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Volumn 17, Issue 5, 2007, Pages 533-546

Pharmacophores and biological activities of severe acute respiratory syndrome viral protease inhibitors

Author keywords

Cysteine protease; Fluorescence assay; High throughput screening; Rational drug design; SARS coronavirus

Indexed keywords

ANILIDE; ANTIVIRUS AGENT; AZIRIDINE DERIVATIVE; BENZOTRIAZOLE DERIVATIVE; CINANSERIN; CYSTEINE PROTEINASE; ESCIN; ETACRYNIC ACID; GLYCOPEPTIDE; HEXACHLOROPHENE; ISATIN DERIVATIVE; LOPINAVIR; LOPINAVIR PLUS RITONAVIR; MAC 13985; MAC 22272; MAC 30731; MAC 5576; MAC 8120; PHENYLMERCURIC ACETATE; PROTEINASE INHIBITOR; RESERPINE; RISTOCETIN; RUPINTRIVIR; TANNIN; TEICOPLANIN; THIOMERSAL; UNCLASSIFIED DRUG; UNINDEXED DRUG; VANCOMYCIN; ZENULLOSE; ZINC ACETATE; ZINC COMPLEX; ZINCUM GLUCONICUM;

EID: 34248344209     PISSN: 13543776     EISSN: None     Source Type: Journal    
DOI: 10.1517/13543776.17.5.533     Document Type: Review
Times cited : (9)

References (72)
  • 1
    • 0141889936 scopus 로고    scopus 로고
    • Isolation and characterizarion of viruses related to tile SARS coronavirus from animals in southern China
    • GUAN Y, ZHENG BJ, HE YQ et al.: Isolation and characterizarion of viruses related to tile SARS coronavirus from animals in southern China. Science (2003) 302:276-278.
    • (2003) Science , vol.302 , pp. 276-278
    • GUAN, Y.1    ZHENG, B.J.2    HE, Y.Q.3
  • 2
    • 0013255608 scopus 로고    scopus 로고
    • A cluster of cases of severe acute respiratory syndrome in Hong Kong
    • TSANG KW, HO PL, OOI GC et al.: A cluster of cases of severe acute respiratory syndrome in Hong Kong. N. Eng. J. Med. (2003) 348:1977-1985.
    • (2003) N. Eng. J. Med , vol.348 , pp. 1977-1985
    • TSANG, K.W.1    HO, P.L.2    OOI, G.C.3
  • 3
    • 0013165966 scopus 로고    scopus 로고
    • Identification of severe acute respiratory syndrome in Canada
    • POUTANEN SM, LOW DE, HENRY B et al.: Identification of severe acute respiratory syndrome in Canada. N. Eng. J. Med. (2003) 348:1995-2005.
    • (2003) N. Eng. J. Med , vol.348 , pp. 1995-2005
    • POUTANEN, S.M.1    LOW, D.E.2    HENRY, B.3
  • 4
    • 0038076030 scopus 로고    scopus 로고
    • A novel coronavirus associated with severe acute respiratory syndrome
    • KSIAZEK TG, ERDMAN D, GOLDSMITH CS et al.: A novel coronavirus associated with severe acute respiratory syndrome. N. Eng. J. Med. (2003) 348:1953-1966.
    • (2003) N. Eng. J. Med , vol.348 , pp. 1953-1966
    • KSIAZEK, T.G.1    ERDMAN, D.2    GOLDSMITH, C.S.3
  • 5
    • 0038523806 scopus 로고    scopus 로고
    • Identification of a novel coronavirus in patients with severe acute respiratory syndrome
    • DROSTEN C, GUNTHER S, PREISER W et al.: Identification of a novel coronavirus in patients with severe acute respiratory syndrome. J. Med. (2003) 348:1967-1976.
    • (2003) J. Med , vol.348 , pp. 1967-1976
    • DROSTEN, C.1    GUNTHER, S.2    PREISER, W.3
  • 7
    • 0038326554 scopus 로고    scopus 로고
    • HOLM ES KV: SARS-associated coronavirus. N. Eng. J. Med. (2003) 348:1948-1951.
    • HOLM ES KV: SARS-associated coronavirus. N. Eng. J. Med. (2003) 348:1948-1951.
