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.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

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 Histone-Arginine N-Methyltransferase Histone-Arginine N-Methyltransferase Histone Arginine N Methyltransferase N-Methyltransferase, Histone-Arginine Myelin Basic Protein (Arginine) Methyltransferase Myelin Basic Protein (Arginine) Methyltransferase (Myelin Basic Protein)-Arginine N-Methyltransferase

Below are MeSH descriptors whose meaning is more general than "Protein-Arginine N-Methyltransferases".

Chemicals and Drugs [D]
Enzymes and Coenzymes [D08]
Enzymes [D08.811]
Transferases [D08.811.913]
One-Carbon Group Transferases [D08.811.913.555]
Methyltransferases [D08.811.913.555.500]
Protein Methyltransferases [D08.811.913.555.500.800]
Protein-Arginine N-Methyltransferases [D08.811.913.555.500.800.750]

Below are MeSH descriptors whose meaning is related to "Protein-Arginine N-Methyltransferases".

Below are MeSH descriptors whose meaning is more specific than "Protein-Arginine N-Methyltransferases".

publications

Timeline | Most Recent

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.

Bar chart showing 18 publications over 11 distinct years, with a maximum of 3 publications in 2016

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
2009	1	1	2
2010	0	1	1
2011	0	1	1
2013	1	0	1
2015	2	0	2
2016	3	0	3
2018	1	0	1
2019	2	0	2
2020	1	1	2
2021	1	0	1
2023	1	1	2

Below are the most recent publications written about "Protein-Arginine N-Methyltransferases" by people in Profiles.

Ferrarotto R, Swiecicki PL, Zandberg DP, Baiocchi RA, Wesolowski R, Rodriguez CP, McKean M, Kang H, Monga V, Nath R, Palmisiano N, Babbar N, Sun W, Hanna GJ. PRT543, a protein arginine methyltransferase 5 inhibitor, in patients with advanced adenoid cystic carcinoma: An open-label, phase I dose-expansion study. Oral Oncol. 2024 02; 149:106634.

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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).

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Genois MM, Gagn? JP, Yasuhara T, Jackson J, Saxena S, Langelier MF, Ahel I, Bedford MT, Pascal JM, Vindigni A, Poirier GG, Zou L. CARM1 regulates replication fork speed and stress response by stimulating PARP1. Mol Cell. 2021 02 18; 81(4):784-800.e8.

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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.

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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.

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Hashimoto H, Kafkov? L, Raczkowski A, Jordan KD, Read LK, Debler EW. Structural Basis of Protein Arginine Methyltransferase Activation by a Catalytically Dead Homolog (Prozyme). J Mol Biol. 2020 01 17; 432(2):410-426.

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Zhou Z, Feng Z, Hu D, Yang P, Gur M, Bahar I, Cristofanilli M, Gradishar WJ, Xie XQ, Wan Y. A novel small-molecule antagonizes PRMT5-mediated KLF4 methylation for targeted therapy. EBioMedicine. 2019 Jun; 44:98-111.

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Kafkov? 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).

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Kafkov? 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.

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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.

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