메뉴 건너뛰기




Volumn 22, Issue 3, 2004, Pages 209-220

Structure-based design of inhibitors of NS3 serine protease of hepatitis C virus

Author keywords

Combinatorial optimisation; Hepatitis C virus; Molecular modelling; NS3 serine protease; Peptidic inhibitors; Structure based molecular design

Indexed keywords

AMINO ACIDS; CARBOXYLIC ACIDS; MOLECULAR STRUCTURE; VIRUSES;

EID: 84962396688     PISSN: 10933263     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1093-3263(03)00161-X     Document Type: Article
Times cited : (53)

References (45)
  • 1
    • 0000361013 scopus 로고    scopus 로고
    • Hepatitis C viruses
    • B.N. Fields, D.M. Knipe, P.M. Howley (Eds.), Lippincott-Raven, Philadelphia, PA
    • M. Houghton, Hepatitis C viruses, in: B.N. Fields, D.M. Knipe, P.M. Howley (Eds.), Fields' Virology, third ed., Lippincott-Raven, Philadelphia, PA, 1996, pp. 1035-1058.
    • (1996) Fields' Virology, Third Ed. , pp. 1035-1058
    • Houghton, M.1
  • 4
    • 0035892034 scopus 로고    scopus 로고
    • Therapy for acute hepatitis C
    • Hoofnagle J.H. Therapy for acute hepatitis C. N. Engl. J. Med. 345:2001;1495-1497.
    • (2001) N. Engl. J. Med. , vol.345 , pp. 1495-1497
    • Hoofnagle, J.H.1
  • 5
    • 0027414062 scopus 로고
    • Characterization of the hepatitis C virus-encoded serine protease: Determination of proteinase-dependent polyprotein cleavage sites
    • Grakoui A., McCourt D.W., Wychowski C., Feinstone S.M., Rice C.M. Characterization of the hepatitis C virus-encoded serine protease: determination of proteinase-dependent polyprotein cleavage sites. J. Virol. 67:1993;2832-2843.
    • (1993) J. Virol. , vol.67 , pp. 2832-2843
    • Grakoui, A.1    Mccourt, D.W.2    Wychowski, C.3    Feinstone, S.M.4    Rice, C.M.5
  • 6
    • 0029962944 scopus 로고    scopus 로고
    • Conservation and variability in the structures of serine proteinases of the chymotrypsin family
    • Lesk A., Fordham W.D. Conservation and variability in the structures of serine proteinases of the chymotrypsin family. J. Mol. Biol. 258:1996;501-537.
    • (1996) J. Mol. Biol. , vol.258 , pp. 501-537
    • Lesk, A.1    Fordham, W.D.2
  • 8
    • 0030592514 scopus 로고    scopus 로고
    • The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site
    • Love R.A., Parge H.E., Wickersham J.A., Hostomsky Z., Habuka N., Moomaw E.W., Adachi T., Hostomska Z. The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site. Cell. 87:1996;331-342.
    • (1996) Cell , vol.87 , pp. 331-342
    • Love, R.A.1    Parge, H.E.2    Wickersham, J.A.3    Hostomsky, Z.4    Habuka, N.5    Moomaw, E.W.6    Adachi, T.7    Hostomska, Z.8
  • 13
    • 0030844455 scopus 로고    scopus 로고
    • Probing the substrate specificity of hepatitis C virus NS3 serine protease by using synthetic peptides
    • Zhang R., Durkin J., Windsor W.T., McNemar C., Ramanathan L., Le H.V. Probing the substrate specificity of hepatitis C virus NS3 serine protease by using synthetic peptides. J. Virol. 71:1997;6208-6213.
    • (1997) J. Virol. , vol.71 , pp. 6208-6213
    • Zhang, R.1    Durkin, J.2    Windsor, W.T.3    Mcnemar, C.4    Ramanathan, L.5    Le, H.V.6
  • 24
    • 0034679653 scopus 로고    scopus 로고
    • Solidphase synthesis of aminoboronic acids: Potent inhibitors of the hepatitis C virus NS3 protease
