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
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MeSH Number(s) |
D08.811.913.555.500.800.750
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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
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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 |
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2017 | 7 | 0 | 7 |
2018 | 3 | 0 | 3 |
2019 | 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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PRMT5 enhances tumorigenicity and glycolysis in pancreatic cancer via the FBW7/cMyc axis. Cell Commun Signal. 2019 03 29; 17(1):30.
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Discovery of 2-substituted-N-(3-(3,4-dihydroisoquinolin-2(1H)-yl)-2-hydroxypropyl)-1,2,3,4-tetrahydroisoquinoline-6-carboxamide as potent and selective protein arginine methyltransferases 5 inhibitors: Design, synthesis and biological evaluation. Eur J Med Chem. 2019 Feb 15; 164:317-333.
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Protein arginine methyltransferase 5 mediates enolase-1 cell surface trafficking in human lung adenocarcinoma cells. Biochim Biophys Acta Mol Basis Dis. 2018 May; 1864(5 Pt A):1816-1827.
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Upregulation of PRMT6 by LPS suppresses Klotho expression through interaction with NF-?B in glomerular mesangial cells. J Cell Biochem. 2018 04; 119(4):3404-3416.
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Development of an AlphaLISA high throughput technique to screen for small molecule inhibitors targeting protein arginine methyltransferases. Mol Biosyst. 2017 Nov 21; 13(12):2509-2520.
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Development of Potent Type I Protein Arginine Methyltransferase (PRMT) Inhibitors of Leukemia Cell Proliferation. J Med Chem. 2017 11 09; 60(21):8888-8905.
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Crosstalk between histone modifications indicates that inhibition of arginine methyltransferase CARM1 activity reverses HIV latency. Nucleic Acids Res. 2017 Sep 19; 45(16):9348-9360.
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Potent, Selective, and Cell Active Protein Arginine Methyltransferase 5 (PRMT5) Inhibitor Developed by Structure-Based Virtual Screening and Hit Optimization. J Med Chem. 2017 07 27; 60(14):6289-6304.
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Adapting AlphaLISA high throughput screen to discover a novel small-molecule inhibitor targeting protein arginine methyltransferase 5 in pancreatic and colorectal cancers. Oncotarget. 2017 Jun 20; 8(25):39963-39977.
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PRMT5 restricts hepatitis B virus replication through epigenetic repression of covalently closed circular DNA transcription and interference with pregenomic RNA encapsidation. Hepatology. 2017 08; 66(2):398-415.