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MetabolomicsThe Metabolomics of Oral Biofilms exposed to Arginine and Fluoride
Not available
ORGANISM(S): Homo sapiens 
ST000583 | MetabolomicsWorkbench
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 
ProteomicsProteomics Profiling of Arginine Methylation Defines PRMT5 Substarate Specificity
Protein arginine methyltransferases (PRMTs) catalyze arginine methylation, an abundant post-translational modification occurring on both chromatin-bound and cytoplasmic proteins. Growing evidence supports the involvement of PRMT5, the major Type II PRMT, in pro-survival and differentiation pathways,...
ORGANISM(S): Homo sapiens (Human) 
2019-04-10 | PXD009070 | Pride
Lc-ms Prmt5 Arginine methylation 
ProteomicsSzewczyk_InhibitionOfPRMT7_P36_2020
This dataset consists of 16 raw MS files, acquired on Orbitrap Fusion Lumos Tribrid mass spectrometer operated in Data Dependent Acquisition (DDA) mode for the 8 input files and DDA with simultaneous parallel reaction monitoring (targeted masses; 599.33, 604.33, 608.23, 606.33, 407.89, 403.22, 651.3...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-01-08 | MSV000084773 | MassIVE
ProteomicsCharacterization of Arginine Methylation in Cancer Cell using LC-MS/MS
Protein arginine methyltransferase 9 (PRMT9) activity has been observed to be elevated in cancer patients, including many types of leukemias, correlating with poor prognosis and decreased response to immune checkpoint inhibitors. By targeting PRMT9, we can eliminate PRMT9-proficient/immune-cold canc...
ORGANISM(S): Homo sapiens (Human) 
2024-01-11 | PXD039441 | Pride
Lc-ms/ms 
ProteomicsProteomics profiling of arginine methylation mediated by PRMT family reveals a critical role of arginine methylation in RNA splicing and cancer cell growth
Protein arginine methylation, catalyzed by the protein arginine methyltransferase (PRMT) family, is recognized as a widespread post-translational modification (PTM) with implications in a plethora of biological processes in eukaryotes. PRMT proteins were classified into three types, type I, II and I...
ORGANISM(S): Homo sapiens (Human) 
2021-01-27 | PXD022424 | Pride
Arginine methylation Prmts Rna splicing 
ProteomicsTherapeutic targeting of RNA splicing catalysis through inhibition of protein arginine methylation
Cancer-associated mutations in RNA splicing factors commonly occur in myeloid and lymphoid leukemias as well as a variety of solid tumors and confer dependence on wild-type (WT) splicing. These observations have led to clinical efforts to directly inhibit the spliceosome in patients with refractory ...
ORGANISM(S): Homo sapiens (Human) 
2019-07-30 | PXD012007 | Pride
Prmt1 Prmt5 Leukemia Methylation 
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 
ProteomicsAn early, novel arginine methylation of KCa3.1 attenuates subsequent T cell exhaustion.
We identified changes in the protein arginine methylome during the initial 30 min of TCR engagement and discovered a novel arginine methylation of a Ca2+ -activated potassium transporter, KCa3.1, which regulates Ca2+ -mediated NFAT1 signaling to ensure optimal activation.
ORGANISM(S): Mus musculus (Mouse) 
2025-05-29 | PXD064423 | Pride
Arginine Protein Methylome 
ProteomicsTudor-based Proteomic Strategy Pan-specifically Enriches and Identifies Protein Arginine Methylation
In current study, we developed a molecular affinity strategy based on the Tudor domain of SMN, a naturally occurring methylarginine reader protein, for comprehensive proteomic profiling of cellular arginine methylation. We demonstrated that the Tudor domain-based approach exhibits broad specificity ...
ORGANISM(S): Homo sapiens (Human) 
2025-12-15 | PXD053390 | Pride
Proteomics Arginine methylation Molecular affinity-enrichment method Eif3d 
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