ReviewEpigenetics2011
Substrate and product specificities of SET domain methyltransferases.
Review in Epigenetics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 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
70 citing papers in PubMed, 135 citations in OpenAlex.
- Article
- Homocysteine and S-adenosyl-L-homocysteine impair development and methylation in yeast and flies.Disease models & mechanisms · 2026Article
- Update of the Methyltransferase Gene Family: Classification, Evolution and Biological Functions.Human genomics · 2026Review
- Mechanistic Insights into SAM-Dependent Methyltransferases: A Review of Computational Approaches.International journal of molecular sciences · 2025Review
- The epigenetic landscape of fate decisions in T cells.Nature immunology · 2025Review
- Menin inhibitors for the treatment of acute myeloid leukemia: challenges and opportunities ahead.Journal of hematology & oncology · 2024Review
- Comparative genome-wide identification and characterization of SET domain-containing and JmjC domain-containing proteins in piroplasms.BMC genomics · 2024Article
- KMT2A and chronic inflammation as potential drivers of sporadic parathyroid adenoma.Clinical and translational medicine · 2024Article
- NovelHeliyon · 2024Article
- Epigenetic Modulators as Therapeutic Agents in Cancer.International journal of molecular sciences · 2023Review
- The Roles of Histone Lysine Methyltransferases in Heart Development and Disease.Journal of cardiovascular development and disease · 2023Review
- Novel investigational approaches for high-risk genetic subsets of AML: TP53, KMT2A, FLT3.Hematology. American Society of Hematology. Education Program · 2022Article
- Review
- Exosomal telomerase transcripts reprogram the microRNA transcriptome profile of fibroblasts and partially contribute to CAF formation.Scientific reports · 2022Article
- Lysine methyltransferase inhibitors: where we are now.RSC chemical biology · 2022Review
- The Role of Lysine Methyltransferase SET7/9 in Proliferation and Cell Stress Response.Life (Basel, Switzerland) · 2022Review
- Structures and biological functions of zinc finger proteins and their roles in hepatocellular carcinoma.Biomarker research · 2022Review
- The Epigenetic Regulation of Nonhistone Proteins by SETD7: New Targets in Cancer.Frontiers in genetics · 2022Review
- New insights into the activities and toxicities of the old anticancer drug doxorubicin.The FEBS journal · 2021Review
- The WNT/β-catenin dependent transcription: A tissue-specific business.WIREs mechanisms of disease · 2021Review
10 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
SET domain lysine methyltransferases (KMTs) catalyze the site- and state-specific methylation of lysine residues in histone and non-histone substrates. These modifications play fundamental roles in transcriptional regulation, heterochromatin formation, X chromosome inactivation and DNA damage response, and have been implicated in the epigenetic regulation of cell identity and fate. The substrate and product specificities of SET domain KMTs are pivotal to eliciting these effects due to the distinct functions associated with site and state-specific protein lysine methylation. Here, we review advances in understanding the molecular basis of these specificities gained through structural and biochemical studies of the human methyltransferases Mixed Lineage Leukemia 1 (MLL1, also known as KMT2A) and SET7/9 (KMT7). We conclude by exploring the broader implications of these findings on the biological functions of protein lysine methylation by SET domain KMTs.
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.