منابع مشابه
Exploiting Thiol Modifications
1714 As the premier biological electron acceptor, molecular oxygen (O2) serves a vital role in fundamental cellular functions, including the process of aerobic respiration. Nevertheless, with the benefi cial properties of O2 comes the inadvertent formation of reactive oxygen species, including superoxide (O2 −), hydrogen peroxide (H2O2), and hydroxyl radical (•OH); these differ from O2 in havin...
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Thiol-disulfide interconversions play a crucial role in the chemistry of biological systems. They participate in the major systems that control the cellular redox potential and prevent oxidative damage. In addition, thiol-disulfide exchange reactions serve as molecular switches in a growing number of redox-regulated proteins. We developed a differential thiol-trapping technique combined with tw...
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Recent studies indicate that glutamatergic signaling involves, and is regulated by, thiol modifying and redox-active compounds. In this study, we examined the role of a reactive cysteine residue, Cys-893, in the cytosolic C-terminal tail of GluA1 AMPA receptor as a potential regulatory target. Elimination of the thiol function by substitution of serine for Cys-893 led to increased steady-state ...
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Oxidation of cysteine to sulfenic acid has emerged as a biologically relevant post-translational modification with particular importance in redox-mediated signal transduction; however, the identity of modified proteins remains largely unknown. We recently reported DAz-1, a cell-permeable chemical probe capable of detecting sulfenic acid modified proteins directly in living cells. Here we descri...
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The reaction product of nitric oxide and superoxide, peroxynitrite, is a potent biological oxidant. The most important oxidative protein modifications described for peroxynitrite are cysteine-thiol oxidation and tyrosine nitration. We have previously demonstrated that intrinsic heme-thiolate (P450)-dependent enzymatic catalysis increases the nitration of tyrosine 430 in prostacyclin synthase an...
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ژورنال
عنوان ژورنال: PLoS Biology
سال: 2004
ISSN: 1545-7885
DOI: 10.1371/journal.pbio.0020400