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ProteomicsComprehensive analysis of symmetric arginine dimethylation in colorectal cancer tissues from patients using immuniaffinity enrichment followed by LC-MS/MS analysis
Post-translational arginine methylation is responsible for regulation of a variety of biological processes. The protein arginine methyltransferase 5 (PRMT5) is the major enzyme responsible for generating monomethyl- and symmetric dimethyl arginine (MMA and SDMA, respectively) in proteins. PRMT5 is e...
ORGANISM(S): Homo sapiens (Human) 
2020-06-01 | PXD015653 | Pride
Prmt5 Immunoaffinity enrichment Colorectal cancer Mass spectrometry Symmetric arginine methylation 
ProteomicsDeep protein methylation profiling by combined chemical and immunoaffinity approaches reveals novel PRMT1 targets
Protein methylation has been implicated in many important biological contexts including signaling, metabolism, and transcriptional control. Despite the importance of this post- translational modification, the global analysis of protein methylation by mass spectrometry-based proteomics has not been e...
ORGANISM(S): Homo sapiens (Human) 
2019-08-28 | PXD012357 | Pride
Prmt1 Prmt Ptm Liquid chromatography Methylation Lysine Sdma Mma Mass spectrometry Posttranslational modification Dimethyl Monomethyl Adma Proteomics Q exactive plus Arginine Lcms 
ProteomicsPRMT5-mediated arginine methylation activates AKT kinase to govern tumorigenesis
AKT is involved in a number of key cellular processes including cell proliferation, apoptosis and metabolism. Hyperactivation of AKT is associated with many pathological conditions, particularly cancers. Emerging evidence indicates that arginine methylation is involved in modulating AKT signaling pa...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD026071 | Pride
Tumorigenesis Prmt5 Akt Arginine methylation 
TranscriptomicsProtein arginine methyltransferase AtPRMT5 is involved in pre-mRNA splicing in Arabidopsis thaliana
In this study, we analyzed the Arabidopsis homologue of PRMT5, AtPRMT5M-bM-^@M-^Ys function in RNA processing. RNA-seq analyses revealed that AtPRMT5 is involved in a subset of pre-mRNA splicing. Several RNA processing factors involved in regulating flowering time were validated that the correspondi...
ORGANISM(S): Arabidopsis thaliana 
2010-10-07 | E-GEOD-21323 | biostudies-arrayexpress
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 
ProteomicsImproved discrimination of asymmetric and symmetric protein arginine dimethylation by optimizing the normalized collision energy in LC-MS proteomics
Here we optimize the HCD Normalized Collision Energy (NCE) in order to generate neutral losses of monomethylamine and dimethylamine which can be lost by symmetric dimethylarginine and asymmetric dimethylarginine, respectively. By testing a range of NCEs across two different methyl enrichment techniq...
ORGANISM(S): Homo sapiens (Human) 
2020-05-27 | PXD017193 | Pride
Arginine Prmt Mass spectrometry Methylation Adma Ptm Hcd Neutral loss Proteomics Sdma Lcms 
ProteomicsA complex of C9ORF72 and p62 uses arginine methylation to eliminate stress granules by autophagy - PART 3
Mutations in proteins like FUS which cause Amyotrophic Lateral Sclerosis (ALS) result in the aberrant formation of stress granules while ALS-linked mutations in other proteins impede elimination of stress granules. Repeat expansions in C9ORF72, the major cause of ALS, reduce C9ORF72 levels but how t...
ORGANISM(S): Homo sapiens (Human) 
2018-07-25 | PXD009760 | Pride
Lc-msms Prmt5 Arginine dimethylation Fus Als Oxidate stress 
ProteomicsEnhanced Proteomic Mapping of Arginine Methylation Using Electron Transfer Dissociation Reveals Novel PRMT5 Substrates and Arginine Trimethylation
PRMT5 is the major enzyme that catalyzes the symmetric dimethylation of arginine (sDMA) in mammalian cells. Its activity is crucial for many biological processes including transcriptional regulation, mRNA processing, as well as DNA damage and repair. However, the protein substrates identified for PR...
ORGANISM(S): Homo sapiens (Human) 
2024-04-30 | PXD037425 | Pride
Prmt5 Etd Methylation Proteomics 
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 
ProteomicsRole of PRMT5 in DNA damage response
Protein arginine methyltransferase (PRMT5) has emerged as a crucial symmetric dimethylating enzyme involved in the methylation of a myriad of substrates critical for epigenetic regulation, DNA damage signalling, RNA splicing, and cell fate decision. Here we have uploaded the PRMT5 interactome with t...
ORGANISM(S): Homo sapiens (Human) 
2026-03-16 | PXD057645 | Pride
Mitochondrial homeostasis Post translational modification Prmt5 Mitochondrial biogenesis Tfam Mtdna damage 
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