ArticleJournal of the American Chemical Society2016
Nucleosome Binding Alters the Substrate Bonding Environment of Histone H3 Lysine 36 Methyltransferase NSD2.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Assembling Ternary Dead-End Complex for Covalent Trapping of Protein Lysine Methyltransferases.Journal of the American Chemical Society · 2026Article
- Identification of potential methyltransferase NSD2 enzymatic inhibitors through a multi-step structure-based drug design.Molecular diversity · 2025Article
- Epigenetic Modulators as Therapeutic Agents in Cancer.International journal of molecular sciences · 2023Review
- Allosteric regulation of histone lysine methyltransferases: from context-specific regulation to selective drugs.Biochemical Society transactions · 2021Review
- The Role of Methyltransferase NSD2 as a Potential Oncogene in Human Solid Tumors.OncoTargets and therapy · 2020Review
- Substrate-Differentiated Transition States of SET7/9-Catalyzed Lysine Methylation.Journal of the American Chemical Society · 2019Article
- NSD2 promotes ventricular remodelling mediated by the regulation of H3K36me2.Journal of cellular and molecular medicine · 2019Article
- Chemical and Biochemical Perspectives of Protein Lysine Methylation.Chemical reviews · 2018Review
- The Transition-State Structure for Human MAT2A from Isotope Effects.Journal of the American Chemical Society · 2017Article
- The Role of Nuclear Receptor-Binding SET Domain Family Histone Lysine Methyltransferases in Cancer.Cold Spring Harbor perspectives in medicine · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Nuclear receptor-binding SET domain protein 2 (NSD2) is a histone H3 lysine 36 (H3K36)-specific methyltransferase enzyme that is overexpressed in a number of cancers, including multiple myeloma. NSD2 binds to S-adenosyl-l-methionine (SAM) and nucleosome substrates to catalyze the transfer of a methyl group from SAM to the ε-amino group of histone H3K36. Equilibrium binding isotope effects and density functional theory calculations indicate that the SAM methyl group is sterically constrained in complex with NSD2, and that this steric constraint is released upon nucleosome binding. Together, these results show that nucleosome binding to NSD2 induces a significant change in the chemical environment of enzyme-bound SAM.
Indexed as
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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.