The use of genetically encoded redox sensors in phagocytized bacteria reveals that, among the toxic cocktail of oxidants released into the neutrophil's phagolysosome, HOCl is the main component responsible for the oxidative modification of bacterial protein thiols.

The chloroplast 2-cysteine peroxiredoxin is central player and missing link in the chloroplast thiol-disulfide redox regulatory network, and participates in oxidative inactivation of reductively activated enzymes in photosynthesis.

African trypanosomes have a trypanothione-based mitochondrial thiol redox metabolism.

A sudden fall in the levels of the coenzyme NADPH within cells could have a central role in the process of aging.

ATF4, the master regulator of transcription during the Integrated Stress Response (ISR), causes global changes in cysteine sulfhydration of proteins and this event causes cellular metabolic reprogramming.

The major protein disulfide isomerase family member, PDIA1, is essential in beta cells of mice fed a high-fat diet to maintain glucose homeostasis, proinsulin maturation and organelle integrity.

The common post-translational modification trans-4-hydroxy-L-proline is reversed by gut microbes with the help of hydroxyproline dehydratase (HypD), an enzyme that performs a radical chemical mechanism.

The regulatory switch from protection to assimilation, which plants use to exploit natural, fluctuating light, involves movement of the enzyme ferredoxin:NADP(H) oxidoreductase between chloroplast membrane complexes.

Building on previous work (Wang et al., 2014), it is shown that the nucleotide exchange factor of the chaperone BiP (Sil1) unexpectedly facilitates the reduction of oxidized BiP.

The characterization of a previously unidentified “outward-facing open” conformational state provides a new framework for understanding the CLC transport mechanism.