Uracil DNA glycosylase specifically interacts with Vpr of both human immunodeficiency virus type 1 and simian immunodeficiency virus of sooty mangabeys, but binding does not correlate with cell cycle arrest
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作者:
Selig, L
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机构:INSERM U372, F-13276 MARSEILLE 9, FRANCE
Selig, L
Benichou, S
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机构:INSERM U372, F-13276 MARSEILLE 9, FRANCE
Benichou, S
Rogel, ME
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机构:INSERM U372, F-13276 MARSEILLE 9, FRANCE
Rogel, ME
Wu, LI
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机构:INSERM U372, F-13276 MARSEILLE 9, FRANCE
Wu, LI
Vodicka, MA
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机构:INSERM U372, F-13276 MARSEILLE 9, FRANCE
Vodicka, MA
Sire, J
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机构:INSERM U372, F-13276 MARSEILLE 9, FRANCE
Sire, J
Benarous, R
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机构:INSERM U372, F-13276 MARSEILLE 9, FRANCE
Benarous, R
Emerman, M
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机构:INSERM U372, F-13276 MARSEILLE 9, FRANCE
Emerman, M
机构:
[1] INSERM U372, F-13276 MARSEILLE 9, FRANCE
[2] FRED HUTCHINSON CANC RES CTR, SEATTLE, WA 98109 USA
The Vpr protein encoded by human immunodeficiency virus type 1 (HIV-1) is important for growth of virus in macrophages and prevents infected cells from passing into mitosis (G(2) arrest). The cellular target for these functions is not known, but Vpr of HIV-1 and the related Vpr from simian immunodeficiency virus of sooty mangabeys (STVSM) bind the DNA repair enzyme UNG, while the Vpx protein of SIVSM does not. Nonetheless, a mutational analysis of Vpr showed that binding to UNG is neither necessary nor sufficient for the effect of Vpr on the cell cycle.