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Volumn 581, Issue , 2006, Pages 37-41

Deubiquitinating activity of the SARS-CoV papain-like protease

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EID: 84934443585     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-0-387-33012-9_5     Document Type: Conference Paper
Times cited : (32)

References (7)
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    • Kim J.C., R.A. Spence, P.F. Currier, X. Lu and M.R. Denison. 1995. Coronavirus protein processing and RNA synthesis is inhibited by the cysteine proteinase inhibitor E64d. Virology 208:1-8.
    • (1995) Virology , vol.208 , pp. 1-8
    • Kim, J.C.1    Spence, R.A.2    Currier, P.F.3    Lu, X.4    Denison, M.R.5
  • 2
    • 10044268025 scopus 로고    scopus 로고
    • Identification of severe acute respiratory syndrome coronavirus replicase products and characterization of papain-like protease activity
    • Harcourt, B.H., D. Jukneliene, A. Kanjanahaluethai, J. Bechill, K.M. Severson, C.M. Smith, P.A. Rota and S.C. Baker. 2004. Identification of severe acute respiratory syndrome coronavirus replicase products and characterization of papain-like protease activity. J. Virol. 78:13600-13612.
    • (2004) J. Virol , vol.78 , pp. 13600-13612
    • Harcourt, B.H.1    Jukneliene, D.2    Kanjanahaluethai, A.3    Bechill, J.4    Severson, K.M.5    Smith, C.M.6    Rota, P.A.7    Baker, S.C.8
  • 3
    • 29744455503 scopus 로고    scopus 로고
    • The papain-like protease of Severe Acute Respiratory Syndrome (SARS) coronavirus has deubiquitinating activity
    • Barretto, N., D. Jukneliene, K. Ratia, Z. Chen, A.D. Mesecar and S.C. Baker. The papain-like protease of Severe Acute Respiratory Syndrome (SARS) coronavirus has deubiquitinating activity. J. Virol. 79: 15189-15198.
    • J. Virol , vol.79 , pp. 15189-15198
    • Barretto, N.1    Jukneliene, D.2    Ratia, K.3    Chen, Z.4    Mesecar, A.D.5    Baker, S.C.6
  • 4
    • 0033591345 scopus 로고    scopus 로고
    • 2+ binding finger connecting the two domains of a papain-like fold
    • 2+ binding finger connecting the two domains of a papain-like fold. J. Biol. Chem. 274:14918-14925.
    • (1999) J. Biol. Chem , vol.274 , pp. 14918-14925
    • Herold, J.1    Siddell, S.G.2    Gorbalenya, A.E.3
  • 5
    • 0031011721 scopus 로고    scopus 로고
    • Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution
    • Johnston, S.C., C.N. Larsen, W.J. Cook, K.D. Wilkinson, and C.P. Hill. 1997. Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution. EMBO J. 16:3787-3796.
    • (1997) EMBO J , vol.16 , pp. 3787-3796
    • Johnston, S.C.1    Larsen, C.N.2    Cook, W.J.3    Wilkinson, K.D.4    Hill, C.P.5
  • 6
    • 15244348284 scopus 로고    scopus 로고
    • Deubiquitination, a new function of the severe acute respiratory syndrome coronavirus papain-like protease?
    • Sulea T., H.A. Lindner, E.O. Purisima and R. Menard. 2005. Deubiquitination, a new function of the severe acute respiratory syndrome coronavirus papain-like protease? J. Virol. 79:4550-4551.
    • (2005) J. Virol , vol.79 , pp. 4550-4551
    • Sulea, T.1    Lindner, H.A.2    Purisima, E.O.3    Menard, R.4
  • 7
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    • Crystal structure of a UBP-family deubiquitinating enzyme in isolation and complex with ubiquitin aldehyde
    • Hu, M., P.Li, M. Li, W. Li, T. Yao, J.W. Wu, W. Gu, R.E. Cohen and Y. Shi. 2002. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and complex with ubiquitin aldehyde. Cell. 111:1041-1054.
    • (2002) Cell , vol.111 , pp. 1041-1054
    • Hu, M.1    Li, P.2    Li, M.3    Li, W.4    Yao, T.5    Wu, J.W.6    Gu, W.7    Cohen, R.E.8    Shi, Y.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.