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Volumn 5, Issue , 2004, Pages

Coronavirus 3CLpro proteinase cleavage sites: Possible relevance to SARS virus pathology

Author keywords

[No Author keywords available]

Indexed keywords

CLEAVAGE SITES; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATORS; HIGH SPECIFICITY; POSSIBLE FUTURES; PREDICTION METHODS; PROTEINASE INHIBITORS; PROTEOLYTIC CLEAVAGE; SEVERE ACUTE RESPIRATORY SYNDROME;

EID: 13244289882     PISSN: 14712105     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2105-5-72     Document Type: Article
Times cited : (88)

References (38)
  • 4
    • 0026072461 scopus 로고
    • Identification of polypeptides encoded in open reading frame 1b of the putative polymerase gene of the murine coronavirus mouse hepatitis virus A59
    • Denison MR, Zoltick PW, Leibowitz JL, Pachuk CJ, Weiss SR: Identification of polypeptides encoded in open reading frame 1b of the putative polymerase gene of the murine coronavirus mouse hepatitis virus A59. J Virol 1991, 65:3076-3082.
    • (1991) J. Virol. , vol.65 , pp. 3076-3082
    • Denison, M.R.1    Zoltick, P.W.2    Leibowitz, J.L.3    Pachuk, C.J.4    Weiss, S.R.5
  • 5
    • 0029017145 scopus 로고
    • Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity
    • Ziebuhr J, Herold J, Siddell SG: Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity. J Virol 1995, 69:4331-4338.
    • (1995) J. Virol. , vol.69 , pp. 4331-4338
    • Ziebuhr, J.1    Herold, J.2    Siddell, S.G.3
  • 6
    • 0028865888 scopus 로고
    • Inhibition of coronavirus MHV-A59 replication by proteinase inhibitors
    • Denison MR, Kim JC, Ross T: Inhibition of coronavirus MHV-A59 replication by proteinase inhibitors. Adv Exp Med Biol 1995, 380:391-397.
    • (1995) Adv. Exp. Med. Biol. , vol.380 , pp. 391-397
    • Denison, M.R.1    Kim, J.C.2    Ross, T.3
  • 7
    • 0038120984 scopus 로고    scopus 로고
    • Coronavirus main proteinase (3CLpro) structure: Basis for design of anti-SARS drugs
    • Anand K, Ziebuhr J, Wadhwani P, Mesters JR, Hilgenfeld R: 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    Mesters, J.R.4    Hilgenfeld, R.5
  • 8
    • 0038103690 scopus 로고    scopus 로고
    • Virology. The SARS coronavirus: A postgenomic era
    • Holmes KV, Enjuanes L: Virology. The SARS coronavirus: a postgenomic era. Science 2003, 300:1377-1378.
    • (2003) Science , vol.300 , pp. 1377-1378
    • Holmes, K.V.1    Enjuanes, L.2
  • 9
    • 0024467328 scopus 로고
    • Degradation of cellular proteins during poliovirus infection: Studies by two-dimensional gel electrophoresis
    • Urzainqui A, Carrasco L: Degradation of cellular proteins during poliovirus infection: studies by two-dimensional gel electrophoresis. J Virol 1989, 63:4729-4735.
    • (1989) J. Virol. , vol.63 , pp. 4729-4735
    • Urzainqui, A.1    Carrasco, L.2
  • 10
    • 0029846866 scopus 로고    scopus 로고
    • Cleavage site analysis in picornaviral polyproteins: Discovering cellular targets by neural networks
    • Blom N, Hansen J, Blaas D, Brunak S: Cleavage site analysis in picornaviral polyproteins: discovering cellular targets by neural networks. Protein Sci 1996, 5:2203-2216.
    • (1996) Protein Sci. , vol.5 , pp. 2203-2216
    • Blom, N.1    Hansen, J.2    Blaas, D.3    Brunak, S.4
  • 11
    • 0034646690 scopus 로고    scopus 로고
    • Enteroviral protease 2A directly cleaves dystrophin and is inhibited by a dystrophin-based substrate analogue
    • Badorff C, Berkely N, Mehrotra S, Talhouk JW, Rhoads RE, Knowlton KU: Enteroviral protease 2A directly cleaves dystrophin and is inhibited by a dystrophin-based substrate analogue. J Biol Chem 2000, 275:11191-11197.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11191-11197
    • Badorff, C.1    Berkely, N.2    Mehrotra, S.3    Talhouk, J.W.4    Rhoads, R.E.5    Knowlton, K.U.6
  • 13
    • 0014942114 scopus 로고
    • Mapping the active site of papain with the aid of peptide substrates and inhibitors
    • Berger A, Schechter I: Mapping the active site of papain with the aid of peptide substrates and inhibitors. Philos Trans R Soc Lond B Biol Sci 1970, 257:249-264.
    • (1970) Philos. Trans. R Soc. Lond. B Biol. Sci. , vol.257 , pp. 249-264
    • Berger, A.1    Schechter, I.2
