메뉴 건너뛰기




Volumn 77, Issue 5, 2003, Pages 3319-3325

Reversible oxidative modification as a mechanism for regulating retroviral protease dimerization and activation

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE; PROTEINASE; SULFUR; VIRUS ENZYME;

EID: 0037370725     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.77.5.3319-3325.2003     Document Type: Article
Times cited : (41)

References (25)
  • 2
    • 0034163437 scopus 로고    scopus 로고
    • HIV-2 protease is inactivated after oxidation at the dimer interface and activity can be partly restored with methionine sulphoxide reductase
    • Davis, D. A., F. M. Newcomb, J. Moskovitz, P. T. Wingfield, S. J. Stahl, J. Kaufman, H. M. Fales, R. L. Levine, and R. Yarchoan. 2000. HIV-2 protease is inactivated after oxidation at the dimer interface and activity can be partly restored with methionine sulphoxide reductase. Biochem. J. 346:305-311.
    • (2000) Biochem. J. , vol.346 , pp. 305-311
    • Davis, D.A.1    Newcomb, F.M.2    Moskovitz, J.3    Wingfield, P.T.4    Stahl, S.J.5    Kaufman, J.6    Fales, H.M.7    Levine, R.L.8    Yarchoan, R.9
  • 3
    • 0030851732 scopus 로고    scopus 로고
    • Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro
    • Davis, D. A., F. M. Newcomb, D. W. Starke, D. E. Ott, J. M. Mieyal, and R. Yarchoan. 1997. Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro. J. Biol. Chem. 272:25935-25940.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25935-25940
    • Davis, D.A.1    Newcomb, F.M.2    Starke, D.W.3    Ott, D.E.4    Mieyal, J.M.5    Yarchoan, R.6
  • 4
    • 0032902555 scopus 로고    scopus 로고
    • The conserved cysteines of the human immunodeficiency type 1 protease are involved in regulation of polyprotein processing and viral maturation of immature virions
    • Davis, D. A., K. Yusa, L. A. Gillim, F. M. Newcomb, H. Mitsuya, and R. Yarchoan. 1999. The conserved cysteines of the human immunodeficiency type 1 protease are involved in regulation of polyprotein processing and viral maturation of immature virions. J. Virol. 13:1156-1164.
    • (1999) J. Virol. , vol.13 , pp. 1156-1164
    • Davis, D.A.1    Yusa, K.2    Gillim, L.A.3    Newcomb, F.M.4    Mitsuya, H.5    Yarchoan, R.6
  • 5
    • 0026787837 scopus 로고
    • Use of protein unfolding studies to determine the conformational and dimeric stabilities of HIV-1 and SIV proteases
    • Grant, S. K., I. C. Deckman, J. S. Culp, M. D. Minnich, and I. S. Brooks. 1992. Use of protein unfolding studies to determine the conformational and dimeric stabilities of HIV-1 and SIV proteases. Biochemistry 31:9491-9501.
    • (1992) Biochemistry , vol.31 , pp. 9491-9501
    • Grant, S.K.1    Deckman, I.C.2    Culp, J.S.3    Minnich, M.D.4    Brooks, I.S.5
  • 6
    • 0030055931 scopus 로고    scopus 로고
    • Structure of equine infectious anemia virus proteinase complexed with an inhibitor
    • Gustchina, A., J. Kervinen, D. J. Powell, A. Zdanov, J. Kay, and A. Wlodawer. 1996. Structure of equine infectious anemia virus proteinase complexed with an inhibitor. Protein Sci. 5:1453-1465.
    • (1996) Protein Sci. , vol.5 , pp. 1453-1465
    • Gustchina, A.1    Kervinen, J.2    Powell, D.J.3    Zdanov, A.4    Kay, J.5    Wlodawer, A.6
  • 8
    • 0033525874 scopus 로고    scopus 로고
    • Stabilization from autoproteolysis and kinetic characterization of the human T-cell leukemia virus type 1 proteinase
    • Louis, J. M., S. Oroszlan, and J. Tozser. 1999. Stabilization from autoproteolysis and kinetic characterization of the human T-cell leukemia virus type 1 proteinase. J. Biol. Chem. 274:6660-6666.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6660-6666
    • Louis, J.M.1    Oroszlan, S.2    Tozser, J.3
  • 9
    • 0028821437 scopus 로고
    • Overexpression of human immunodeficiency virus type 1 protease increases intracellular cleavage of Gag and reduces virus infectivity
    • Luukkonen, B. G., E. M. Fenyo, and S. Schwartz. 1995. Overexpression of human immunodeficiency virus type 1 protease increases intracellular cleavage of Gag and reduces virus infectivity. Virology 206:854-865.
    • (1995) Virology , vol.206 , pp. 854-865
    • Luukkonen, B.G.1    Fenyo, E.M.2    Schwartz, S.3
  • 11
    • 0035807841 scopus 로고    scopus 로고
    • Activation of the Mason-Pfizer monkey virus protease within immature capsids in vitro
