Trapping redox partnerships in oxidant-sensitive proteins with a small, thiol-reactive cross-linker

Volume: 101, Pages: 356 - 366
Published: Dec 1, 2016
Abstract
A broad range of redox-regulated proteins undergo reversible disulfide bond formation on oxidation-prone cysteine residues. Heightened reactivity of the thiol groups in these cysteines also increases susceptibility to modification by organic electrophiles, a property that can be exploited in the study of redox networks. Here, we explored whether divinyl sulfone (DVSF), a thiol-reactive bifunctional electrophile, cross-links oxidant-sensitive...
Paper Details
Title
Trapping redox partnerships in oxidant-sensitive proteins with a small, thiol-reactive cross-linker
Published Date
Dec 1, 2016
Volume
101
Pages
356 - 366
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