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Volumn 15, Issue 1 SPEC. ISS., 2005, Pages 31-34

Inhibiting protein-protein interactions using designed molecules

Author keywords

[No Author keywords available]

Indexed keywords

IMIDAZOLE; PEPTIDE DERIVATIVE; PROTEIN; PROTEIN BCL XL; PROTEIN INHIBITOR; PROTEIN P53; SCAFFOLD PROTEIN; TEREPHTHALIC ACID; TUMOR SUPPRESSOR PROTEIN;

EID: 13844275835     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2005.01.005     Document Type: Review
Times cited : (81)

References (34)
  • 2
    • 0034644509 scopus 로고    scopus 로고
    • Signaling networks: The origins of cellular multitasking
    • J.D. Jordan, E.M. Landau, and R. Iyengar Signaling networks: the origins of cellular multitasking Cell 103 2000 193 200
    • (2000) Cell , vol.103 , pp. 193-200
    • Jordan, J.D.1    Landau, E.M.2    Iyengar, R.3
  • 3
    • 5044232018 scopus 로고    scopus 로고
    • Connecting proliferation and apoptosis in development and disease
    • D.R. Hipfner, and S.M. Cohen Connecting proliferation and apoptosis in development and disease Nat Rev Mol Cell Biol 5 2004 805 815
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 805-815
    • Hipfner, D.R.1    Cohen, S.M.2
  • 4
    • 0037061646 scopus 로고    scopus 로고
    • Inhibition of protein-protein association by small molecules: Approaches and progress
    • P.L. Toogood Inhibition of protein-protein association by small molecules: approaches and progress J Med Chem 45 2002 1543 1558
    • (2002) J Med Chem , vol.45 , pp. 1543-1558
    • Toogood, P.L.1
  • 5
    • 0037860938 scopus 로고    scopus 로고
    • Modulation of protein-protein interactions with small organic molecules
    • T. Berg Modulation of protein-protein interactions with small organic molecules Angew Chem Int Ed Engl 42 2003 2462 2481
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 2462-2481
    • Berg, T.1
  • 6
    • 0037212039 scopus 로고    scopus 로고
    • Small molecule antagonists of proteins
    • T.R. Gadek, and J.B. Nicholas Small molecule antagonists of proteins Biochem Pharmacol 65 2003 1 8
    • (2003) Biochem Pharmacol , vol.65 , pp. 1-8
    • Gadek, T.R.1    Nicholas, J.B.2
  • 7
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • M.R. Arkin, and J.A. Wells 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
  • 9
    • 0036514662 scopus 로고    scopus 로고
    • Cyclization strategies in peptide derived drug design
    • P. Li, and P.P. Roller Cyclization strategies in peptide derived drug design Curr Top Med Chem 2 2002 325 341
    • (2002) Curr Top Med Chem , vol.2 , pp. 325-341
    • Li, P.1    Roller, P.P.2
  • 10
    • 2342633291 scopus 로고    scopus 로고
    • Chemistry and biology of cyclic peptides of medicinal and biological interest
    • F. Sarabia, S. Chammaa, A.S. Ruiz, L.M. Ortiz, and F.J.L. Herrera Chemistry and biology of cyclic peptides of medicinal and biological interest Curr Med Chem 11 2004 1309 1332
    • (2004) Curr Med Chem , vol.11 , pp. 1309-1332
    • Sarabia, F.1    Chammaa, S.2    Ruiz, A.S.3    Ortiz, L.M.4    Herrera, F.J.L.5
  • 14
    • 0141706365 scopus 로고    scopus 로고
    • Helix-stabilized cyclic peptides as selective inhibitors of steroid receptor-coactivator interactions
