메뉴 건너뛰기




Volumn 270, Issue 1, 2000, Pages 173-179

The effect of mutant peptide cofactors on adenovirus protease activity and virus infection

Author keywords

Adenovirus type 2; Cysteine protease; Peptide inhibitors

Indexed keywords

CYSTEINE PROTEINASE; MUTANT PROTEIN; SYNTHETIC PEPTIDE; VIRUS ENZYME;

EID: 0034712776     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.2000.0253     Document Type: Article
Times cited : (13)

References (26)
  • 1
    • 0030691114 scopus 로고    scopus 로고
    • Viral proteases: Evolution of diverse structural motifs to optimize function
    • Babe L. M., Craik C. S. Viral proteases: Evolution of diverse structural motifs to optimize function. Cell. 91:1997;427-430.
    • (1997) Cell , vol.91 , pp. 427-430
    • Babe, L.M.1    Craik, C.S.2
  • 2
    • 0031048266 scopus 로고    scopus 로고
    • Activation of the adenovirus protease requires sequence elements from both ends of the activating peptide
    • Cabrita G., Iqbal M., Reddy H., Kemp G. Activation of the adenovirus protease requires sequence elements from both ends of the activating peptide. J. Biol. Chem. 272:1997;5635-5639.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5635-5639
    • Cabrita, G.1    Iqbal, M.2    Reddy, H.3    Kemp, G.4
  • 3
    • 0028883978 scopus 로고
    • The adenovirus protease is required for virus entry into host cells
    • Cotten M., Weber J. M. The adenovirus protease is required for virus entry into host cells. Virology. 213:1995;494-502.
    • (1995) Virology , vol.213 , pp. 494-502
    • Cotten, M.1    Weber, J.M.2
  • 4
    • 0029914251 scopus 로고    scopus 로고
    • Crystal structure of the human adenovirus proteinase with its 11 amino acid factor
    • Ding J., McGrath W. J., Sweet R. M., Mangel W. F. Crystal structure of the human adenovirus proteinase with its 11 amino acid factor. EMBO J. 15:1996;1778-1783.
    • (1996) EMBO J. , vol.15 , pp. 1778-1783
    • Ding, J.1    McGrath, W.J.2    Sweet, R.M.3    Mangel, W.F.4
  • 5
    • 0028869814 scopus 로고
    • Functional characterization of the adenovirus proteinase using fluorogenic substrates
    • Diouri M., Geoghegan K. F., Weber J. M. Functional characterization of the adenovirus proteinase using fluorogenic substrates. Protein Peptide Lett. 6:1995;363-370.
    • (1995) Protein Peptide Lett. , vol.6 , pp. 363-370
    • Diouri, M.1    Geoghegan, K.F.2    Weber, J.M.3
  • 7
    • 0029983628 scopus 로고    scopus 로고
    • The role of the adenovirus protease in virus entry into cells
    • Greber U. F., Webster P., Weber J., Helenius A. The role of the adenovirus protease in virus entry into cells. EMBO J. 15:1996;1766-1777.
    • (1996) EMBO J. , vol.15 , pp. 1766-1777
    • Greber, U.F.1    Webster, P.2    Weber, J.3    Helenius, A.4
  • 8
    • 0029775058 scopus 로고    scopus 로고
    • Activation of the protease from human adenovirus type 2 is accompanied by a conformational change which is dependent on cysteine-104
    • Jones S. J., Iqbal M., Grierson A. W., Kemp G. Activation of the protease from human adenovirus type 2 is accompanied by a conformational change which is dependent on cysteine-104. J. Gen. Virol. 77:1996;1821-1824.
    • (1996) J. Gen. Virol. , vol.77 , pp. 1821-1824
    • Jones, S.J.1    Iqbal, M.2    Grierson, A.W.3    Kemp, G.4
  • 9
    • 0029012762 scopus 로고
    • Adenovirus protease expressed in insect cells cleaves adenovirus proteins, ovalbumin and baculovirus protease in the absence of activating peptide
    • Keyvani-Amineh H., Labrecque P., Cai F., Carstens E. B., Weber J. M. Adenovirus protease expressed in insect cells cleaves adenovirus proteins, ovalbumin and baculovirus protease in the absence of activating peptide. Virus Res. 37:1995;87-97.
    • (1995) Virus Res. , vol.37 , pp. 87-97
    • Keyvani-Amineh, H.1    Labrecque, P.2    Cai, F.3    Carstens, E.B.4    Weber, J.M.5
  • 11
    • 0028279779 scopus 로고
    • Proteolytic cleavage of vaccinia virus virion proteins. Mutational analysis of the specificity determinants
    • Lee P., Hruby D. E. Proteolytic cleavage of vaccinia virus virion proteins. Mutational analysis of the specificity determinants. J. Biol. Chem. 269:1994;8616-8622.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8616-8622
    • Lee, P.1    Hruby, D.E.2
  • 12
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • Li S., Hochstrasser M. A new protease required for cell-cycle progression in yeast. Nature. 398:1999;246-251.
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.1    Hochstrasser, M.2
  • 13
    • 0024383385 scopus 로고
