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ProteomicsProteome-wide identification of arginine methylation in colorectal cancer tissues from patients
High-throughput identification of arginine methylation using clinical samples has not previously been studied.
ORGANISM(S): Homo sapiens (Human) 
2020-08-05 | PXD011765 | Pride
Colorectal cancer Protein arginine methylation Mass spectrometry Asymmetric dimethyl-arginine Mono-methyl arginine 
ProteomicsMouse Muscle Quadricep Methylation CARM1 KO
CARM1 muscle KO mice were generated and quadricep muscle tissue was subjected to high pH strong cation exchange and immunoaffinity purification to enrich methyl peptides.
ORGANISM(S): Mus musculus (Mouse) 
2022-08-05 | PXD028884 | Pride
Arginine Carm1 Prmt4 Immunoaffinity Adma Methylation Mouse Sdma Lcms Muscle 
ProteomicsArginine (di)methylated Human Leukocyte Antigen class I peptides are favorably presented by HLA-B*07
Specific alterations in protein post-translational modification (PTMs) are recognized hallmarks of diseases. These modifications potentially provide a unique disease-related source of Human Leukocyte Antigen (HLA) class I-presented peptide antigens that can elicit specific immune responses. Although...
ORGANISM(S): Homo sapiens (Human) 
2016-08-15 | PXD004233 | Pride
Methylation Dimethylation Ethcd Hla-class i 
TranscriptomicsActin R256 mono-methylation is a conserved post-translational modification involved in transcription
Nuclear actin has been elusive due to the lack of molecular mechanisms. From actin-containing chromatin remodeling complexes, we discovered an arginine mono-methylation mark on evolutionarily conserved R256 residue of actin (R256me1). Actin R256 mutations in yeast affect nuclear functions, and cause...
ORGANISM(S): Saccharomyces cerevisiae 
2020-08-26 | GSE156817 | GEO
ProteomicsArginine methylation during transcriptional arrest
The covalent attachment of methyl groups to the side-chain of arginine residues is known to play essential roles in regulation of transcription, protein function and RNA metabolism. The specific N-methylation of arginine residues is catalyzed by a small family of gene products known as protein argin...
ORGANISM(S): Homo sapiens (Human) 
2019-11-25 | PXD000559 | Pride
Human cell culture 
UnknownInvestigation of the molecular origins of protein-arginine methyltransferase I (PRMT1) product specificity reveals a role for two conserved methionine residues.
Not available
S-EPMC3190719 | biostudies-literature
UnknownProteomic analysis of arginine methylation sites in human cells reveals dynamic regulation during transcriptional arrest.
Not available
S-EPMC4125738 | biostudies-literature
ProteomicsAntibodies against the mono-methylated Arginine-Glycine repeat (MMA-RG) of the Epstein-Barr virus nuclear antigen 1 (EBNA1) identify potential cellular proteins targeted in viral transformation
The viral nuclear antigen 1 (EBNA1) of Epstein Barr (EBV) features two functionally redundant Arginine-Glycine (RG) repeats that contain symmetrically and asymmetrically di-methylated (SDMA/ADMA) and also mono-methylated (MMA) Arginine residues. We generated mouse monoclonal antibodies against the m...
ORGANISM(S): Homo sapiens (Human) Human herpesvirus 4 
2025-03-05 | PXD051181 | Pride
Epstein-barr virus Arginine-methylation Ebna1 Mono-methyl-arginine 
ProteomicsChanges in protein arginine methylation by GSK3368712
Type I Protein Arginine Methyltransferases (PRMTs) catalyze asymmetric dimethylation of arginine residues on numerous proteins. Type I PRMTs and their substrates have been implicated in human cancers, suggesting that inhibiting Type I PRMT activity offers a tractable approach for therapeutic interve...
ORGANISM(S): Homo sapiens (Human) 
2019-09-10 | PXD012747 | Pride
Lc-msms Human Arginine methyltransferases Cancer cell lines Immunoproteomic Antibody Type i prmt Methylscan 
UnknownThe Identification of a Sub-Micromolar Peptide-Based Protein Arginine Methyltransferase 1 (PRMT1) Inhibitor from a Plate-Based Screening Assay.
Not available
S-EPMC12650519 | biostudies-literature
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