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- W120711708 abstract "The activation of cyclic nucleotide-gated (CNG) channels is the final step in olfactory and visual transduction. Over the past several years, CNG channels have been found in various other cell types where they might fulfill various physiological functions. CNG channels rely on the binding of at least two molecules of cyclic adenosine monophosphate or cyclic guanosine 5′-monophosphate at intracellular sites on the channel protein to open a nonspecific cation conductance with a significant permeability to Ca ions. In addition to their activation by cyclic nucleotides, nitric oxide (NO)-generating compounds can directly open the olfactory CNG channels through a redox reaction that results in the S-nitrosylation of a free SH group on a cysteine residue. This cysteine is located in the C-linker region of the channel, which is known to be important in channel gating. Kinetic analyses suggest that at least two of these cysteine residues on different channel subunits are involved in the direct activation by NO." @default.
- W120711708 created "2016-06-24" @default.
- W120711708 creator A5053002588 @default.
- W120711708 date "2004-01-01" @default.
- W120711708 modified "2023-09-24" @default.
- W120711708 title "S-Nitrosylation of Cyclic Nucleotide-Gated Channels" @default.
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- W120711708 doi "https://doi.org/10.1007/978-1-59259-806-9_9" @default.
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