  • 9
    • 0042198682 scopus 로고    scopus 로고
    • Newly discovered coronavirus as tile primary cause of severe acute respiratory syndrome
    • KUIKEN T, FOUCHIER RA, SCHUTTEN M et al.: Newly discovered coronavirus as tile primary cause of severe acute respiratory syndrome. Lancet (2003) 362:263-270.
    • (2003) Lancet , vol.362 , pp. 263-270
    • KUIKEN, T.1    FOUCHIER, R.A.2    SCHUTTEN, M.3
  • 10
    • 0028235532 scopus 로고
    • Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein
    • MATTHEWS DA, SMITH WW, FERRE RA et al.: Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein. Cell (1994) 77(5):761-771.
    • (1994) Cell , vol.77 , Issue.5 , pp. 761-771
    • MATTHEWS, D.A.1    SMITH, W.W.2    FERRE, R.A.3
  • 12
    • 9144268403 scopus 로고    scopus 로고
    • Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase
    • FAN K, WEI P, FENG Q et al.: Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase. J. Biol. Chem. (2004) 279:1637-1642.
    • (2004) J. Biol. Chem , vol.279 , pp. 1637-1642
    • FAN, K.1    WEI, P.2    FENG, Q.3
  • 13
    • 2442435903 scopus 로고    scopus 로고
    • Characterization of SARS main protease and inhibitor assay using a fluorogenic substrate
    • KUO CJ, CHI YH, HSU JT-A et al.: Characterization of SARS main protease and inhibitor assay using a fluorogenic substrate. Biochem. Biophys. Res. Commum. (2004) 318:862-867.
    • (2004) Biochem. Biophys. Res. Commum , vol.318 , pp. 862-867
    • KUO, C.J.1    CHI, Y.H.2    HSU, J.T.-A.3
  • 14
    • 5544272766 scopus 로고    scopus 로고
    • High-throughput screening identifies inhibitors of the SARS coronavirus main protease
    • BLANCHARD JE, ELOWE NH, HUITEMA C et al.: High-throughput screening identifies inhibitors of the SARS coronavirus main protease. Chem. Biol. (2004) 11:1445-1453.
    • (2004) Chem. Biol , vol.11 , pp. 1445-1453
    • BLANCHARD, J.E.1    ELOWE, N.H.2    HUITEMA, C.3
  • 15
    • 33646169548 scopus 로고    scopus 로고
    • Enzymatic activity of the SARS coronavirus main protease
    • GRAZIANO V, MCGRATH WJ, DEGUCCIO AM et al.: Enzymatic activity of the SARS coronavirus main protease. FEBS Lett. (2006) 580:2577-2583.
    • (2006) FEBS Lett , vol.580 , pp. 2577-2583
    • GRAZIANO, V.1    MCGRATH, W.J.2    DEGUCCIO, A.M.3
  • 16
    • 3142613358 scopus 로고    scopus 로고
    • 3C-like proteinase from SARS coronavirus catalyzes substrate hydrolysis by a general base mechanism
    • HUANG C, WEI P, FAN K et al.: 3C-like proteinase from SARS coronavirus catalyzes substrate hydrolysis by a general base mechanism. Biochemistry (2004) 43:4568-4574.
    • (2004) Biochemistry , vol.43 , pp. 4568-4574
    • HUANG, C.1    WEI, P.2    FAN, K.3
  • 17
    • 0038120984 scopus 로고    scopus 로고
    • Coronavirus main proteinase (3CLpro) structure: Basis for design of anti-SARS drugs
    • ANAND K, ZIEBUHR J, WADHWANI P et al.: 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
  • 18
    • 0036646055 scopus 로고    scopus 로고
    • Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra-helical domain
    • ANARD K, PALM GJ, MESTERS JR et al.: Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra-helical domain. EMBO J. (2002) 21:3213-3224.
    • (2002) EMBO J , vol.21 , pp. 3213-3224
    • ANARD, K.1    PALM, G.J.2    MESTERS, J.R.3
  • 19
    • 0345255626 scopus 로고    scopus 로고
    • The crystal structures of severe acute respiratory, syndrome virus main protease and its complex with an inhibitor
    • YANG H, YANG M, DING Y et al.: The crystal structures of severe acute respiratory, syndrome virus main protease and its complex with an inhibitor. Proc. Natl. Acad. Sci. USA. (2003) 100:13190-13195.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13190-13195
    • YANG, H.1    YANG, M.2    DING, Y.3
  • 20
    • 24744432305 scopus 로고    scopus 로고
    • Mechanism of the maturation process of SAP, S-CoV 3CL protease
    • HSU MF, KUO CJ, CHANG KT et al.: Mechanism of the maturation process of SAP, S-CoV 3CL protease. J. Biol. Chem. (2005) 280:31257-31266.
