Distribution of histone H3.3 in hematopoietic cell lineages
about
H3.3/H2A.Z double variant-containing nucleosomes mark 'nucleosome-free regions' of active promoters and other regulatory regionsDynamics of histone variant H3.3 and its coregulation with H2A.Z at enhancers and promotersHistone H3 mutations--a special role for H3.3 in tumorigenesis?Distinct factors control histone variant H3.3 localization at specific genomic regionsCalcium-dependent dephosphorylation of the histone chaperone DAXX regulates H3.3 loading and transcription upon neuronal activationH3.3 demarcates GC-rich coding and subtelomeric regions and serves as potential memory mark for virulence gene expression in Plasmodium falciparumOrganismal differences in post-translational modifications in histones H3 and H4.Dynamic replacement of histone H3 variants reprograms epigenetic marks in early mouse embryos.Genetic variation stimulated by epigenetic modification.Histone variants: emerging players in cancer biology.Chromatin environment of histone variant H3.3 revealed by quantitative imaging and genome-scale chromatin and DNA immunoprecipitation.Distinct chromatin signature of histone H3 variant H3.3 in human cells.Transcription factor EKLF (KLF1) recruitment of the histone chaperone HIRA is essential for β-globin gene expression.Crucial roles for chromatin dynamics in cellular memory.Histone H3 variants and their potential role in indexing mammalian genomes: the "H3 barcode hypothesis"BS69/ZMYND11 reads and connects histone H3.3 lysine 36 trimethylation-decorated chromatin to regulated pre-mRNA processingDrosophila GAGA factor directs histone H3.3 replacement that prevents the heterochromatin spreading.Nucleosome stability mediated by histone variants H3.3 and H2A.Z.Physical chemistry of nucleic acids and their complexes.Hexavalent Chromium (Cr(VI)) Down-Regulates Acetylation of Histone H4 at Lysine 16 through Induction of Stressor Protein Nupr1.The nucleosome: a little variation goes a long way.DAXX-dependent supply of soluble (H3.3-H4) dimers to PML bodies pending deposition into chromatinCigarette smoke component acrolein modulates chromatin assembly by inhibiting histone acetylation.Inducible deposition of the histone variant H3.3 in interferon-stimulated genes.H3.3 actively marks enhancers and primes gene transcription via opening higher-ordered chromatin.Mechanisms Underlying Acrolein-Mediated Inhibition of Chromatin AssemblyChromatin dynamics: H3K4 methylation and H3 variant replacement during development and in cancer.The Histone Variant H3.3 in Transcriptional Regulation and Human Disease.Acetylation of EKLF is essential for epigenetic modification and transcriptional activation of the beta-globin locus.Phosphorylated serine 28 of histone H3 is associated with destabilized nucleosomes in transcribed chromatin.Epigenetic changes during hematopoietic cell granulocytic differentiation--comparative analysis of primary CD34+ cells, KG1 myeloid cells and mature neutrophils.The histone variant H3.3 regulates gene expression during lytic infection with herpes simplex virus type 1.Epigenetics meets metabolism through PHB-mediated histone H3.3 deposition by HIRA.Regulation of Chromatin Assembly and Cell Transformation by Formaldehyde Exposure in Human Cells.The effects of acetaldehyde exposure on histone modifications and chromatin structure in human lung bronchial epithelial cells.
P2860
Q24317641-8B34243C-1397-49AC-BAB0-DCFDB6929FA2Q26851348-8E801DDF-A636-4493-BD19-BED76415A654Q26865965-E6F08681-9DDF-4E4B-9108-8A562EC57B37Q28275277-061B000A-6015-418B-BDF8-06F87EEA76FCQ28586252-6C9210A7-F5DA-42D3-94DE-7721B5F1BA61Q30043364-C7577E2D-6412-42C6-B688-6B2384286FF0Q30442461-B12029D6-3B1D-45AA-9A66-A4C100E74EC0Q31036608-CAEC754F-570A-440E-9E7A-E059A1E830C2Q33396468-4D510E95-BE3B-47D5-A389-D3A2A9117B94Q33630867-0936AEE8-BC88-4661-89F9-3C6A8C243BE7Q33881683-1F8E90AB-9205-4ECD-8BBF-D1618FBC0EA5Q34183341-C7439874-6810-4D93-B66B-84CE075074BFQ34218452-89F0C58F-04F8-43C5-A5F3-B64F011CFE63Q34616998-DB2E0AA0-002B-45B1-8018-A20B0D946F2DQ35025031-7D9C6958-53A0-4DA6-94E1-C1EC61292D42Q35186308-F426B4B8-4289-4902-8A15-A4EC1869BE89Q35677275-B8E9E31F-FDE4-4891-8420-1CC08954CBB4Q35840889-3C6DEAFD-2C44-4A50-B91C-26FB01051A04Q36040914-308D65C2-1EE0-48B1-A2AD-4C19F28510E7Q36048134-E15A0EDA-DE42-4CC6-B01A-786C121B8934Q36579363-51AEE337-1622-4E2A-A7DD-CB68B02878FAQ36660130-1FC3C4DA-B5E8-495D-AACB-F7B5D87C1CA1Q37048366-234151C8-6895-4AF4-B682-E583F5E477E0Q37169493-6B99DB2F-C50B-4962-AA8C-B08FBDCC043EQ37362553-67131AAD-511B-4C1E-8A14-4B1F5A2455C9Q37413682-70AE0522-C17E-4182-8CEF-1F1B8E460C48Q38199995-97F66A20-FE71-449A-9A69-5E75FD28277AQ39022741-D4573ECE-6DDA-4599-BFC5-D910C1035312Q39949590-2ECD1E2B-EDFB-4363-8905-48D7A8146901Q40696790-14840C27-E752-4392-ACAD-209F35468CB6Q41888823-7CB56A83-DAE9-4D16-B08E-2524BFF8377CQ42066826-FE38200C-3982-43A8-B267-D7C0C3F1B344Q42342118-2DBDA276-558C-4A8B-B689-34782827DAC7Q42777824-984EEB3F-65B0-491C-9321-3DBCC30751F9Q52641105-AAB176C9-16A4-437A-9DFE-95C0692021FC
P2860
Distribution of histone H3.3 in hematopoietic cell lineages
description
2006 nî lūn-bûn
@nan
2006 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հունվարին 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
Distribution of histone H3.3 in hematopoietic cell lineages
@ast
Distribution of histone H3.3 in hematopoietic cell lineages
@en
Distribution of histone H3.3 in hematopoietic cell lineages
@nl
type
label
Distribution of histone H3.3 in hematopoietic cell lineages
@ast
Distribution of histone H3.3 in hematopoietic cell lineages
@en
Distribution of histone H3.3 in hematopoietic cell lineages
@nl
prefLabel
Distribution of histone H3.3 in hematopoietic cell lineages
@ast
Distribution of histone H3.3 in hematopoietic cell lineages
@en
Distribution of histone H3.3 in hematopoietic cell lineages
@nl
P2860
P356
P1476
Distribution of histone H3.3 in hematopoietic cell lineages
@en
P2093
Chunyuan Jin
Gary Felsenfeld
P2860
P304
P356
10.1073/PNAS.0509974103
P407
P577
2006-01-05T00:00:00Z