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.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2000 | 0 | 1 | 1 |
| 2004 | 0 | 1 | 1 |
| 2005 | 1 | 0 | 1 |
| 2006 | 1 | 1 | 2 |
| 2009 | 1 | 0 | 1 |
| 2010 | 0 | 1 | 1 |
| 2014 | 0 | 1 | 1 |
| 2015 | 1 | 0 | 1 |
| 2016 | 1 | 1 | 2 |
| 2017 | 2 | 0 | 2 |
| 2018 | 1 | 0 | 1 |
| 2019 | 1 | 0 | 1 |
| 2020 | 2 | 1 | 3 |
| 2021 | 2 | 1 | 3 |
| 2022 | 0 | 1 | 1 |
| 2023 | 1 | 1 | 2 |
| 2024 | 2 | 0 | 2 |
| 2025 | 1 | 0 | 1 |
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Below are the most recent publications written about "Protein-Arginine N-Methyltransferases" by people in Profiles.
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A feedback loop comprising PRMT7 and miR-24-2 interplays with Oct4, Nanog, Klf4 and c-Myc to regulate stemness. Nucleic Acids Res. 2016 12 15; 44(22):10603-10618.
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PRMT9 is a type II methyltransferase that methylates the splicing factor SAP145. Nat Commun. 2015 Mar 04; 6:6428.
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A gain-of-function mouse model identifies PRMT6 as a NF-?B coactivator. Nucleic Acids Res. 2014 Jul; 42(13):8297-309.
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A TR-FRET-based functional assay for screening activators of CARM1. Chembiochem. 2013 May 10; 14(7):827-35.
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Trans-tail regulation of MLL4-catalyzed H3K4 methylation by H4R3 symmetric dimethylation is mediated by a tandem PHD of MLL4. Genes Dev. 2012 Dec 15; 26(24):2749-62.
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Identification of small-molecule enhancers of arginine methylation catalyzed by coactivator-associated arginine methyltransferase 1. J Med Chem. 2012 Nov 26; 55(22):9875-90.
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Acyl derivatives of p-aminosulfonamides and dapsone as new inhibitors of the arginine methyltransferase hPRMT1. Bioorg Med Chem. 2011 Jun 15; 19(12):3717-31.
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Crosstalk between Arg?1175 methylation and Tyr?1173 phosphorylation negatively modulates EGFR-mediated ERK activation. Nat Cell Biol. 2011 Feb; 13(2):174-81.
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CARM1 is required for proper control of proliferation and differentiation of pulmonary epithelial cells. Development. 2010 Jul; 137(13):2147-56.
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PRMT5 regulates Golgi apparatus structure through methylation of the golgin GM130. Cell Res. 2010 Sep; 20(9):1023-33.