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Open access, freely available online Research Digest Synopses of Research Articles A New Way to Look at Oxidative Stress thiol modi?cations in proteins subjected to varying redox conditions in a living organism, the bacteria Escherichia coli. This technique is capable of providing a global snapshot of the redox state of protein cysteines during normal and oxidative stress conditions in the cell. To detect proteins that have the ability to undergo stress-induced thiol modi?cations, Leichert and Jakob differentially labeled the thiol groups of thiol-modi?ed and non-thiol-modi?ed proteins.The proteins were then separated on two-dimensional gels based on their charge and molecular weight. If the technique worked, most thiol- modi?ed proteins should be detected in the oxidizing environment of the E. coli periplasm (the region between the cell’s membrane layers), and they were. After proving the method’s ability to detect proteins whose thiol groups were oxidized, the next logical step was to determine what proteins DsbA—the enzyme that catalyzes disul?de bond formation in the E. coli periplasm—was targeting. In E. coli mutant strains that lack DsbA, Leichert and Jakob identi?ed a number of proteins with either many metabolic changes that occur in oxidatively stressed cells. Leichert and Jakob’s technique should be applicable to many different cell types and organisms and can be used to investigate the in vivo thiol status of cellular proteins exposed to virtually any physiological or pathological condition that is accompanied by oxidative stress. The next step will be to investigate just how thiol modi?cations mediate the various functions of redox-regulated proteins. DOI: 10.1371/journal.pbio.0020374 Chemical reactions lie at the heart of many biological processes, from photosynthesis and respiration to cell signaling and drug metabolism.Thanks to an atmosphere rich in oxygen, many organisms use oxygen to carry out these life processes. But oxygen metabolism prod