Evidence map›Paper›PMID 36838987›Full record

ReviewMolecules (Basel, Switzerland)2023

Targeting Epigenetic Changes Mediated by Members of the SMYD Family of Lysine Methyltransferases.

Alyssa Padilla, John F Manganaro, Lydia Huesgen, Deborah A Roess, Mark A Brown, Debbie C Crans

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

12 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Special Issue "Protein Methyltransferases in Human Health and Diseases".International journal of molecular sciences · 2026
    Article
  3. Genes · 2026
    Article
  4. Article
  5. Review
  6. Review
  7. Direct lysine dimethylation of IRF3 by the methyltransferase SMYD3 attenuates antiviral innate immunity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Hsf1 is essential for proteotoxic stress response in smyd1b-deficient embryos and fish survival under heat shock.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. 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

6 authors at 2 institutions in 1 country.

Alyssa PadillaDepartment of Biomedical Sciences, Colorado State University, Fort Collins, CO 80523-1617, USA.
John F ManganaroDepartment of Chemistry, Colorado State University, Fort Collins, CO 80523-1872, USA.
Lydia HuesgenDepartment of Biomedical Sciences, Colorado State University, Fort Collins, CO 80523-1617, USA.
Deborah A RoessDepartment of Biomedical Sciences, Colorado State University, Fort Collins, CO 80523-1617, USA.
Mark A BrownCell and Molecular Biology Program, Colorado State University, Fort Collins, CO 80523-1005, USA.
Debbie C CransDepartment of Chemistry, Colorado State University, Fort Collins, CO 80523-1872, USA.ORCID 0000-0001-7792-3450
Colorado State University · USColorado School of Public Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A comprehensive understanding of the mechanisms involved in epigenetic changes in gene expression is essential to the clinical management of diseases linked to the SMYD family of lysine methyltransferases. The five known SMYD enzymes catalyze the transfer of donor methyl groups from S-adenosylmethionine (SAM) to specific lysines on histones and non-histone substrates. SMYDs family members have distinct tissue distributions and tissue-specific functions, including regulation of development, cell differentiation, and embryogenesis. Diseases associated with SMYDs include the repressed transcription of SMYD1 genes needed for the formation of ion channels in the heart leading to heart failure, SMYD2 overexpression in esophageal squamous cell carcinoma (ESCC) or p53-related cancers, and poor prognosis associated with SMYD3 overexpression in more than 14 types of cancer including breast cancer, colon cancer, prostate cancer, lung cancer, and pancreatic cancer. Given the importance of epigenetics in various pathologies, the development of epigenetic inhibitors has attracted considerable attention from the pharmaceutical industry. The pharmacologic development of the inhibitors involves the identification of molecules regulating both functional SMYD SET (Suppressor of variegation, Enhancer of Zeste, Trithorax) and MYND (Myeloid-Nervy-DEAF1) domains, a process facilitated by available X-ray structures for SMYD1, SMYD2, and SMYD3. Important leads for potential pharmaceutical agents have been reported for SMYD2 and SMYD3 enzymes, and six epigenetic inhibitors have been developed for drugs used to treat myelodysplastic syndrome (Vidaza, Dacogen), cutaneous T-cell lymphoma (Zoinza, Isrodax), and peripheral T-cell lymphoma (Beleodag, Epidaza). The recently demonstrated reversal of SMYD histone methylation suggests that reversing the epigenetic effects of SMYDs in cancerous tissues may be a desirable target for pharmacological development.

Indexed as

Epigenesis, GeneticHistone-Lysine N-MethyltransferaseDNA-Binding ProteinsHistonesHumansLysineNeoplasmsTranscription FactorsDEAF1 protein, humanDNA-Binding ProteinsHistone-Lysine N-MethyltransferaseHistonesLysineSMYD2 protein, humanSMYD3 protein, humanTranscription Factorsbreast cancercancerscardiac tissueepigenetic drugsleukemialysine methyltransferasesMYNDrepressed transcription of SMYD genesSMYD proteinsSMYD SET

Identifiers

PMID36838987
PMCPMC9967872
OpenAlexW4321458353

What Socratic 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 Socratic graph.