin M.R., and Wells J.A. Small-molecule inhibitors of protein-protein interactions: progressing towards the dream. Nat. Rev. Drug Discov. 3 (2004) 301-317
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 18
    • 56249144184 scopus 로고    scopus 로고
    • Discovery of an orally bioavailable small molecule inhibitor of prosurvival B-cell lymphoma 2 proteins
    • Park C.M., et al. Discovery of an orally bioavailable small molecule inhibitor of prosurvival B-cell lymphoma 2 proteins. J. Med. Chem. 51 (2008) 6902-6915
    • (2008) J. Med. Chem. , vol.51 , pp. 6902-6915
    • Park, C.M.1
  • 19
    • 0036893020 scopus 로고    scopus 로고
    • Side-chain conformational entropy at protein-protein interfaces
    • Cole C., and Warwicker J. Side-chain conformational entropy at protein-protein interfaces. Protein Sci. 11 (2002) 2860-2870
    • (2002) Protein Sci. , vol.11 , pp. 2860-2870
    • Cole, C.1    Warwicker, J.2
  • 20
    • 48749127628 scopus 로고    scopus 로고
    • What has virtual screening ever done for drug discovery?
    • Clark D.E. What has virtual screening ever done for drug discovery?. Expert Opin. Drug Discov. 3 (2008) 841-851
    • (2008) Expert Opin. Drug Discov. , vol.3 , pp. 841-851
    • Clark, D.E.1
  • 21
    • 33746058237 scopus 로고    scopus 로고
    • Streamlining lead discovery by aligning in silico and high-throughput screening
    • Davies J.W., et al. Streamlining lead discovery by aligning in silico and high-throughput screening. Curr. Opin. Chem. Biol. 10 (2006) 343-351
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , pp. 343-351
    • Davies, J.W.1
  • 22
    • 41949125119 scopus 로고    scopus 로고
    • Characterization and prediction of protein interfaces to infer protein-protein interaction networks
    • Keskin O., et al. Characterization and prediction of protein interfaces to infer protein-protein interaction networks. Curr. Pharm. Biotechnol. 9 (2008) 67-76
    • (2008) Curr. Pharm. Biotechnol. , vol.9 , pp. 67-76
    • Keskin, O.1
  • 23
    • 8844263008 scopus 로고    scopus 로고
    • Docking and scoring in virtual screening for drug discovery: methods and applications
    • Kitchen D.B., et al. Docking and scoring in virtual screening for drug discovery: methods and applications. Nat. Rev. Drug Discov. 3 (2004) 935-949
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 935-949
    • Kitchen, D.B.1
  • 24
    • 34547126694 scopus 로고    scopus 로고
    • Novel therapeutic strategies for the treatment of protein-misfolding diseases
    • Rochet J.C. Novel therapeutic strategies for the treatment of protein-misfolding diseases. Expert Rev. Mol. Med. 9 (2007) 1-34
    • (2007) Expert Rev. Mol. Med. , vol.9 , pp. 1-34
    • Rochet, J.C.1
  • 25
    • 11144298973 scopus 로고    scopus 로고
    • Exploring biology with small organic molecules
    • Stockwell B.R. Exploring biology with small organic molecules. Nature 432 (2004) 846-854
    • (2004) Nature , vol.432 , pp. 846-854
    • Stockwell, B.R.1
  • 26
    • 33750303565 scopus 로고    scopus 로고
    • Hot-spot mimicry of a cytokine receptor by a small molecule
    • Thanos C.D., et al. Hot-spot mimicry of a cytokine receptor by a small molecule. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 15422-15427
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 15422-15427
    • Thanos, C.D.1
  • 27
    • 44949154279 scopus 로고    scopus 로고
    • Small molecular weight protein-protein interaction antagonists: an insurmountable challenge?