    • Parker, S. D., and E. Hunter. 2001. Activation of the Mason-Pfizer monkey virus protease within immature capsids in vitro. Proc. Natl. Acad. Sci. USA 98:14631-14636.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14631-14636
    • Parker, S.D.1    Hunter, E.2
  • 12
    • 0025854741 scopus 로고
    • Processing of the precursor of NF-kappa B by the HIV-1 protease during acute infection
    • Riviere, Y., V. Blank, P. Kourilsky, and A. Israel. 1991. Processing of the precursor of NF-kappa B by the HIV-1 protease during acute infection. Nature 350:625-626.
    • (1991) Nature , vol.350 , pp. 625-626
    • Riviere, Y.1    Blank, V.2    Kourilsky, P.3    Israel, A.4
  • 14
    • 0026013758 scopus 로고
    • Non-viral cellular substrates for human immunodeficiency virus type 1 protease
    • Shoeman, R. L., C. Kesselmier, E. Mothes, B. Honer, and P. Traub. 1991. Non-viral cellular substrates for human immunodeficiency virus type 1 protease. FEBS Lett. 278:199-203.
    • (1991) FEBS Lett. , vol.278 , pp. 199-203
    • Shoeman, R.L.1    Kesselmier, C.2    Mothes, E.3    Honer, B.4    Traub, P.5
  • 17
    • 0032561137 scopus 로고    scopus 로고
    • The structural stability of the HIV-1 protease
    • Todd, M. J., N. Semo, and E. Freire. 1998. The structural stability of the HIV-1 protease. J. Mol. Biol. 283:475-488.
    • (1998) J. Mol. Biol. , vol.283 , pp. 475-488
    • Todd, M.J.1    Semo, N.2    Freire, E.3
  • 19
    • 0033780526 scopus 로고    scopus 로고
    • Comparison of the substrate specificity of the human T-cell leukemia virus and human immunodeficiency virus proteinases
    • Tozser, J., G. Zahuczky, P. Bagossi, J. M. Louis, T. D. Copeland, S. Oroszlan, R. W. Harrison, and I. T. Weber. 2000. Comparison of the substrate specificity of the human T-cell leukemia virus and human immunodeficiency virus proteinases. Eur. J. Biochem. 267:6287-6295.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6287-6295
    • Tozser, J.1    Zahuczky, G.2    Bagossi, P.3    Louis, J.M.4    Copeland, T.D.5    Oroszlan, S.6    Harrison, R.W.7    Weber, I.T.8
  • 20
    • 0024507215 scopus 로고
    • Construction of mutant and chimeric genes using the polymerase chain reaction
    • Vallette, F., E. Mege, A. Reiss, and M. Adesnik. 1989. Construction of mutant and chimeric genes using the polymerase chain reaction. Nucleic Acids Res. 17:723-733.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 723-733
    • Vallette, F.1    Mege, E.2    Reiss, A.3    Adesnik, M.4
  • 21
    • 0035818541 scopus 로고    scopus 로고
    • HIV-1 protease cleaves eukaryotic initiation factor 4G and inhibits cap-dependent translation
    • Ventoso, I., R. Blanco, C. Perales, and L. Carrasco. 2001. HIV-1 protease cleaves eukaryotic initiation factor 4G and inhibits cap-dependent translation. Proc. Natl. Acad. Sci. USA 98:12966-12971.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12966-12971
    • Ventoso, I.1    Blanco, R.2    Perales, C.3    Carrasco, L.4
  • 22
    • 0029757151 scopus 로고    scopus 로고
    • Solution NMR evidence that the HIV-1 protease catalytic aspartyl groups have different ionization states in the complex formed with the asymmetric drug KNI-272
    • Erratum, 36:280, 1997
    • Wang, Y. X., D. I. Freedberg, T. Yamazaki, P. T. Wingfield, S. J. Stahl, J. D. Kaufman, Y. Kiso, and D. A. Torchia. 1996. Solution NMR evidence that the HIV-1 protease catalytic aspartyl groups have different ionization states in the complex formed with the asymmetric drug KNI-272. Biochemistry 35: 9945-9950. (Erratum, 36:280, 1997.)
    • (1996) Biochemistry , vol.35 , pp. 9945-9950
    • Wang, Y.X.1    Freedberg, D.I.2    Yamazaki, T.3    Wingfield, P.T.4    Stahl, S.J.5    Kaufman, J.D.6    Kiso, Y.7    Torchia, D.A.8
  • 23
    • 0028959773 scopus 로고
    • Circular dichroism
    • Woody, R. W. 1995. Circular dichroism. Methods Enzymol. 246:34-71.
    • (1995) Methods Enzymol. , vol.246 , pp. 34-71
    • Woody, R.W.1
  • 25
    • 0031968983 scopus 로고    scopus 로고
    • A proline-rich motif (PPPY) in the Gag polyprotein of Mason-Pfizer monkey virus plays a maturation-independent role in virion release
    • Yasuda, J., and E. Hunter. 1998. A proline-rich motif (PPPY) in the Gag polyprotein of Mason-Pfizer monkey virus plays a maturation-independent role in virion release. J. Virol. 72:4095-4103.
    • (1998) J. Virol. , vol.72 , pp. 4095-4103
    • Yasuda, J.1    Hunter, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.