A novel approach for predicting protein S-glutathionylation.

ABSTRACT:

Background

S-glutathionylation is the formation of disulfide bonds between the tripeptide glutathione and cysteine residues of the protein, protecting them from irreversible oxidation and in some cases causing change in their functions. Regulatory glutathionylation of proteins is a controllable and reversible process associated with cell response to the changing redox status. Prediction of cysteine residues that undergo glutathionylation allows us to find new target proteins, which function can be altered in pathologies associated with impaired redox status. We set out to analyze this issue and create new tool for predicting S-glutathionylated cysteine residues.

Results

One hundred forty proteins with experimentally proven S-glutathionylated cysteine residues were found in t

SUBMITTER: Anashkina AA 

PROVIDER: S-EPMC7489215 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature