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ABSTRACT: Aims
Protein S-glutathionylation is a widely distributed post-translational modification of thiol groups with glutathione that can function as a redox-sensitive switch to mediate redox regulation and signal transduction. The malaria parasite Plasmodium falciparum is exposed to intense oxidative stress and possesses the enzymatic system required to regulate protein S-glutathionylation, but despite its potential importance, protein S-glutathionylation has not yet been studied in malaria parasites. In this work we applied a method based on enzymatic deglutathionylation, affinity purification of biotin-maleimide-tagged proteins, and proteomic analyses to characterize the Plasmodium glutathionylome.Results
We identified 493 targets of protein S-glutathionylation in Plasmodium. F
SUBMITTER: Kehr S
PROVIDER: S-EPMC4932784 | biostudies-literature | 2011 Dec
REPOSITORIES: biostudies-literature