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Volumn 25, Issue 11, 2004, Pages 1857-1864

Polyprotein cleavage mechanism of SARS CoV M pro and chemical modification of the octapeptide

Author keywords

Coronavirus main proteinase; Distorted key theory; Drug design; Inhibitor; KZ7088; Octapeptide; SARS

Indexed keywords

ALANYLVALYLLEUCYLGLUTAMYLSERYLGLYCYLPHENYLALANYLARGININE; CARBONYL DERIVATIVE; CYSTEINE; GLUTAMINE; HISTIDINE; OCTAPEPTIDE; POLYPROTEIN; PROTEINASE; SERINE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 6344236941     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2004.06.018     Document Type: Article
Times cited : (91)

References (37)
  • 1
    • 0027236748 scopus 로고
    • Kinetic studies with the nonnucleoside HIV-1 reverse transcriptase inhibitor U-88204E
    • I.W. Althaus, J.J. Chou, A.J. Gonzales, M.R. Diebel, K.C. Chou, and F.J. Kezdy Kinetic studies with the nonnucleoside HIV-1 reverse transcriptase inhibitor U-88204E Biochemistry 32 1993 6548 6554
    • (1993) Biochemistry , vol.32 , pp. 6548-6554
    • Althaus, I.W.1    Chou, J.J.2    Gonzales, A.J.3    Diebel, M.R.4    Chou, K.C.5    Kezdy, F.J.6
  • 2
    • 0027462167 scopus 로고
    • Steady-state kinetic studies with the non-nucleoside HIV-1 reverse transcriptase inhibitor U-87201E
    • I.W. Althaus, J.J. Chou, A.J. Gonzales, M.R. Diebel, K.C. Chou, and F.J. Kezdy Steady-state kinetic studies with the non-nucleoside HIV-1 reverse transcriptase inhibitor U-87201E J. Biol. Chem. 268 1993 6119 6124
    • (1993) J. Biol. Chem. , vol.268 , pp. 6119-6124
    • Althaus, I.W.1    Chou, J.J.2    Gonzales, A.J.3    Diebel, M.R.4    Chou, K.C.5    Kezdy, F.J.6
  • 3
    • 0027957602 scopus 로고
    • Steady-state kinetic studies with the polysulfonate U-9843, an HIV reverse transcriptase inhibitor
    • I.W. Althaus, J.J. Chou, A.J. Gonzales, M.R. Diebel, K.C. Chou, and F.J. Kezdy Steady-state kinetic studies with the polysulfonate U-9843, an HIV reverse transcriptase inhibitor Experientia 50 1994 23 28
    • (1994) Experientia , vol.50 , pp. 23-28
    • Althaus, I.W.1    Chou, J.J.2    Gonzales, A.J.3    Diebel, M.R.4    Chou, K.C.5    Kezdy, F.J.6
  • 7
    • 0038120984 scopus 로고    scopus 로고
    • Coronavirus main proteinase (3CLpro) structure: Basis for design of anti-SARS drugs
    • K. Anand, J. Ziebuhr, P. Wadhwani, J.R. Mesters, and R. Hilgenfeld Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs Science 300 2003 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
  • 8
    • 0027170793 scopus 로고
    • A formulation for correlating properties of peptides and its application to predicting human immunodeficiency virus protease-cleavable sites in proteins
    • J.J. Chou A formulation for correlating properties of peptides and its application to predicting human immunodeficiency virus protease-cleavable sites in proteins Biopolymers 33 1993 1405 1414
    • (1993) Biopolymers , vol.33 , pp. 1405-1414
    • Chou, J.J.1
  • 9
    • 0027325504 scopus 로고
    • Predicting cleavability of peptide sequences by HIV protease via correlation-angle approach
    • J.J. Chou Predicting cleavability of peptide sequences by HIV protease via correlation-angle approach J. Protein Chem. 12 1993 291 302
    • (1993) J. Protein Chem. , vol.12 , pp. 291-302
    • Chou, J.J.1
  • 10
    • 0033525591 scopus 로고    scopus 로고
    • Solution structure of BID, an intracellular amplifier of apoptotic signaling
    • J.J. Chou, H. Li, G.S. Salvesen, J. Yuan, and G. Wagner Solution structure of BID, an intracellular amplifier of apoptotic signaling Cell 96 1999 615 624
    • (1999) Cell , vol.96 , pp. 615-624
    • Chou, J.J.1    Li, H.2    Salvesen, G.S.3    Yuan, J.4    Wagner, G.5
