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UnknownFunctional roles of purified yapsins from Candida glabrata (Nakaseomyces glabratus) in immune modulation and cross-species biofilm formation.
Not available
S-EPMC12402140 | 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
ProteomicsTotal membrane proteome analysis of Candida glabrata wild-type and eleven CgYapsins-deficient strain Cgyps1-11∆.
The project is aimed at characterizing the effect of loss of a family of eleven aspartyl proteases (Cg Yapsins) on the global membrane proteome of Candida glabrata.
ORGANISM(S): Candida glabrata (Yeast) (Torulopsis glabrata) 
2022-04-04 | PXD029614 | Pride
Total membrane fractions (tmfs) Candida glabrata Membrane proteome Lc-ms/ms 
ProteomicsRevealing Candida glabrata biofilm matrix proteome: global characterization and pH response
Candida glabrata is a clinically relevant human pathogen with ability to form high recalcitrant biofilms that contribute to the establishment and persistence of infection. A defining trait of biofilms is the auto-produced matrix, which is suggested to have structural, virulent and protective roles. ...
ORGANISM(S): Candida glabrata (Yeast) (Torulopsis glabrata) 
2024-02-22 | PXD022597 | Pride
Biofilm secretome Environmental ph Adhesins Β-glucans Candidiasis Yapsins 
ProteomicsLabel-free quantitative total membrane proteome analysis of Candida glabrata wild-type and eleven CgYapsins-deficient strain Cgyps1-11∆.
The project is aimed at characterizing the effect of loss of a family of eleven aspartyl proteases (Cg Yapsins) on the abundance of proteins in the total membrane factions of Candida glabrata.
ORGANISM(S): Candida glabrata (Yeast) (Torulopsis glabrata) 
2022-04-04 | PXD029629 | Pride
Total membrane fractions (tmfs) Label-free quantitative mass spectrometry Candida glabrata Membrane proteome 
ProteomicsSecretome analysis of Candida glabrata wild-type and aspartyl protease-deficient strains
The project is aimed at characterizing the secretome of a human opportunistic fungal pathogen Candida glabrata. Additionally, the effect of loss of a family of eleven aspartyl proteases (Cg Yapsins) on the Candida glabrata secretome is studied.
ORGANISM(S): Candida glabrata (Yeast) (Torulopsis glabrata) 
2019-10-25 | PXD015131 | Pride
Secretory proteins Mucin msb2 Cell wall proteins Candida glabrata Secretome of yeasts 
UnknownAspartyl proteases target host actin nucleator complex protein to limit epithelial innate immunity.
Not available
S-EPMC11549443 | biostudies-literature
UnknownThe GPI-Anchored Aspartyl Proteases Encoded by the <i>YPS1</i> and <i>YPS7</i> Genes of <i>Candidozyma auris</i> and Their Role Under Stress Conditions.
Not available
S-EPMC12387857 | biostudies-literature
UnknownGlobal Secretome Characterization of the Pathogenic Yeast <i>Candida glabrata</i>.
Not available
S-EPMC6947636 | biostudies-literature
UnknownThe yapsin family of aspartyl proteases regulate glucose homeostasis in Candida glabrata.
Not available
S-EPMC8844688 | biostudies-literature
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