    • A.M. Leduc, J.O. Trent, J.L. Wittliff, K.S. Bramlett, S.L. Briggs, N.Y. Chirgadze, Y. Wang, T.P. Burris, and A.F. Spatola Helix-stabilized cyclic peptides as selective inhibitors of steroid receptor-coactivator interactions Proc Natl Acad Sci USA 100 2003 11273 11278 Lactam and disulfide cross-linked peptides have potent activity against the estrogen receptor-coactivator interaction.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11273-11278
    • Leduc, A.M.1    Trent, J.O.2    Wittliff, J.L.3    Bramlett, K.S.4    Briggs, S.L.5    Chirgadze, N.Y.6    Wang, Y.7    Burris, T.P.8    Spatola, A.F.9
  • 15
    • 1542285113 scopus 로고    scopus 로고
    • Thermodynamic profiling of conformationally constrained cyclic ligands for the PDZ domain
    • T. Li, D. Saro, and M.R. Spaller Thermodynamic profiling of conformationally constrained cyclic ligands for the PDZ domain Bioorg Med Chem Lett 14 2004 1385 1388 A lactam-constrained peptide corresponding to the C-terminal sequence of the CRIPT protein is described that binds to the PDZ3 domain of the protein PSD-95.
    • (2004) Bioorg Med Chem Lett , vol.14 , pp. 1385-1388
    • Li, T.1    Saro, D.2    Spaller, M.R.3
  • 16
    • 1542375100 scopus 로고    scopus 로고
    • Inhibition of ICAM-1/LFA-1-mediated heterotypic T-cell adhesion to epithelial cells: Design of ICAM-1 cyclic peptides
    • M.E. Anderson, T. Yakovleva, Y.B. Hu, and T.J. Siahaan Inhibition of ICAM-1/LFA-1-mediated heterotypic T-cell adhesion to epithelial cells: design of ICAM-1 cyclic peptides Bioorg Med Chem Lett 14 2004 1399 1402
    • (2004) Bioorg Med Chem Lett , vol.14 , pp. 1399-1402
    • Anderson, M.E.1    Yakovleva, T.2    Hu, Y.B.3    Siahaan, T.J.4
  • 17
    • 4043087650 scopus 로고    scopus 로고
    • Small-molecule dimerization inhibitors of wild-type and mutant HIV protease: A focused library approach
    • M.D. Shultz, Y.W. Ham, S.G. Lee, D.A. Davis, C. Brown, and J. Chmielewski Small-molecule dimerization inhibitors of wild-type and mutant HIV protease: a focused library approach J Am Chem Soc 126 2004 9886 9887 A library of agents is described that target the dimerization interface of HIV-1 protease. Cross-reactivity with drug-resistant forms of HIV protease is demonstrated.
    • (2004) J Am Chem Soc , vol.126 , pp. 9886-9887
    • Shultz, M.D.1    Ham, Y.W.2    Lee, S.G.3    Davis, D.A.4    Brown, C.5    Chmielewski, J.6
  • 18
    • 3142658710 scopus 로고    scopus 로고
    • A unidirectional crosslinking strategy for HIV-1 protease dimerization inhibitors
    • Y.S. Hwang, and J. Chmielewski A unidirectional crosslinking strategy for HIV-1 protease dimerization inhibitors Bioorg Med Chem Lett 14 2004 4297 4300 Potent inhibitors of HIV-1 protease dimerization are described, together with a novel strategy for cross-linking interfacial peptides.
    • (2004) Bioorg Med Chem Lett , vol.14 , pp. 4297-4300
    • Hwang, Y.S.1    Chmielewski, J.2
  • 19
    • 15444380612 scopus 로고    scopus 로고
    • Development of low molecular weight HIV-1 protease dimerization inhibitors
    • in press.
    • Hwang YS, Chmielewski J: Development of low molecular weight HIV-1 protease dimerization inhibitors. J Med Chem 2005, in press.
