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Our roGFP2 measurements confirm (i) that dynamic roGFP2 sensing (or the physiological glutathionylation/deglutathionylation of regular surface-exposed cysteinyl residues) requires a glutaredoxin activity, and (ii) that glutathionylated proteins or metabolites should be very transient redox species when GSH and glutaredoxins are present (unless they are stabilized by a kinetic uncoupling mechanism) 5,32,34,35,61,62,63,64
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Intriguingly, despite structural similarity to 5-HT, neither 5-HTP nor 5-HIAA confers protection against ferroptosis-inducing stimuli (e.g., RAS-selective lethal 3 exposure or GPX4 inactivation) (Liu et al., 2023)
Herbert, D
Toxicol Appl Pharmacol (2014) 279(3):26674
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