메뉴 건너뛰기




Volumn 79, Issue 24, 2005, Pages 15199-15208

The papain-like protease from the severe acute respiratory syndrome coronavirus is a deubiquitinating enzyme

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE DERIVATIVE; AMINO ACID; COUMARIN DERIVATIVE; ENZYME INHIBITOR; HERPESVIRUS ASSOCIATED UBIQUITIN SPECIFIC PROTEASE; HYBRID PROTEIN; PAPAIN LIKE PROTEASE; POLYPROTEIN; POLYUBIQUITIN; PROTEINASE; SYNTHETIC PEPTIDE; UBIQUITIN; UBIQUITIN 7 AMINO 4 METHYLCOUMARIN; UNCLASSIFIED DRUG;

EID: 29744463886     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.24.15199-15208.2005     Document Type: Article
Times cited : (318)

References (46)
  • 1
    • 9644268864 scopus 로고    scopus 로고
    • Mechanism and function of deubiquitinating enzymes
    • Amerik, A. Y., and M. Hochstrasser. 2004, Mechanism and function of deubiquitinating enzymes. Biochim. Biophys. Acta 1695:189-207.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 189-207
    • Amerik, A.Y.1    Hochstrasser, M.2
  • 2
    • 0035808469 scopus 로고    scopus 로고
    • African swine fever virus protease. A new viral member of the SUMO-1-specific protease family
    • Andres, G., A. Alejo, C. Simon-Mateo, and M. L. Salas. 2001. African swine fever virus protease. a new viral member of the SUMO-1-specific protease family. J. Biol. Chem. 276:780-787.
    • (2001) J. Biol. Chem. , vol.276 , pp. 780-787
    • Andres, G.1    Alejo, A.2    Simon-Mateo, C.3    Salas, M.L.4
  • 3
    • 0030272645 scopus 로고    scopus 로고
    • Protein expression using ubiquitin fusion and cleavage
    • Baker, R. T. 1996. Protein expression using ubiquitin fusion and cleavage. Curr. Opin. Biotechnol. 7:541-546.
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 541-546
    • Baker, R.T.1
  • 4
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 13844266546 scopus 로고    scopus 로고
    • Purification of recombinant proteins from mammalian cell culture using a generic double-affinity chromatography scheme
    • Cass, B., P. L. Pham, A. Kamen, and Y. Durocher. 2005. Purification of recombinant proteins from mammalian cell culture using a generic double-affinity chromatography scheme. Protein Expr. Purif. 40:77-85.
    • (2005) Protein Expr. Purif. , vol.40 , pp. 77-85
    • Cass, B.1    Pham, P.L.2    Kamen, A.3    Durocher, Y.4
  • 8
    • 0033616143 scopus 로고    scopus 로고
    • Deubiquitinating enzymes: Their diversity and emerging roles
    • Chung, C. H., and S. H. Baek. 1999. Deubiquitinating enzymes: their diversity and emerging roles. Biochem. Biophys. Res. Commun. 266:633-640.
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 633-640
    • Chung, C.H.1    Baek, S.H.2
  • 10
    • 0032539582 scopus 로고    scopus 로고
    • Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes
    • Dang, L. C., F. D. Melandri, and R. L. Stein. 1998. Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes. Biochemistry 37:1868-1879.
    • (1998) Biochemistry , vol.37 , pp. 1868-1879
    • Dang, L.C.1    Melandri, F.D.2    Stein, R.L.3
  • 11
    • 21344473677 scopus 로고    scopus 로고
    • ISG15: A ubiquitin-like enigma
    • Dao, C. T., and D. E. Zhang. 2005. ISG15: a ubiquitin-like enigma. Front. Biosci. 10:2701-2722.
    • (2005) Front. Biosci. , vol.10 , pp. 2701-2722
    • Dao, C.T.1    Zhang, D.E.2
  • 12
    • 77049143386 scopus 로고
    • The determination of enzyme inhibitor constants
    • Dixon, M. 1953. The determination of enzyme inhibitor constants. Biochem. J. 1:170-171.
    • (1953) Biochem. J. , vol.1 , pp. 170-171
    • Dixon, M.1
  • 13
