Proteomics

Dataset Information

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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 global membrane proteome of Candida glabrata.

INSTRUMENT(S): LTQ Orbitrap Velos

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

SUBMITTER: Rupinder Kaur  

LAB HEAD: Rupinder Kaur

PROVIDER: PXD029614 | Pride | 2022-04-04

REPOSITORIES: Pride

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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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