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MetabolomicsApplication of the Protease-Resistant Antimicrobial Peptide R7I, Composed of Natural Amino Acids, as a Functional Food Ingredient for Modulating Intestinal Health

Foodborne pathogenic bacterial infections pose significant challenges to global food safety and public health, while the issue of antimicrobial resistance (AMR) has worsened in recent years, creating an urgent need for safe, natural alternatives to combat foodborne pathogens and associated intest...

2025-11-09 | MTBLS13292 | MetaboLights
ProteomicsTAILS identifies candidate substrates and biomarkers of ADAMTS7, a therapeutic protease target in coronary artery disease
MacDonald BT, Keshishian H, Mundorff CC, Arduini A, Lai D, Bendinelli K, Popp NR, Bhandary B, Clauser KR, Specht H, Elowe NH, Laprise D, Xing Y, Kaushik VK, Carr SA, Ellinor PT. Loss-of-function mutations in the secreted enzyme ADAMTS7 (a disintegrin and metalloproteinase with thrombospondin motifs ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2021-12-03 | MSV000088508 | MassIVE
TranscriptomicsPaf1C plays novel subunit-specific roles in alternative cleavage and polyadenylation
The PAF complex (Paf1C) has been shown to regulate chromatin modifications, gene transcription, and PolII elongation. Here, we provide the first genome-wide analysis of chromatin occupancy by the entire PAF complex in mammalian cells. We show that Paf1C is recruited not only to promoters and gene bo...
ORGANISM(S): Mus musculus 
2016-01-15 | E-GEOD-72574 | biostudies-arrayexpress
ProteomicsHERV protease specificity - Identification of Protease Specificity by Combining Proteome-Derived Peptide Libraries and Quantitative Proteomics
Proteome-derived peptide libraries are a powerful tool for the investigation of protease specificity, conventionally involving the biotinylation of cleavage products to enable for their enrichment. Here we present a modified strategy for protease specificity profiling using proteome-derived peptide ...
ORGANISM(S): Escherichia coli 
2016-05-02 | PXD003833 | Pride
Protease 
ProteomicsDirect in-gel profiling of protease specificity (DIPPS)
Determination of protease specificity is of crucial importance for understanding protease function. We have developed the first gel-based label-free proteomic approach (DIPPS) that enables quick and reliable determination of protease cleavage specificities under large variety of experimental conditi...
ORGANISM(S): Aeropyrum pernix Homo sapiens (Human) 
2017-07-06 | PXD004218 | Pride
Specificity profiling Protease Legumain Cathepsin Degradomics 
ProteomicsCleavage preference of metalloprotease EA1
The cleavage preference of the thermophilic metalloprotease from Geobacillus sp. EA1 was characterised using mass spectrometry, confirming its similarity to thermolysin in preferring P1’ hydrophobic amino acids. While EA1 showed similar efficiencies for cleavage of short peptides with one of six hyd...
ORGANISM(S): Escherichia coli Geobacillus sp. EFT1 Bacillus thermoproteolyticus 
2025-11-25 | PXD064530 | Pride
Protease cleavage assay Thermolysin Itraq 
ProteomicsThe MNV-1 ProPol precursor Cleaves a Novel Site in the NS1-2 Protein
Human noroviruses (HuNV) are members of the Caliciviridae family and are a significant cause of gastroenteritis worldwide. Cell culture models are challenging for studying the intracellular replication of HuNV, with murine norovirus (MNV) routinely used to study norovirus replication. Norovirus geno...
ORGANISM(S): Murine norovirus 1 
2026-06-08 | PXD074184 | Pride
Norovirus Tails Non-structural polyprotein Protease cleavage 
ProteomicsUltraPlex: Expanding isobaric hyperplexing via orthogonal protease cleavage
Sample preparation was conducted using an adaptation of our SimPLIT workflow10. Four cell pellets corresponding to four different colorectal cancer cell lines were lysed in a buffer containing 1% sodium deoxycholate (SDC, Merck, Cat. No. 30970), 100 mM triethylammonium bicarbonate (TEAB, Merck, Cat....
ORGANISM(S): Homo sapiens (Human) 
2026-01-30 | PXD070352 | Pride
ProteomicsSnake venom serine proteinases specificity mapping by proteomic identification of cleavage sites
Serine proteinases have been shown to play the role of toxins in the venoms of many snakes. They act mainly on components of the coagulation cascade, and fibrinolytic and kallikrein-kinin systems to trigger various pathological effects observed in the envenomation. Despite showing high similarity in...
ORGANISM(S): Bothrops jararaca (Jararaca) (Bothrops jajaraca) 
2014-10-30 | PXD001217 | Pride
Serine proteinase Pproteomic identification of protease cleavage sites Mass spectrometry Snake venom Proteinase 
TranscriptomicsRNAseq of titin cleavage in neonatal mouse cardiomyocytes
RNAseq of WT and TEVsite-titin (TEVs-TTN) neonatal mouse cardiomyocytes before and after titin cleavage with TEV protease (TEVp) expression.
ORGANISM(S): Mus musculus 
2025-04-13 | E-MTAB-14985 | biostudies-arrayexpress
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