  • 11
    • 0032563323 scopus 로고    scopus 로고
    • Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment
    • J.J. Chou, H. Matsuo, H. Duan, and G. Wagner Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment Cell 94 1998 171 180
    • (1998) Cell , vol.94 , pp. 171-180
    • Chou, J.J.1    Matsuo, H.2    Duan, H.3    Wagner, G.4
  • 12
    • 0030049315 scopus 로고    scopus 로고
    • Review: Prediction of HIV protease cleavage sites in proteins
    • K.C. Chou Review: prediction of HIV protease cleavage sites in proteins Anal. Biochem. 233 1996 1 14
    • (1996) Anal. Biochem. , vol.233 , pp. 1-14
    • Chou, K.C.1
  • 13
    • 0027219970 scopus 로고
    • A vectorized sequence-coupling model for predicting HIV protease cleavage sites in proteins
    • K.C. Chou A vectorized sequence-coupling model for predicting HIV protease cleavage sites in proteins J. Biol. Chem. 268 1993 16938 16948
    • (1993) J. Biol. Chem. , vol.268 , pp. 16938-16948
    • Chou, K.C.1
  • 14
    • 0036079733 scopus 로고    scopus 로고
    • Prediction of the tertiary structure of the beta-secretase zymogen
    • K.C. Chou, and W.J. Howe Prediction of the tertiary structure of the beta-secretase zymogen Biochem. Biophys. Res. Commun. 292 2002 702 708
    • (2002) Biochem. Biophys. Res. Commun. , vol.292 , pp. 702-708
    • Chou, K.C.1    Howe, W.J.2
  • 15
    • 0031449933 scopus 로고    scopus 로고
    • Prediction of the tertiary structure and substrate binding site of caspase-8
    • K.C. Chou, D. Jones, and R.L. Heinrikson Prediction of the tertiary structure and substrate binding site of caspase-8 FEBS Lett. 419 1997 49 54
    • (1997) FEBS Lett. , vol.419 , pp. 49-54
    • Chou, K.C.1    Jones, D.2    Heinrikson, R.L.3
  • 16
    • 0028071544 scopus 로고
    • Review: Steady-state inhibition kinetics of processive nucleic acid polymerases and nucleases
    • K.C. Chou, F.J. Kezdy, and F. Reusser Review: Steady-state inhibition kinetics of processive nucleic acid polymerases and nucleases Anal. Biochem. 221 1994 217 230
    • (1994) Anal. Biochem. , vol.221 , pp. 217-230
    • Chou, K.C.1    Kezdy, F.J.2    Reusser, F.3
  • 17
    • 0034737556 scopus 로고    scopus 로고
    • Prediction of the tertiary structure of a caspase-9/inhibitor complex
    • K.C. Chou, A.G. Tomasselli, and R.L. Heinrikson Prediction of the tertiary structure of a caspase-9/inhibitor complex FEBS Lett. 470 2000 249 256
    • (2000) FEBS Lett. , vol.470 , pp. 249-256
    • Chou, K.C.1    Tomasselli, A.G.2    Heinrikson, R.L.3
  • 19
    • 0033532596 scopus 로고    scopus 로고
    • A Model of the complex between cyclin-dependent kinase 5(Cdk5) and the activation domain of neuronal Cdk5 activator
    • K.C. Chou, K.D. Watenpaugh, and R.L. Heinrikson A Model of the complex between cyclin-dependent kinase 5(Cdk5) and the activation domain of neuronal Cdk5 activator Biochem. Biophys. Res. Commun. 259 1999 420 428
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 420-428
    • Chou, K.C.1    Watenpaugh, K.D.2    Heinrikson, R.L.3
  • 20
    • 0041848237 scopus 로고    scopus 로고
    • Binding mechanism of coronavirus main proteinase with ligands and its implication to drug design against SARS (erratum: Ibid.vol.310, 675)
    • K.C. Chou, D.Q. Wei, and W.Z. Zhong Binding mechanism of coronavirus main proteinase with ligands and its implication to drug design against SARS (erratum: ibid.vol.310, 675) Biochem. Biophys. Res. Commun. 308 2003 148 151
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 148-151
    • Chou, K.C.1    Wei, D.Q.2    Zhong, W.Z.3
  • 21
    • 0029157083 scopus 로고
    • Review: Prediction of protein structural classes
