Interaction of human immunodeficiency virus type 1 Tat with a unique site of TFIID inhibits negative cofactor Dr1 and stabilizes the TFIID-TFIIA complex.

We have previously reported the direct physical interaction between the human immunodeficiency virus (HIV) type I Tat protein and the basal transcription factor TBP/TFIID. Affinity chromatography demonstrated that wild-type Tat, but not a transactivation mutant of Tat, was capable of depleting TBP/T...

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Opis bibliograficzny
Wydane w:	J Virol
Główni autorzy:	Kashanchi, F, Khleif, S N, Duvall, J F, Sadaie, M R, Radonovich, M F, Cho, M, Martin, M A, Chen, S Y, Weinmann, R, Brady, J N
Format:	Artigo
Język:	Inglês
Wydane:	American Society for Microbiology (ASM) 1996
Hasła przedmiotowe:	Research Article
Dostęp online:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC190508/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8764062/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.70.8.5503-5510.1996
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Interaction of human immunodeficiency virus type 1 Tat with a unique site of TFIID inhibits negative cofactor Dr1 and stabilizes the TFIID-TFIIA complex.

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