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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
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Associations of Thiol with other chemical compounds
The majority of RNS-sensitive E. coli proteins differ from E. coli proteins that harbour H2O2-sensitive thiol groups, implying that reactive oxygen and nitrogen species affect distinct physiological processes in bacteria [1].
In vivo labeling of proteins with [(35)S]cysteine and nonreducing two-dimensional PAGE analyses revealed that a large subset of proteins previously identified as having redox-sensitive thiols are modified by cysteine in response to treatment with the thiol-specific oxidant diamide [2].
Thiol modification with polyethylene glycol-maleimide showed disulfide bond formation at the active site of TRP32 in cells exposed to As(III) [3].
