The evolutionary differentiation of two histone H2A.Z variants in chordates (H2A.Z-1 and H2A.Z-2) is mediated by a stepwise mutation process that affects three amino acid residues.
about
Molecular turnover, the H3.3 dilemma and organismal aging (hypothesis)Every amino acid matters: essential contributions of histone variants to mammalian development and diseaseStructural polymorphism in the L1 loop regions of human H2A.Z.1 and H2A.Z.2The Histone Database: an integrated resource for histones and histone fold-containing proteinsA combination of H2A.Z and H4 acetylation recruits Brd2 to chromatin during transcriptional activationA unified phylogeny-based nomenclature for histone variantsNap1 and Chz1 have separate Htz1 nuclear import and assembly functions.Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates.H2A.Z acidic patch couples chromatin dynamics to regulation of gene expression programs during ESC differentiation.Identification of novel transcriptional regulators involved in macrophage differentiation and activation in U937 cells.Insights into chromatin structure and dynamics in plantsHistone variants: emerging players in cancer biology.Sometimes one just isn't enough: do vertebrates contain an H2A.Z hyper-variant?Histone variant innovation in a rapidly evolving chordate lineage.Identification and characterization of the two isoforms of the vertebrate H2A.Z histone variant.Proteomic analysis of endothelial cold-adaptationHistone H2A (H2A.X and H2A.Z) variants in molluscs: molecular characterization and potential implications for chromatin dynamics.USP10 deubiquitylates the histone variant H2A.Z and both are required for androgen receptor-mediated gene activationRegulation of u-PAR gene expression by H2A.Z is modulated by the MEK-ERK/AP-1 pathway.A conserved function for the H2A.Z C terminus.H2A.Z.2.2 is an alternatively spliced histone H2A.Z variant that causes severe nucleosome destabilizationMultivalent binding of PWWP2A to H2A.Z regulates mitosis and neural crest differentiation.Histone H2A variants in nucleosomes and chromatin: more or less stable?Epigenetic regulation of the ribosomal cistron seasonally modulates enrichment of H2A.Z and H2A.Zub in response to different environmental inputs in carp (Cyprinus carpio)The characterization of macroH2A beyond vertebrates supports an ancestral origin and conserved role for histone variants in chromatinRegulation of Reprogramming and Cellular Plasticity through Histone Exchange and Histone Variant Incorporation.Crystal structures of heterotypic nucleosomes containing histones H2A.Z and H2ASolution structure of variant H2A.Z.1 nucleosome investigated by small-angle X-ray and neutron scatterings.SUMO modification system facilitates the exchange of histone variant H2A.Z-2 at DNA damage sites.Characterization of mussel H2A.Z.2: a new H2A.Z variant preferentially expressed in germinal tissues from Mytilus.Post-Translational Modifications of H2A Histone Variants and Their Role in Cancer.
P2860
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P2860
The evolutionary differentiation of two histone H2A.Z variants in chordates (H2A.Z-1 and H2A.Z-2) is mediated by a stepwise mutation process that affects three amino acid residues.
description
2009 nî lūn-bûn
@nan
2009 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
The evolutionary differentiati ...... cts three amino acid residues.
@ast
The evolutionary differentiati ...... cts three amino acid residues.
@en
type
label
The evolutionary differentiati ...... cts three amino acid residues.
@ast
The evolutionary differentiati ...... cts three amino acid residues.
@en
prefLabel
The evolutionary differentiati ...... cts three amino acid residues.
@ast
The evolutionary differentiati ...... cts three amino acid residues.
@en
P2093
P2860
P356
P1476
The evolutionary differentiati ...... cts three amino acid residues.
@en
P2093
Deanna Dryhurst
Juan Ausió
Rodrigo González-Romero
P2860
P2888
P356
10.1186/1471-2148-9-31
P577
2009-02-04T00:00:00Z
P5875
P6179
1048037225