Document Detail

Organizing the genome with H2A histone variants.
MedLine Citation:
PMID:  23301656     Owner:  NLM     Status:  In-Data-Review    
Chromatin acts as an organizer and indexer of genomic DNA and is a highly dynamic and regulated structure with properties directly related to its constituent parts. Histone variants are abundant components of chromatin that replace canonical histones in a subset of nucleosomes, thereby altering nucleosomal characteristics. The present review focuses on the H2A variant histones, summarizing current knowledge of how H2A variants can introduce chemical and functional heterogeneity into chromatin, the positions that nucleosomes containing H2A variants occupy in eukaryotic genomes, and the regulation of these localization patterns.
Catherine B Millar
Related Documents :
12834756 - Measurement of dna breaks and oxidative damage in polymorphonuclear and mononuclear whi...
10432996 - Radiation-induced comet-formation in human skin fibroblasts from radiotherapy patients ...
18157506 - Sodium selenite enhances glutathione peroxidase activity and dna strand breaks in hepat...
22850446 - Dendron modified surfaces provide an ideal environment for stem loop dna probes.
21691656 - Branched rna nanostructures for rna interference.
25402206 - Persistence of dna in carcasses, slime and avian feces may affect interpretation of env...
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Biochemical journal     Volume:  449     ISSN:  1470-8728     ISO Abbreviation:  Biochem. J.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-01-10     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  England    
Other Details:
Languages:  eng     Pagination:  567-79     Citation Subset:  IM    
Faculty of Life Sciences, Michael Smith Building, University of Manchester, Manchester M13 9PT, U.K.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Phenyl linker-induced dense PEG conformation improves the efficacy of C-terminally monoPEGylated sta...
Next Document:  Residue mutations and their impact on protein structure and function: detecting beneficial and patho...