The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Protein Arginine Methylation in Mammals: Who, What, and Why
Open accessAbstract
The covalent marking of proteins by methyl group addition to arginine residues can promote their recognition by binding partners or can modulate their biological activity. A small family of gene products that catalyze such methylation reactions in eukaryotes (PRMTs) work in conjunction with a changing cast of associated subunits to recognize distinct cellular substrates. These reactions display many of the attributes of reversible covalent modifications such as protein phosphorylation or protein lysine methylation; however, it is unclear to what extent protein arginine demethylation occurs. Physiological roles for protein arginine methylation have been established in signal transduction, mRNA splicing, transcriptional control, DNA repair, and protein translocation.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Luscombe, N. M. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.13.2860 · Cited by 981
Protein lysine methyltransferase G9a acts on non-histone targets
Rathert, P., Dhayalan, A., Murakami, M., Zhang, X., Tamas, R., Jurkowska, R., Komatsu, Y., Shinkai, Y., Cheng, X., & Jeltsch, A. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.88 · Cited by 347
Cited by
Regulation of chromatin by histone modifications
Bannister, A. J., & Kouzarides, T. (2011) · Cell Research · doi:10.1038/cr.2011.22 · Cited by 6,012
Protein arginine methyltransferases and cancer
Yang, Y., & Bedford, M. T. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3409 · Cited by 1,083
Self-citationArginine Methylation: The Coming of Age
Blanc, R. S., & Richard, S. (2017) · Molecular Cell · doi:10.1016/j.molcel.2016.11.003 · Cited by 1,054
Regulation of nucleosome dynamics by histone modifications
Zentner, G. E., & Henikoff, S. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2470 · Cited by 923
Advances in Fmoc solid‐phase peptide synthesis
Behrendt, R., White, P., & Offer, J. (2016) · Journal of Peptide Science · doi:10.1002/psc.2836 · Cited by 760
Metadata
- Authors
- Bedford, M. T., & Clarke, S. G.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2009-01
- Volume
- 33
- Issue
- 1
- Pages
- 1-13
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2076142854
- Cited by
- 1,792
- References
- 2
- FWCI
- 36.73
- Type
- journal article
- Language
- en
- Open access
- bronze
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Protein Arginine Methylation in Mammals: Who, What, and Why. https://app.cochat.ai/papers/10.1016/j.molcel.2008.12.013
- The paper
- Bedford, M. T., & Clarke, S. G. (2009). Protein Arginine Methylation in Mammals: Who, What, and Why. Molecular Cell. https://doi.org/10.1016/j.molcel.2008.12.013
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.