    • (2005) J. Biol. Chem , vol.280 , pp. 31257-31266
    • HSU, M.F.1    KUO, C.J.2    CHANG, K.T.3
  • 21
    • 2642545063 scopus 로고    scopus 로고
    • Dissection study on the SARS 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme: Defining the extra domain as a new target of highly specific protease inhibitors
    • SHI JH, WEI Z, SONG JX: Dissection study on the SARS 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme: defining the extra domain as a new target of highly specific protease inhibitors. J. Biol. Chem. (2004) 279:24765-24773.
    • (2004) J. Biol. Chem , vol.279 , pp. 24765-24773
    • SHI, J.H.1    WEI, Z.2    SONG, J.X.3
  • 22
    • 20744453676 scopus 로고    scopus 로고
    • Critical assessment of important regions in the subunit association and catalytic action of the severe acute respiratory syndrome coronavirus main protease
    • HSU WC, CHANG HC, CHOU CY et al.: Critical assessment of important regions in the subunit association and catalytic action of the severe acute respiratory syndrome coronavirus main protease. J. Biol. Chem. (2005) 280:22741-22748.
    • (2005) J. Biol. Chem , vol.280 , pp. 22741-22748
    • HSU, W.C.1    CHANG, H.C.2    CHOU, C.Y.3
  • 23
    • 33845585220 scopus 로고    scopus 로고
    • Long-range cooperative interactions modulate dimerization in SARS 3CLpro
    • BARRILA J, USMAN B, ERNESTO F: Long-range cooperative interactions modulate dimerization in SARS 3CLpro. Biochemistry (2006) 45:14908-14916.
    • (2006) Biochemistry , vol.45 , pp. 14908-14916
    • BARRILA, J.1    USMAN, B.2    ERNESTO, F.3
  • 24
    • 33845386744 scopus 로고    scopus 로고
    • SARS CoV main proteinase: The monomer-dimer equilibrium dissociation constant
    • GRAZIANO V, MCGRATH WJ, YANG L, MANGEL WF: SARS CoV main proteinase: the monomer-dimer equilibrium dissociation constant. Biochemistry (2006) 45:14632-14641.
    • (2006) Biochemistry , vol.45 , pp. 14632-14641
    • GRAZIANO, V.1    MCGRATH, W.J.2    YANG, L.3    MANGEL, W.F.4
  • 25
    • 28844479986 scopus 로고    scopus 로고
    • The N-terminal octapeptide acts as a dimerization inhibitor of SARS coronavirus 3C-like proteinase
    • WEI P, FAN K, CHEN H et al.: The N-terminal octapeptide acts as a dimerization inhibitor of SARS coronavirus 3C-like proteinase. Biochem. Biophys. Res. Commun. (2006) 339:865-872.
    • (2006) Biochem. Biophys. Res. Commun , vol.339 , pp. 865-872
    • WEI, P.1    FAN, K.2    CHEN, H.3
  • 26
    • 33646141403 scopus 로고    scopus 로고
    • Characterization and inhibition of SARS-coronavirus main protease
    • LIANG PH: Characterization and inhibition of SARS-coronavirus main protease. Curr. Top. Med. Chem. (2006) 6:361-376.
    • (2006) Curr. Top. Med. Chem , vol.6 , pp. 361-376
    • LIANG, P.H.1
  • 27
    • 3142594446 scopus 로고    scopus 로고
    • WUCY, JAN JT, MA SH et al.: Small molecules targeting severe acute respiratory syndrome human coronavirus. Proc. Natl. Acad. Sci. USA. (2004) 101:10012-10017.
    • WUCY, JAN JT, MA SH et al.: Small molecules targeting severe acute respiratory syndrome human coronavirus. Proc. Natl. Acad. Sci. USA. (2004) 101:10012-10017.
  • 28
    • 0036669203 scopus 로고    scopus 로고
    • A quick diversity-oriented amide-forming reaction to optimize P-subsite residues of HIV protease inhibitors
    • BRIKA, LIN YC, ELDER JH, WONG CH: A quick diversity-oriented amide-forming reaction to optimize P-subsite residues of HIV protease inhibitors. Chem. Biol. (2002) 9:891-896.
