Protein-Arginine N-Methyltransferases
"Protein-Arginine N-Methyltransferases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Enzymes that catalyze the methylation of arginine residues of proteins to yield N-mono- and N,N-dimethylarginine. This enzyme is found in many organs, primarily brain and spleen.
| Descriptor ID |
D011484
|
| MeSH Number(s) |
D08.811.913.555.500.800.750
|
| Concept/Terms |
Protein-Arginine N-Methyltransferases- Protein-Arginine N-Methyltransferases
- N-Methyltransferases, Protein-Arginine
- Protein Arginine N Methyltransferases
- Protein Arginine Methyltransferase
- Arginine Methyltransferase, Protein
- Methyltransferase, Protein Arginine
- Protein Methyltransferase I
- Protein-Arginine N-Methyltransferase
- N-Methyltransferase, Protein-Arginine
- Protein Arginine N Methyltransferase
- Arginine Methylase
- Protein Methylase I
|
Below are MeSH descriptors whose meaning is more general than "Protein-Arginine N-Methyltransferases".
Below are MeSH descriptors whose meaning is more specific than "Protein-Arginine N-Methyltransferases".
This graph shows the total number of publications written about "Protein-Arginine N-Methyltransferases" by people in this website by year, and whether "Protein-Arginine N-Methyltransferases" was a major or minor topic of these publications.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 2009 | 1 | 0 | 1 |
| 2011 | 0 | 1 | 1 |
| 2013 | 1 | 0 | 1 |
| 2015 | 1 | 0 | 1 |
| 2016 | 3 | 0 | 3 |
| 2018 | 1 | 0 | 1 |
| 2020 | 1 | 1 | 2 |
| 2023 | 1 | 0 | 1 |
To return to the timeline,
click here.
Below are the most recent publications written about "Protein-Arginine N-Methyltransferases" by people in Profiles.
-
Mady LJ, Zhong Y, Dhawan P, Christakos S. Role of Coactivator Associated Arginine Methyltransferase 1 (CARM1) in the Regulation of the Biological Function of 1,25-Dihydroxyvitamin D3. Cells. 2023 05 17; 12(10).
-
Barbarino M, Cesari D, Bottaro M, Luzzi L, Namagerdi A, Bertolino FM, Bellan C, Proietti F, Somma P, Micheli M, de Santi MM, Guazzo R, Mutti L, Pirtoli L, Paladini P, Indovina P, Giordano A. PRMT5 silencing selectively affects MTAP-deleted mesothelioma: In vitro evidence of a novel promising approach. J Cell Mol Med. 2020 05; 24(10):5565-5577.
-
Karakashev S, Fukumoto T, Zhao B, Lin J, Wu S, Fatkhutdinov N, Park PH, Semenova G, Jean S, Cadungog MG, Borowsky ME, Kossenkov AV, Liu Q, Zhang R. EZH2 Inhibition Sensitizes CARM1-High, Homologous Recombination Proficient Ovarian Cancers to PARP Inhibition. Cancer Cell. 2020 02 10; 37(2):157-167.e6.
-
Kafková L, Tu C, Pazzo KL, Smith KP, Debler EW, Paul KS, Qu J, Read LK. Trypanosoma brucei PRMT1 Is a Nucleic Acid Binding Protein with a Role in Energy Metabolism and the Starvation Stress Response. mBio. 2018 12 18; 9(6).
-
Kafková L, Debler EW, Fisk JC, Jain K, Clarke SG, Read LK. The Major Protein Arginine Methyltransferase in Trypanosoma brucei Functions as an Enzyme-Prozyme Complex. J Biol Chem. 2017 02 10; 292(6):2089-2100.
-
Jain K, Warmack RA, Debler EW, Hadjikyriacou A, Stavropoulos P, Clarke SG. Protein Arginine Methyltransferase Product Specificity Is Mediated by Distinct Active-site Architectures. J Biol Chem. 2016 08 26; 291(35):18299-308.
-
Debler EW, Jain K, Warmack RA, Feng Y, Clarke SG, Blobel G, Stavropoulos P. A glutamate/aspartate switch controls product specificity in a protein arginine methyltransferase. Proc Natl Acad Sci U S A. 2016 Feb 23; 113(8):2068-73.
-
Epstein DM, Buck E. Old dog, new tricks: extracellular domain arginine methylation regulates EGFR function. J Clin Invest. 2015 Dec; 125(12):4320-2.
-
Abbas T, Mueller AC, Shibata E, Keaton M, Rossi M, Dutta A. CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-Set7/Set8-mediated cellular migration. Mol Cell. 2013 Mar 28; 49(6):1147-58.
-
Kirino Y. [Role of arginine methylation in the Piwi-interacting RNA pathway]. Seikagaku. 2011 Apr; 83(4):312-6.