    • Gly-Gly-X, a novel consensus sequence for the proteolytic processing of viral and cellular proteins
    • Lopez-Otin C., Simon-Mateo C., Martinez L., Vinuela E. Gly-Gly-X, a novel consensus sequence for the proteolytic processing of viral and cellular proteins. J. Biol. Chem. 264:1989;9107-9110.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9107-9110
    • Lopez-Otin, C.1    Simon-Mateo, C.2    Martinez, L.3    Vinuela, E.4
  • 14
    • 0027390796 scopus 로고
    • Viral DNA and a viral peptide can act as cofactors of adenovirus virion proteinase activity
    • Mangel W. F., McGrath W. J., Toledo D. L., Anderson C. W. Viral DNA and a viral peptide can act as cofactors of adenovirus virion proteinase activity. Nature. 361:1993;274-275.
    • (1993) Nature , vol.361 , pp. 274-275
    • Mangel, W.F.1    McGrath, W.J.2    Toledo, D.L.3    Anderson, C.W.4
  • 15
    • 0018869427 scopus 로고
    • Quantitation of the interaction between adenovirus types 2 and 5 and microtubules inside infected cells
    • Miles B. D., Luftig R. B., Weatherbee J. A., Weihing R. R., Weber J. Quantitation of the interaction between adenovirus types 2 and 5 and microtubules inside infected cells. Virology. 105:1980;265-269.
    • (1980) Virology , vol.105 , pp. 265-269
    • Miles, B.D.1    Luftig, R.B.2    Weatherbee, J.A.3    Weihing, R.R.4    Weber, J.5
  • 16
    • 0018386119 scopus 로고
    • Uncoating of adenovirus type 2
    • Mirza M. A., Weber J. Uncoating of adenovirus type 2. J. Virol. 30:1979;462-471.
    • (1979) J. Virol. , vol.30 , pp. 462-471
    • Mirza, M.A.1    Weber, J.2
  • 17
    • 0031736007 scopus 로고    scopus 로고
    • Protease inhibitors as antiviral agents
    • Patick A. K., Potts K. E. Protease inhibitors as antiviral agents. Clin. Microbiol. Rev. 4:1998;614-627.
    • (1998) Clin. Microbiol. Rev. , vol.4 , pp. 614-627
    • Patick, A.K.1    Potts, K.E.2
  • 18
    • 0029070235 scopus 로고
    • Proline 137 is critical for adenovirus protease encapsidation and activation but not enzyme activity
    • Rancourt C., Keyvani-Amineh H., Sircar S., Labrecque P., Weber J. M. Proline 137 is critical for adenovirus protease encapsidation and activation but not enzyme activity. Virology. 209:1995;167-173.
    • (1995) Virology , vol.209 , pp. 167-173
    • Rancourt, C.1    Keyvani-Amineh, H.2    Sircar, S.3    Labrecque, P.4    Weber, J.M.5
  • 19
    • 0029121773 scopus 로고
    • Adenovirus structure by X-ray crystallography and electron microscopy
    • Stewart P. L., Burnett R. M. Adenovirus structure by X-ray crystallography and electron microscopy. Curr. Top. Microbiol. Immunol. 199/I:1995;25-38.
    • (1995) Curr. Top. Microbiol. Immunol. , vol.1991 , pp. 25-38
    • Stewart, P.L.1    Burnett, R.M.2
  • 21
    • 0020611226 scopus 로고
    • In vitro cleavage specificity of the adenovirus type 2 proteinase
    • Tremblay M., Dery C., Talbot B., Weber J. M. In vitro cleavage specificity of the adenovirus type 2 proteinase. Biochim. Biophys. Acta. 743:1983;239-245.
    • (1983) Biochim. Biophys. Acta , vol.743 , pp. 239-245
    • Tremblay, M.1    Dery, C.2    Talbot, B.3    Weber, J.M.4
  • 22
    • 0017237714 scopus 로고
    • Genetic analysis of adenovirus type 2. III. Temperature sensitivity of processing of viral proteins
    • Weber J. M. Genetic analysis of adenovirus type 2. III. Temperature sensitivity of processing of viral proteins. J. Virol. 17:1976;462-471.
    • (1976) J. Virol. , vol.17 , pp. 462-471
    • Weber, J.M.1
  • 23
    • 0029121775 scopus 로고
    • The adenovirus endopeptidase and its role in virus infection
    • W. Doerfler, & P. Bohm. Berlin: Springer-Verlag
    • Weber J. M. The adenovirus endopeptidase and its role in virus infection. Doerfler W., Bohm P. Molecular Repertoire of Adenoviruses, 1995;227-235 Springer-Verlag, Berlin.
    • (1995) Molecular Repertoire of Adenoviruses , pp. 227-235
    • Weber, J.M.1
  • 25
    • 0028672655 scopus 로고
    • Adenovirus endopeptidases
    • Weber J. M., Tihanyi K. Adenovirus endopeptidases. Methods Enzym. 244:1994;595-604.
    • (1994) Methods Enzym. , vol.244 , pp. 595-604
    • Weber, J.M.1    Tihanyi, K.2
  • 26
    • 0027509951 scopus 로고
    • The adenovirus protease is activated by a virus-coded disulphide-linked peptide
    • Webster A., Hay R. T., Kemp G. The adenovirus protease is activated by a virus-coded disulphide-linked peptide. Cell. 72:1993;97-104.
    • (1993) Cell , vol.72 , pp. 97-104
    • Webster, A.1    Hay, R.T.2    Kemp, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.