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

A remodeled protein arginine methyltransferase 1 (PRMT1) generates symmetric dimethylarginine.

The Journal of biological chemistry - 28 Mar 2014

Gui Shanying, Gathiaka Symon, Li Jun, Qu Jun, Acevedo Orlando, Hevel Joan M

Abstract excerpt

Protein arginine methylation is emerging as a significant post-translational modification involved in various cell processes and human diseases. As the major arginine methylation enzyme, protein arginine methyltransferase 1 (PRMT1) strictly generates monomethylarginine and asymmetric dimethylarginine (ADMA), but not symmetric dimethylarginine (SDMA). The two types of dimethylarginines can lead to distinct...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Catalytic Domain
Share to Molecular Dynamics Simulation

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

Share to Mutation

Share to Protein-Arginine N-Methyltransferases

Share to Substrate Specificity

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 24478314
DOI: 10.1074/jbc.M113.535278
PMCID: PMC3979365

Genes

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

A remodeled protein arginine methyltransferase 1 (PRMT1) generates symmetric dimethylarginine.PMID 24478314Read ↗

Unraveling the Origins of Changing Product Specificity Properties of Arginine Methyltransferase PRMT7 by the E181D and E181D/Q329A Mutations through QM/MM MD and Free-Energy Simulations.Semantic proximity Read ↗

Transient Kinetics Define a Complete Kinetic Model for Protein Arginine Methyltransferase 1.Semantic proximity Read ↗

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

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

Peptide backbone conformation affects the substrate preference of protein arginine methyltransferase I.Semantic proximity Read ↗

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

Structural and biochemical evaluation of bisubstrate inhibitors of protein arginine N-methyltransferases PRMT1 and CARM1 (PRMT4).Semantic proximity Read ↗

Oligomerization of PRMT1 Regulated RNA-Binding Protein Cascade Promotes Pancreatic Ductal AdenocarcinomaSemantic proximity Read ↗

Selective Targeting of Protein Arginine Methyltransferase 1 (PRMT1) Mutant Activity by a Small Molecule Activation Strategy.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 ↗

Role of active site arginine residues in substrate recognition by PPM1A.Semantic proximity Read ↗

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