Evidence map›Paper›PMID 29931239›Full record

ArticleNucleic acids research2018

Effects of histone H2B ubiquitylation on the nucleosome structure and dynamics.

Wladyslaw A Krajewski, Jiabin Li, Yali Dou

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

24 citing papers in PubMed, 40 citations in OpenAlex.

  1. Mapping Allosteric Communication in the Nucleosome with Conditional Activity.Journal of chemical information and modeling · 2026
    Article
  2. Article
  3. Particulate matter-induced epigenetic modifications and lung complications.European respiratory review : an official journal of the European Respiratory Society · 2024
    Review
  4. Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review
  5. Hexasomal particles: consequence or also consequential?Current opinion in genetics & development · 2024
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Decoding histone ubiquitylation.Frontiers in cell and developmental biology · 2022
    Review
  14. Article
  15. Review
  16. Article
  17. The Histone Chaperone HIRA Is a Positive Regulator of Seed Germination.International journal of molecular sciences · 2021
    Article
  18. Review
  19. Pioneer factors and their in vitro identification methods.Molecular genetics and genomics : MGG · 2020
    Review
  20. Review
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

3 authors at 2 institutions in 3 countries.

Wladyslaw A KrajewskiN.K. Koltsov Institute of Developmental Biology, Russian Academy of Sciences, Vavilova Str. 26, Moscow, 119334, Russia.
Jiabin LiSchool of Life Sciences, University of Science and Technology of China, Hefei 230026, China.
Yali DouDepartment of Pathology, University of Michigan, Ann Arbor, MI 48109, USA.
University of Michigan–Ann Arbor · USUniversity of Science and Technology of China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA in nucleosomes has restricted nucleosome dynamics and is refractory to DNA-templated processes. Histone post-translational modifications play important roles in regulating DNA accessibility in nucleosomes. Whereas most histone modifications function either by mitigating the electrostatic shielding of histone tails or by recruiting 'reader' proteins, we show that ubiquitylation of H2B K34, which is located in a tight space protected by two coils of DNA superhelix, is able to directly influence the canonical nucleosome conformation via steric hindrances by ubiquitin groups. H2B K34 ubiquitylation significantly enhances nucleosome dynamics and promotes generation of hexasomes both with symmetrically or asymmetrically modified nucleosomes. Our results indicate a direct mechanism by which a histone modification regulates the chromatin structural states.

Indexed as

UbiquitinationAnimalsChromatinHistonesLysineNucleosomesProtein Processing, Post-TranslationalXenopus laevisXenopus ProteinsChromatinHistonesLysineNucleosomesXenopus Proteins

Identifiers

PMID29931239
PMCPMC6125632
OpenAlexW2809388448

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.