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. - Wikidata - wikimedia - TriplyDB

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.

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.

http://www.wikidata.org/entity/Q44061963

about

CDK11 complexes promote pre-mRNA splicing Comparative genomics of cyclin-dependent kinases suggest co-evolution of the RNAP II C-terminal domain and CTD-directed CDKs HIV-1 Tat interacts with LIS1 protein Tat gets the "green" light on transcription initiation Nuclear protein phosphatase-1 regulates HIV-1 transcription Protein phosphatase-1 dephosphorylates the C-terminal domain of RNA polymerase-II Antiviral activity of CYC202 in HIV-1-infected cells SNPs in the HIV-1 TATA box and the AIDS pandemic.The identification of unique serum proteins of HIV-1 latently infected long-term non-progressor patients.A cell-intrinsic inhibitor of HIV-1 reverse transcription in CD4(+) T cells from elite controllers p53 Interacts with RNA polymerase II through its core domain and impairs Pol II processivity in vivo.Network-based prediction and analysis of HIV dependency factors ViralPhos: incorporating a recursively statistical method to predict phosphorylation sites on virus proteins.Expression of a protein phosphatase 1 inhibitor, cdNIPP1, increases CDK9 threonine 186 phosphorylation and inhibits HIV-1 transcription 1E7-03, a low MW compound targeting host protein phosphatase-1, inhibits HIV-1 transcription.Inhibition of PP2A by LIS1 increases HIV-1 gene expression.Phosphorylation of HIV-1 Tat by CDK2 in HIV-1 transcription.A novel binding pocket of cyclin-dependent kinase 2.The Establishment of a Hyperactive Structure Allows the Tumour Suppressor Protein p53 to Function through P-TEFb during Limited CDK9 Kinase Inhibition.Identifying protein phosphorylation sites with kinase substrate specificity on human viruses.Recent progress in the discovery and development of cyclin-dependent kinase inhibitors.Iron chelators ICL670 and 311 inhibit HIV-1 transcription.HIV-1 Resistant CDK2-Knockdown Macrophage-Like Cells Generated from 293T Cell-Derived Human Induced Pluripotent Stem Cells CDK2 regulates HIV-1 transcription by phosphorylation of CDK9 on serine 90.Role of cellular iron and oxygen in the regulation of HIV-1 infection.Transcriptional and post-transcriptional regulation of HIV-1 gene expression: role of cellular factors for Tat and Rev.Retroviral proteomics and interactomes: intricate balances of cell survival and viral replication.Ebola VP40 in Exosomes Can Cause Immune Cell Dysfunction.Regulation of HIV-1 transcription at 3% versus 21% oxygen concentration Regulation of CDK9 activity by phosphorylation and dephosphorylation.Analysis of the roles of HIV-derived microRNAs.Strategies to Block HIV Transcription: Focus on Small Molecule Tat Inhibitors.Protein Phosphatase-1 -targeted Small Molecules, Iron Chelators and Curcumin Analogs as HIV-1 Antivirals.A CDK2 activity signature predicts outcome in CDK2-low cancers.A novel anticancer agent ARC antagonizes HIV-1 and HCV.Nuclear targeting of protein phosphatase-1 by HIV-1 Tat protein.RNA polymerase II C-terminal heptarepeat domain Ser-7 phosphorylation is established in a mediator-dependent fashion.T-Cell Signaling in HIV-1 Infection.HIV-1 Tat phosphorylation on Ser-16 residue modulates HIV-1 transcription.Post-translational Modification-Based Regulation of HIV Replication

P2860

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P2860

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.

http://www.wikidata.org/entity/Q44061963

description

2002 nî lūn-bûn

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2002年の論文

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年學術文章

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2002年學術文章

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2002年學術文章

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name

HIV-1 Tat interaction with RNA ...... scription from HIV-1 promoter.

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HIV-1 Tat interaction with RNA polymerase II C-terminal domain

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type

label

HIV-1 Tat interaction with RNA ...... scription from HIV-1 promoter.

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HIV-1 Tat interaction with RNA polymerase II C-terminal domain

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HIV-1 Tat interaction with RNA ...... scription from HIV-1 promoter.

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HIV-1 Tat interaction with RNA polymerase II C-terminal domain

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P1433

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Journal of Biological Chemistry

P1476

HIV-1 Tat interaction with RNA ...... scription from HIV-1 promoter.

@en

P2093

Anne Pumfery

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Fatah Kashanchi

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Longwen Deng

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Sergei Nekhai

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Tatyana Ammosova

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P2860

Identification of multiple cyclin subunits of human P-TEFb

Purification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcription

CDK9 autophosphorylation regulates high-affinity binding of the human immunodeficiency virus type 1 tat-P-TEFb complex to TAR RNA

The HIV transactivator TAT binds to the CDK-activating kinase and activates the phosphorylation of the carboxy-terminal domain of RNA polymerase II

Three-dimensional structure of human cyclin H, a positive regulator of the CDK-activating kinase

Tat modifies the activity of CDK9 to phosphorylate serine 5 of the RNA polymerase II carboxyl-terminal domain during human immunodeficiency virus type 1 transcription

Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription

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

Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain

The C-terminal domain of RNA polymerase II couples mRNA processing to transcription

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33922-33929

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10.1074/JBC.M111349200

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37

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277

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11263224

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12114499

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phosphorylation