ArticleBiophysical journal2014
Distinct features of the histone core structure in nucleosomes containing the histone H2A.B variant.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 29 citations in OpenAlex.
- Structural basis of RNAPII transcription on the nucleosome containing histone variant H2A.B.The EMBO journal · 2025Article
- Solution conformational differences between conventional and CENP-A nucleosomes are accentuated by reversible deformation under high pressure.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025Article
- Unusual nucleosome formation and transcriptome influence by the histone H3mm18 variant.Nucleic acids research · 2022Article
- Effects of H2A.B incorporation on nucleosome structures and dynamics.Biophysical journal · 2021Article
- Histone variant H2A.B-H2B dimers are spontaneously exchanged with canonical H2A-H2B in the nucleosome.Communications biology · 2021Article
- Deuteration Aiming for Neutron Scattering.Biophysics and physicobiology · 2021Article
- Molecular mechanism of histone variant H2A.B on stability and assembly of nucleosome and chromatin structures.Epigenetics & chromatin · 2020Article
- Structural Studies of Overlapping Dinucleosomes in Solution.Biophysical journal · 2020Article
- Review
- A cassette of basic amino acids in histone H2B regulates nucleosome dynamics and access to DNA damage.The Journal of biological chemistry · 2018Article
- Identification of the amino acid residues responsible for stable nucleosome formation by histone H3.Y.Nucleus (Austin, Tex.) · 2017Article
- A new link between transcriptional initiation and pre-mRNA splicing: The RNA binding histone variant H2A.B.PLoS genetics · 2017Article
- Solution structure of variant H2A.Z.1 nucleosome investigated by small-angle X-ray and neutron scatterings.Biochemistry and biophysics reports · 2015Article
- Nucleosome adaptability conferred by sequence and structural variations in histone H2A-H2B dimers.Current opinion in structural biology · 2015Review
- Nucleosome structure and function.Chemical reviews · 2015Review
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nucleosomes containing a human histone variant, H2A.B, in an aqueous solution were analyzed by small-angle neutron scattering utilizing a contrast variation technique. Comparisons with the canonical H2A nucleosome structure revealed that the DNA termini of the H2A.B nucleosome are detached from the histone core surface, and flexibly expanded toward the solvent. In contrast, the histone tails are compacted in H2A.B nucleosomes compared to those in canonical H2A nucleosomes, suggesting that they bind to the surface of the histone core and/or DNA. Therefore, the histone tail dynamics may function to regulate the flexibility of the DNA termini in the nucleosomes.
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