Evidence map›Paper›PMID 32664941›Full record

ArticleEpigenetics & chromatin2020

Molecular mechanism of histone variant H2A.B on stability and assembly of nucleosome and chromatin structures.

Junhui Peng, Chuang Yuan, Xinfan Hua, Zhiyong Zhang

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Epigenetics & chromatin, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.8field-weighted citation impact, top 29% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Genome modeling: From chromatin fibers to genes.Current opinion in structural biology · 2023
    Review
  9. Article
  10. Article
  11. Article
  12. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 2 countries.

Junhui PengMOE Key Laboratory for Membraneless Organelles & Cellular Dynamics, National Science Center for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China.
Chuang YuanMOE Key Laboratory for Membraneless Organelles & Cellular Dynamics, National Science Center for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China.
Xinfan HuaMOE Key Laboratory for Membraneless Organelles & Cellular Dynamics, National Science Center for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China.
Zhiyong ZhangMOE Key Laboratory for Membraneless Organelles & Cellular Dynamics, National Science Center for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China. zzyzhang@ustc.edu.cn.ORCID 0000-0001-8202-9672
University of Science and Technology of China · CN

Funding

National Natural Science Foundation of China 21573205National Natural Science Foundation of China 91953101the Strategic Priority Research Program of the Chinese Academy of Science XDB37040202
6 · The paper itself

Abstract

backgroundH2A.B, the most divergent histone variant of H2A, can significantly modulate nucleosome and chromatin structures. However, the related structural details and the underlying mechanism remain elusive to date. In this work, we built atomic models of the H2A.B-containing nucleosome core particle (NCP), chromatosome, and chromatin fiber. Multiscale modeling including all-atom molecular dynamics and coarse-grained simulations were then carried out for these systems.

resultsIt is found that sequence differences at the C-terminal tail, the docking domain, and the L2 loop, between H2A.B and H2A are directly responsible for the DNA unwrapping in the H2A.B NCP, whereas the N-terminus of H2A.B may somewhat compensate for the aforementioned unwrapping effect. The assembly of the H2A.B NCP is more difficult than that of the H2A NCP. H2A.B may also modulate the interactions of H1 with both the NCP and the linker DNA and could further affect the higher-order structure of the chromatin fiber.

conclusionsThe results agree with the experimental results and may shed new light on the biological function of H2A.B. Multiscale modeling may be a valuable tool for investigating structure and dynamics of the nucleosome and the chromatin induced by various histone variants.

Indexed as

HistonesHumansMolecular Dynamics SimulationMutationNucleosomesProtein BindingProtein StabilityHistonesNucleosomesCoarse-grained simulationsHistone variant H2A.BMolecular dynamicsMultiscale modeling

Identifiers

PMID32664941
PMCPMC7362417
OpenAlexW3042953820

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.