    • (2002) Chem. Biol , vol.9 , pp. 891-896
    • BRIKA, L.I.N.1    YC, E.L.D.E.R.2    JH, W.C.3
  • 29
    • 10744223243 scopus 로고    scopus 로고
    • Treatment of severe acute respiratory syndrome with lopinavir/ritonavir: A multicentre retrospective matched cohort study
    • CHAN KS, LAI ST, CHU CM et al.: Treatment of severe acute respiratory syndrome with lopinavir/ritonavir: a multicentre retrospective matched cohort study. Hong Kong Med. J. (2003) 9:399-406.
    • (2003) Hong Kong Med. J , vol.9 , pp. 399-406
    • CHAN, K.S.1
  • 30
    • 4644343545 scopus 로고    scopus 로고
    • Identification of novel small-molecule inhibitors of severe acute respiratory syndrome-associated coronavirus by chemical genetics
    • KAO RY, TSUI WHW, LEE TSW et al.: Identification of novel small-molecule inhibitors of severe acute respiratory syndrome-associated coronavirus by chemical genetics. Chem. Biol. (2004) 11:1293-1299.
    • (2004) Chem. Biol , vol.11 , pp. 1293-1299
    • KAO, R.Y.1    TSUI, W.H.W.2    LEE, T.S.W.3
  • 31
    • 6344270316 scopus 로고    scopus 로고
    • Characterization of SARS-CoV main protease and identification of biologically active small molecule inhibitors using a continuous fluorescence-based assay
    • KAO RY, TO AP, NG LW et al.: Characterization of SARS-CoV main protease and identification of biologically active small molecule inhibitors using a continuous fluorescence-based assay. FEBS Lett. (2004) 576:325-330.
    • (2004) FEBS Lett , vol.576 , pp. 325-330
    • KAO, R.Y.1    TO, A.P.2    NG, L.W.3
  • 32
    • 4444368730 scopus 로고    scopus 로고
    • Evaluation of metal-conjugated compounds as inhibitors of 3CL protease of SARS-CoV
    • HSU JTA, KUO CJ, HSIH HP et al.: Evaluation of metal-conjugated compounds as inhibitors of 3CL protease of SARS-CoV. FEBS Lett. (2004) 574:116-120.
    • (2004) FEBS Lett , vol.574 , pp. 116-120
    • HSU, J.T.A.1    KUO, C.J.2    HSIH, H.P.3
  • 33
    • 34248361348 scopus 로고    scopus 로고
    • ROWE RC, SHESKEY PJ, WELLER PJ: Handbook of Pharmaceutical Excipients. (Ed.). Pharmaceutical Press (2003) 4.
    • ROWE RC, SHESKEY PJ, WELLER PJ: Handbook of Pharmaceutical Excipients. (Ed.). Pharmaceutical Press (2003) 4.
  • 34
    • 20444433493 scopus 로고    scopus 로고
    • Screening of drugs by FRET analysis identifies inhibitors of SARS-CoV 3CL protease
    • LIU YC, HUANG V, CHAO TC et al.: Screening of drugs by FRET analysis identifies inhibitors of SARS-CoV 3CL protease. Biochem. Biophys. Res. Commun. (2005) 333:194-199.
    • (2005) Biochem. Biophys. Res. Commun , vol.333 , pp. 194-199
    • LIU, Y.C.1    HUANG, V.2    CHAO, T.C.3
  • 35
    • 24344464802 scopus 로고    scopus 로고
    • Inhibition of SARS-CoV 3C-like protease activity by theaflavin-3,3-digallate (TF3)
    • CHEN CN, LIN CPC, HUANG KK et al.: Inhibition of SARS-CoV 3C-like protease activity by theaflavin-3,3-digallate (TF3). ECAM (2005) 2:209-215.
    • (2005) ECAM , vol.2 , pp. 209-215
    • CHEN, C.N.1    LIN, C.P.C.2    HUANG, K.K.3
  • 36
    • 0034856072 scopus 로고    scopus 로고
    • Theaflavins in black tea and catechins in green tea are equally effective antioxidants
    • LEUNG LK, SU Y, CHEN R et al.: Theaflavins in black tea and catechins in green tea are equally effective antioxidants. J. Nutr. (2001) 131:2248-2251.