    • Domling A. 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
    • Domling, A.1
  • 28
    • 33645377497 scopus 로고    scopus 로고
    • Structure-based development of target-specific compound libraries
    • Orry A.J., et al. Structure-based development of target-specific compound libraries. Drug Discov. Today 11 (2006) 261-266
    • (2006) Drug Discov. Today , vol.11 , pp. 261-266
    • Orry, A.J.1
  • 29
    • 43149092276 scopus 로고    scopus 로고
    • Principles of protein-protein interactions: what are the preferred ways for proteins to interact?
    • Keskin O., et al. Principles of protein-protein interactions: what are the preferred ways for proteins to interact?. Chem. Rev. 108 (2008) 1225-1244
    • (2008) Chem. Rev. , vol.108 , pp. 1225-1244
    • Keskin, O.1
  • 30
    • 3342908718 scopus 로고    scopus 로고
    • Emerging classes of protein-protein interaction inhibitors and new tools for their development
    • Pagliaro L., et al. Emerging classes of protein-protein interaction inhibitors and new tools for their development. Curr. Opin. Chem. Biol. 8 (2004) 442-449
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 442-449
    • Pagliaro, L.1
  • 31
    • 22144454687 scopus 로고    scopus 로고
    • Strategies for targeting protein-protein interactions with synthetic agents
    • Yin H., and Hamilton A.D. Strategies for targeting protein-protein interactions with synthetic agents. Angew. Chem. Int. Ed. Engl. 44 (2005) 4130-4163
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 4130-4163
    • Yin, H.1    Hamilton, A.D.2
  • 32
    • 33845594315 scopus 로고    scopus 로고
    • Protein-protein interactions as targets for small molecule drug discovery
    • Fry D.C. 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
  • 33
    • 34648833340 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction inhibitors by chemoinformatics and machine learning methods
    • Neugebauer A., et al. 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
  • 34
    • 0000733018 scopus 로고
    • Molecular profiles novel geometry-dependent molecular descriptors
    • Randic M. Molecular profiles novel geometry-dependent molecular descriptors. New J. Chem. 19 (1995) 781-791
    • (1995) New J. Chem. , vol.19 , pp. 781-791
    • Randic, M.1
  • 35
  • 37
    • 33646484507 scopus 로고    scopus 로고
    • In silico studies using radial distribution function approach for predicting affinity of 1 alpha,25-dihydroxyvitamin D(3) analogues for vitamin D receptor
    • Gonzalez M.P., et al. In silico studies using radial distribution function approach for predicting affinity of 1 alpha,25-dihydroxyvitamin D(3) analogues for vitamin D receptor. Steroids 71 (2006) 510-527
    • (2006) Steroids , vol.71 , pp. 510-527
    • Gonzalez, M.P.1
  • 38
    • 16244394858 scopus 로고    scopus 로고
    • Quantitative structure-activity relationship to predict differential inhibition of aldose reductase by flavonoid compounds
    • Fernandez M. Quantitative structure-activity relationship to predict differential inhibition of aldose reductase by flavonoid compounds. Bioorg. Med. Chem. 13 (2005) 3269-3277
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 3269-3277
    • Fernandez, M.1
  • 39
    • 0034648807 scopus 로고    scopus 로고
    • Prediction of three-dimensional molecular structures using information from infrared spectra
    • Hemmer M. Prediction of three-dimensional molecular structures using information from infrared spectra. Anal. Chim. Acta 420 (2000) 145-154
    • (2000) Anal. Chim. Acta , vol.420 , pp. 145-154
    • Hemmer, M.1
  • 40
    • 0001219854 scopus 로고    scopus 로고
    • Deriving the 3D structure of organic molecules from their infrared spectra
    • Hemmer M. Deriving the 3D structure of organic molecules from their infrared spectra. Vib. Spectrosc. 19 (1999) 151-164
    • (1999) Vib. Spectrosc. , vol.19 , pp. 151-164
    • Hemmer, M.1


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