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A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1.
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scholarly article
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stated in
PubMed
PubMed ID
14690608
retrieved
1 December 2016
title
A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1.
(English)
1 reference
stated in
PubMed
PubMed ID
14690608
retrieved
1 December 2016
main subject
Swr1 complex
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stated in
Gene Ontology release 2020-05-02
Gene Ontology ID
GO:0000812
author
Stephen Buratowski
series ordinal
15
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Michael-Christopher Keogh
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2
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Robin Haw
object named as
Robin A Haw
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7
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Andrew Emili
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13
object named as
Andrew Emili
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Nevan Krogan
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1
object named as
Nevan J Krogan
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author name string
Nira Datta
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3
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Chika Sawa
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4
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Owen W Ryan
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5
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Huiming Ding
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6
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Jeffrey Pootoolal
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8
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Amy Tong
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9
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Veronica Canadien
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10
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Dawn P Richards
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11
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Xiaorong Wu
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12
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Timothy R Hughes
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14
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Jack F Greenblatt
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16
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language of work or name
English
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publication date
December 2003
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published in
Molecular Cell
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PubMed
PubMed ID
14690608
retrieved
1 December 2016
volume
12
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page(s)
1565-76
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issue
6
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cites work
H2A.Z is required for global chromatin integrity and for recruitment of RNA polymerase II under specific conditions
1 reference
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The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly
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Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae
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RSC, an essential, abundant chromatin-remodeling complex
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Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23.
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Screening the yeast "disruptome" for mutants affecting resistance to the immunosuppressive drug, mycophenolic acid
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A histone variant, Htz1p, and a Sir1p-like protein, Esc2p, mediate silencing at HMR.
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Multiple links between the NuA4 histone acetyltransferase complex and epigenetic control of transcription.
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Functional organization of the yeast proteome by systematic analysis of protein complexes
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Global analysis of protein expression in yeast
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Tails of intrigue: phosphorylation of RNA polymerase II mediates histone methylation
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Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae
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Heterochromatic deposition of centromeric histone H3-like proteins
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Global analysis of protein localization in budding yeast
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A likely histone H2A.F/Z variant in Saccharomyces cerevisiae.
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Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription
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RNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach
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Inactivating chromosomes: a macro domain that minimizes transcription
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Bromodomains mediate an acetyl-histone encoded antisilencing function at heterochromatin boundaries
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Yaf9, a novel NuA4 histone acetyltransferase subunit, is required for the cellular response to spindle stress in yeast
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Conserved Histone Variant H2A.Z Protects Euchromatin from the Ectopic Spread of Silent Heterochromatin
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A mutation in CSE4, an essential gene encoding a novel chromatin-associated protein in yeast, causes chromosome nondisjunction and cell cycle arrest at mitosis
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Characterization of the imitation switch subfamily of ATP-dependent chromatin-remodeling factors in Saccharomyces cerevisiae
1 reference
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Crossref
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7 January 2021
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inferred from DOI database lookup
DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis
1 reference
stated in
Crossref
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7 January 2021
based on heuristic
inferred from DOI database lookup
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1 reference
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Crossref
reference URL
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7 January 2021
based on heuristic
inferred from DOI database lookup
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1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS1097-2765%2803%2900497-0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Identifiers
DOI
10.1016/S1097-2765(03)00497-0
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4480010
OpenCitations bibliographic resource ID
4480010
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4480010
PubMed ID
14690608
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4480010
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