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Genomics
Degradomics reads to inform beet curly top virus infection
PRJNA1009842 | ENA
UnknownNovel Biological Substrates of Human Kallikrein 7 Identified through Degradomics.
Not available
S-EPMC4505025 | biostudies-literature
UnknownDegradomics-Based Analysis of Tetanus Toxoids as a Quality Control Assay.
Not available
S-EPMC7712181 | biostudies-literature
UnknownTracking proteasome degradation: A cross-organ analysis via intact degradomics mass spectrometry.
Not available
S-EPMC11874349 | biostudies-literature
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 
UnknownIdentification of Novel Natural Substrates of Fibroblast Activation Protein-alpha by Differential Degradomics and Proteomics.
Not available
S-EPMC6317473 | biostudies-literature
ProteomicsDegradomics-based analysis of tetanus toxoids as a quality control assay
Degradomics-based analysis of tetanus toxoids as a quality control assay
ORGANISM(S): Clostridium Tetani E88 (ncbitaxon:212717) 
2020-11-02 | MSV000086396 | MassIVE
ProteomicsIdentification of novel natural substrates of fibroblast activation protein by differential degradomics and proteomics
Fibroblast Activation Protein (FAP) is a cell-surface transmembrane-anchored anchored dimeric protease. This unique constitutively active serine protease has both dipeptidyl aminopeptidase and endopeptidase activities, and can hydrolyse post-proline bonds. FAP expression is very low in adult organs,...
ORGANISM(S): Mus musculus (Mouse) 
2018-12-19 | PXD004754 | Pride
Protease 
UnknownInsights into the keratin efficient degradation mechanism mediated by Bacillus sp. CN2 based on integrating functional degradomics.
Not available
S-EPMC10071666 | biostudies-literature
ProteomicsIdentification of novel natural substrates of fibroblast activation protein by differential degradomics and proteomics (TAILS dataset)
Fibroblast Activation Protein (FAP) is a cell-surface transmembrane-anchored anchored dimeric protease. This unique constitutively active serine protease has both dipeptidyl aminopeptidase and endopeptidase activities, and can hydrolyse post-proline bonds. FAP expression is very low in adult organs,...
ORGANISM(S): Mus musculus (Mouse) 
2018-12-19 | PXD004757 | Pride
Seprase Proteolysis 
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