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ProteomicsCandida glabrata GPI-anchored cell surface associated aspartyl protease CgYps1 and CgYps7 interactome analysis in the total cell extracts of A-498 human renal epithelial cell line
The project is aimed at identifying host epithelial proteins that interact with two different cell-surface associated aspartyl proteases (CgYps1 and CgYps7) in Candida glabrata cells.
ORGANISM(S): Homo sapiens (Human) 
2024-08-22 | PXD053938 | Pride
Arp2/3 complex Aspartyl proteases Lc-ms/ms. Candida glabrata Epithelial cells 
ProteomicsInteractome identification of a glycosylphosphatidylinositol-linked aspartyl protease, CgYps1, in the pathogenic yeast Candida glabrata
The major goal of this project is to identify proteins that interact with CgYps1 aspartyl protease in logarithmic-phase Candida glabrata cells.
ORGANISM(S): Candida glabrata (Yeast) (Torulopsis glabrata) 
2021-02-08 | PXD022766 | Pride
Aspartyl protease Polyclonal antisera Immunoprecipitation Lc-ms/ms 
UnknownPlasmepsin-like Aspartyl Proteases in Babesia.
Not available
S-EPMC8540915 | biostudies-literature
UnknownIntramembrane proteolysis by signal peptide peptidases: a comparative discussion of GXGD-type aspartyl proteases.
Not available
S-EPMC2682845 | biostudies-literature
UnknownAspartyl proteases target host actin nucleator complex protein to limit epithelial innate immunity.
Not available
S-EPMC11549443 | biostudies-literature
UnknownA family of glycosylphosphatidylinositol-linked aspartyl proteases is required for virulence of Candida glabrata.
Not available
S-EPMC1863504 | biostudies-literature
UnknownCysteine and Aspartyl Proteases Contribute to Protein Digestion in the Gut of Freshwater Planaria.
Not available
S-EPMC4976874 | biostudies-literature
UnknownThe yapsin family of aspartyl proteases regulate glucose homeostasis in Candida glabrata.
Not available
S-EPMC8844688 | biostudies-literature
UnknownModeling and resistant alleles explain the selectivity of antimalarial compound 49c towards apicomplexan aspartyl proteases.
Not available
S-EPMC5881632 | biostudies-literature
TranscriptomicsThe GPI-anchored aspartyl proteases encoded by the YPS1 and YPS7 genes of Candidozyma auris and their role under stress conditions.
Candidozyma auris is a multidrug resistance opportunistic pathogen, distinguished because of their thermotolerance, osmotolerance, and persistence in biotic and abiotic surfaces, attributes that seem linked to the cell wall composition. Here, seven putative genes encoding yapsins, extracellular aspa...
ORGANISM(S): Candidozyma auris 
2025-07-17 | GSE302916 | GEO
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