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- W3022740890 abstract "Publisher SummaryThis chapter discusses cyclic nucleotide-gated ion channels, which are sensitively and directly activated by the binding of cGMP and/or cAMP. The chapter discusses several concepts related to cyclic nucleotides, including control by cyclic nucleotide enzyme cascades, molecular structure, and functional modulation. The discussion on functional properties includes channel gating and permeation, selectivity, and block. Similar to other cyclic nucleotide-regulated proteins, CNG channels are powerful modifiers of cell function. They are found in photoreceptors and olfactory cells, where their role in sensory transduction is well established. CNG channels are mostly, nonselective cation channels, whose opening produces membrane depolarization and Ca2+ entry. In an olfactory cell, an odorant receptor with bound odorant activates a G protein, which stimulates adenylate cyclase to synthesize cAMP from ATP. The molecular mechanisms of modulation, and aspects of channel function modulated are currently under study. CNG channels have striking gating and permeation properties. CNG channel gating is very fast, typically giving very rapid flickers in single-channel currents. Amino acid sequences of cloned CNG channels suggest that they belong to the same channel superfamily as the voltage-gated Na+, K+, and Ca2+ channels. CNG channels were initially thought to be homo-oligomers, but it is now clear that they have at least two distinct types of subunits. The correlation of CNG channel structure and function is an exciting, fast-moving area of current research, which is leading to substantial insights into the mechanisms of channel gating and ion permeation." @default.
- W3022740890 created "2020-05-13" @default.
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- W3022740890 date "2001-01-01" @default.
- W3022740890 modified "2023-09-27" @default.
- W3022740890 title "Cyclic Nucleotide-Gated Ion Channels" @default.
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- W3022740890 doi "https://doi.org/10.1016/b978-012656976-6/50139-6" @default.
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