    • (2005) J Med Chem
    • Hwang, Y.S.1    Chmielewski, J.2
  • 20
    • 0033568644 scopus 로고    scopus 로고
    • Computational alanine scanning to probe protein-protein interactions: A novel approach to evaluate binding free energies
    • I. Massova, and P.A. Kollman Computational alanine scanning to probe protein-protein interactions: a novel approach to evaluate binding free energies J Am Chem Soc 121 1999 8133 8143
    • (1999) J Am Chem Soc , vol.121 , pp. 8133-8143
    • Massova, I.1    Kollman, P.A.2
  • 22
    • 3543098742 scopus 로고    scopus 로고
    • Helical beta-peptide inhibitors of the p53-hDM2 interaction
    • J.A. Kritzer, J.D. Lear, M.E. Hodsdon, and A. Schepartz Helical beta-peptide inhibitors of the p53-hDM2 interaction J Am Chem Soc 126 2004 9468 9469 A 14-helix β-peptide helix is used as a scaffold to display the relevant functionality of the interfacial p53 helix. Inhibition of the p53-HDM2 interaction is described.
    • (2004) J Am Chem Soc , vol.126 , pp. 9468-9469
    • Kritzer, J.A.1    Lear, J.D.2    Hodsdon, M.E.3    Schepartz, A.4
  • 23
    • 4544342753 scopus 로고    scopus 로고
    • Using a beta-hairpin to mimic an alpha-helix: Cyclic peptidomimetic inhibitors of the p53-HDM2 protein-protein interaction
    • R. Fasan, Dias RLA, K. Moehle, O. Zerbe, J.W. Vrijbloed, D. Obrecht, and J.A. Robinson Using a beta-hairpin to mimic an alpha-helix: cyclic peptidomimetic inhibitors of the p53-HDM2 protein-protein interaction Angew Chem Int Ed Engl 43 2004 2109 2112 A β-hairpin structure is used as a scaffold to display the relevant functionality of the interfacial p53 helix. Inhibition of the p53-HDM2 interaction is described.
    • (2004) Angew Chem Int Ed Engl , vol.43 , pp. 2109-2112
    • Fasan, R.1    Dias, R.L.A.2    Moehle, K.3    Zerbe, O.4    Vrijbloed, J.W.5    Obrecht, D.6    Robinson, J.A.7
  • 24
    • 0037048711 scopus 로고    scopus 로고
    • Development of a potent Bcl-x(L) antagonist based on alpha-helix mimicry
    • O. Kutzki, H.S. Park, J.T. Ernst, B.P. Orner, H. Yin, and A.D. Hamilton Development of a potent Bcl-x(L) antagonist based on alpha-helix mimicry J Am Chem Soc 124 2002 11838 11839
    • (2002) J Am Chem Soc , vol.124 , pp. 11838-11839
    • Kutzki, O.1    Park, H.S.2    Ernst, J.T.3    Orner, B.P.4    Yin, H.5    Hamilton, A.D.6
  • 25
    • 1542285103 scopus 로고    scopus 로고
    • Terephthalamide derivatives as mimetics of the helical region of Bak peptide target Bcl-xL protein
    • L interaction is described.
    • (2004) Bioorg Med Chem Lett , vol.14 , pp. 1375-1379
    • Yin, H.1    Hamilton, A.D.2
  • 26
    • 0141718393 scopus 로고    scopus 로고
    • Small molecule inhibition of hepatitis C virus E2 binding to CD81
    • S.E. VanCompernolle, A.V. Wiznycia, J.R. Rush, M. Dhanasekaran, P.W. Baures, and S.C. Todd Small molecule inhibition of hepatitis C virus E2 binding to CD81 Virology 314 2003 371 380 A novel bis-imidazole scaffold was used to generate a series of compounds that mimic (in a similar orientation and spatial arrangement) helix D of CD81. The inhibitors are found to bind reversibly to hepatitis C virus E2.