  • 14
    • 0034072633 scopus 로고    scopus 로고
    • Virus-encoded proteinases and proteolytic processing in the Nidovirales
    • Ziebuhr J, Snijder EJ, Gorbalenya AE: Virus-encoded proteinases and proteolytic processing in the Nidovirales. J Gen Virol 2000, 81:853-879.
    • (2000) J. Gen. Virol. , vol.81 , pp. 853-879
    • Ziebuhr, J.1    Snijder, E.J.2    Gorbalenya, A.E.3
  • 15
    • 0036187709 scopus 로고    scopus 로고
    • Conservation of substrate specificities among coronavirus main proteases
    • Hegyi A, Ziebuhr J: Conservation of substrate specificities among coronavirus main proteases. J Gen Virol 2002, 83:595-599.
    • (2002) J. Gen. Virol. , vol.83 , pp. 595-599
    • Hegyi, A.1    Ziebuhr, J.2
  • 17
    • 0029117427 scopus 로고
    • Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. Implications for cap-dependent and cap-independent translational initiation
    • Lamphear BJ, Kirchweger R, Skern T, Rhoads RE: Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. Implications for cap-dependent and cap-independent translational initiation. J Biol Chem 1995, 270:21975-21983.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21975-21983
    • Lamphear, B.J.1    Kirchweger, R.2    Skern, T.3    Rhoads, R.E.4
  • 18
    • 0025130462 scopus 로고
    • A transcriptionally active form of TFIIIC is modified in poliovirus-infected HeLa cells
    • Clark ME, Dasgupta A: A transcriptionally active form of TFIIIC is modified in poliovirus-infected HeLa cells. Mol Cell Biol 1990, 10:5106-5113.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 5106-5113
    • Clark, M.E.1    Dasgupta, A.2
  • 19
    • 0025885346 scopus 로고
    • Poliovirus proteinase 3C converts an active form of transcription factor IIIC to an inactive form: A mechanism for inhibition of host cell polymerase III transcription by poliovirus
    • Clark ME, Hammerle T, Wimmer E, Dasgupta A: Poliovirus proteinase 3C converts an active form of transcription factor IIIC to an inactive form: a mechanism for inhibition of host cell polymerase III transcription by poliovirus. EMBO J 1991, 10:2941-2947.
    • (1991) EMBO J. , vol.10 , pp. 2941-2947
    • Clark, M.E.1    Hammerle, T.2    Wimmer, E.3    Dasgupta, A.4
  • 20
    • 0030010748 scopus 로고    scopus 로고
    • DNA binding domain and subunit interactions of transcription factor IIIC revealed by dissection with poliovirus 3C protease
    • Shen Y, Igo M, Yalamanchili P, Berk AJ, Dasgupta A: DNA binding domain and subunit interactions of transcription factor IIIC revealed by dissection with poliovirus 3C protease. Mol Cell Biol 1996, 16:4163-4171.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 4163-4171
    • Shen, Y.1    Igo, M.2    Yalamanchili, P.3    Berk, A.J.4    Dasgupta, A.5
  • 21
    • 0031016644 scopus 로고    scopus 로고
    • Inhibition of host cell transcription by poliovirus: Cleavage of transcription factor CREB by poliovirus-encoded protease 3Cpro
    • Yalamanchili P, Datta U, Dasgupta A: Inhibition of host cell transcription by poliovirus: cleavage of transcription factor CREB by poliovirus-encoded protease 3Cpro. J Virol 1997, 71: 220-1226.
    • (1997) J. Virol. , vol.71 , pp. 1220-1226
    • Yalamanchili, P.1    Datta, U.2    Dasgupta, A.3
  • 22
    • 0031458316 scopus 로고    scopus 로고
    • Cleavage of transcriptional activator Oct-1 by poliovirus encoded protease 3Cpro
    • Yalamanchili P, Weidman K, Dasgupta A: Cleavage of transcriptional activator Oct-1 by poliovirus encoded protease 3Cpro. Virology 1997, 239:176-185.
    • (1997) Virology , vol.239 , pp. 176-185
    • Yalamanchili, P.1    Weidman, K.2    Dasgupta, A.3
  • 23
    • 0023774851 scopus 로고
    • An RNA polymerase II transcription factor inactivated in poliovirus-infected cells copurifies with transcription factor TFIID
    • Kliewer S, Dasgupta A: An RNA polymerase II transcription factor inactivated in poliovirus-infected cells copurifies with transcription factor TFIID. Mol Cell Biol 1988, 8: 175-3182.
    • (1988) Mol. Cell Biol. , vol.8 , pp. 3175-3182
    • Kliewer, S.1    Dasgupta, A.2
  • 24
    • 0035695178 scopus 로고    scopus 로고
    • Poliovirus 3C protease-mediated degradation of transcriptional activator p53 requires a cellular activity