    • (2001) J. Nutr , vol.131 , pp. 2248-2251
    • LEUNG, L.K.1    SU, Y.2    CHEN, R.3
  • 37
    • 33746867596 scopus 로고    scopus 로고
    • Development of a red-shifted fluorescence-based assay for SARS-coronavirus 3CL protease: Identification of a novel class of anti-SARS agents from the tropical marine sponge Axinella corrugate
    • HAMILL P, HUDSON D, RICHARD Y et al.: Development of a red-shifted fluorescence-based assay for SARS-coronavirus 3CL protease: identification of a novel class of anti-SARS agents from the tropical marine sponge Axinella corrugate. Biol. Chem. (2006) 387:1063-1074
    • (2006) Biol. Chem , vol.387 , pp. 1063-1074
    • HAMILL, P.1    HUDSON, D.2    RICHARD, Y.3
  • 38
    • 0033535596 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 PS, PRINS TJ, ZHOU R 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. (1999) 42:1213-1224.
    • (1999) J. Med. Chem , vol.42 , pp. 1213-1224
    • DRAGOVICH, P.S.1    PRINS, T.J.2    ZHOU, R.3
  • 39
    • 0032870120 scopus 로고    scopus 로고
    • In vitro antiviral activity of AG7088, a potent inhibitor of human rhinovirus 3C protease
    • PATICK AK, BINFORD SL, BROTHERS MA et al.: In vitro antiviral activity of AG7088, a potent inhibitor of human rhinovirus 3C protease. Antimicrob. Agent, Chemother. (1999) 43:2444-2450.
    • (1999) Antimicrob. Agent, Chemother , vol.43 , pp. 2444-2450
    • PATICK, A.K.1    BINFORD, S.L.2    BROTHERS, M.A.3
  • 40
    • 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 DA, DRAGOVICH PS, WEBBER SE 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. USA (1999) 96:11000-11007.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11000-11007
    • MATTHEWS, D.A.1    DRAGOVICH, P.S.2    WEBBER, S.E.3
  • 41
    • 26444498493 scopus 로고    scopus 로고
    • Design of wide-spectrum inhibitors targeting coronavirus main proteases
    • YANG H, XIE W, XUE X et al.: Design of wide-spectrum inhibitors targeting coronavirus main proteases. PLoS Biol. (2005) 3: 1742-1752.
    • (2005) PLoS Biol , vol.3 , pp. 1742-1752
    • YANG, H.1    XIE, W.2    XUE, X.3
  • 42
    • 33746886624 scopus 로고    scopus 로고
    • Synthesis, crystal structure, structure-activity relationship, and antiviral activity of a potent SARS coronavirus 3CL protease inhibitor
    • YANG S, CHEN SJ, HSU MF et al.: Synthesis, crystal structure, structure-activity relationship, and antiviral activity of a potent SARS coronavirus 3CL protease inhibitor. J. Med. Chem. (2006) 49:4971-4980.
    • (2006) J. Med. Chem , vol.49 , pp. 4971-4980
    • YANG, S.1    CHEN, S.J.2    HSU, M.F.3
  • 43
    • 22844437876 scopus 로고    scopus 로고
    • Inhibition of the severe acute respiratory syndrome 3CL protease by peptidomimetic α,β-unsaturated esters
    • SHIE JJ, FANG IM, KUO TH et al.: Inhibition of the severe acute respiratory syndrome 3CL protease by peptidomimetic α,β-unsaturated esters. Bioorg. Med. Chem. (2005) 13:5240-5252.
    • (2005) Bioorg. Med. Chem , vol.13 , pp. 5240-5252
    • SHIE, J.J.1    FANG, I.M.2    KUO, T.H.3
  • 44
    • 21244442337 scopus 로고    scopus 로고
    • Discovery of potent anilide inhibitors against the severe acute respiratory syndrome 3CL protease
    • SHIE JJ, FANG JM, KUO CJ et al.: Discovery of potent anilide inhibitors against the severe acute respiratory syndrome 3CL protease. J. Med. Chem. (2005) 48:4469-4473.
    • (2005) J. Med. Chem , vol.48 , pp. 4469-4473
    • SHIE, J.J.1    FANG, J.M.2    KUO, C.J.3
  • 45
    • 9744247544 scopus 로고    scopus 로고
    • Synthesis and evaluation of keto-glutamine analogues as potent inhibitors of severe acute respiratory syndrome 3CLpro
    • JAIN RP, PETTERSSON HI, ZHANG J et al.: Synthesis and evaluation of keto-glutamine analogues as potent inhibitors of severe acute respiratory syndrome 3CLpro. J. Med. Chem. (2004) 47:6113-6116.
