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UnknownDeletion of cysteine cathepsins B or L yields differential impacts on murine skin proteome and degradome.
Not available
S-EPMC3591655 | biostudies-literature
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
UnknownA Systematic Evaluation of Semispecific Peptide Search Parameter Enables Identification of Previously Undescribed N-Terminal Peptides and Conserved Proteolytic Processing in Cancer Cell Lines.
Not available
S-EPMC8162549 | biostudies-literature
UnknownProteomic analysis of lung metastases in a murine breast cancer model reveals divergent influence of CTSB and CTSL overexpression.
Not available
S-EPMC5706009 | biostudies-literature
UnknownProteomic distinction of renal oncocytomas and chromophobe renal cell carcinomas.
Not available
S-EPMC6074034 | biostudies-literature
ProteomicsA systematic evaluation of semispecific peptide search parameter enables identification of previously undescribed N-terminal peptides and conserved proteolytic processing in cancer cell lines
Background: Liquid chromatography- tandem mass spectrometry (LC-MS/MS) has become the most commonly used technique in explorative proteomic research. A variety of open-source tools for peptide-spectrum matching have become available. Most analyses of explorative MS data are performed using conventio...
ORGANISM(S): Escherichia Coli (ncbitaxon:562) Homo Sapiens (ncbitaxon:9606) Mus Musculus (ncbitaxon:10090) 
2021-03-11 | MSV000087034 | 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 
UnknownIdentification of Protease Specificity by Combining Proteome-Derived Peptide Libraries and Quantitative Proteomics.
Not available
S-EPMC4937521 | biostudies-literature
UnknownCharacterization of various cell lines from different ampullary cancer subtypes and cancer associated fibroblast-mediated responses.
Not available
S-EPMC4782372 | biostudies-literature
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 
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