    • Dundson R.M., Greening J.R., Jones P.S., Jordan S., Wilson F.X. Solidphase synthesis of aminoboronic acids: potent inhibitors of the hepatitis C virus NS3 protease. Bioorg. Med. Chem. Lett. 10:2000;1577-1579.
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 1577-1579
    • Dundson, R.M.1    Greening, J.R.2    Jones, P.S.3    Jordan, S.4    Wilson, F.X.5
  • 26
    • 0030937806 scopus 로고    scopus 로고
    • A new concept for the mechanism of action of chymotrypsin: The role of the low-barrier hydrogen bond
    • Cassidy C.S., Lin J., Frey P.A. A new concept for the mechanism of action of chymotrypsin: the role of the low-barrier hydrogen bond. Biochemistry. 36:1997;4576-4584.
    • (1997) Biochemistry , vol.36 , pp. 4576-4584
    • Cassidy, C.S.1    Lin, J.2    Frey, P.A.3
  • 28
    • 0035931471 scopus 로고    scopus 로고
    • Arylalkylidene rhodamine with bulky and hydrophobic functional groups as selective HCV NS3 protease inhibitor
    • Sing W.T., Lee C.L., Yeo S.L., Lim S.P., Sim M.M. Arylalkylidene rhodamine with bulky and hydrophobic functional groups as selective HCV NS3 protease inhibitor. Bioorg. Med. Chem. Lett. 11:2001;91-94.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 91-94
    • Sing, W.T.1    Lee, C.L.2    Yeo, S.L.3    Lim, S.P.4    Sim, M.M.5
  • 30
    • 0034629363 scopus 로고    scopus 로고
    • Inhibition of the hepatitis C virus NS3/4A protease. The crystal structures of two protease-inhibitor complexes
    • (PDB entry codes 1DY8 and 1DY9)
    • Di Marco S., Rizzi M., Volpari C., Walsh M.A., Narjes F., Colarusso S., De Francesco R., Matassa V.G., Sollazzo M. Inhibition of the hepatitis C virus NS3/4A protease. The crystal structures of two protease-inhibitor complexes. J. Biol. Chem. 275:2000;7152-7157. (PDB entry codes 1DY8 and 1DY9).
    • (2000) J. Biol. Chem. , vol.275 , pp. 7152-7157
    • Di Marco, S.1    Rizzi, M.2    Volpari, C.3    Walsh, M.A.4    Narjes, F.5    Colarusso, S.6    De Francesco, R.7    Matassa, V.G.8    Sollazzo, M.9
  • 33
    • 84986527718 scopus 로고
    • Derivation of class II force fields. 1. Methodology and quantum force field for the alkyl functional group and alkane molecules
    • Maple J.R., Hwang M.-J., Stockfish T.P., Dinur U., Waldman M., Ewing C.S., Hagler A.T. Derivation of class II force fields. 1. Methodology and quantum force field for the alkyl functional group and alkane molecules. J. Comput. Chem. 15:1994;162-182.
    • (1994) J. Comput. Chem. , vol.15 , pp. 162-182
    • Maple, J.R.1    Hwang, M.-J.2    Stockfish, T.P.3    Dinur, U.4    Waldman, M.5    Ewing, C.S.6    Hagler, A.T.7
  • 34
    • 0037194141 scopus 로고    scopus 로고
    • Interactions of ligands with macromolecules: Rational design of specific inhibitors of aspartic protease of HIV-1
    • Frecer V., Miertus S. Interactions of ligands with macromolecules: rational design of specific inhibitors of aspartic protease of HIV-1. Macromol. Chem. Phys. 203:2002;1650-1657.
    • (2002) Macromol. Chem. Phys. , vol.203 , pp. 1650-1657
    • Frecer, V.1    Miertus, S.2
  • 35
    • 0033654297 scopus 로고    scopus 로고
    • Generalized Born models of macromolecular solvation effects
    • Bashford D., Case D.A. Generalized Born models of macromolecular solvation effects. Annu. Rev. Phys. Chem. 51:2000;129-152.
    • (2000) Annu. Rev. Phys. Chem. , vol.51 , pp. 129-152
    • Bashford, D.1    Case, D.A.2
  • 36
    • 11744256643 scopus 로고
