UV damage-induced RNA polymerase II stalling stimulates H2B deubiquitylation. - Wikidata - wikimedia - TriplyDB

UV damage-induced RNA polymerase II stalling stimulates H2B deubiquitylation.

UV damage-induced RNA polymerase II stalling stimulates H2B deubiquitylation.

http://www.wikidata.org/entity/Q34144605

about

Ubiquitin-specific peptidase 22 functions and its involvement in disease Anatomy of a nonhost disease resistance response of pea to Fusarium solani: PR gene elicitation via DNase, chitosan and chromatin alterations Histone ubiquitylation and its roles in transcription and DNA damage response Rescue of DNA damage-stalled RNA Pol II: histone H2B in action RNA polymerase II depletion promotes transcription of alternative mRNA species.The SAGA Deubiquitination Module Promotes DNA Repair and Class Switch Recombination through ATM and DNAPK-Mediated γH2AX Formation.Monoubiquitylation of histone H2B contributes to the bypass of DNA damage during and after DNA replication Emerging roles for histone modifications in DNA excision repair.DNA damage-induced histone H1 ubiquitylation is mediated by HUWE1 and stimulates the RNF8-RNF168 pathway.Ubiquitin Specific Peptidase 22 Regulates Histone H2B Mono-Ubiquitination and Exhibits Both Oncogenic and Tumor Suppressor Roles in Cancer.mRNA Processing Factor CstF-50 and Ubiquitin Escort Factor p97 Are BRCA1/BARD1 Cofactors Involved in Chromatin Remodeling during the DNA Damage Response.Nucleotide Excision Repair: From Neurodegeneration to Cancer.

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P2860

UV damage-induced RNA polymerase II stalling stimulates H2B deubiquitylation.

http://www.wikidata.org/entity/Q34144605

description

2014 nî lūn-bûn

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2014 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի օգոստոսին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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name

UV damage-induced RNA polymerase II stalling stimulates H2B deubiquitylation.

@ast

UV damage-induced RNA polymerase II stalling stimulates H2B deubiquitylation.

@en

UV damage-induced RNA polymerase II stalling stimulates H2B deubiquitylation.

@nl

type

label

UV damage-induced RNA polymerase II stalling stimulates H2B deubiquitylation.

@ast

UV damage-induced RNA polymerase II stalling stimulates H2B deubiquitylation.

@en

UV damage-induced RNA polymerase II stalling stimulates H2B deubiquitylation.

@nl

prefLabel

UV damage-induced RNA polymerase II stalling stimulates H2B deubiquitylation.

@ast

UV damage-induced RNA polymerase II stalling stimulates H2B deubiquitylation.

@en

UV damage-induced RNA polymerase II stalling stimulates H2B deubiquitylation.

@nl

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P356

PNAS.1403901111

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Proceedings of the National Academy of Sciences of the United States of America

P1476

UV damage-induced RNA polymerase II stalling stimulates H2B deubiquitylation.

@en

P2093

Kathleen M Dorgan

http://www.w3.org/2001/XMLSchema#string

Michael J Smerdon

http://www.w3.org/2001/XMLSchema#string

Peng Mao

http://www.w3.org/2001/XMLSchema#string

Rithy Meas

http://www.w3.org/2001/XMLSchema#string

P2860

A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing

Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II

The emerging roles of ATP-dependent chromatin remodeling enzymes in nucleotide excision repair

Recognition of DNA damage by the Rad4 nucleotide excision repair protein

Mechanism of Translesion Transcription by RNA Polymerase II and Its Role in Cellular Resistance to DNA Damage

Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8.

Histone H2B ubiquitylation is associated with elongating RNA polymerase II

The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase.

A Rad26-Def1 complex coordinates repair and RNA pol II proteolysis in response to DNA damage.

Regulation of the RSP5 ubiquitin ligase by an intrinsic ubiquitin-binding site

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12811-12816

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scholarly article

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10.1073/PNAS.1403901111

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35

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111

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2014-08-18T00:00:00Z

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25136098

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4156752

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