Evidence map›Paper›PMID 31911441›Full record

ArticleThe Journal of biological chemistry2020

An engineered variant of SETD3 methyltransferase alters target specificity from histidine to lysine methylation.

Shaobo Dai, John R Horton, Alex W Wilkinson, Or Gozani, Xing Zhang, Xiaodong Cheng

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. 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
1.3field-weighted citation impact, top 20% 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, 21 citations in OpenAlex.

  1. Article
  2. Computational Study of Methionine Methylation Process Catalyzed by SETD3.Interdisciplinary sciences, computational life sciences · 2022
    Article
  3. Histidine methyltransferase SETD3 methylates structurally diverse histidine mimics in actin.Protein science : a publication of the Protein Society · 2022
    Article
  4. Review
  5. Article
  6. Article
  7. 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

6 authors at 2 institutions in 1 country.

Shaobo DaiDepartment of Epigenetics and Molecular Carcinogenesis, University of Texas M.D. Anderson Cancer Center, Houston, Texas 77030.
John R HortonDepartment of Epigenetics and Molecular Carcinogenesis, University of Texas M.D. Anderson Cancer Center, Houston, Texas 77030.
Alex W WilkinsonDepartment of Biology, Stanford University, Stanford, California 94305.
Or GozaniDepartment of Biology, Stanford University, Stanford, California 94305.
Xing ZhangDepartment of Epigenetics and Molecular Carcinogenesis, University of Texas M.D. Anderson Cancer Center, Houston, Texas 77030. Electronic address: xzhang21@mdanderson.org.
Xiaodong ChengDepartment of Epigenetics and Molecular Carcinogenesis, University of Texas M.D. Anderson Cancer Center, Houston, Texas 77030. Electronic address: xcheng5@mdanderson.org.
The University of Texas MD Anderson Cancer Center · USStanford University · US

Funding

Histone Lysine deMethylation: Structures, Inhibitions and MechanismsR01GM114306 · NIGMS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI CHENG, XIAODONG · 2015 to 2018
$1.2M
Regulation of Signaling by Histidine Protein MethylationR01GM133051 · NIGMS · STANFORD UNIVERSITY · PI GOZANI, OR P. · 2019 to 2020
$632k
NIGMS NIH HHS R01 GM114306NIGMS NIH HHS R01 GM133051
6 · The paper itself

Abstract

Most characterized SET domain (SETD) proteins are protein lysine methyltransferases, but SETD3 was recently demonstrated to be a protein (

Indexed as

ActinsAmino Acid SubstitutionCatalytic DomainHistidineHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHumansHydrogen BondingLysineMethylationProtein EngineeringSubstrate SpecificityActinsHistidineHistone-Lysine N-MethyltransferaseHistone MethyltransferasesLysineSETD3 protein, humanenzyme catalysisenzyme kineticsglutamine methylationhistidinehistidine methylationlysine methylationprotein methylationS-adenosylmethionine (SAM)structural biology

Identifiers

PMID31911441
PMCPMC7049955
OpenAlexW2999933270

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.