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 26 publications over 14 distinct years, with a maximum of 4 publications in 2011

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

Year	Major Topic	Minor Topic	Total
2006	0	1	1
2007	1	0	1
2008	2	0	2
2009	1	0	1
2010	3	0	3
2011	3	1	4
2012	2	1	3
2013	2	0	2
2014	3	0	3
2015	1	0	1
2016	1	0	1
2018	1	0	1
2019	1	0	1
2022	0	2	2

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

Huang L, Zhang XO, Rozen EJ, Sun X, Sallis B, Verdejo-Torres O, Wigglesworth K, Moon D, Huang T, Cavaretta JP, Wang G, Zhang L, Shohet JM, Lee MM, Wu Q. PRMT5 activates AKT via methylation to promote tumor metastasis. Nat Commun. 2022 07 08; 13(1):3955.

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Creamer KM, Larsen EC, Lawrence JB. ZNF146/OZF and ZNF507 target LINE-1 sequences. G3 (Bethesda). 2022 03 04; 12(3).

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Moena D, Merino P, Lian JB, Stein GS, Stein JL, Montecino M. Switches in histone modifications epigenetically control vitamin D3-dependent transcriptional upregulation of the CYP24A1 gene in osteoblastic cells. J Cell Physiol. 2020 06; 235(6):5328-5339.

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Huang L, Liu J, Zhang XO, Sibley K, Najjar SM, Lee MM, Wu Q. Inhibition of protein arginine methyltransferase 5 enhances hepatic mitochondrial biogenesis. J Biol Chem. 2018 07 13; 293(28):10884-10894.

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Vhuiyan MI, Pak ML, Park MA, Thomas D, Lakowski TM, Chalfant CE, Frankel A. PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X. J Biochem. 2017 Jul 01; 162(1):17-25.

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LeBlanc SE, Wu Q, Lamba P, Sif S, Imbalzano AN. Promoter-enhancer looping at the PPAR?2 locus during adipogenic differentiation requires the Prmt5 methyltransferase. Nucleic Acids Res. 2016 06 20; 44(11):5133-47.

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Zhang L, Tran NT, Su H, Wang R, Lu Y, Tang H, Aoyagi S, Guo A, Khodadadi-Jamayran A, Zhou D, Qian K, Hricik T, C?t? J, Han X, Zhou W, Laha S, Abdel-Wahab O, Levine RL, Raffel G, Liu Y, Chen D, Li H, Townes T, Wang H, Deng H, Zheng YG, Leslie C, Luo M, Zhao X. Cross-talk between PRMT1-mediated methylation and ubiquitylation on RBM15 controls RNA splicing. Elife. 2015 Nov 17; 4.

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Lakowski TM, Pak ML, Szeitz A, Thomas D, Vhuiyan MI, Clement B, Frankel A. Arginine methylation in yeast proteins during stationary-phase growth and heat shock. Amino Acids. 2015 Dec; 47(12):2561-71.

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Wang M, Fuhrmann J, Thompson PR. Protein arginine methyltransferase 5 catalyzes substrate dimethylation in a distributive fashion. Biochemistry. 2014 Dec 23; 53(50):7884-92.

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Tibshirani M, Tradewell ML, Mattina KR, Minotti S, Yang W, Zhou H, Strong MJ, Hayward LJ, Durham HD. Cytoplasmic sequestration of FUS/TLS associated with ALS alters histone marks through loss of nuclear protein arginine methyltransferase 1. Hum Mol Genet. 2015 Feb 01; 24(3):773-86.

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