H2A.Z contributes to the unique 3D structure of the centromere
about
The euchromatic and heterochromatic landscapes are shaped by antagonizing effects of transcription on H2A.Z depositionNew insights into nucleosome and chromatin structure: an ordered state or a disordered affair?Chromatin Dynamics in Vivo: A Game of Musical ChairsDynamics of histone variant H3.3 and its coregulation with H2A.Z at enhancers and promotersEvery amino acid matters: essential contributions of histone variants to mammalian development and diseaseExpression and functionality of histone H2A variants in cancerExpression of P. falciparum var genes involves exchange of the histone variant H2A.Z at the promoterRestricting dosage compensation complex binding to the X chromosomes by H2A.Z/HTZ-1SWI/SNF-like chromatin remodeling factor Fun30 supports point centromere function in S. cerevisiae.The INO80 chromatin remodeling complex prevents polyploidy and maintains normal chromatin structure at centromeresRSF governs silent chromatin formation via histone H2Av replacementHP1 recruits activity-dependent neuroprotective protein to H3K9me3 marked pericentromeric heterochromatin for silencing of major satellite repeatsPlasmodium falciparum centromeres display a unique epigenetic makeup and cluster prior to and during schizogonyHistone variants and epigenetics.Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates.An epichromatin epitope: persistence in the cell cycle and conservation in evolutionGlobal dynamics of newly constructed oligonucleosomes of conventional and variant H2A.Z histoneThe Schizosaccharomyces pombe JmjC-protein, Msc1, prevents H2A.Z localization in centromeric and subtelomeric chromatin domains.The genomic distribution and function of histone variant HTZ-1 during C. elegans embryogenesisThe 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.Discriminating nucleosomes containing histone H2A.Z or H2A based on genetic and epigenetic information.Histone modifications within the human X centromere region.Histone variant H2A.Z regulates centromere silencing and chromosome segregation in fission yeastHistone variants: emerging players in cancer biology.The SWR1 histone replacement complex causes genetic instability and genome-wide transcription misregulation in the absence of H2A.Z.Chromatin higher-order structure and dynamicsGlobal analysis of core histones reveals nucleosomal surfaces required for chromosome bi-orientation.Selection of stable reference genes for quantitative rt-PCR comparisons of mouse embryonic and extra-embryonic stem cellsHistone variants in metazoan developmentCentromeres: unique chromatin structures that drive chromosome segregation.Activity of a C-terminal plant homeodomain (PHD) of Msc1 is essential for function.Tetrameric organization of vertebrate centromeric nucleosomes.Understanding nucleosome dynamics and their links to gene expression and DNA replication.Chromatin remodelling beyond transcription: the INO80 and SWR1 complexes.Epigenetic specification of centromeres.CENP-A nucleosomes localize to transcription factor hotspots and subtelomeric sites in human cancer cellsEpigenetic mechanisms and genome stability.Chromosome segregation and organization are targets of 5'-Fluorouracil in eukaryotic cells.Overlapping Functions between SWR1 Deletion and H3K56 Acetylation in Candida albicans.Acetylation of H2A.Z is a key epigenetic modification associated with gene deregulation and epigenetic remodeling in cancer.
P2860
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P2860
H2A.Z contributes to the unique 3D structure of the centromere
description
2006 nî lūn-bûn
@nan
2006 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
H2A.Z contributes to the unique 3D structure of the centromere
@ast
H2A.Z contributes to the unique 3D structure of the centromere
@en
type
label
H2A.Z contributes to the unique 3D structure of the centromere
@ast
H2A.Z contributes to the unique 3D structure of the centromere
@en
prefLabel
H2A.Z contributes to the unique 3D structure of the centromere
@ast
H2A.Z contributes to the unique 3D structure of the centromere
@en
P2093
P2860
P356
P1476
H2A.Z contributes to the unique 3D structure of the centromere
@en
P2093
Danny Rangasamy
David J Tremethick
Ian K Greaves
Patricia Ridgway
P2860
P304
P356
10.1073/PNAS.0607870104
P407
P577
2006-12-28T00:00:00Z