Title |
Protein Arginine Methylation in Mammals: Who, What, and Why
|
---|---|
Published in |
Molecular Cell, January 2009
|
DOI | 10.1016/j.molcel.2008.12.013 |
Pubmed ID | |
Authors |
Mark T. Bedford, Steven G. Clarke |
Abstract |
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) works 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. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
United States | 8 | <1% |
United Kingdom | 6 | <1% |
Brazil | 3 | <1% |
France | 3 | <1% |
Switzerland | 2 | <1% |
Denmark | 2 | <1% |
Japan | 2 | <1% |
Argentina | 2 | <1% |
Italy | 1 | <1% |
Other | 9 | <1% |
Unknown | 976 | 96% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 263 | 26% |
Researcher | 143 | 14% |
Student > Master | 138 | 14% |
Student > Bachelor | 98 | 10% |
Student > Doctoral Student | 46 | 5% |
Other | 144 | 14% |
Unknown | 182 | 18% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 346 | 34% |
Biochemistry, Genetics and Molecular Biology | 270 | 27% |
Chemistry | 71 | 7% |
Medicine and Dentistry | 52 | 5% |
Pharmacology, Toxicology and Pharmaceutical Science | 23 | 2% |
Other | 61 | 6% |
Unknown | 191 | 19% |