<p>The website presents (A) protein information and annotation, (B) S-glutathionylation sites from published experiment, and (C) prediction result of potential consensus motifs.</p
Background: It is now recognized that protein cysteines exist not only as free thiols or intramolecu...
Thioredoxin glutathione reductase (TGR) is a member of the mammalian thioredoxin reductase family th...
Drug toxicity is often caused by electrophilic reactive metabolites that covalently bind to proteins...
S-glutathionylation, the covalent attachment of a glutathione (GSH) to the sulfur atom of cysteine, ...
<div><p><i>S</i>-glutathionylation, the covalent attachment of a glutathione (GSH) to the sulfur ato...
Lee H-M, Dietz K-J, Hofestädt R. Prediction of thioredoxin and glutaredoxin target proteins by ident...
S-glutathionylation, the reversible formation of mixed disulfides between glutathione(GSH) and cyste...
A significant part of cellular proteins undergo reversible thiol-dependent redox transitions which o...
<p>Graphical overview of the method for prediction of protein <i>S</i>-glutathionylation sites.</p
Thioredoxin glutathione reductase (TGR) is a member of the mammalian thioredoxin reductase family th...
Lee H-M. Bioinformatics pre-selection of thioredoxin/glutaredoxin target proteins for the constructi...
SummaryS-Acylation, S-glutathionylation, S-nitrosylation, and S-sulfenylation are prominent, chemica...
Background: Oxidoreductases of the thioredoxin family of proteins have been thoroughly studied in nu...
<p>Categorization of active site motifs in thioredoxin-like proteins (% of sequences)<sup><a href="h...
SummaryThe thioredoxin family of oxidoreductases plays an important role in redox signaling and cont...
Background: It is now recognized that protein cysteines exist not only as free thiols or intramolecu...
Thioredoxin glutathione reductase (TGR) is a member of the mammalian thioredoxin reductase family th...
Drug toxicity is often caused by electrophilic reactive metabolites that covalently bind to proteins...
S-glutathionylation, the covalent attachment of a glutathione (GSH) to the sulfur atom of cysteine, ...
<div><p><i>S</i>-glutathionylation, the covalent attachment of a glutathione (GSH) to the sulfur ato...
Lee H-M, Dietz K-J, Hofestädt R. Prediction of thioredoxin and glutaredoxin target proteins by ident...
S-glutathionylation, the reversible formation of mixed disulfides between glutathione(GSH) and cyste...
A significant part of cellular proteins undergo reversible thiol-dependent redox transitions which o...
<p>Graphical overview of the method for prediction of protein <i>S</i>-glutathionylation sites.</p
Thioredoxin glutathione reductase (TGR) is a member of the mammalian thioredoxin reductase family th...
Lee H-M. Bioinformatics pre-selection of thioredoxin/glutaredoxin target proteins for the constructi...
SummaryS-Acylation, S-glutathionylation, S-nitrosylation, and S-sulfenylation are prominent, chemica...
Background: Oxidoreductases of the thioredoxin family of proteins have been thoroughly studied in nu...
<p>Categorization of active site motifs in thioredoxin-like proteins (% of sequences)<sup><a href="h...
SummaryThe thioredoxin family of oxidoreductases plays an important role in redox signaling and cont...
Background: It is now recognized that protein cysteines exist not only as free thiols or intramolecu...
Thioredoxin glutathione reductase (TGR) is a member of the mammalian thioredoxin reductase family th...
Drug toxicity is often caused by electrophilic reactive metabolites that covalently bind to proteins...
DOI
Add to ORKG