Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Automethylation of protein arginine methyltransferase 8 (PRMT8) regulates activity by impeding S-adenosylmethionine sensitivity.

The Journal of biological chemistry - 27 Sept 2013

Dillon Myles B C, Rust Heather L, Thompson Paul R, Mowen Kerri A

Abstract excerpt

Protein arginine methyltransferase (PRMT) 8 is unique among the PRMTs, as it has a highly restricted tissue expression pattern and an N terminus that contains two automethylation sites and a myristoylation site. PRMTs catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a peptidylarginine on a protein substrate. Currently, the physiological roles, regulation, and cellular substrates of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalysis
Share to HeLa Cells
Share to Lysine

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Methylation

Share to Phenylalanine

Share to Protein-Arginine N-Methyltransferases

Share to Protein Processing, Post-Translational

Share to S-Adenosylmethionine

Source

Open in PubMed Open full text

Identifiers

PMID: 23946480
DOI: 10.1074/jbc.M113.491092
PMCID: PMC3784702

Genes

PRMT8
PRMT1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Automethylation of protein arginine methyltransferase 8 (PRMT8) regulates activity by impeding S-adenosylmethionine sensitivity.PMID 23946480Read ↗

Profiling substrates of protein arginine N-methyltransferase 3 with S-adenosyl-L-methionine analogues.Semantic proximity Read ↗

Transcriptomic and proteomic regulation through abundant, dynamic, and independent arginine methylation by Type I and Type II PRMTsSemantic proximity Read ↗

A systematic survey of PRMT interactomes reveals key roles of arginine methylation in the global control of RNA splicing and translationSemantic proximity Read ↗

Substrate specificity of human protein arginine methyltransferase 7 (PRMT7): the importance of acidic residues in the double E loop.Semantic proximity Read ↗

Insights into S-adenosyl-l-methionine (SAM)-dependent methyltransferase related diseases and genetic polymorphisms.Semantic proximity Read ↗

A remodeled protein arginine methyltransferase 1 (PRMT1) generates symmetric dimethylarginine.Semantic proximity Read ↗

Protein Arginine Methylation and Citrullination in Epigenetic RegulationSemantic proximity Read ↗

Functional Implications of Protein Arginine Methyltransferases (PRMTs) in Neurodegenerative DiseasesSemantic proximity Read ↗

Proteomic Analysis of Arginine Methylation Sites in Human Cells Reveals Dynamic Regulation During Transcriptional ArrestSemantic proximity Read ↗

Designing Effective Protein Lysine and Arginine Methyltransferase Inhibitors for Chemotherapeutic TargetingSemantic proximity Read ↗

Discovery and characterisation of the automethylation properties of PRDM9.Semantic proximity Read ↗

Methionine adenosyltransferases in cancers: Mechanisms of dysregulation and implications for therapySemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.