Evidence map›Paper›PMID 27723431›Full record

ArticleTranscription2017

H3K36 methylation state and associated silencing mechanisms.

Shota Suzuki, Yota Murakami, Shinya Takahata

Open access · bronzeAbstract read
In one paragraph

Article in Transcription, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.0field-weighted citation impact, top 21% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. The role of NSD1, NSD2, and NSD3 histone methyltransferases in solid tumors.Cellular and molecular life sciences : CMLS · 2022
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Disruption ofMolecular cancer therapeutics · 2018
    Article
  8. 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

3 authors at 1 institution in 1 country.

Shota Suzukia Department of Chemistry , Faculty of Science, Hokkaido University , Sapporo , Japan.
Yota Murakamia Department of Chemistry , Faculty of Science, Hokkaido University , Sapporo , Japan.
Shinya Takahataa Department of Chemistry , Faculty of Science, Hokkaido University , Sapporo , Japan.
Hokkaido University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epigenetic marks determine cell fate via numerous reader proteins. H3K36 methylation is a common epigenetic mark that is thought to be associated with the activities of the RNA polymerase 2 C-terminal domain. We discuss a novel silencing mechanism regulated by Set2-dependent H3K36 methylation that involves exosome-dependent RNA processing.

Indexed as

Gene SilencingEpigenesis, GeneticExonsHistone-Lysine N-MethyltransferaseHistonesHumansLysineMaleMethylationProtein DomainsRNA Polymerase IIHistone-Lysine N-MethyltransferaseHistonesLysineRNA Polymerase IIepigeneticsexosomeH3K36meHDACheterochromatinSet2

Identifiers

PMID27723431
PMCPMC5279713
OpenAlexW2531192440

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.