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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 
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 
ProteomicsProtease specificity profiling in a pipette tip using “charge-synchronized” proteome-derived peptide libraries
About 2% of the genome of human and other organisms codes for proteases. An important step toward deciphering the biological function of a protease and designing inhibitors is the profiling of protease specificity. In this work we present a novel, label-free, proteomics-based protease specificity pr...
ORGANISM(S): Escherichia coli 
2018-04-26 | PXD007556 | Pride
Charged-synchronized peptide library Protease specificity Chafratip Label-free 
ProteomicsD. magna CT448 protease specificity
Mass developments of toxin-producing cyanobacteria are frequently observed in freshwater ecosystems due to eutrophication and global warming. These mass developments can partly be attributed to cyanobacterial toxins, such as protease inhibitors (PIs), which inhibit digestive serine proteases of Daph...
ORGANISM(S): Daphnia magna 
2018-10-04 | PXD010978 | Pride
Ct448 pics protease specificity 
ProteomicsTag-Free Identification of Protease Specificity Using Proteome-Derived Peptide Libraries
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 | PXD002785 | Pride
Proteolysis 
ProteomicsAtLEGbeta / gamma protease specificity characterization by PICS
Arabidopsis thaliana Legumain (aka VPE) beta / gamma proteases were characterized for their cleavage specificity by PICS (Proteomic Identification of protease Cleavage Sites).
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) Escherichia coli 
2020-07-29 | PXD019220 | Pride
Arabidopsis legumain beta gamma protease 
Genomics
Protease specificity profiling
PRJNA586896 | ENA
ProteomicsMapping specificity, entropy, allosteric changes and substrates in blood coagulation proteases by a high-throughput protease screen
Proteases are crucial physiologic regulators of protein structure and function. While proteomic methods contributed extensively to protease characterization efforts, technical challenges remain in terms of throughput, scalability and large datasets of protease cleavages remain scarce. Here, we descr...
ORGANISM(S): Homo sapiens (Human) 
2021-02-05 | PXD018976 | Pride
High-throughput protease screen Substrates Blood coagulation proteases Specificity Entropy Allostery 
ProteomicsSirtilin protease specificity - Sirtilins - the new old members of the vitamin K-dependent coagulation factor family
Here we describe an additional member of the Vitamin K-dependent protease family comprising the Gla-EGF1-EGF2-SP domain architecture. These proteases were found in different vertebrate classes including jawless fish, cartilaginous fish, bony fish, reptiles, birds and marsupials but not in other mamm...
ORGANISM(S): Escherichia coli 
2019-02-22 | PXD010679 | Pride
Sirtilin pics protease specificity 
ProteomicsQuantifying missing (phospho)proteome regions with the broad-specificity protease subtilisin
Despite huge efforts to map the human proteome using mass spectrometry the overall sequence coverage achieved to date is still below 50%. Reasons for missing areas of the proteome comprise protease-resistant domains including the lack/excess of enzymatic cleavage sites, non-unique peptide sequences,...
ORGANISM(S): Homo sapiens (Human) 
2017-11-30 | PXD008068 | Pride
Novel phosphorylation sites Proteome coverage Pro-rich regions Alternative enzymes Trypsin Sample preparation Missing proteins 
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