    • Weidman MK, Yalamanchili P, Ng B, Tsai W, Dasgupta A: Poliovirus 3C protease-mediated degradation of transcriptional activator p53 requires a cellular activity. Virology 2001, 291: 60-271.
    • (2001) Virology , vol.291 , pp. 260-271
    • Weidman, M.K.1    Yalamanchili, P.2    Ng, B.3    Tsai, W.4    Dasgupta, A.5
  • 25
    • 0032475885 scopus 로고    scopus 로고
    • Stimulation of p53-mediated transcriptional activation by the p53-binding proteins, 53BP1 and 53BP2
    • Iwabuchi K, Li B, Massa HF, Trask BJ, Date T, Fields S: Stimulation of p53-mediated transcriptional activation by the p53-binding proteins, 53BP1 and 53BP2. J Biol Chem 1998, 273: 6061-26068.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26061-26068
    • Iwabuchi, K.1    Li, B.2    Massa, H.F.3    Trask, B.J.4    Date, T.5    Fields, S.6
  • 26
    • 0026672767 scopus 로고
    • Poliovirus infection results in structural alteration of a microtubule-associated protein
    • Joachims M, Etchison D: Poliovirus infection results in structural alteration of a microtubule-associated protein. J Virol 1992, 66:5797-5804.
    • (1992) J. Virol. , vol.66 , pp. 5797-5804
    • Joachims, M.1    Etchison, D.2
  • 27
    • 0029126160 scopus 로고
    • Poliovirus protease 3C mediates cleavage of microtubule-associated protein 4
    • Joachims M, Harris KS, Etchison D: Poliovirus protease 3C mediates cleavage of microtubule-associated protein 4. Virology 1995, 211:451-461.
    • (1995) Virology , vol.211 , pp. 451-461
    • Joachims, M.1    Harris, K.S.2    Etchison, D.3
  • 28
    • 0037133048 scopus 로고    scopus 로고
    • Alveolar epithelial type I cells contain transport proteins and transport sodium, supporting an active role for type I cells in regulation of lung liquid homeostasis
    • Johnson MD, Widdicombe JH, Allen L, Barbry P, Dobbs LG: Alveolar epithelial type I cells contain transport proteins and transport sodium, supporting an active role for type I cells in regulation of lung liquid homeostasis. Proc Natl Acad Sci U S A 2002, 99: 966-1971.
    • (2002) Proc. Natl. Acad. Sci. U S A , vol.99 , pp. 1966-1971
    • Johnson, M.D.1    Widdicombe, J.H.2    Allen, L.3    Barbry, P.4    Dobbs, L.G.5
  • 31
    • 0142200324 scopus 로고    scopus 로고
    • Prediction of proteinase cleavage sites in polyproteins of coronaviruses and its applications in analyzing SARS-CoV genomes
    • Gao F, Ou HY, Chen LL, Zheng WX, Zhang CT: Prediction of proteinase cleavage sites in polyproteins of coronaviruses and its applications in analyzing SARS-CoV genomes. FEBS Lett 2003, 553:451-456.
    • (2003) FEBS Lett. , vol.553 , pp. 451-456
    • Gao, F.1    Ou, H.Y.2    Chen, L.L.3    Zheng, W.X.4    Zhang, C.T.5
  • 32
    • 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: 48-151.
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 148-151
    • Chou, K.C.1    Wei, D.Q.2    Zhong, W.Z.3
  • 34
    • 84856043672 scopus 로고
    • A mathematical theory of communication
    • 379-423
    • Shannon CE: A mathematical theory of communication. Bell System Tech J 1948, 27:379-423. 623-656
    • (1948) Bell System Tech. J. , vol.27 , pp. 623-656
    • Shannon, C.E.1
  • 35
    • 0025008168 scopus 로고
    • Sequence logos: A new way to display consensus sequences
    • Schneider TD, Stephens RM: Sequence logos: a new way to display consensus sequences. Nucleic Acids Res 1990, 18: 097-6100.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 36
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, von Heijne G: Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 1997, 10: -6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 37
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
    • Blom N, Gammeltoft S, Brunak S: Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 1999, 294:1351-1362.
    • (1999) J. Mol. Biol. , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 38
    • 0016772212 scopus 로고
    • Comparison of the predicted and observed secondary structure of T4 phage lysozyme
    • Matthews BW: Comparison of the predicted and observed secondary structure of T4 phage lysozyme. Biochim Biophys Acta 1975, 405:442-451.
    • (1975) Biochim. Biophys. Acta , vol.405 , pp. 442-451
    • Matthews, B.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.