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ProteomicsMSP-MS of Cathepsin B and Cathepsin K pH 4.6 pH 7.2
MSP-MS of Cathepsin B and Cathepsin K pH 4.6 pH 7.2
ORGANISM(S): Synthetic Construct (ncbitaxon:32630) 
2022-02-28 | MSV000088932 | MassIVE
ProteomicsMSP-MS of PC1 and PC2 pH 5.5 at 37C
MSP-MS of PC1 and PC2 pH 5.5 at 37C. Part of Neuropeptide processing study
ORGANISM(S): Synthetic Construct (ncbitaxon:32630) 
MSV000088092 | MassIVE
ProteomicsMSP-MS of Cathepsin L and Cathepsin V pH 5.5
MSP-MS of Cathepsin L and Cathepsin V pH 5.5 at 37C
ORGANISM(S): Synthetic Construct (ncbitaxon:32630) 
MSV000088091 | MassIVE
ProteomicsCathepsin B MSP-MS at pH 4.6 and 7.2 without inhibitor
MSP-MS of Cathepsin B at pH 4.6 and pH 7.2 without inhibitor
ORGANISM(S): Synthetic Construct (ncbitaxon:32630) 
2020-11-12 | MSV000086449 | MassIVE
ProteomicsCathepsin B MSP-MS at pH 4.6 and pH 7.2
MSP-MS of Cathepsin B protease at acidic and neutral pH
ORGANISM(S): Synthetic Construct (ncbitaxon:32630) 
2020-11-12 | MSV000086447 | MassIVE
ProteomicsThe human pathobiont Malassezia furfur secreted protease MfSAP1 regulates cell dispersal and exacerbates skin inflammation
Malassezia forms the dominant eukaryotic microbial community on the human skin. The Malassezia genus possesses a repertoire of secretory hydrolytic enzymes involved in protein and lipid metabolism which alter the external cutaneous environment. The exact role of most Malassezia secreted enzymes, inc...
ORGANISM(S): Cellular Organisms 
2022-11-11 | PXD033336 | JPOST Repository
ProteomicsAn aspartyl pseudoprotease dominates the secretory hydrolase landscape of the skin commensal Malassezia in situ
Malassezia globosa is abundant and prevalent on sebaceous areas of the human skin. Genome annotation reveals that M. globosa possesses a repertoire of secreted hydrolytic enzymes relevant for lipid and protein metabolism on the skin. In-gel proteomics identifies a predicted aspartyl protease, MGL_33...
ORGANISM(S): Cellular Organisms 
2023-11-23 | PXD042508 | JPOST Repository
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