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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 
ProteomicsSelective regulation of aspartyl intramembrane protease activity by calnexin
Signal peptide peptidase-like 2c (SPPL2c) is a testis-specific aspartyl intramembrane protease that contributes to male gamete function both by catalytic and non-proteolytic mechanisms. Here, we provide an unbiased characterisation of the in vivo interactome of SPPL2c identifying the ER chaperone ca...
ORGANISM(S): Mus musculus (Mouse) 
2025-05-07 | PXD052965 | Pride
Co-ip Signal peptide peptidase-like 2c Mouse Calnexin Sppl2c Testis 
TranscriptomicsAn aspartyl protease defines a novel pathway for export of Toxoplasma proteins into the host cell
Toxoplasma gondii is an obligate intracellular Apicomplexan parasite capable of invading and surviving within nucleated cells in most warm-blooded animals. This remarkable task is achieved through the delivery of effector proteins from the parasite into the parasitophorous vacuole and host cell cyto...
ORGANISM(S): Homo sapiens 
2015-11-19 | E-GEOD-73986 | biostudies-arrayexpress
ProteomicsToxoplasma gondii aspartyl protease 3
The micronemes and rhoptries are specialized organelles that secrete their contents at the apical tip of apicomplexan parasites in a sequential and regulated manner. Microneme and rhoptry proteins crucially participate in motility, invasion, and egress from infected cells. They first traffic through...
ORGANISM(S): Toxoplasma gondii 
2018-01-30 | PXD006235 | Pride
Protease substrate screen Positional proteomics Tails 
ProteomicsSecretome analysis of Candida glabrata aspartyl protease-deficient strains
The project is aimed at characterizing the effect of deletion of surface associated aspartyl protease(s) on the secretome of of the human opportunistic fungal pathogen Candida glabrata.
ORGANISM(S): Candida glabrata (Yeast) (Torulopsis glabrata) 
2019-10-24 | PXD015132 | Pride
Secretory proteins Mucin msb2 Cell wall proteins Candida glabrata Secretome of yeasts 
ProteomicsAspartyl protease in the secretome of honey bee trypanosomatid parasite contributes to infection of the host
Exoproteome represents the proteome consisting of all secreted proteins and proteins derived from the cell surface and lysed cell. The exoproteome of the trypanosomatid parasite should interact with the host cells and the associated microbiota; however, the roles of infecting insect hosts are not ye...
ORGANISM(S): Lotmaria passim 
2024-02-18 | PXD040336 | Pride
Aspartyl protease Chitinase Exoproteome Trypanosomatid parasite Secretome Lotmaria passim 
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 
UnknownEvolutionary Selection on Barrier Activity: Bar1 Is an Aspartyl Protease with Novel Substrate Specificity.
Not available
S-EPMC4669382 | biostudies-literature
UnknownAspartyl Protease Inhibitors as Anti-Filarial Drugs.
Not available
S-EPMC9227574 | biostudies-literature
UnknownNK Cell Maturation and Cytotoxicity Are Controlled by the Intramembrane Aspartyl Protease SPPL3.
Not available
S-EPMC4779696 | biostudies-literature
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