    • (2004) J. Med. Chem , vol.47 , pp. 6113-6116
    • JAIN, R.P.1    PETTERSSON, H.I.2    ZHANG, J.3
  • 46
    • 32344449198 scopus 로고    scopus 로고
    • Design and synthesis of dipeptidyl glutaminyl fluoromethyl ketones as potent severe acute respiratory syndrome coronovirus (SARS-CoV) inhibitors
    • ZHANG HZ, ZHANG H, KEMNITZER W et al.: Design and synthesis of dipeptidyl glutaminyl fluoromethyl ketones as potent severe acute respiratory syndrome coronovirus (SARS-CoV) inhibitors. J. Med. Chem. (2006) 49:1198-1201.
    • (2006) J. Med. Chem , vol.49 , pp. 1198-1201
    • ZHANG, H.Z.1    ZHANG, H.2    KEMNITZER, W.3
  • 47
    • 27444439747 scopus 로고    scopus 로고
    • Screening of electrophilic compounds yields an aziridinyl peptide as new active-site directed SARS-CoV main protease inhibitor
    • MARTINA E, STIEFL N, DEGEL B et al.: Screening of electrophilic compounds yields an aziridinyl peptide as new active-site directed SARS-CoV main protease inhibitor. Bioorg. Med. Chem. Lett. (2005) 15:5365-5369.
    • (2005) Bioorg. Med. Chem. Lett , vol.15 , pp. 5365-5369
    • MARTINA, E.1    STIEFL, N.2    DEGEL, B.3
  • 48
    • 27144538090 scopus 로고    scopus 로고
    • Crystal structures of the main peptidase from the SARS coronavirus inhibited by a substrate-like aza-peptide epoxide
    • LEE TW, CHERNEY MM, HUITEMA C et al.: Crystal structures of the main peptidase from the SARS coronavirus inhibited by a substrate-like aza-peptide epoxide. J. Mol. Biol. (2005) 353:1137-1151.
    • (2005) J. Mol. Biol , vol.353 , pp. 1137-1151
    • LEE, T.W.1    CHERNEY, M.M.2    HUITEMA, C.3
  • 49
    • 12644306888 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of nonpeptidic inhibitors of human thinovirus 3C prorease
    • WEBBER SE, TIKHE J, WORLAND ST et al.: Design, synthesis, and evaluation of nonpeptidic inhibitors of human thinovirus 3C prorease. 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
  • 50
    • 19944378080 scopus 로고    scopus 로고
    • Synthesis and evaluation of isatin derivatives as effective SARS coronavirus 3CL protease inhibitors
    • CHEN LP, WANG YC, LIN YW et al.: Synthesis and evaluation of isatin derivatives as effective SARS coronavirus 3CL protease inhibitors. Bioorg. Med. Chem. Lett. (2005) 15:3058-3062.
    • (2005) Bioorg. Med. Chem. Lett , vol.15 , pp. 3058-3062
    • CHEN, L.P.1    WANG, Y.C.2    LIN, Y.W.3
  • 51
    • 33745176602 scopus 로고    scopus 로고
    • Isatin compounds as noncovalent SARS coronavirus 3C-like protease inhibitors
    • ZHOU L, LIU Y, ZHANG W et al.: Isatin compounds as noncovalent SARS coronavirus 3C-like protease inhibitors. J. Med. Chem. (2006) 49:3440-3443.
    • (2006) J. Med. Chem , vol.49 , pp. 3440-3443
    • ZHOU, L.1    LIU, Y.2    ZHANG, W.3
  • 52
    • 7044230857 scopus 로고    scopus 로고
    • Cys-His proteases are among the wired proteins of the cell
    • LOCKWOOD TD: Cys-His proteases are among the wired proteins of the cell. Arch. Biochem. Biophys. (2004) 432:12-24.
    • (2004) Arch. Biochem. Biophys , vol.432 , pp. 12-24
    • LOCKWOOD, T.D.1
  • 53
    • 0034045399 scopus 로고    scopus 로고
    • Characterization of the zinc binding activity of the rubella virus non-structural protease
    • LIU X, LIANG J, GHAZI AM, FREY TK: Characterization of the zinc binding activity of the rubella virus non-structural protease. J. Virol. (2000) 74:5949-5956.
