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Volumn 45, Issue 3, 2005, Pages 716-724

Human rhinovirus 3C protease: Generation of pharmacophore models for peptidic and nonpeptidic inhibitors and their application in virtual screening

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; COMPUTER SOFTWARE; DATABASE SYSTEMS; ENZYME INHIBITION; ENZYMES; SCREENING;

EID: 20444377675     PISSN: 15499596     EISSN: 1549960X     Source Type: Journal    
DOI: 10.1021/ci049638a     Document Type: Article
Times cited : (25)

References (28)
  • 1
    • 12644306888 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of nonpeptidic inhibitors of human rhinovirus 3C protease
    • Webber, S. E.; Tikhe, J.; Worland, S. T.; Fuhrman, S. A.; Hendrickson, T. F. et al. Design, Synthesis, and Evaluation of Nonpeptidic Inhibitors of Human Rhinovirus 3C Protease. J. Med Chem. 1996, 39, 5072-5082.
    • (1996) J. Med Chem. , vol.39 , pp. 5072-5082
    • Webber, S.E.1    Tikhe, J.2    Worland, S.T.3    Fuhrman, S.A.4    Hendrickson, T.F.5
  • 2
    • 0036679896 scopus 로고    scopus 로고
    • Recent advances in the synthesis, design and selection of cysteine protease inhibitors
    • Hernandez, A. A.; Roush, W. R. Recent advances in the synthesis, design and selection of cysteine protease inhibitors. Curr. Opin. Chem. Biol. 2002, 6, 459-465.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 459-465
    • Hernandez, A.A.1    Roush, W.R.2
  • 3
    • 13044300859 scopus 로고    scopus 로고
    • Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes
    • Matthews, D. A.; Dragovich, P. S.; Webber, S. E.; Fuhrman, S. A.; Patick, A. K. et al. Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes. Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 11000-11007.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 11000-11007
    • Matthews, D.A.1    Dragovich, P.S.2    Webber, S.E.3    Fuhrman, S.A.4    Patick, A.K.5
  • 5
    • 0038120984 scopus 로고    scopus 로고
    • Coronavirus main proteinase (3CLpro) structure: Basis for design of anti-SARS drugs
    • Anand, K.; Ziebuhr, J.; Wadhwani, P.; Mesters, J. R.; Hilgenfeld, R. Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs. Science 2003, 300, 1763-1767.
    • (2003) Science , vol.300 , pp. 1763-1767
    • Anand, K.1    Ziebuhr, J.2    Wadhwani, P.3    Mesters, J.R.4    Hilgenfeld, R.5
  • 6
    • 1842737055 scopus 로고    scopus 로고
    • Exploring the binding mechanism of the main proteinase in SARS-associated Coronavirus and its implication to anti-SARS drug design
    • Zhang, X. W.; Yap, Y. L. Exploring the binding mechanism of the main proteinase in SARS-associated Coronavirus and its implication to anti-SARS drug design. Bioorg. Med. Chem. 2004, 12, 2219-2223.
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 2219-2223
    • Zhang, X.W.1    Yap, Y.L.2
  • 7
    • 0242348704 scopus 로고    scopus 로고
    • Identifying inhibitors of the SARS coronavirus proteinase
    • Jenwitheesuk, E.; Samudrala, R. Identifying inhibitors of the SARS coronavirus proteinase. Bioorg. Med. Chem. Lett. 2003, 13, 3989-3992.
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 3989-3992
    • Jenwitheesuk, E.1    Samudrala, R.2
  • 8
    • 0033535579 scopus 로고    scopus 로고
    • Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 3. Structure-activity studies of ketomethylene-containing peptidomimetics
    • Dragovich, P. S.; Prins, T. J.; Zhou, R.; Fuhrman, S. A.; Patick, A. K. et al. Structure-Based Design, Synthesis, and Biological Evaluation of Irreversible Human Rhinovirus 3C Protease Inhibitors. 3. Structure-Activity Studies of Ketomethylene-Containing Peptidomimetics. J. Med. Chem. 1999, 42, 1203-1212.
    • (1999) J. Med. Chem. , vol.42 , pp. 1203-1212
    • Dragovich, P.S.1    Prins, T.J.2    Zhou, R.3    Fuhrman, S.A.4    Patick, A.K.5
  • 9
    • 0033822494 scopus 로고    scopus 로고
