ReviewCells2025
Functional Dynamics of Arginine Mono- and Di-Methylation.
Review in Cells, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed.
- S-Adenosylmethionine-Dependent Methylation, Protein Arginine Methyltransferases and Cardiovascular Diseases.Biomolecules · 2026Review
- Biomarkers in Clinical Medicine Research: A Literature Survey in the PubMed Database and a Critical Evaluation.Journal of clinical medicine · 2026Review
- Assay for In-Vitro Arginine Methylation of RNA Binding Proteins Followed by RNA Binding.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Control of Gene Expression by Proteins That Bind Many Alternative Nucleic Acid Structures Through the Same Domain.International journal of molecular sciences · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arginine methylation is a crucial post-translational modification (PTM) that plays a significant role in various biological processes. It occurs in two primary forms: mono-methylation (MMA) and di-methylation (DMA), with the latter further classified into symmetric (SDMA) and asymmetric methylation (ADMA). This review examines the functional implications of these methylation states, current detection methodologies, proteomics-based analytical approaches, and the different impacts of these methylations on protein function. Finally, the role of protein arginine methyltransferases (PRMTs) and their substrate specificity in shaping the arginine methylome are discussed.
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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.