    • (2000) J. Virol , vol.74 , pp. 5949-5956
    • LIU, X.1    LIANG, J.2    GHAZI, A.M.3    FREY, T.K.4
  • 54
    • 0033570164 scopus 로고    scopus 로고
    • The structure of the 2A proteinase from a common cold virus: A proteinase responsible for the shut-off of host-cell protein synthesis
    • PETERSEN JF, CHERNEY MM, LIEBIG HD et al.: The structure of the 2A proteinase from a common cold virus: a proteinase responsible for the shut-off of host-cell protein synthesis. EMBO J. (1999) 18:5463-5475.
    • (1999) EMBO J , vol.18 , pp. 5463-5475
    • PETERSEN, J.F.1    CHERNEY, M.M.2    LIEBIG, H.D.3
  • 55
    • 0033950355 scopus 로고    scopus 로고
    • Treatment of Wilson's disease with zinc. XVII: Treatment during pregnancy
    • BREWER GJ, JOHNSON VD, DICK RD et al.: Treatment of Wilson's disease with zinc. XVII: treatment during pregnancy. Hepatology (2000) 31:364-370.
    • (2000) Hepatology , vol.31 , pp. 364-370
    • BREWER, G.J.1    JOHNSON, V.D.2    DICK, R.D.3
  • 56
    • 0037259386 scopus 로고    scopus 로고
    • Effect of zincum gluconicum nasal gel on the duration and symptom severity of the common cold in otherwise healthy adults
    • MOSSAD SB: Effect of zincum gluconicum nasal gel on the duration and symptom severity of the common cold in otherwise healthy adults. Q. J. Med. (2003) 96:35-43.
    • (2003) Q. J. Med , vol.96 , pp. 35-43
    • MOSSAD, S.B.1
  • 57
    • 0016336405 scopus 로고
    • Zinc ions inhibit replication of rhinoviruses
    • KORANT BD, KAUER JC, BUTTERWORTH BE: Zinc ions inhibit replication of rhinoviruses. Nature (1974) 248:588-590.
    • (1974) Nature , vol.248 , pp. 588-590
    • KORANT, B.D.1    KAUER, J.C.2    BUTTERWORTH, B.E.3
  • 58
  • 60
    • 27444440007 scopus 로고    scopus 로고
    • A new lead for nonpeptidic active-site-directed inhibitors of the severe acute respiratory syndrome coronavirus main protease discovered by a combination of screening and docking methods
    • KAEPPLER U, STIEFL N, SCHILLER M et al.: A new lead for nonpeptidic active-site-directed inhibitors of the severe acute respiratory syndrome coronavirus main protease discovered by a combination of screening and docking methods. J. Med. Chem. (2005) 3:6832-42.
    • (2005) J. Med. Chem , vol.3 , pp. 6832-6842
    • KAEPPLER, U.1    STIEFL, N.2    SCHILLER, M.3
  • 61
    • 33646079601 scopus 로고    scopus 로고
    • Stable benzotriazole esters as mechanism-based inactivators of the severe acute respiratory, syndrome 3CL protease
    • WU CY, KING KY, KUO CJ et al.: Stable benzotriazole esters as mechanism-based inactivators of the severe acute respiratory, syndrome 3CL protease. Chem. Biol. (2006) 13:261-268.
    • (2006) Chem. Biol , vol.13 , pp. 261-268
    • WU, C.Y.1    KING, K.Y.2    KUO, C.J.3
  • 62
    • 33747458480 scopus 로고    scopus 로고
    • Structure-based drug design and structural biology study of novel non-peptide inhibitors of severe acute respiratory syndrome coronavirus main protease
    • LU IL, MAHINDROO N, LIANG PH et al.: Structure-based drug design and structural biology study of novel non-peptide inhibitors of severe acute respiratory syndrome coronavirus main protease. J. Med. Chem. (2006) 49:5154-5161.
    • (2006) J. Med. Chem , vol.49 , pp. 5154-5161
    • LU, I.L.1    MAHINDROO, N.2    LIANG, P.H.3
  • 63
    • 33745133367 scopus 로고    scopus 로고
    • Discovery of a novel Family of SARS-CoV protease inhibitors by virtual screening and 3D-QSAR studies
    • TSAI KC, CHEN SY, LIANG PH et al.: Discovery of a novel Family of SARS-CoV protease inhibitors by virtual screening and 3D-QSAR studies. J. Med. Chem. (2006) 49:3485-3495.
