ArticleThe Journal of biological chemistry2011
Histone methyltransferase SETD3 regulates muscle differentiation.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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.
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.
Who cites it
57 citing papers in PubMed, 101 citations in OpenAlex.
- Histidine Ethylation by Histidine Methyltransferases SETD3 and METTL9.Chembiochem : a European journal of chemical biology · 2026Article
- The emerging paradigms of SETD family enzymes as epigenetic regulators of the immune response in inflammatory diseases.Frontiers in immunology · 2026Review
- Review
- Unveiling the Role of Histone Methyltransferases in Psoriasis Pathogenesis: Insights from Transcriptomic Analysis.International journal of molecular sciences · 2025Article
- Regulatory mechanism of circular RNAs in brain and neurodegenerative diseases.Frontiers in molecular neuroscience · 2025Review
- Article
- Examining prestructured β-actin peptides as substrates of histidine methyltransferase SETD3.Scientific reports · 2024Article
- Regulatory mechanism of circular RNAs in neurodegenerative diseases.CNS neuroscience & therapeutics · 2024Review
- Diverse and dynamic forms of gene regulation by the S. cerevisiae histone methyltransferase Set1.Current genetics · 2023Review
- Structural and functional specificity of H3K36 methylation.Epigenetics & chromatin · 2022Review
- SETD4-mediated KU70 methylation suppresses apoptosis.Cell reports · 2022Article
- Histidine methyltransferase SETD3 methylates structurally diverse histidine mimics in actin.Protein science : a publication of the Protein Society · 2022Article
- Methyltransferase SET domain family and its relationship with cardiovascular development and diseases.Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2022Article
- Stabilization of SETD3 by deubiquitinase USP27 enhances cell proliferation and hepatocellular carcinoma progression.Cellular and molecular life sciences : CMLS · 2022Article
- SETD3 Methyltransferase Regulates PLK1 Expression to PromoteFrontiers in oncology · 2022Article
- Changes of Gene Expression Patterns of Muscle Pathophysiology-Related Transcription Factors During Denervated Muscle Atrophy.Frontiers in physiology · 2022Article
- The Structure, Activity, and Function of the SETD3 Protein Histidine Methyltransferase.Life (Basel, Switzerland) · 2021Review
- SETD3 Downregulation Mediates PTEN Upregulation-Induced Ischemic Neuronal Death Through Suppression of Actin Polymerization and Mitochondrial Function.Molecular neurobiology · 2021Article
- WHSC1/NSD2 regulates immune infiltration in prostate cancer.Journal for immunotherapy of cancer · 2021Article
- SVFX: a machine learning framework to quantify the pathogenicity of structural variants.Genome biology · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Histone lysine methylation, as one of the most important factors in transcriptional regulation, is associated with a various physiological conditions. Using a bioinformatics search, we identified and subsequently cloned mouse SET domain containing 3 (SETD3) with SET (Su(var)3-9, Enhancer-of-zeste and Trithorax) and Rubis-subs-bind domains. SETD3 is a novel histone H3K4 and H3K36 methyltransferase with transcriptional activation activity. SETD3 is expressed abundantly in muscular tissues and, when overexpressed, activates transcription of muscle-related genes, myogenin, muscle creatine kinase (MCK), and myogenic factor 6 (Myf6), thereby inducing muscle cell differentiation. Conversely, knockdown of SETD3 by shRNA significantly retards muscle cell differentiation. In this study, SETD3 was recruited to the myogenin gene promoter along with MyoD where it activated transcription. Together, these data indicate that SETD3 is a H3K4/K36 methyltransferase and plays an important role in the transcriptional regulation of muscle cell differentiation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.