Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Key functional regions in the histone variant H2A.Z C-terminal docking domain.

Molecular and cellular biology - 1 Sept 2011

Wang Alice Y, Aristizabal Maria J, Ryan Colm, Krogan Nevan J, Kobor Michael S

Abstract excerpt

The incorporation of histone variants into nucleosomes represents one way of altering the chromatin structure to accommodate diverse functions. Histone variant H2A.Z has specific roles in gene regulation, heterochromatin boundary formation, and genomic integrity. The precise features required for H2A.Z to function and specify an identity different from canonical H2A remain to be fully explored. Analysis of the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Histone Chaperones
Share to Histones
Share to Adenosine Triphosphatases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Chromatin

Share to Chromatin Assembly and Disassembly

Share to Chromatin Immunoprecipitation

Share to Nucleosomes

Share to Transcriptional Activation

Source

Open in PubMed Open full text

Identifiers

PMID: 21791612
DOI: 10.1128/MCB.05182-11
PMCID: PMC3165728

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Key functional regions in the histone variant H2A.Z C-terminal docking domain.PMID 21791612Read ↗

Histone H2A.Z acid patch residues required for deposition and function.Semantic proximity Read ↗

Mutations in non-acid patch residues disrupt H2A.Z's association with chromatin through multiple mechanisms.Semantic proximity Read ↗

What makes a histone variant a variant: Changing H2A to become H2A.Z.Semantic proximity Read ↗

Replacement of Arabidopsis H2A.Z with human H2A.Z orthologs reveals extensive functional conservation and limited importance of the N-terminal tail sequence for Arabidopsis developmentSemantic proximity Read ↗

Global analysis for functional residues of histone variant Htz1 using the comprehensive point mutant library.Semantic proximity Read ↗

Patterning chromatin: form and function for H2A.Z variant nucleosomes.Semantic proximity Read ↗

Cancer histone H2A.Z missense mutations disrupt function through distinct local and allosteric effectsSemantic proximity Read ↗

NAP1-RELATED PROTEIN1 and 2 negatively regulate H2A.Z abundance in chromatin in Arabidopsis.Semantic proximity Read ↗

Non-redundant functions of H2A.Z.1 and H2A.Z.2 in chromosome segregation and cell cycle progressionSemantic proximity Read ↗

H2A.Z functions to regulate progression through the cell cycle.Semantic proximity Read ↗

The many tales of a tail: carboxyl-terminal tail heterogeneity specializes histone H2A variants for defined chromatin function.Semantic proximity Read ↗

Deposition of histone variant H2A.Z within gene bodies regulates responsive genes.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.