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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 
ProteomicsCharacterization of LysargiNase for use in phosphoproteomics experiments, part 1
Use of parallel digest with LysargiNase (former name: ulilysin) and trypsin to cover complementary phosphosites / characterization of phospho-motifs preferentially identified by each protease
ORGANISM(S): Homo sapiens (Human) 
2014-12-16 | PXD001121 | Pride
Phosphopeptides Mda-mb 231 Lysarginase Human Trypsin 
ProteomicsSpecificity profiling of LysargiNase in comparison to trypsin
Protease cleavage site preferences of LysargiNase (former name: ulilysin) and trypsin were tested using proteome-derived peptide libraries (Schilling et al Nature Protocols 2011)
ORGANISM(S): Escherichia coli 
2014-12-16 | PXD001122 | Pride
Protease Pics Sequence specificity 
UnknownLeptolysin, a Leptospira secreted metalloprotease of the pappalysin family with broad-spectrum activity.
Not available
S-EPMC9445424 | biostudies-literature
UnknownDissecting Cytophagalysin: Structural and Biochemical Studies of a Bacterial Pappalysin-Family Metallopeptidase.
Not available
S-EPMC11674741 | biostudies-literature
UnknownOn the relevance of the Met-turn methionine in metzincins.
Not available
S-EPMC2859557 | biostudies-literature
UnknownStructure-based mechanism of cysteine-switch latency and of catalysis by pappalysin-family metallopeptidases.
Not available
S-EPMC6949598 | biostudies-literature
ProteomicsTryp-N: A thermostable protease for the production of N-terminal argininyl and lysinyl peptides
Identification and characterization of Tryp-N, A thermostable protease for the production of N-terminal argininyl and lysinyl peptides
ORGANISM(S): Bos taurus (Bovine) Oryctolagus cuniculus (Rabbit) Escherichia coli Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) Saccharomyces cerevisiae (Baker's yeast) Gallus gallus (Chicken) 
2020-04-22 | PXD017024 | Pride
Arginine Thermostable Proteomics Lys-n Ulilysin Lysarginase Tryp-n Lysine Trypsin Metalloprotease 
ProteomicsTryp-N: A thermostable protease for the production of N-terminal argininyl and lysinyl peptides
Identification and characterization of Tryp-N, A thermostable protease for the production of N-terminal argininyl and lysinyl peptides
ORGANISM(S): Homo sapiens (Human) 
2020-04-22 | PXD017023 | Pride
Arginine Thermostable Proteomics Lys-n Ulilysin Lysarginase Tryp-n Lysine Trypsin Metalloprotease 
ProteomicsTryp-N: A thermostable protease for the production of N-terminal argininyl and lysinyl peptides
Identification and characterization of Tryp-N, A thermostable protease for the production of N-terminal argininyl and lysinyl peptides
ORGANISM(S): Escherichia coli 
2020-04-22 | PXD017048 | Pride
Arginine Thermostable Proteomics Lys-n Ulilysin Lysarginase Tryp-n Lysine Trypsin Metalloprotease 
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