ArticleProtein science : a publication of the Protein Society2024
Oligomerization of protein arginine methyltransferase 1 and its effect on methyltransferase activity and substrate specificity.
Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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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Who cites it
5 citing papers in PubMed.
- Negative allosteric regulation of protein arginine methyltransferase 1 (PRMT1) through half-of-sites reactivity.The Journal of biological chemistry · 2026Article
- PRMT1 oligomerization regulates RNA-binding protein cascade to promote pancreatic cancer.Life science alliance · 2025Article
- Review
- Hetero-oligomeric interaction as a new regulatory mechanism for protein arginine methyltransferases.Biochemical Society transactions · 2024Review
- Oligomerization of protein arginine methyltransferase 1 and its effect on methyltransferase activity and substrate specificity.Protein science : a publication of the Protein Society · 2024Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Proper protein arginine methylation by protein arginine methyltransferase 1 (PRMT1) is critical for maintaining cellular health, while dysregulation is often associated with disease. How the activity of PRMT1 is regulated is therefore paramount, but is not clearly understood. Several studies have observed higher order oligomeric species of PRMT1, but it is unclear if these exist at physiological concentrations and there is confusion in the literature about how oligomerization affects activity. We therefore sought to determine which oligomeric species of PRMT1 are physiologically relevant, and quantitatively correlate activity with specific oligomer forms. Through quantitative western blotting, we determined that concentrations of PRMT1 available in a variety of human cell lines are in the sub-micromolar to low micromolar range. Isothermal spectral shift binding data were modeled to a monomer/dimer/tetramer equilibrium with an EC
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Registered trials
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