Proteomics

Dataset Information

0

Label-free quantitative total membrane proteome analysis of Candida glabrata wild-type and eleven CgYapsins-deficient strain Cgyps1-11∆.


ABSTRACT: 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.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Candida Glabrata (yeast) (torulopsis Glabrata)

SUBMITTER: Rupinder Kaur  

LAB HEAD: Rupinder Kaur

PROVIDER: PXD029629 | Pride | 2022-04-04

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
C1.raw Raw
C2.raw Raw
SEC-102.pdResult Other
T1.raw Raw
T2.raw Raw
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Publications

The yapsin family of aspartyl proteases regulate glucose homeostasis in Candida glabrata.

Askari Fizza F   Rasheed Mubashshir M   Kaur Rupinder R  

The Journal of biological chemistry 20220117 2


Invasive candidiasis poses a major healthcare threat. The human opportunistic fungal pathogen Candida glabrata, which causes mucosal and deep-seated infections, is armed with distinct virulence attributes, including a family of 11 glycosylphosphatidylinositol-linked aspartyl proteases, CgYapsins. Here, we have profiled total membrane proteomes of the C. glabrata wildtype and 11 proteases-deficient strain, Cgyps1-11Δ, by mass spectrometry analysis and uncovered a novel role for fungal yapsins in  ...[more]

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