ReviewProgress in molecular biology and translational science2009
Roles of histone H3-lysine 4 methyltransferase complexes in NR-mediated gene transcription.
Review in Progress in molecular biology and translational science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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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.
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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.
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Who cites it
23 citing papers in PubMed, 35 citations in OpenAlex.
- Article
- Bile acid metabolism and signaling in health and disease: molecular mechanisms and therapeutic targets.Signal transduction and targeted therapy · 2024Review
- Circadian clock function does not require the histone methyltransferase MLL3.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- CaSWC4 regulates the immunity-thermotolerance tradeoff by recruiting CabZIP63/CaWRKY40 to target genes and activating chromatin in pepper.PLoS genetics · 2022Article
- Article
- The histone H3-lysine 4-methyltransferase Mll4 regulates the development of growth hormone-releasing hormone-producing neurons in the mouse hypothalamus.Nature communications · 2021Article
- Epigenetics and Beyond: Targeting Histone Methylation to Treat Type 2 Diabetes Mellitus.Frontiers in pharmacology · 2021Review
- KMT2C/D COMPASS complex-associated diseases [KClinical epigenetics · 2020Review
- UBE3A Suppresses Overnutrition-Induced Expression of the Steatosis Target Genes of MLL4 by Degrading MLL4.Hepatology (Baltimore, Md.) · 2019Article
- Identification and functional characterization of Lys-trimethylation of lactate dehydrogenase A.OncoTargets and therapy · 2019Article
- Alterations of Histone Modifications Contribute to Pregnane X Receptor-Mediated Induction of CYP3A4 by Rifampicin.Molecular pharmacology · 2017Article
- SET/MLL family proteins in hematopoiesis and leukemia.International journal of hematology · 2017Review
- Epigenetics in preimplantation mammalian development.Theriogenology · 2016Review
- Epigenetic Modulation of Human Podocyte Vitamin D Receptor in HIV Milieu.Journal of molecular biology · 2015Article
- Critical Roles of the LIM Domains of Lhx3 in Recruiting Coactivators to the Motor Neuron-Specifying Isl1-Lhx3 Complex.Molecular and cellular biology · 2015Article
- Nuclear receptors and epigenetic regulation: opportunities for nutritional targeting and disease prevention.Advances in nutrition (Bethesda, Md.) · 2014Review
- A role for WDR5 in integrating threonine 11 phosphorylation to lysine 4 methylation on histone H3 during androgen signaling and in prostate cancer.Molecular cell · 2014Article
- Histone H3K27 trimethylation inhibits H3 binding and function of SET1-like H3K4 methyltransferase complexes.Molecular and cellular biology · 2013Article
- Epigenomic regulation of bile acid metabolism: emerging role of transcriptional cofactors.Molecular and cellular endocrinology · 2013Review
- Skirting the pitfalls: a clear-cut nomenclature for H3K4 methyltransferases.Clinical genetics · 2013Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Transcriptional regulation by nuclear hormone receptors (NRs) requires multiple coregulators that modulate chromatin structures by catalyzing a diverse array of posttranslational modifications of histones. Different combinations of these modifications yield dynamic functional outcomes, constituting an epigenetic histone code. This code is inscribed by histone-modifying enzymes and decoded by effector proteins that recognize specific covalent marks. One important modification associated with active chromatin structures is methylation of histone H3-lysine 4 (H3K4). Crucial roles for this modification in NR transactivation have been recently highlighted through our purification and subsequent characterization of a steady-state complex associated with ASC-2, a coactivator of NRs and other transcription factors. This complex, designated ASCOM for ASC-2 complex, contains H3K4-methyltransferase MLL3/HALR or its paralogue MLL4/ALR and represents the first Set1-like H3K4-methyltransferase complex to be reported in vertebrates. This review focuses on recent progress in our understanding of how ASCOM-MLL3 and ASCOM-MLL4 influence NR-mediated gene transcription and of their physiological function.
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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.