    • 0037082158 scopus 로고    scopus 로고
    • High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells
    • Durocher, Y., S. Perret, and A. Kamen. 2002. High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells. Nucleic Acids Res. 30:E9.
    • (2002) Nucleic Acids Res , vol.30
    • Durocher, Y.1    Perret, S.2    Kamen, A.3
  • 14
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman, M. H., and A. Ciechanover. 2002. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82:373-428.
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 16
    • 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
  • 18
    • 0033591345 scopus 로고    scopus 로고
    • A human RNA viral cysteine proteinase that depends upon a unique Zn2+-binding finger connecting the two domains of a papain-like fold
    • Herold, J., S. G. Siddell, and A. E. Gorbalenya. 1999. A human RNA viral cysteine proteinase that depends upon a unique Zn2+-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
  • 19
    • 0000783145 scopus 로고
    • Ubiquitin-aldehyde: A general inhibitor of ubiquitin-recycling processes
    • Hershko, A., and I. A. Rose. 1987. Ubiquitin-aldehyde: a general inhibitor of ubiquitin-recycling processes. Proc. Natl. Acad. Sci. USA 84:1829-1833.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1829-1833
    • Hershko, A.1    Rose, I.A.2
  • 20
    • 0037184947 scopus 로고    scopus 로고
    • Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in 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 in 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
  • 21
    • 4344641279 scopus 로고    scopus 로고
    • Advancements in the battle against severe acute respiratory syndrome
    • Hui, D. S., and G. W. Wong. 2004, Advancements in the battle against severe acute respiratory syndrome. Expert. Opin. Pharmacother. 5:1687-1693.
    • (2004) Expert. Opin. Pharmacother. , vol.5 , pp. 1687-1693
    • Hui, D.S.1    Wong, G.W.2
  • 22
    • 0033565867 scopus 로고    scopus 로고
    • Structural basis for the specificity of ubiquitin C-terminal hydrolases
    • Johnston, S. C., S. M. Riddle, R. E. Cohen, and C. P. Hill. 1999. Structural basis for the specificity of ubiquitin C-terminal hydrolases. EMBO J. 18:3877-3887.
    • (1999) EMBO J , vol.18 , pp. 3877-3887
    • Johnston, S.C.1    Riddle, S.M.2    Cohen, R.E.3    Hill, C.P.4
  • 24
    • 0023876086 scopus 로고
    • A 15-kDa interferon-induced protein is derived by COOH-terminal processing of a 17-kDa precursor
    • Knight, E. J., D. Fahey, B. Cordova, M. Hillman, R. Kutny, N. Reich, and D. Blomstrom. 1988. A 15-kDa interferon-induced protein is derived by COOH-terminal processing of a 17-kDa precursor. J. Biol. Chem. 263:4520-4522.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4520-4522
    • Knight, E.J.1    Fahey, D.2    Cordova, B.3    Hillman, M.4    Kutny, R.5    Reich, N.6    Blomstrom, D.7
  • 26
    • 20544456584 scopus 로고    scopus 로고
    • Pathogenesis of severe acute respiratory syndrome
    • Lau, Y. L., and J. M. Peiris. 2005. Pathogenesis of severe acute respiratory syndrome. Curr. Opin. Immunol. 17:404-410.
    • (2005) Curr. Opin. Immunol. , vol.17 , pp. 404-410
    • Lau, Y.L.1    Peiris, J.M.2
  • 29
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira, P. 1987. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262:10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 33
    • 11844256960 scopus 로고    scopus 로고
    • Expression and purification of histidine-tagged bacteriophage T7 DNA polymerase
