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• W1979017029 abstract "Ryanodine receptors (RyRs) are intracellular membrane channels playing key roles in many Ca(2+) signaling pathways and, as such, are emerging novel therapeutic and insecticidal targets. RyRs are so named because they bind the plant alkaloid ryanodine with high affinity and although it is established that ryanodine produces profound changes in all aspects of function, our understanding of the mechanisms underlying altered gating is minimal. We address this issue using detailed single-channel gating analysis, mathematical modeling, and energetic evaluation of state transitions establishing that, with ryanodine bound, the RyR pore adopts an extremely stable open conformation. We demonstrate that stability of this state is influenced by interaction of divalent cations with both activating and inhibitory cytosolic sites and, in the absence of activating Ca(2+), trans-membrane voltage. Comparison of the conformational stability of ryanodine- and Imperatoxin A-modified channels identifies significant differences in the mechanisms of action of these qualitatively similar ligands." @default.
• W1979017029 created "2016-06-24" @default.
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• W1979017029 creator A5046935369 @default.
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• W1979017029 date "2014-07-07" @default.
• W1979017029 modified "2023-09-26" @default.
• W1979017029 title "Insights into the Gating Mechanism of the Ryanodine-Modified Human Cardiac Ca²⁺-Release Channel (Ryanodine Receptor 2)" @default.
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• W1979017029 doi "https://doi.org/10.1124/mol.114.093757" @default.
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