Dulhunty, Angela; Haarmann, Claudia; Green, Daniel; Hart, James
RyRs contain 80-100 cysteine residues per subunit, of which ~25% are free for covalent modification, while the remainder are either modified or form intraprotein disulfides. Oxidizing and nitrosylating reagents have several effects on single RyR channel activity, which depend on the type of modifying reagent, the isoform of the RyR, and ligands bound to the channel. We present evidence here for four major classes of functional cysteine residues associated with RyR channels, i.e., two classes...[Show more]
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