    • S-nitrosothiols as novel, reversible inhibitors of human rhinovirus 3C protease
    • Xian, M.; Wang, Q. M.; Chen, X.; Wang, K.; Wang, P. G. S-Nitrosothiols as Novel, Reversible Inhibitors of Human Rhinovirus 3C Protease. Bioorg. Med. Chem. Lett. 2000, 10, 2097-2100.
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 2097-2100
    • Xian, M.1    Wang, Q.M.2    Chen, X.3    Wang, K.4    Wang, P.G.5
  • 10
    • 0037061621 scopus 로고    scopus 로고
    • Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 6. Structure-activity studies of orally bioavailable, 2-pyridone-containing peptidomimetics
    • Dragovich, P. S.; Prins, T. J.; Zhou, R.; Brown, E. L.; Maldonado, F. C. et al. Structure-Based Design, Synthesis, and Biological Evaluation of Irreversible Human Rhinovirus 3C Protease Inhibitors. 6. Structure-Activity Studies of Orally Bioavailable, 2-Pyridone-Containing Peptidomimetics. J. Med. Chem. 2002, 45, 1607-1623.
    • (2002) J. Med. Chem. , vol.45 , pp. 1607-1623
    • Dragovich, P.S.1    Prins, T.J.2    Zhou, R.3    Brown, E.L.4    Maldonado, F.C.5
  • 11
    • 10744228371 scopus 로고    scopus 로고
    • Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 8. Pharmacological optimization of orally bioavailable 2-pyridone-containing peptidomimetics
    • Dragovich, P. S.; Prins, T. J.; Zhou, R.; Johnson, O. T.; Hua, Y. et al. Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 8. Pharmacological optimization of orally bioavailable 2-pyridone-containing peptidomimetics. J. Med. Chem. 2003, 46, 4572-4585.
    • (2003) J. Med. Chem. , vol.46 , pp. 4572-4585
    • Dragovich, P.S.1    Prins, T.J.2    Zhou, R.3    Johnson, O.T.4    Hua, Y.5
  • 12
    • 0037060908 scopus 로고    scopus 로고
    • Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. Part 7: Structure-activity studies of bicyclic 2-pyridone-containing peptidomimetics
    • Dragovich, P. S.; Prins, T. J.; Zhou, R.; Johnson, T. O.; Brown, E. L. et al. Structure-Based Design, Synthesis, and Biological Evaluation of Irreversible Human Rhinovirus 3C Protease Inhibitors. Part 7: Structure-Activity Studies of Bicyclic 2-Pyridone-Containing Peptidomimetics. Bioorg. Med. Chem. Lett. 2002, 12, 733-738.
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 733-738
    • Dragovich, P.S.1    Prins, T.J.2    Zhou, R.3    Johnson, T.O.4    Brown, E.L.5
  • 13
    • 0034084923 scopus 로고    scopus 로고
    • Substituted benzamide inhibitors of human rhinovirus 3C protease: Structure-based design, synthesis, and biological evaluation
    • Reich, S. H.; Johnson, T.; Wallace, M. B.; Kephart, S. E.; Fuhrman, S. A. et al. Substituted Benzamide Inhibitors of Human Rhinovirus 3C Protease: Structure-Based Design, Synthesis, and Biological Evaluation. J. Med. Chem. 2000, 43, 1670-1683.
    • (2000) J. Med. Chem. , vol.43 , pp. 1670-1683
    • Reich, S.H.1    Johnson, T.2    Wallace, M.B.3    Kephart, S.E.4    Fuhrman, S.A.5
  • 14
    • 0025868141 scopus 로고
    • Structure and stereochemistry of thysanone: A novel human rhinovirus 3C-protease inhibitor from Thysanophora penicilloides
    • Singh, S. B.; Cordingley, M., G.; Ball, R. G.; Smith, J. L. M.; Dombrowski, A. W. et al. Structure and stereochemistry of thysanone: a novel human rhinovirus 3C-protease inhibitor from Thysanophora penicilloides. Tetrahedron Lett. 1991, 32, 5279-5282.
    • (1991) Tetrahedron Lett. , vol.32 , pp. 5279-5282
    • Singh, S.B.1    Cordingley, M.G.2    Ball, R.G.3    Smith, J.L.M.4    Dombrowski, A.W.5
  • 15
    • 0027992173 scopus 로고
    • Citrinin hydrate and radicinin: Human rhinovirus 3C-protease inhibitors discovered in a target-directed microbial screen
    • Kadam, S.; Poddig, J.; Humphrey, P.; Karwowski, J.; Jackson, M. et al. Citrinin hydrate and radicinin: human rhinovirus 3C-protease inhibitors discovered in a target-directed microbial screen. J. Antibiot. 1994, 47, 836-839.
    • (1994) J. Antibiot. , vol.47 , pp. 836-839
