Evidence map›Paper›PMID 28628358›Full record

ReviewNucleus (Austin, Tex.)2017

H2B ubiquitination: Conserved molecular mechanism, diverse physiologic functions of the E3 ligase during meiosis.

Liying Wang, Chunwei Cao, Fang Wang, Jianguo Zhao, Wei Li

Open access · goldAbstract readReview
In one paragraph

Review in Nucleus (Austin, Tex.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Decoding RNF20: an epigenetic modifier and beyond.Frontiers in cell and developmental biology · 2026
    Review
  4. Review
  5. Article
  6. Genome research · 2024
    Article
  7. Article
  8. Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review
  9. Article
  10. Paf1 complex subunit Rtf1 stimulates H2B ubiquitylation by interacting with the highly conserved N-terminal helix of Rad6.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

5 authors at 1 institution in 1 country.

Liying Wanga State Key Laboratory of Stem Cell and Reproductive Biology , Institute of Zoology, Chinese Academy of Sciences , Beijing , P.R. China.ORCID 0000-0002-3093-1311
Chunwei Caoa State Key Laboratory of Stem Cell and Reproductive Biology , Institute of Zoology, Chinese Academy of Sciences , Beijing , P.R. China.
Fang Wanga State Key Laboratory of Stem Cell and Reproductive Biology , Institute of Zoology, Chinese Academy of Sciences , Beijing , P.R. China.ORCID 0000-0001-7640-3584
Jianguo Zhaoa State Key Laboratory of Stem Cell and Reproductive Biology , Institute of Zoology, Chinese Academy of Sciences , Beijing , P.R. China.
Wei Lia State Key Laboratory of Stem Cell and Reproductive Biology , Institute of Zoology, Chinese Academy of Sciences , Beijing , P.R. China.ORCID 0000-0002-6235-0749
Chinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNF20/Bre1 mediated H2B ubiquitination (H2Bub) has various physiologic functions. Recently, we found that H2Bub participates in meiotic recombination by promoting chromatin relaxation during meiosis. We then analyzed the phylogenetic relationships among the E3 ligase for H2Bub, its E2 Rad6 and their partner WW domain-containing adaptor with a coiled-coil (WAC) or Lge1, and found that the molecular mechanism underlying H2Bub is evolutionarily conserved from yeast to mammals. However, RNF20 has diverse physiologic functions in different organisms, which might be caused by the evolutionary divergency of their domain/motif architectures. In the current extra view, we not only elucidate the evolutionarily conserved molecular mechanism underlying H2Bub, but also discuss the diverse physiologic functions of RNF20 during meiosis.

Indexed as

MeiosisUbiquitinationAnimalsConserved SequenceEvolution, MolecularHistonesHumansUbiquitin-Protein LigasesHistonesUbiquitin-Protein LigasesevolutionH2B ubiquitinationmeiosisphylogenetic analysisRNF20

Identifiers

PMID28628358
PMCPMC5703235
OpenAlexW2705097630

What OpenQuestion holds

Textmetadata
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.