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Christine H. Herrmann

Researcher at Baylor College of Medicine

Publications -  21
Citations -  2115

Christine H. Herrmann is an academic researcher from Baylor College of Medicine. The author has contributed to research in topics: Cyclin T1 & Transactivation. The author has an hindex of 20, co-authored 21 publications receiving 2056 citations.

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Journal ArticleDOI

The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein

TL;DR: It is shown that the cyclin domain of hCycT1 is necessary and sufficient to interact with Tat and promote cooperative binding to TAR RNA in vitro, as well as mediate Tat transactivation in vivo.
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Lentivirus Tat proteins specifically associate with a cellular protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II: candidate for a Tat cofactor.

TL;DR: It is demonstrated that TAK fulfills the genetic criteria established for a Tat cofactor, and an in vitro substrate of TAK, the carboxyl-terminal domain of the large subunit of RNA polymerase II is identified.
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TAK, an HIV Tat-associated kinase, is a member of the cyclin-dependent family of protein kinases and is induced by activation of peripheral blood lymphocytes and differentiation of promonocytic cell lines

TL;DR: In HIV-infected individuals TAK may be induced in T cells following activation and in macrophages following differentiation, thus contributing to high levels of viral transcription and the escape from latency of transcriptionally silent proviruses.
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Tat-Associated Kinase, TAK, Activity Is Regulated by Distinct Mechanisms in Peripheral Blood Lymphocytes and Promonocytic Cell Lines

TL;DR: The results suggest that cyclin T1 and TAK function may be required in differentiated monocytes and further show that TAK activity can be regulated by distinct mechanisms in different cell types.
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The human immunodeficiency virus Tat proteins specifically associate with TAK in vivo and require the carboxyl-terminal domain of RNA polymerase II for function.

TL;DR: Observations strengthen the proposal that the mechanism of action of Tat involves the recruitment or activation of TAK, resulting in activated transcription through phosphorylation of the CTD.