    • (2003) Virology , vol.314 , pp. 371-380
    • Vancompernolle, S.E.1    Wiznycia, A.V.2    Rush, J.R.3    Dhanasekaran, M.4    Baures, P.W.5    Todd, S.C.6
  • 29
    • 3042598803 scopus 로고    scopus 로고
    • Privileged scaffolds for blocking protein-protein interactions: 1,4-disubstituted naphthalene antagonists of transcription factor complex HOX-PBX/DNA
    • T. Ji, M. Lee, S.C. Pruitt, and D.G. Hangauer Privileged scaffolds for blocking protein-protein interactions: 1,4-disubstituted naphthalene antagonists of transcription factor complex HOX-PBX/DNA Bioorg Med Chem Lett 14 2004 3875 3879
    • (2004) Bioorg Med Chem Lett , vol.14 , pp. 3875-3879
    • Ji, T.1    Lee, M.2    Pruitt, S.C.3    Hangauer, D.G.4
  • 30
    • 0038183834 scopus 로고    scopus 로고
    • Synthetic inhibitors of proline-rich ligand-mediated protein-protein interaction: Potent analogs of UCS15A
    • C. Oneyama, T. Agatsuma, Y. Kanda, H. Nakano, S.V. Sharma, S. Nakano, F. Narazaki, and K. Tatsuta Synthetic inhibitors of proline-rich ligand-mediated protein-protein interaction: potent analogs of UCS15A Chem Biol 10 2003 443 451 A less toxic, smaller synthetic molecule was discovered to inhibit proline-rich ligand-mediated interaction between the Fyn SH3 domain and Sam68.
    • (2003) Chem Biol , vol.10 , pp. 443-451
    • Oneyama, C.1    Agatsuma, T.2    Kanda, Y.3    Nakano, H.4    Sharma, S.V.5    Nakano, S.6    Narazaki, F.7    Tatsuta, K.8
  • 31
    • 0141958040 scopus 로고    scopus 로고
    • A selective irreversible inhibitor targeting a PDZ protein interaction domain
    • N. Fujii, J.J. Haresco, Novak KAP, D. Stokoe, I.D. Kuntz, and R.K. Guy A selective irreversible inhibitor targeting a PDZ protein interaction domain J Am Chem Soc 125 2003 12074 12075 Structure-based design was used to devise agents that mimic CRIPT, a ligand of the PDZ3 domain of the protein PSD-95. A designed compound was found that blocks ligand binding to the MAGI3 PDZ2 domain irreversibly.
    • (2003) J Am Chem Soc , vol.125 , pp. 12074-12075
    • Fujii, N.1    Haresco, J.J.2    Novak, K.A.P.3    Stokoe, D.4    Kuntz, I.D.5    Guy, R.K.6
  • 33
    • 1942470110 scopus 로고    scopus 로고
    • Design, synthesis and evaluation of potential inhibitors of HIV gp120-CD4 interactions
    • C. Boussard, T. Klimkait, N. Mahmood, M. Pritchard, and I.H. Gilbert Design, synthesis and evaluation of potential inhibitors of HIV gp120-CD4 interactions Bioorg Med Chem Lett 14 2004 2673 2676
    • (2004) Bioorg Med Chem Lett , vol.14 , pp. 2673-2676
    • Boussard, C.1    Klimkait, T.2    Mahmood, N.3    Pritchard, M.4    Gilbert, I.H.5
  • 34
    • 1642581072 scopus 로고    scopus 로고
    • Design, synthesis, and in vitro biological evaluation of small molecule inhibitors of estrogen receptor a coactivator binding
    • A.L. Rodriguez, A. Tamrazi, M.L. Collins, and J.A. Katzenellenbogen Design, synthesis, and in vitro biological evaluation of small molecule inhibitors of estrogen receptor a coactivator binding J Med Chem 47 2004 600 611
    • (2004) J Med Chem , vol.47 , pp. 600-611
    • Rodriguez, A.L.1    Tamrazi, A.2    Collins, M.L.3    Katzenellenbogen, J.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.