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- W1525532830 abstract "Oxidation and modification of protein cysteines can have profound effects on protein structure and function. Using tubulin and microtubule‐associated proteins (MAP) tau and MAP2 as examples, this chapter summarizes methods employed to characterize total cysteine modification using thiol‐specific reagent 5‐iodoacetamido‐fluorescein labeling. Western blot analysis of peroxynitrite‐damaged tubulin under nonreducing conditions reveals the formation of higher molecular weight dimers and tetramers. Disulfides in microtubule proteins are substrates for both the thioredoxin reductase system and the glutaredoxin/glutathione reductase system. The yield of disulfides formed by peroxynitrite anion is quantitated by monitoring the oxidation of NADPH, a cofactor required by the thioredoxin reductase system. Treatment of proteins with S‐nitrosothiols, including S‐nitrosoglutathione and S‐nitroso‐N‐acetyl penicillamine, can yield either disulfides or protein S‐nitrosation. In the case of tubulin, both types of cysteine modification were detected." @default.
- W1525532830 created "2016-06-24" @default.
- W1525532830 creator A5013916225 @default.
- W1525532830 date "2008-01-01" @default.
- W1525532830 modified "2023-09-27" @default.
- W1525532830 title "Protein Thiol Modification by Peroxynitrite Anion and Nitric Oxide Donors" @default.
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- W1525532830 doi "https://doi.org/10.1016/s0076-6879(07)00805-1" @default.
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