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Volumn 331, Issue 4, 2005, Pages 1554-1559

Mutational and inhibitive analysis of SARS coronavirus 3C-like protease by fluorescence resonance energy transfer-based assays

Author keywords

3C like protease; FRET based proteolytic assay; SARS coronavirus

Indexed keywords

PAPAIN; PEPTIDE DERIVATIVE; PROTEINASE; SERINE PROTEINASE;

EID: 18844448391     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.04.072     Document Type: Article
Times cited : (21)

References (19)
  • 2
    • 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
  • 4
    • 0036646055 scopus 로고    scopus 로고
    • Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain
    • K. Anand, G.J. Palm, J.R. Mesters, S.G. Siddell, J. Ziebuhr, and R. Hilgenfeld Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain EMBO J. 21 2002 3213 3224
    • (2002) EMBO J. , vol.21 , pp. 3213-3224
    • Anand, K.1    Palm, G.J.2    Mesters, J.R.3    Siddell, S.G.4    Ziebuhr, J.5    Hilgenfeld, R.6
  • 5
    • 0031047974 scopus 로고    scopus 로고
    • The refined crystal structure of the 3C gene product from hepatitis a virus: Specific proteinase activity and RNA recognition
    • E.M. Bergmann, S.C. Mosimann, M.M. Chernaia, B.A. Malcolm, and M.N. James The refined crystal structure of the 3C gene product from hepatitis A virus: specific proteinase activity and RNA recognition J. Virol. 71 1997 2436 2448
    • (1997) J. Virol. , vol.71 , pp. 2436-2448
    • Bergmann, E.M.1    Mosimann, S.C.2    Chernaia, M.M.3    Malcolm, B.A.4    James, M.N.5
  • 8
    • 2642545063 scopus 로고    scopus 로고
    • Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme: Defining the extra domain as a new target for design of highly specific protease inhibitors
    • J. Shi, Z. Wei, and J. Song Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme: defining the extra domain as a new target for design of highly specific protease inhibitors J. Biol. Chem. 279 2004 24765 24773
    • (2004) J. Biol. Chem. , vol.279 , pp. 24765-24773
    • Shi, J.1    Wei, Z.2    Song, J.3
  • 9
    • 0038819069 scopus 로고    scopus 로고
    • SARS coronavirus: A new challenge for prevention and therapy
    • K.V. Holmes SARS coronavirus: a new challenge for prevention and therapy J. Clin. Invest. 111 2003 1605 1609
    • (2003) J. Clin. Invest. , vol.111 , pp. 1605-1609
    • Holmes, K.V.1
  • 12
    • 2142713046 scopus 로고    scopus 로고
    • Identification of novel inhibitors of the SARS coronavirus main protease 3CLpro
    • U. Bacha, J. Barrila, A. Velazquez-Campoy, S.A. Leavitt, and E. Freire Identification of novel inhibitors of the SARS coronavirus main protease 3CLpro Biochemistry 43 2004 4906 4912
    • (2004) Biochemistry , vol.43 , pp. 4906-4912
    • Bacha, U.1    Barrila, J.2    Velazquez-Campoy, A.3    Leavitt, S.A.4    Freire, E.5
  • 13
    • 0029056450 scopus 로고
    • An internally quenched fluorogenic substrate of prohormone convertase 1 and furin leads to a potent prohormone convertase inhibitor
    • F. Jean, A. Basak, J. DiMaio, N.G. Seidah, and C. Lazure An internally quenched fluorogenic substrate of prohormone convertase 1 and furin leads to a potent prohormone convertase inhibitor Biochem. J. 307 Pt. 3 1995 689 695
    • (1995) Biochem. J. , vol.307 , Issue.PART 3 , pp. 689-695
    • Jean, F.1    Basak, A.2    Dimaio, J.3    Seidah, N.G.4    Lazure, C.5
  • 15
    • 0033729426 scopus 로고    scopus 로고
    • Generation of deletion and point mutations with one primer in a single cloning step
    • O. Makarova, E. Kamberov, and B. Margolis Generation of deletion and point mutations with one primer in a single cloning step Biotechniques 29 2000 970 972
    • (2000) Biotechniques , vol.29 , pp. 970-972
    • Makarova, O.1    Kamberov, E.2    Margolis, B.3
  • 16
    • 3142613358 scopus 로고    scopus 로고
    • 3C-like proteinase from SARS coronavirus catalyzes substrate hydrolysis by a general base mechanism
    • C. Huang, P. Wei, K. Fan, Y. Liu, and L. Lai 3C-like proteinase from SARS coronavirus catalyzes substrate hydrolysis by a general base mechanism Biochemistry 43 2004 4568 4574
    • (2004) Biochemistry , vol.43 , pp. 4568-4574
    • Huang, C.1    Wei, P.2    Fan, K.3    Liu, Y.4    Lai, L.5
  • 18
    • 9144268403 scopus 로고    scopus 로고
    • Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase
    • K. Fan, P. Wei, Q. Feng, S. Chen, C. Huang, L. Ma, B. Lai, J. Pei, Y. Liu, J. Chen, and L. Lai Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase J. Biol. Chem. 279 2004 1637 1642
    • (2004) J. Biol. Chem. , vol.279 , pp. 1637-1642
    • Fan, K.1    Wei, P.2    Feng, Q.3    Chen, S.4    Huang, C.5    Ma, L.6    Lai, B.7    Pei, J.8    Liu, Y.9    Chen, J.10    Lai, L.11
  • 19
    • 12844272193 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus 3C-like proteinase N terminus is indispensable for proteolytic activity but not for enzyme dimerization. Biochemical and thermodynamic investigation in conjunction with molecular dynamics simulations
    • S. Chen, L. Chen, J. Tan, J. Chen, L. Du, T. Sun, J. Shen, K. Chen, H. Jiang, and X. Shen Severe acute respiratory syndrome coronavirus 3C-like proteinase N terminus is indispensable for proteolytic activity but not for enzyme dimerization. Biochemical and thermodynamic investigation in conjunction with molecular dynamics simulations J. Biol. Chem. 280 2005 164 173
    • (2005) J. Biol. Chem. , vol.280 , pp. 164-173
    • Chen, S.1    Chen, L.2    Tan, J.3    Chen, J.4    Du, L.5    Sun, T.6    Shen, J.7    Chen, K.8    Jiang, H.9    Shen, X.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.