Nuclear protein phosphatase-1 regulates HIV-1 transcription (Q28177130)

7

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Monique Beullens

3

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Ajit Kumar

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object named as

Ajit Kumar

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author name string

Tatyana Ammosova

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Marina Jerebtsova

2

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Yaroslav Voloshin

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Patricio E Ray

5

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Sergei Nekhai

Journal of Biological Chemistry

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language of work or name

English

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publication date

22 August 2003

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published in

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volume

278

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issue

34

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page(s)

32189-94

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cites work

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A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA

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Recruitment of a protein complex containing Tat and cyclin T1 to TAR governs the species specificity of HIV-1 Tat.

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Phosphorylation of the RNA polymerase II carboxyl-terminal domain by CDK9 is directly responsible for human immunodeficiency virus type 1 Tat-activated transcriptional elongation

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Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro

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NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation

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Protein phosphatase-1 dephosphorylates the C-terminal domain of RNA polymerase-II

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Signaling by protein phosphatases in the nucleus

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HIV-1 Tat-associated RNA polymerase C-terminal domain kinase, CDK2, phosphorylates CDK7 and stimulates Tat-mediated transcription

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C-terminal domain phosphatase sensitivity of RNA polymerase II in early elongation complexes on the HIV-1 and adenovirus 2 major late templates

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Regulation of carboxyl-terminal domain phosphatase by HIV-1 tat protein

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A protein phosphatase from human T cells augments tat transactivation of the human immunodeficiency virus type 1 long-terminal repeat

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HIV-1 Tat interaction with RNA polymerase II C-terminal domain (CTD) and a dynamic association with CDK2 induce CTD phosphorylation and transcription from HIV-1 promoter

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Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1.

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Adenovirus-mediated correction of the genetic defect in hepatocytes from patients with familial hypercholesterolemia

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Mapping of the RNA-binding and endoribonuclease domains of NIPP1, a nuclear targeting subunit of protein phosphatase 1

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The protein phosphatase-1 regulator NIPP1 is also a splicing factor involved in a late step of spliceosome assembly

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Phosphorylation-dependent interaction between the splicing factors SAP155 and NIPP1

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Functional interaction between nuclear inhibitor of protein phosphatase type 1 (NIPP1) and protein phosphatase type 1 (PP1) in Drosophila: consequences of over-expression of NIPP1 in flies and suppression by co-expression of PP1.

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Subunit structure and regulation of protein phosphatase-1 in rat liver nuclei

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