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

Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition.

Nature communications - 24 May 2017

Shishkova Evgenia, Zeng Hao, Liu Fabao, Kwiecien Nicholas W, Hebert Alexander S, Coon Joshua J, Xu Wei

Abstract excerpt

Protein arginine methyltransferases (PRMTs) introduce arginine methylation, a post-translational modification with the increasingly eminent role in normal physiology and disease. PRMT4 or coactivator-associated arginine methyltransferase 1 (CARM1) is a propitious target for cancer therapy; however, few CARM1 substrates are known, and its mechanism of substrate recognition is poorly understood. Here we employed a...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Gene Knockout Techniques

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to MCF-7 Cells

Share to Methylation

Share to Molecular Targeted Therapy

Share to Proline

Share to Protein-Arginine N-Methyltransferases

Share to Tandem Mass Spectrometry

Source

Open in PubMed Open full text

Identifiers

PMID: 28537268
DOI: 10.1038/ncomms15571
PMCID: PMC5458078

Genes

CARM1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition.PMID 28537268Read ↗

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

Decoding isozyme-specific substrate recognition in protein arginine deiminases by proteome-wide citrullination mappingSemantic 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 ↗

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

Automethylation of CARM1 allows coupling of transcription and mRNA splicing.Semantic proximity Read ↗

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

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

Machine learning-based exploration of enzyme-substrate networks: SET8-mediated methyllysine and its changing impact within cancer proteomesSemantic proximity Read ↗

HDAC6 Substrate Discovery Using Proteomics-Based Substrate Trapping: HDAC6 Deacetylates PRMT5 to Influence Methyltransferase Activity.Semantic proximity Read ↗

Structural basis for substrate recognition by the human N-terminal methyltransferase 1.Semantic proximity Read ↗

Expression and sub-cellular localization of an epigenetic regulator, co-activator arginine methyltransferase 1 (CARM1), is associated with specific breast cancer subtypes and ethnicitySemantic proximity Read ↗

Tyrosine phosphorylation of CARM1 promotes its enzymatic activity and alters its target specificity.Semantic proximity Read ↗

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