Histone H2A monoubiquitination represses transcription by inhibiting RNA polymerase II transcriptional elongation (Q24642681)

Gene Ontology release 2020-05-02

7

Christopher K Glass

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author name string

Wenlai Zhou

1

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Ping Zhu

2

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Jianxun Wang

3

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Gabriel Pascual

4

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Kenneth A Ohgi

5

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Jean Lozach

6

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Michael G Rosenfeld

A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation

8

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language of work or name

English

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publication date

18 January 2008

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published in

Molecular Cell

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volume

29

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page(s)

69-80

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issue

1

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cites work

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

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Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation

7 April 2017

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7 April 2017

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7 April 2017

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7 April 2017

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7 April 2017

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7 April 2017

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7 April 2017

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7 April 2017

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7 April 2017

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7 April 2017

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27 September 2017

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27 September 2017

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27 September 2017

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The RING domain of Mdm2 mediates histone ubiquitylation and transcriptional repression.

27 September 2017

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27 September 2017

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IRF3 mediates a TLR3/TLR4-specific antiviral gene program

27 September 2017

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RING domains: master builders of molecular scaffolds?

27 September 2017

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27 September 2017

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27 September 2017

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30 May 2018

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Nucleosomes can form a polar barrier to transcript elongation by RNA polymerase II

28 November 2018

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12 December 2020

Isolation and characterization of protein A24, a "histone-like" non-histone chromosomal protein

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Structure of polyubiquitinated histone H2A

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Ring1b-mediated H2A ubiquitination associates with inactive X chromosomes and is involved in initiation of X inactivation

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10.1016/J.MOLCEL.2007.11.002

Identifiers

DOI

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1110479

1110479

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1 reference

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