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ProteomicsThe Skin Barrier Defects Caused by Keratinocyte-Specific Deletion of ADAM17 or EGFR are Based on Highly Similar Proteome and Degradome Alterations
ADAM17 and EGFR are essential key players for epidermal integrity. Keratinocyte-specific deletion of ADAM17 in mice results in pronounced alterations in terminal differentiation of keratinocytes leading to severe epidermal barrier defects with enhanced transepidermal water loss. Thereby, mice defici...
ORGANISM(S): Mus musculus (Mouse) 
2016-04-20 | PXD002597 | Pride
Proteomics Skin Degradomics 
UnknownDouble deficiency of cathepsins B and L results in massive secretome alterations and suggests a degradative cathepsin-MMP axis.
Not available
S-EPMC11113308 | 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 
ProteomicsIsolation of intact and active FoF1 ATP synthase using a FLAG-tagged subunit from the cyanobacterium Synechocystis sp. PCC 6803
The FoF1 ATP synthase (ATPase) is one of the most important protein complexes in the energy metabolism, with many open questions about its assembly, regulation, and functions. The isolation of functional ATPase complexes is fundamental for their subsequent biochemical and structural analysis. This p...
ORGANISM(S): Synechocystis Sp. Pcc 6803 (ncbitaxon:1148) 
2022-06-03 | MSV000089593 | 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 
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