    • Molecular interactions in solutions: An overview of methods based on continuous distribution of the solvent
    • Tomasi J., Persico M. Molecular interactions in solutions: an overview of methods based on continuous distribution of the solvent. Chem. Rev. 94:1994;2027-2094.
    • (1994) Chem. Rev. , vol.94 , pp. 2027-2094
    • Tomasi, J.1    Persico, M.2
  • 37
    • 84946893847 scopus 로고
    • Electrostatic interaction of a solute with a continuum. A direct utilization of ab initio molecular potentials for the prevision of solvent effects
    • Miertus S., Scrocco E., Tomasi J. Electrostatic interaction of a solute with a continuum. A direct utilization of ab initio molecular potentials for the prevision of solvent effects. Chem. Phys. 55:1981;117-129.
    • (1981) Chem. Phys. , vol.55 , pp. 117-129
    • Miertus, S.1    Scrocco, E.2    Tomasi, J.3
  • 38
    • 84990662822 scopus 로고
    • Polarizable continuum model of solvation for biopolymers
    • Frecer V., Miertus S. Polarizable continuum model of solvation for biopolymers. Int. J. Quant. Chem. 42:1992;1449-1468.
    • (1992) Int. J. Quant. Chem. , vol.42 , pp. 1449-1468
    • Frecer, V.1    Miertus, S.2
  • 39
    • 0000161809 scopus 로고
    • Molecular polarizabilities calculated with a modified dipole interaction
    • Thole B.T. Molecular polarizabilities calculated with a modified dipole interaction. Chem. Phys. 59:1981;341-350.
    • (1981) Chem. Phys. , vol.59 , pp. 341-350
    • Thole, B.T.1
  • 40
    • 84961979617 scopus 로고    scopus 로고
    • Interpretation of biological activity data of bacterial endotoxins by simple molecular models of mechanism of action
    • Frecer V., Ho B., Ding J.L. Interpretation of biological activity data of bacterial endotoxins by simple molecular models of mechanism of action. Eur. J. Biochem. 267:2000;837-852.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 837-852
    • Frecer, V.1    Ho, B.2    Ding, J.L.3
  • 41
    • 0035936581 scopus 로고    scopus 로고
    • Role of charged residues in the catalytic mechanism of hepatitis C virus NS3 protease: Electrostatic precollision guidance and transition-state stabilisation
    • Koch U., Biasol G., Brunetti M., Fattori D., Pallaoro M., Steinkühler C. Role of charged residues in the catalytic mechanism of hepatitis C virus NS3 protease: electrostatic precollision guidance and transition-state stabilisation. Biochemistry. 40:2001;631-640.
    • (2001) Biochemistry , vol.40 , pp. 631-640
    • Koch, U.1    Biasol, G.2    Brunetti, M.3    Fattori, D.4    Pallaoro, M.5    Steinkühler, C.6
  • 42
    • 0024260626 scopus 로고
    • Weakly polar interactions in proteins
    • Burley S.K., Petsko G.A. Weakly polar interactions in proteins. Adv. Protein. Chem. 39:1988;125-189.
    • (1988) Adv. Protein. Chem. , vol.39 , pp. 125-189
    • Burley, S.K.1    Petsko, G.A.2
  • 43
    • 0029758171 scopus 로고    scopus 로고
    • Protonation state dependence of hydrogen bond strengths and exchange rates in a serine protease catalytic triad: Bovine chymotrypsinogen
    • Markley J.L., Westler W. Protonation state dependence of hydrogen bond strengths and exchange rates in a serine protease catalytic triad: bovine chymotrypsinogen. Biochemistry. 35:1996;11092-11097.
    • (1996) Biochemistry , vol.35 , pp. 11092-11097
    • Markley, J.L.1    Westler, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.