    • (2006) J. Med. Chem , vol.49 , pp. 3485-3495
    • TSAI, K.C.1    CHEN, S.Y.2    LIANG, P.H.3
  • 64
    • 21044456863 scopus 로고    scopus 로고
    • Cinanserin is an inhibitor of the 3C-like proteinase of severe acute respiratory syndrome coronavirus mad strongly reduces virus replication in vitro
    • CHEN L, GUI C, LUO X et al.: Cinanserin is an inhibitor of the 3C-like proteinase of severe acute respiratory syndrome coronavirus mad strongly reduces virus replication in vitro. J. Virol. (2005) 79:7095-7103.
    • (2005) J. Virol , vol.79 , pp. 7095-7103
    • CHEN, L.1    GUI, C.2    LUO, X.3
  • 65
    • 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
  • 66
    • 0041848237 scopus 로고    scopus 로고
    • Binding mechanism of coronavirus main proteinase with ligands and its implication to drug design against SARS
    • CHOU KC, WEI DQ, ZHONG WZ: Binding mechanism of coronavirus main proteinase with ligands and its implication to drug design against SARS. Biochem. Biophys. Res. Commun. (2003) 308:148-151.
    • (2003) Biochem. Biophys. Res. Commun , vol.308 , pp. 148-151
    • CHOU, K.C.1    WEI, D.Q.2    ZHONG, W.Z.3
  • 67
    • 12444278968 scopus 로고    scopus 로고
    • A 3D model of SARS-CoV 3CL proteinase and its inhibitors design by virtual screening
    • XIONG B, GUI CS, XU XY et al.: A 3D model of SARS-CoV 3CL proteinase and its inhibitors design by virtual screening. Acta. Pharmacol. Sin. (2003) 24:497-501.
    • (2003) Acta. Pharmacol. Sin , vol.24 , pp. 497-501
    • XIONG, B.1    GUI, C.S.2    XU, X.Y.3
  • 68
    • 2142657824 scopus 로고    scopus 로고
    • Old drug as lead compounds for a new disease? Binding analysis of SARS coronavirus main protease with HIV, psychotic and parasite drugs
    • ZHANG XW, YAP YL: Old drug as lead compounds for a new disease? Binding analysis of SARS coronavirus main protease with HIV, psychotic and parasite drugs. Bioorgan. Med. Chem. (2004) 12:2517-2521.
    • (2004) Bioorgan. Med. Chem , vol.12 , pp. 2517-2521
    • ZHANG, X.W.1    YAP, Y.L.2
  • 69
    • 1242318794 scopus 로고    scopus 로고
    • Sabadinine: A potential non-peptide anti-severe acute respiratory, syndrome agent identified using structure-aided design
    • TONEY JH, NAVAS-MARTIN S. WEISS SR, KOELLER A et al.: Sabadinine: a potential non-peptide anti-severe acute respiratory, syndrome agent identified using structure-aided design. J. Med. Chem. (2004) 47:1079-1080.
    • (2004) J. Med. Chem , vol.47 , pp. 1079-1080
    • TONEY, J.H.1    NAVAS-MARTIN, S.2    WEISS, S.R.3    KOELLER, A.4
  • 71
    • 11844290106 scopus 로고    scopus 로고
    • Generation of predictive pharmacophore model for SARS-coronavirus main proteinase
    • ZHANG XW, YAP YL, ALTMEYER RM: Generation of predictive pharmacophore model for SARS-coronavirus main proteinase. Eur. J. Med. Chem. (2005) 40:57-62.
    • (2005) Eur. J. Med. Chem , vol.40 , pp. 57-62
    • ZHANG, X.W.1    YAP, Y.L.2    ALTMEYER, R.M.3
  • 72
    • 13244290092 scopus 로고    scopus 로고
    • Molecular modeling and chemical modification for finding peptide inhibitor against severe acute respiratory syndrome coronavirus main proteinase
    • DU Q, WANG S, WEI D, SIROIS S, CHOU KC: Molecular modeling and chemical modification for finding peptide inhibitor against severe acute respiratory syndrome coronavirus main proteinase. Anal. Biochem. (2005) 337:262-270.
    • (2005) Anal. Biochem , vol.337 , pp. 262-270
    • DU, Q.1    WANG, S.2    WEI, D.3    SIROIS, S.4    CHOU, K.C.5


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