    • K.C. Chou, and C.T. Zhang Review: Prediction of protein structural classes Crit. Rev. Biochem. Mol. Biol. 30 1995 275 349
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 275-349
    • Chou, K.C.1    Zhang, C.T.2
  • 22
  • 27
    • 0346995214 scopus 로고    scopus 로고
    • N-terminal domain of the murine coronavirus receptor CEACAM1 is responsible for fusogenic activation and conformational changes of the spike protein
    • H.S. Miura, K. Nakagaki, and F. Taguchi N-terminal domain of the murine coronavirus receptor CEACAM1 is responsible for fusogenic activation and conformational changes of the spike protein J. Virol. 78 2004 216 223
    • (2004) J. Virol. , vol.78 , pp. 216-223
    • Miura, H.S.1    Nakagaki, K.2    Taguchi, F.3
  • 28
    • 0004313709 scopus 로고    scopus 로고
    • Montreal, Quebec, Canada: Chemical Computing Group;
    • Molecular operating environment (MOE). Montreal, Quebec, Canada: Chemical Computing Group; 2003.
    • (2003) Molecular Operating Environment (MOE)
  • 31
    • 0346732065 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome and influenza: Virus incursions from southern China
    • K.F. Shortridge Severe acute respiratory syndrome and influenza: virus incursions from southern China Am. J. Respir. Crit. Care Med. 168 2003 1416 1420
    • (2003) Am. J. Respir. Crit. Care Med. , vol.168 , pp. 1416-1420
    • Shortridge, K.F.1
  • 32
    • 2942750460 scopus 로고    scopus 로고
    • Virtual screening for SARS CoV protease based on KZ7088 pharmacophore points
    • S. Sirois, D.Q. Wei, Q. Du, and K.C. Chou Virtual screening for SARS CoV protease based on KZ7088 pharmacophore points J. Chem. Inf. Comput. Sci. 44 2004 1111 1122
    • (2004) J. Chem. Inf. Comput. Sci. , vol.44 , pp. 1111-1122
    • Sirois, S.1    Wei, D.Q.2    Du, Q.3    Chou, K.C.4
  • 33
    • 0004155427 scopus 로고
    • 3rd ed. W.H. Freeman and Company New York
    • L. Stryer Biochemistry 3rd ed. 1988 W.H. Freeman and Company New York
    • (1988) Biochemistry
    • Stryer, L.1
  • 34
    • 0345255626 scopus 로고    scopus 로고
    • The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor
    • H. Yang, M. Yang, Y. Ding, Y. Liu, Z. Lou, and Z. Zhou The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor Proc. Natl. Acad. Sci. U.S.A. 100 2003 13190 13195
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 13190-13195
    • Yang, H.1    Yang, M.2    Ding, Y.3    Liu, Y.4    Lou, Z.5    Zhou, Z.6
  • 35
    • 0028181020 scopus 로고
    • An alternate-subsite-coupled model for predicting HIV protease cleavage sites in proteins
    • C.T. Zhang, and K.C. Chou An alternate-subsite-coupled model for predicting HIV protease cleavage sites in proteins Protein Eng. 7 1993 65 73
    • (1993) Protein Eng. , vol.7 , pp. 65-73
    • Zhang, C.T.1    Chou, K.C.2
  • 36
    • 0037102948 scopus 로고    scopus 로고
    • Identification of the N-terminal functional domains of Cdk5 by molecular truncation and computer modeling
    • J. Zhang, C.H. Luan, K.C. Chou, and G.V.W. Johnson Identification of the N-terminal functional domains of Cdk5 by molecular truncation and computer modeling Proteins: Struct. Funct. Genet. 48 2002 447 453
    • (2002) Proteins: Struct. Funct. Genet. , vol.48 , pp. 447-453
    • Zhang, J.1    Luan, C.H.2    Chou, K.C.3    Johnson, G.V.W.4
  • 37
    • 0037233515 scopus 로고    scopus 로고
    • Subcellular location prediction of apoptosis proteins
    • G.P. Zhou, and K. Doctor Subcellular location prediction of apoptosis proteins Proteins: Struct. Funct. Genet. 50 2003 44 48
    • (2003) Proteins: Struct. Funct. Genet. , vol.50 , pp. 44-48
    • Zhou, G.P.1    Doctor, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.