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Histone H2A variants H2AX and H2AZ
scientific article (publication date: April 2002)
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title
Histone H2A variants H2AX and H2AZ
(English)
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author name string
Christophe Redon
series ordinal
1
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Duane Pilch
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2
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Emmy Rogakou
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3
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Olga Sedelnikova
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4
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Kenneth Newrock
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5
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William Bonner
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6
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language of work or name
English
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publication date
April 2002
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published in
Current Opinion in Genetics & Development
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volume
12
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page(s)
162-9
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issue
2
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cites work
Non-allelic variants of histones 2a, 2b and 3 in mammals
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Stage-Specific Switches in Histone Synthesis During Embryogenesis of the Sea Urchin
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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Histone 2A, a heteromorphous family of eight protein species
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MacroH2A, a core histone containing a large nonhistone region
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MACROH2A2, a new member of the MARCOH2A core histone family
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Histone H2A variants and the inactive X chromosome: identification of a second macroH2A variant
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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H2A.X. a histone isoprotein with a conserved C-terminal sequence, is encoded by a novel mRNA with both DNA replication type and polyA 3' processing signals
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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Essential and nonessential histone H2A variants in Tetrahymena thermophila
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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7 January 2021
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DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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Megabase chromatin domains involved in DNA double-strand breaks in vivo
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A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage
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ATM phosphorylates histone H2AX in response to DNA double-strand breaks
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p53 binding protein 1 (53BP1) is an early participant in the cellular response to DNA double-strand breaks
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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Tumor suppressor p53 binding protein 1 (53BP1) is involved in DNA damage-signaling pathways
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Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress
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A role for Saccharomyces cerevisiae histone H2A in DNA repair.
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Response to RAG-mediated VDJ cleavage by NBS1 and gamma-H2AX
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Recombinational DNA double-strand breaks in mice precede synapsis
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Initiation of DNA fragmentation during apoptosis induces phosphorylation of H2AX histone at serine 139
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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Two complexes that contain histones are required for nucleosome assembly in vitro: role of nucleoplasmin and N1 in Xenopus egg extracts
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DNA-dependent phosphorylation of histone H2A.X during nucleosome assembly in Xenopus laevis oocytes: involvement of protein phosphorylation in nucleosome spacing.
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Mre11 protein complex prevents double-strand break accumulation during chromosomal DNA replication.
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Minor Histone 2A Variants and Ubiquinated Forms in the Native H2A:H2B Dimer
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H2A.F: an extremely variant histone H2A sequence expressed in the chicken embryo
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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7 January 2021
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Sequence of cDNAs for mammalian H2A.Z, an evolutionarily diverged but highly conserved basal histone H2A isoprotein species
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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7 January 2021
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Either of the major H2A genes but not an evolutionarily conserved H2A.F/Z variant of Tetrahymena thermophila can function as the sole H2A gene in the yeast Saccharomyces cerevisiae
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7 January 2021
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Histone H2A.Z regulats transcription and is partially redundant with nucleosome remodeling complexes
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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7 January 2021
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Analysis of a histone H2A variant from fission yeast: evidence for a role in chromosome stability.
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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7 January 2021
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Regions of variant histone His2AvD required for Drosophila development.
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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7 January 2021
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A histone variant, H2AvD, is essential in Drosophila melanogaster
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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7 January 2021
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Histone variant H2A.Z is required for early mammalian development
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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7 January 2021
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Temporal and spatial association of histone H2A variant hv1 with transcriptionally competent chromatin during nuclear development in Tetrahymena thermophila
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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7 January 2021
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Histone H2A.Z acetylation modulates an essential charge patch
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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7 January 2021
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Histone H2A.Z is widely but nonrandomly distributed in chromosomes of Drosophila melanogaster.
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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Crystal structure of a nucleosome core particle containing the variant histone H2A.Z
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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Characterization of the stability and folding of H2A.Z chromatin particles: implications for transcriptional activation
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7 January 2021
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A histone variant, Htz1p, and a Sir1p-like protein, Esc2p, mediate silencing at HMR.
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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7 January 2021
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H2A.Z is required for global chromatin integrity and for recruitment of RNA polymerase II under specific conditions
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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Site- and time-specific gene targeting in the mouse
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AID is required to initiate Nbs1/gamma-H2AX focus formation and mutations at sites of class switching
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https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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UV-induced replication arrest in the xeroderma pigmentosum variant leads to DNA double-strand breaks, gamma -H2AX formation, and Mre11 relocalization
1 reference
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reference URL
https://api.crossref.org/works/10.1016%2FS0959-437X%2802%2900282-4
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7 January 2021
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Identifiers
DOI
10.1016/S0959-437X(02)00282-4
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
699094
OpenCitations bibliographic resource ID
699094
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
699094
PubMed ID
11893489
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
699094
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