Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69
We show that Thioredoxin 1 is essential for maintaining the content of S-nitrosylated molecules in endothelial cells
Thioredoxin 1 is a known redox regulator that is implicated in the redox control of cell growth and apoptosis inhibition
We show that Trx is essential for maintaining the content of S-nitrosylated molecules in endothelial cells
Trx itself is S-nitrosylated at cysteine 69 under basal conditions, and this S-nitrosylation is required for scavenging reactive oxygen species and for preserving the redox regulatory activity of Trx
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