Evidence map›Paper›PMID 37863247›Full record

ReviewJournal of molecular biology2024

Defining Biological and Biochemical Functions of Noncanonical SET Domain Proteins.

Winny Sun, Isabella Justice, Erin M Green

Open access · greenAbstract readReview
In one paragraph

Review in Journal of molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

6 citing papers in PubMed, 6 citations in OpenAlex.

  1. Set202 is a histone lysine methyltransferase that enablesbioRxiv : the preprint server for biology · 2026
    Article
  2. Alterations to the yeast chromatin landscape during hypoxia.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. 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 2 institutions in 1 country.

Winny SunDepartment of Biological Sciences, University of Maryland Baltimore County, Baltimore, MD 21250, United States.
Isabella JusticeDepartment of Biological Sciences, University of Maryland Baltimore County, Baltimore, MD 21250, United States.
Erin M GreenDepartment of Biological Sciences, University of Maryland Baltimore County, Baltimore, MD 21250, United States; Marlene and Stewart Greenebaum Comprehensive Cancer Center, University of Maryland School of Medicine, Baltimore, MD 21201, United States. Electronic address: egreen@umbc.edu.
University of Maryland, Baltimore County · USUniversity of Maryland, Baltimore · US

Funding

Lysine methylation at chromatin and cellular responses to stressR01GM124342 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI GREEN, ERIN · 2017 to 2021
$1.5M
NIGMS NIH HHS R01 GM124342
6 · The paper itself

Abstract

Within the SET domain superfamily of lysine methyltransferases, there is a well-conserved subfamily, frequently referred to as the Set3 SET domain subfamily, which contain noncanonical SET domains carrying divergent amino acid sequences. These proteins are implicated in diverse biological processes including stress responses, cell differentiation, and development, and their disruption is linked to diseases including cancer and neurodevelopmental disorders. Interestingly, biochemical and structural analysis indicates that they do not possess catalytic methyltransferase activity. At the molecular level, Set3 SET domain proteins appear to play critical roles in the regulation of gene expression, particularly repression and heterochromatin maintenance, and in some cases, via scaffolding other histone modifying activities at chromatin. Here, we explore the common and unique functions among Set3 SET domain subfamily proteins and analyze what is known about the specific contribution of the conserved SET domain to functional roles of these proteins, as well as propose areas of investigation to improve understanding of this important, noncanonical subfamily of proteins.

Indexed as

Histone-Lysine N-MethyltransferasePR-SET DomainsAmino Acid SequenceAnimalsChromatinHumansChromatinHistone-Lysine N-Methyltransferasechromatingene regulationhistone modificationmethylationSET domain

Identifiers

PMID37863247
PMCPMC10957327
OpenAlexW4387765899

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.