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HDA2 and HDA3 are related proteins that interact with and are essential for the activity of the yeast histone deacetylase HDA1
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scholarly article
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PubMed
PubMed ID
11287668
retrieved
1 December 2016
title
HDA2 and HDA3 are related proteins that interact with and are essential for the activity of the yeast histone deacetylase HDA1
(English)
1 reference
stated in
PubMed
PubMed ID
11287668
retrieved
1 December 2016
main subject
HDA1 complex
1 reference
stated in
Gene Ontology release 2020-05-02
Gene Ontology ID
GO:0070823
Hda2p YDR295C
1 reference
stated in
GOA release 2020-03-11
Hda3p YPR179C
1 reference
stated in
GOA release 2020-03-11
Histone deacetylase HDA1 YNL021W
1 reference
stated in
GOA release 2020-03-11
author
Michael Grunstein
series ordinal
5
object named as
M Grunstein
0 references
author name string
R Kobayashi
series ordinal
3
0 references
N Suka
series ordinal
4
0 references
J Wu
series ordinal
1
0 references
A A Carmen
series ordinal
2
0 references
language of work or name
English
0 references
publication date
10 April 2001
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published in
Proceedings of the National Academy of Sciences of the United States of America
1 reference
stated in
PubMed
PubMed ID
11287668
retrieved
1 December 2016
volume
98
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page(s)
4391-6
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issue
8
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ImageQuant
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stated in
Europe PubMed Central
retrieved
11 June 2022
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/PMC31845/fullTextXML
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inferred from PubMed Central ID database lookup
cites work
TUP1 utilizes histone H3/H2B-specific HDA1 deacetylase to repress gene activity in yeast
1 reference
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PubMed Central
reference URL
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20 March 2017
Yeast HOS3 forms a novel trichostatin A-insensitive homodimer with intrinsic histone deacetylase activity
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reference URL
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20 March 2017
Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation
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PubMed Central
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Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle- and developmentally regulated promoter.
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20 March 2017
Three proteins define a class of human histone deacetylases related to yeast Hda1p
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PubMed Central
reference URL
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The DNA replication and damage checkpoint pathways induce transcription by inhibition of the Crt1 repressor
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Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex generates a highly localized domain of repressed chromatin in vivo
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PubMed Central
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Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4 by RPD3.
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PubMed Central
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Repression by Ume6 involves recruitment of a complex containing Sin3 corepressor and Rpd3 histone deacetylase to target promoters
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PubMed Central
reference URL
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20 March 2017
HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription
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PubMed Central
reference URL
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Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4.
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20 March 2017
HDA1 and HDA3 are components of a yeast histone deacetylase (HDA) complex
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PubMed Central
reference URL
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20 March 2017
Repression by SSN6-TUP1 is directed by MIG1, a repressor/activator protein
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A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
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Spreading of transcriptional repressor SIR3 from telomeric heterochromatin
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Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: a molecular model for the formation of heterochromatin in yeast
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Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases
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Histone deacetylases: silencers for hire.
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29 September 2017
Sin meets NuRD and other tails of repression.
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29 September 2017
Global histone acetylation and deacetylation in yeast
1 reference
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PubMed Central
reference URL
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retrieved
2 June 2018
The protein phosphatase calcineurin is essential for NaCl tolerance of Saccharomyces cerevisiae.
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PubMed Central
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2 June 2018
Transcriptional repression directed by the yeast alpha 2 protein in vitro
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1073%2FPNAS.081560698
retrieved
21 January 2018
Identifiers
DOI
10.1073/PNAS.081560698
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3351743
ADS bibcode
2001PNAS...98.4391W
0 references
OpenCitations bibliographic resource ID
3351743
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3351743
PMCID
31845
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3351743
PubMed ID
11287668
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3351743
ResearchGate publication ID
12045618
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