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ProteomicsProteomic identification of cysteine cathepsin substrates shed from the surface of cancer cells
Extracellular cysteine cathepsins are known to drive cancer progression, but besides degradation of extracellular matrix proteins little is known about their physiological substrates and thus the molecular mechanisms they deploy. One of the major mechanisms used by other extracellular proteases to f...
ORGANISM(S): Homo sapiens (Human) 
2015-06-23 | PXD002192 | Pride
Cancer Substrates Degradomics Shedding Proteases Cathepsins 
ProteomicsMembrane substrates of HtrA from Helicobacter pylori
High temperature requirement A (HtrA) is a serine protease secreted by the group-I carcinogen Helicobacter pylori (H. pylori). The human cell adhesion protein and tumor suppressor E-cadherin (hCdh1) expressed on the surface of gastric epithelial cells was identified as the first HtrA substrate. HtrA...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD025360 | Pride
Protease Desmoglein Substrate Membrane Htra Helicobacter pylori 
ProteomicsProteomic study of S erythrea bioprocess
Proteome composition of Saccharopolyspora erythrea during the fermentation bioprocess was studied. Samples were collected at two timepoints (prior to the rapid growth phase and at the start of the rapid growth phase), and relative differences in protein abundance were determined by spectral counting...
ORGANISM(S): Saccharopolyspora erythraea (Streptomyces erythraeus) 
2016-05-26 | PXD002472 | Pride
Saccharopolyspora erythrea Bioprocess Lc-ms/ms 
ProteomicsProteomic profiling of cathepsin specificity by FPPS
Identification of protease substrates and determination of their specificities can provide important insights into their function. In the past decade, several proteomic approaches for identification of protease cleavage sites were developed, each relying on various strategies for peptide labelling a...
ORGANISM(S): Homo sapiens (Human) 
2015-02-10 | PXD001553 | Pride
Degradomics Proteases Cathepsins 
ProteomicsProteomic analysis of septic renal acute phase response
Sepsis-induced acute kidney injury (AKI) is the most common form of AKI with poor outcomes. Renal proteomic analysis after bacterial lipopolysaccharide (LPS) administration revealed that the local renal acute phase reaction (APR) is one of the strongest responses of the kidney during septic AKI in m...
ORGANISM(S): Mus musculus (Mouse) 
2020-01-08 | PXD014664 | Pride
Lipopolysaccharide Mouse Sepsis Kidney Lc-ms/ms 
Proteomicsmembrane substrates of gingipains
Porphyromonas gingivalis secretes cysteine proteases named gingipains which can cleave an array of proteins and importantly contribute to the development of periodontitis. In this study we focused on gingipain-exerted proteolysis at the cell surface of human gingival epithelial cells (telomerase imm...
ORGANISM(S): Homo sapiens (Human) 
2020-04-28 | PXD015679 | Pride
Protease Shedding Gingipain Anoikis Proteolysis 
ProteomicsProteomic identification of IqgC binding partners
Putative binding partners of IQGAP-related protein IqgC were identified by LC-MS/MS. Recombinant GST-tagged IqgC was purified from E. coli and immobilised to glutathione agarose. Interactors from cell lysate of D discoideum AX2 cells were applied to prepared affinity resin and bound proteins were id...
ORGANISM(S): Dictyostelium discoideum (Slime mold) 
2018-12-21 | PXD006311 | Pride
Iqgc Dictyostelium Gtpase Macropinocytosis Ras 
ProteomicsCharacterization of legumain degradation of intact proteins
Legumain or asparagine endopeptidase is a unique cysteine endopeptidase with a distinctive specificity for the hydrolysis of peptide bonds after asparagine and to a lesser extent after aspartate. In order to improve our understanding of legumain substrate recognition we have performed proteomic prof...
ORGANISM(S): Homo sapiens (Human) 
2018-11-29 | PXD010466 | Pride
Degradome Proteases Legumain Cleavage specificity Proteolysis 
ProteomicsIdentification of differentially expressed proteins during the fermentation of Saccharopolyspora erythraea
At selected timepoints during the S erythrea fermentation process, samples of fermentation broth were collected. Proteins in the samples were separated by 2D-PAGE and differentially expressed proteins were identified by LC-MS/MS.
ORGANISM(S): Saccharopolyspora erythraea (Streptomyces erythraeus) 
2016-05-26 | PXD002677 | Pride
Proteomics Saccharopolyspora erythraea Erythromycin 2d-page 
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 
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