Evidence map›Paper›PMID 37443729›Full record

ArticleCells2023

Lysine Methyltransferase SMYD1 Regulates Myogenesis via skNAC Methylation.

Li Zhu, Mark A Brown, Robert J Sims, Gayatri R Tiwari, Hui Nie, R Dayne Mayfield, Haley O Tucker

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cells, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.2field-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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

7 authors at 2 institutions in 1 country.

Li ZhuDepartment of Molecular Biosciences, The University of Texas at Austin, 1 University Station A5000, Austin, TX 78712, USA.
Mark A BrownDepartment of Molecular Biosciences, The University of Texas at Austin, 1 University Station A5000, Austin, TX 78712, USA.
Robert J SimsDepartment of Molecular Biosciences, The University of Texas at Austin, 1 University Station A5000, Austin, TX 78712, USA.
Gayatri R TiwariCenter for Biomedical Research Services, Department of Neuroscience, The University of Texas at Austin, 2500 Speedway A4800, Austin, TX 78712, USA.
Hui NieDepartment of Molecular Biosciences, The University of Texas at Austin, 1 University Station A5000, Austin, TX 78712, USA.
R Dayne MayfieldCenter for Biomedical Research Services, Department of Neuroscience, The University of Texas at Austin, 2500 Speedway A4800, Austin, TX 78712, USA.
Haley O TuckerDepartment of Molecular Biosciences, The University of Texas at Austin, 1 University Station A5000, Austin, TX 78712, USA.ORCID 0000-0001-7735-2862
The University of Texas at Austin · USThe University of Texas MD Anderson Cancer Center · US

Funding

GENE EXPRESSION IN THE HUMAN ALCOHOLIC BRAINR01AA012404 · NIAAA · UNIVERSITY OF TEXAS AUSTIN · PI MAYFIELD, ROY DAYNE · 2000 to 2025
$10.7M
Next Generation Sequencing of Human Alcoholic BrainU01AA020926 · NIAAA · UNIVERSITY OF TEXAS AT AUSTIN · PI Roy DAYNE MAYFIELD · 2011 to 2026
$6.7M
MAR MEDIATED GENETIC SWITCH FOR IGH ENHANCER CONTROLR01CA031534 · NCI · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI TUCKER, HALEY O · 1985 to 2012
$2.9M
NCI NIH HHS R01 CA031534NIAAA NIH HHS R01 AA012404NIAAA NIH HHS U01 AA020926NIH HHS AA012404NIH HHS AA020926NIH HHS R01CA31534
6 · The paper itself

Abstract

The SMYD family is a unique class of lysine methyltransferases (KMTases) whose catalytic SET domain is split by a MYND domain. Among these, Smyd1 was identified as a heart- and skeletal muscle-specific KMTase and is essential for cardiogenesis and skeletal muscle development. SMYD1 has been characterized as a histone methyltransferase (HMTase). Here we demonstrated that SMYD1 methylates is the Skeletal muscle-specific splice variant of the Nascent polypeptide-Associated Complex (skNAC) transcription factor. SMYD1-mediated methylation of skNAC targets K1975 within the carboxy-terminus region of skNAC. Catalysis requires physical interaction of SMYD1 and skNAC via the conserved MYND domain of SMYD1 and the PXLXP motif of skNAC. Our data indicated that skNAC methylation is required for the direct transcriptional activation of

Indexed as

DNA-Binding ProteinsGene Expression Regulation, DevelopmentalHistone-Lysine N-MethyltransferaseMolecular ChaperonesMuscle DevelopmentMuscle ProteinsTranscriptional ActivationTranscription FactorsCatalysisHEK293 CellsHumansMethylationMutationProtein DomainsProtein IsoformsDNA-Binding ProteinsHistone-Lysine N-MethyltransferaseMolecular ChaperonesMuscle Proteinsnascent-polypeptide-associated complexProtein IsoformsSMYD1 protein, humanTranscription Factorsheart and skeletal musclemethyltransferasetranscriptional regulation

Identifiers

PMID37443729
PMCPMC10340688
OpenAlexW4381802255

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.