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ProteomicsSILAC-iTRAQ-TAILS - Monitoring matrix metalloproteinase activity at the epidermal-dermal interface by SILAC-iTRAQ-TAILS
Secreted proteases act on interstitial tissue secretomes released from multiple cell types. Thus, substrate proteins might be part of higher molecular complexes constituted by many proteins with diverse and potentially unknown cellular origin. In cell culture these might be reconstituted by mixing n...
ORGANISM(S): Mus musculus (Mouse) 
2015-05-11 | PXD001643 | Pride
Skin Basement membrane Tails Silac Itraq Mmp 
ProteomicsTAILS proteomics of murine pancreatic tumors
Aberrant proteolysis by cysteine cathepsins is implicated in carcinogenesis, but knowledge of cathepsin substrates mediating tumor-promoting or suppressing effects is limited. Here we characterize tumor proteome and in vivo cathepsin substrates using cathepsin knockout mice and the RIP1-Tag2 model o...
ORGANISM(S): Mus musculus (Mouse) 
2016-08-08 | PXD003637 | Pride
Pancreatic neuroendocrine cancer Ecm Proteomics Substrate discovery Proteolytic processing Degradation Proteases Tails n-terminomics Cysteine cathepsins 
ProteomicsMMP10 degradomics in keratinocytes
Matrix metalloproteinases (MMPs) are important players in skin homeostasis, wound repair, and in the pathogenesis of skin cancer. One member – MMP10 – is specifically expressed in wound keratinocytes and in epithelial cancer cells, but its function is unclear and epidermal substrates are poorly char...
ORGANISM(S): Mus musculus (Mouse) 
2015-10-19 | PXD002474 | Pride
Itraq-tails Keratinocytes Mmp10 Skin Degradomics 
ProteomicspNPs N-terminomics - Determination of the substrate repertoire of ADAMTS2, 3, and 14 significantly broadens their functions and identifies extracellular matrix organization and TGF-β signaling as primary targets
N-terminomics (iTRAQ-TAILS) applied to the ADAMTS2, 3 and 14.
ORGANISM(S): Homo sapiens (Human) 
2016-01-12 | PXD002354 | Pride
Adamts14 Adamts2 Adamts3 
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 
ProteomicsSILAC-iTRAQ-TAILS - Monitoring matrix metalloproteinase activity at the epidermal-dermal interface by SILAC-iTRAQ-TAILS
Secreted proteases act on interstitial tissue secretomes released from multiple cell types. Thus, substrate proteins might be part of higher molecular complexes constituted by many proteins with diverse and potentially unknown cellular origin. In cell culture these might be reconstituted by mixing n...
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2025-11-20 | MSV000099979 | MassIVE
ProteomicsDeciphering changes to human platelet proteome and degradome during storage before transfusion
Proteases, and specifically metalloproteinases, have been linked to the loss of platelet function during storage before transfusion, albeit the mechanism remains unknown. We used a dedicated N-terminomics technique, multiplex iTRAQ-TAILS (Terminal Amine Isotope Labeling of Substrates), to characteri...
ORGANISM(S): Homo sapiens (Human) 
2014-10-24 | PXD000906 | Pride
Platelets Metalloproteinases Degradome Proteases Tails Human Ls-msms 
ProteomicsTime-resolved substrate degradomics
20110318_GluC: Cell culture supernatants from Balb/c 3T3 mouse fibroblasts that had been incubated with the endoproteinase GluC (Staphylococcus aureus protease V8) as test protease for 1, 2, 4, 8, and 16 hours or buffer alone (0, 12, and 16 hours controls) were subjected to 8plex-iTRAQ-TAILS analys...
ORGANISM(S): Mus musculus (Mouse) 
2013-12-13 | PXD000503 | Pride
Protease 8plex-itraq Tails Kinetics Mmp 
ProteomicsIn Vivo Assessment of Protease Dynamics in Cutaneous Wound Healing by Degradomics Analysis of Porcine Wound Exudates
Proteases control complex tissue responses by modulating inflammation, cell proliferation and migration, and matrix remodeling. All these processes are orchestrated in cutaneous wound healing to restore the skin’s barrier function upon injury. Altered protease activity has been implicated in the p...
ORGANISM(S): Sus scrofa domesticus (domestic pig) 
2014-12-19 | PXD001198 | Pride
N-terminome Wound healing Protease Tails Wound fluids 
UnknownA statistics-based platform for quantitative N-terminome analysis and identification of protease cleavage products.
Not available
S-EPMC2871423 | biostudies-literature
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