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.
The molecular microenvironment of coronaviral replicase complexes provides functional and spatial links between conserved cellular processes and viral RNA synthesis, and highlights potential targets for the development of novel antivirals.
Key sequence motifs, defined using the first reported structure of a monotopic membrane protein with a reentrant helix, enable identification of new monotopic membrane protein families previously predicted as membrane spanning.
An in vivo disulfide crosslinking assay shows preferential disassembly of nucleosomes with two H2A.Z histones by transcription machinery in yeast and conjugation to one or two ubiquitin moieties in human cells.