Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor (Q28216750)

1

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Ian R Logan

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Susan Cook

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Craig N Robson

Journal of Biological Chemistry

5

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language of work or name

English

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publication date

19 July 2002

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published in

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volume

277

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issue

29

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page(s)

25904-13

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cites work

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Gene activation by histone and factor acetyltransferases

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Transcriptional activators direct histone acetyltransferase complexes to nucleosomes

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GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors

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The SRC family of nuclear receptor coactivators

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Steroid receptor coactivator-1 is a histone acetyltransferase

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p300 and CBP: partners for life and death

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The transcriptional coactivators p300 and CBP are histone acetyltransferases

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The histone acetylase PCAF is a nuclear receptor coactivator.

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A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression

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SMRT isoforms mediate repression and anti-repression of nuclear receptor heterodimers

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Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase

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Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain

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Histone deacetylases specifically down-regulate p53-dependent gene activation

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A role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: inhibition of the myogenic program

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Acetylation of MyoD directed by PCAF is necessary for the execution of the muscle program

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p300 and p300/cAMP-response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation

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release_2du4537bijgwfhcypkbc2dkkom

21 January 2018

Identifiers

DOI

10.1074/JBC.M203423200

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Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/2du4537bijgwfhcypkbc2dkkom