HATs off: selective synthetic inhibitors of the histone acetyltransferases p300 and PCAF. (Q33908350)

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English	HATs off: selective synthetic inhibitors of the histone acetyltransferases p300 and PCAF.	scientific article

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

HATs off: selective synthetic inhibitors of the histone acetyltransferases p300 and PCAF. (English)

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Europe PubMed Central

PubMed publication ID

29 July 2017

author name string

Lau OD

1

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29 July 2017

Kundu TK

2

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29 July 2017

Soccio RE

3

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29 July 2017

Ait-Si-Ali S

4

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29 July 2017

Khalil EM

5

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PubMed publication ID

29 July 2017

Vassilev A

6

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29 July 2017

Wolffe AP

7

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PubMed publication ID

29 July 2017

Nakatani Y

8

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29 July 2017

Roeder RG

9

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29 July 2017

Cole PA

10

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29 July 2017

publication date

1 March 2000

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29 July 2017

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Europe PubMed Central

PubMed publication ID

29 July 2017

5

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PubMed publication ID

29 July 2017

3

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29 July 2017

589-595

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Europe PubMed Central

PubMed publication ID

29 July 2017

The CBP co-activator is a histone acetyltransferase

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Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily

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Differential inhibition of histone and polyamine acetylases by multisubstrate analogues

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Conjunction dysfunction: CBP/p300 in human disease.

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

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Acetylation of general transcription factors by histone acetyltransferases

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A Potent Inhibitor of the Melatonin Rhythm Enzyme

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Mechanism-based inhibition of the melatonin rhythm enzyme: pharmacologic exploitation of active site functional plasticity

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Transcription factor-specific requirements for coactivators and their acetyltransferase functions

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p300 and estrogen receptor cooperatively activate transcription via differential enhancement of initiation and reinitiation

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Human TFIIIC relieves chromatin-mediated repression of RNA polymerase III transcription and contains an intrinsic histone acetyltransferase activity

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Xenopus NF-Y pre-sets chromatin to potentiate p300 and acetylation-responsive transcription from the Xenopus hsp70 promoter in vivo

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p300 stimulates transcription instigated by ligand-bound thyroid hormone receptor at a step subsequent to chromatin disruption

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Linking histone acetylation to transcriptional regulation

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The transcriptional coactivators p300 and CBP are histone acetyltransferases

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Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide

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Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates

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Histone acetylation and transcriptional regulatory mechanisms

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Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator

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A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p

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TFIIIC1 acts through a downstream region to stabilize TFIIIC2 binding to RNA polymerase III promoters

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Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase

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Identifiers

10.1016/S1097-2765(00)80452-9

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

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