ArticleMethods (San Diego, Calif.)2022
Pan-methylarginine antibody generation using PEG linked GAR motifs as antigens.
Article in Methods (San Diego, Calif.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 13 citations in OpenAlex.
- Acquired Resistance to the PRMT5 Inhibitor Confers Collateral Sensitivity to MEK Inhibition inBiomolecules · 2026Article
- Selective Targeting of Protein Arginine Methyltransferase 1 (PRMT1) Mutant Activity by a Small Molecule Activation Strategy.ACS chemical biology · 2026Article
- Acquired resistance to the PRMT5 inhibitor confers collateral sensitivity to MEK inhibition in MTAP-null non-small cell lung cancer.bioRxiv : the preprint server for biology · 2026Article
- Development of motif-specific monoclonal antibodies for global protein citrullination detection with minimal cross-reactivity to homocitrullination.Cell reports methods · 2026Article
- Regulation of protein arginine methyltransferase in osteoporosis: a narrative review.Frontiers in cell and developmental biology · 2025Review
- SART3 reads methylarginine-marked glycine- and arginine-rich motifs.Cell reports · 2024Article
- PRMT blockade induces defective DNA replication stress response and synergizes with PARP inhibition.Cell reports. Medicine · 2023Article
- PRMT1 orchestrates with SAMTOR to govern mTORC1 methionine sensing via Arg-methylation of NPRL2.Cell metabolism · 2023Article
- Autophagy dictates sensitivity to PRMT5 inhibitor in breast cancer.Scientific reports · 2023Article
- Effectors and effects of arginine methylation.Biochemical Society transactions · 2023Article
- Article
- Asymmetric and symmetric protein arginine methylation in methionine-addicted human cancer cells.PloS one · 2023Article
- Arginine methylation of BRD4 by PRMT2/4 governs transcription and DNA repair.Science advances · 2022Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Arginine methylation is a prevalent posttranslational modification which is deposited by a family of protein arginine methyltransferases (PRMTs), and is found in three different forms in mammalian cells: monomethylarginine (MMA), asymmetric dimethylarginine (ADMA) and symmetric dimethylarginine (SDMA). Pan-methylarginine antibodies are critical for identifying proteins that are methylated on arginine residues, and are also used for evaluating signaling pathways that modulate this methyltransferase activity. Although good pan-MMA, -ADMA and -SDMA antibodies have been developed over the years, there is still room for improvement. Here we use a novel antigen approach, which involves the separation of short methylated motifs with inert polyethylene glycol (PEG) linkers, to generate a set of pan antibodies to the full range of methylarginine marks. Using these antibodies, we observed substrate scavenging by PRMT1, when PRMT5 activity is blocked. Specifically, we find that the splicing factor SmD1 displays increased ADMA levels upon PRMT5 inhibitor treatment. Furthermore, when the catalysis of both SDMA and ADMA is blocked with small molecule inhibitors, we demonstrate that SmD1 and SMN no longer interact. This could partially explain the synergistic effect of PRMT5 and type I PRMT inhibition on RNA splicing and cancer cell growth.
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Registered trials
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