ArticleCell reports methods2021
Global analysis of protein arginine methylation.
Article in Cell reports methods, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed, 54 citations in OpenAlex.
- Targeting PRMTs with small-molecule inhibitors: a comprehensive review.RSC medicinal chemistry · 2026Review
- The N-terminal extension of ribosomal protein Rps2 shapes its early fate through Chaperone-Importin competition and arginine methylation.The Journal of biological chemistry · 2026Article
- Negative allosteric regulation of protein arginine methyltransferase 1 (PRMT1) through half-of-sites reactivity.The Journal of biological chemistry · 2026Article
- Homocysteine and S-adenosyl-L-homocysteine impair development and methylation in yeast and flies.Disease models & mechanisms · 2026Article
- The Role of Histone Methylation in Heart Failure: Epigenetic Mechanisms and Therapeutic Perspectives.Drug design, development and therapy · 2026Review
- An NMR-Based Approach for Global Arginine Methylation Analysis.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Protein arginine methylation regulates anti-inflammatory programming in response to aging stress.iScience · 2025Article
- Cardiac-specific overexpression of PRMT5 exacerbates pressure overload-induced hypertrophy and heart failure.Journal of biomedical science · 2025Article
- Protein Arginine Methyltransferases from Regulatory Function to Clinical Implication in Central Nervous System.Cellular and molecular neurobiology · 2025Review
- BRD9 functions as a methylarginine reader to regulate AKT-EZH2 signaling.Science advances · 2025Article
- Spatial recognition and semi-quantification of epigenetic events in pancreatic cancer subtypes with multiplexed molecular imaging and machine learning.Scientific reports · 2025Article
- Prmt5 is essential for intestinal stem cell maintenance and homeostasis.Cell regeneration (London, England) · 2025Article
- Metabolic labeling based methylome profiling enables functional dissection of histidine methylation in C3H1 zinc fingers.Nature communications · 2024Article
- Oligomerization of protein arginine methyltransferase 1 and its effect on methyltransferase activity and substrate specificity.Protein science : a publication of the Protein Society · 2024Article
- Article
- Exploring Residue-Level Interactions between the Biofilm-Driving R2ab Protein and Polystyrene Nanoparticles.Langmuir : the ACS journal of surfaces and colloids · 2024Article
- New insight into arginine and tryptophan metabolism in macrophage activation during tuberculosis.Frontiers in immunology · 2024Review
- The arginine methyltransferase Prmt1 coordinates the germline arginine methylome essential for spermatogonial homeostasis and male fertility.Nucleic acids research · 2023Article
- Exploring the Residue-Level Interactions between the R2ab Protein and Polystyrene Nanoparticles.bioRxiv : the preprint server for biology · 2023Article
- Chemical probes and methods for the study of protein arginine methylation.RSC chemical biology · 2023Review
Corrections and comments
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Authors and funding
23 authors at 3 institutions in 2 countries.
Funding
Abstract
Quantitative information about the levels and dynamics of post-translational modifications (PTMs) is critical for an understanding of cellular functions. Protein arginine methylation (ArgMet) is an important subclass of PTMs and is involved in a plethora of (patho)physiological processes. However, because of the lack of methods for global analysis of ArgMet, the link between ArgMet levels, dynamics, and (patho)physiology remains largely unknown. We utilized the high sensitivity and robustness of nuclear magnetic resonance (NMR) spectroscopy to develop a general method for the quantification of global protein ArgMet. Our NMR-based approach enables the detection of protein ArgMet in purified proteins, cells, organoids, and mouse tissues. We demonstrate that the process of ArgMet is a highly prevalent PTM and can be modulated by small-molecule inhibitors and metabolites and changes in cancer and during aging. Thus, our approach enables us to address a wide range of biological questions related to ArgMet in health and disease.
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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 Socratic graph.