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Rosemary Kiernan

Researcher at Centre national de la recherche scientifique

Publications -  22
Citations -  2641

Rosemary Kiernan is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: Transcription (biology) & PCAF. The author has an hindex of 14, co-authored 19 publications receiving 2516 citations.

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Journal ArticleDOI

Post-activation Turn-off of NF-κB-dependent Transcription Is Regulated by Acetylation of p65

TL;DR: This work shows that the p65 subunit of NF-κB is acetylated by both p300 and PCAF on lysines 122 and 123 and proposes that acetylation of p65 plays a key role in IκΒα-mediated attenuation ofNF-κΓ transcriptional activity which is an important process that restores the latent state in post-induced cells.
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HIV-1 tat transcriptional activity is regulated by acetylation.

TL;DR: It is shown that p300 and PCAF also directly acetylate Tat, suggesting that acetylation of Tat regulates two discrete and functionally critical steps in transcription, binding to an RNAP II CTD‐kinase and release of Tat from TAR RNA.
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HIV-1 Tat Assembles a Multifunctional Transcription Elongation Complex and Stably Associates with the 7SK snRNP

TL;DR: The purified HIV-1 Tat-associated factors from HeLa nuclear extract are purified and show that Tat forms two distinct and stable complexes, Tatcom1 and Tatcom2, which are important for P-TEFb function.
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Suv39H1 and HP1γ are responsible for chromatin-mediated HIV-1 transcriptional silencing and post-integration latency

TL;DR: It is shown that Suv39H1, HP1γ and histone H3Lys9 trimethylation play a major role in chromatin‐mediated repression of integrated HIV‐1 gene expression and that HIV‐ 1 reactivation could be achieved after HP 1γ RNA interference.
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A non-proteolytic role for ubiquitin in Tat-mediated transactivation of the HIV-1 promoter

TL;DR: It is shown that the proto-oncoprotein Hdm2 interacts with Tat and mediates its ubiquitination in vitro and in vivo, supporting the notion that ubiquitin has a non-proteolytic function in Tat-mediated transactivation.