    • Schlicke, M., and S. Brakmann. 2005. Expression and purification of histidine-tagged bacteriophage T7 DNA polymerase. Protein Expr. Purif. 39:247-253.
    • (2005) Protein Expr. Purif. , vol.39 , pp. 247-253
    • Schlicke, M.1    Brakmann, S.2
  • 36
    • 2442591389 scopus 로고    scopus 로고
    • Deubiquitinating enzymes: Their functions and substrate specificity
    • Soboleva, T. A., and R. T. Baker. 2004. Deubiquitinating enzymes: their functions and substrate specificity. Curr. Protein Pept. Sci. 5:191-200.
    • (2004) Curr. Protein Pept. Sci. , vol.5 , pp. 191-200
    • Soboleva, T.A.1    Baker, R.T.2
  • 37
    • 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
  • 38
    • 0344628701 scopus 로고    scopus 로고
    • Expression of murine coronavirus recombinant papain-like proteinase: Efficient cleavage is dependent on the lengths of both the substrate and the proteinase polypeptides
    • Teng, H., J. D. Pinon, and S. R. Weiss. 1999. Expression of murine coronavirus recombinant papain-like proteinase: efficient cleavage is dependent on the lengths of both the substrate and the proteinase polypeptides. J. Virol. 73:2658-2666.
    • (1999) J. Virol. , vol.73 , pp. 2658-2666
    • Teng, H.1    Pinon, J.D.2    Weiss, S.R.3
  • 40
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman, A. M. 2001. Themes and variations on ubiquitylation. Nat. Rev. Mol. Cell Biol. 2:169-178.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 41
    • 0030660073 scopus 로고    scopus 로고
    • Regulation of ubiquitin-dependent processes by deubiquitinating enzymes
    • Wilkinson, K. D. 1997. Regulation of ubiquitin-dependent processes by deubiquitinating enzymes. FASEB J. 11:1245-1256.
    • (1997) FASEB J , vol.11 , pp. 1245-1256
    • Wilkinson, K.D.1
  • 42
    • 0346456011 scopus 로고    scopus 로고
    • Summary of probable SARS cases with onset of illness from 1 November 2002 to 31 July 2003
    • Online
    • World Health Organization. 2004. Summary of probable SARS cases with onset of illness from 1 November 2002 to 31 July 2003. Communicable Disease Surveillance and Response (CSR). [Online.] http://www.who.int/csr /sars/country/table2004_04_21/en.
    • (2004) Communicable Disease Surveillance and Response (CSR)
  • 43
    • 0035253852 scopus 로고    scopus 로고
    • Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein
    • Yuan, W., and R. M. Krug. 2001. Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein. EMBO J. 20:362-371.
    • (2001) EMBO J , vol.20 , pp. 362-371
    • Yuan, W.1    Krug, R.M.2
  • 44
    • 0034072633 scopus 로고    scopus 로고
    • Virus-encoded proteinases and proteolytic processing in the Nidovirales
    • Ziebuhr, J., E. J. Snijder, and A. E. Gorbalenya. 2000. Virus-encoded proteinases and proteolytic processing in the Nidovirales. J. Gen. Virol. 81:853-879.
    • (2000) J. Gen. Virol. , vol.81 , pp. 853-879
    • Ziebuhr, J.1    Snijder, E.J.2    Gorbalenya, A.E.3
  • 45
    • 0035980126 scopus 로고    scopus 로고
    • The autocatalytic release of a putative RNA virus transcription factor from its polyprotein precursor involves two paralogous papain-like proteases that cleave the same peptide bond
    • Ziebuhr, J., V. Thiel, and A. E. Gorbalenya. 2001. The autocatalytic release of a putative RNA virus transcription factor from its polyprotein precursor involves two paralogous papain-like proteases that cleave the same peptide bond. J. Biol. Chem. 276:33220-33232.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33220-33232
    • Ziebuhr, J.1    Thiel, V.2    Gorbalenya, A.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.