    • Kadam, S.1    Poddig, J.2    Humphrey, P.3    Karwowski, J.4    Jackson, M.5
  • 16
    • 8944236089 scopus 로고    scopus 로고
    • Novel triterpene sulfates from Fusarium compactum using a rhinovirus 3C protease inhibitor screen
    • Brill, G. M.; Kati, W. M.; Montgomery, D.; Karwowski, J. P.; Humphrey, P. E. et al. Novel triterpene sulfates from Fusarium compactum using a rhinovirus 3C protease inhibitor screen. J. Antibiot. 1996, 49, 541-546.
    • (1996) J. Antibiot. , vol.49 , pp. 541-546
    • Brill, G.M.1    Kati, W.M.2    Montgomery, D.3    Karwowski, J.P.4    Humphrey, P.E.5
  • 18
    • 0037046546 scopus 로고    scopus 로고
    • Structure-based design of a parallel synthetic array directed toward the discovery of irreversible inhibitors of human rhinovirus 3C protease
    • Johnson, T. O.; Hua, Y.; Luu, H. T.; Brown, E. L.; Chan, F. et al. Structure-Based Design of a Parallel Synthetic Array Directed Toward the Discovery of Irreversible Inhibitors of Human Rhinovirus 3C Protease. J. Med. Chem. 2002, 45, 2016-2023.
    • (2002) J. Med. Chem. , vol.45 , pp. 2016-2023
    • Johnson, T.O.1    Hua, Y.2    Luu, H.T.3    Brown, E.L.4    Chan, F.5
  • 19
    • 0033601364 scopus 로고    scopus 로고
    • Azodicarboxamides: A new class of cysteine protease inhibitor for hepatitis a virus and human rhinovirus 3C enzymes
    • Hill, R. D.; Vederas, J. C. Azodicarboxamides: A New Class of Cysteine Protease Inhibitor for Hepatitis A Virus and Human Rhinovirus 3C Enzymes. J. Org. Chem. 1999, 64, 9538-9546.
    • (1999) J. Org. Chem. , vol.64 , pp. 9538-9546
    • Hill, R.D.1    Vederas, J.C.2
  • 20
    • 0035904857 scopus 로고    scopus 로고
    • Total synthesis, HRV 3C-protease inhibitory activity, and structure-activity relationships of 2-methoxystypandrone and its analogues
    • Singh, S. B.; Graham, P. L.; Reamer, R. A.; Cordingley, M. G. Discovery, Total Synthesis, HRV 3C-Protease Inhibitory Activity, and Structure-Activity Relationships of 2-Methoxystypandrone and Its Analogues. Bioorg. Med. Chem. Lett. 2001, 11, 3143-3146.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 3143-3146
    • Singh, S.B.1    Graham, P.L.2    Reamer, R.A.3    Discovery, C.M.G.4
  • 21
    • 3843062990 scopus 로고    scopus 로고
    • San Diego
    • Accelrys Inc., Catalyst, version 4.7, San Diego 2002. http://www.accelrys.com.
    • (2002) Catalyst, Version 4.7
  • 23
    • 14444269890 scopus 로고    scopus 로고
    • Tripeptide aldehyde inhibitors of human rhinovirus 3C protease: Design, synthesis, biological evaluation, and cocrystal structure solution of P1 glutamine isosteric replacements
    • Webber, S. E.; Okano, K.; Little, T. L.; Reich, S. H.; Xin, Y.; Fuhrman, S. A. et al. Tripeptide Aldehyde Inhibitors of Human Rhinovirus 3C Protease: Design, Synthesis, Biological Evaluation, and Cocrystal Structure Solution of P1 Glutamine Isosteric Replacements. J. Med. Chem. 1998, 41, 2786-2805.
    • (1998) J. Med. Chem. , vol.41 , pp. 2786-2805
    • Webber, S.E.1    Okano, K.2    Little, T.L.3    Reich, S.H.4    Xin, Y.5    Fuhrman, S.A.6
  • 24
    • 20444418791 scopus 로고    scopus 로고
    • Brookhaven National Laboratory: Protein Data Bank, http://www.rcsb.org/ pdb/.
  • 26
    • 0035935181 scopus 로고    scopus 로고
    • Design and synthesis of irreversible depsipeptidyl human rhinovirus 3C protease inhibitors
    • Webber, S. E.; Marakovits, J. T.; Dragovich, P. S.; Prins, T. J.; Zhou, R. et al. Design and Synthesis of Irreversible Depsipeptidyl Human Rhinovirus 3C Protease Inhibitors. Bioorg. Med. Chem. Lett. 2001, 11, 2683-2686.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 2683-2686
    • Webber, S.E.1    Marakovits, J.T.2    Dragovich, P.S.3    Prins, T.J.4    Zhou, R.5
  • 27
    • 5344249597 scopus 로고    scopus 로고
    • Tintagel
    • Maybridge Database, Tintagel, http://www.maybridge.com/.
    • Maybridge Database


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