ArticleThe Journal of general physiology2000
The interaction of a neutral ryanoid with the ryanodine receptor channel provides insights into the mechanisms by which ryanoid binding is modulated by voltage.
Article in The Journal of general physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- CaAmerican journal of physiology. Endocrinology and metabolism · 2023Review
- Multiple modes of ryanodine receptor 2 inhibition by flecainide.Molecular pharmacology · 2014Article
- A mechanistic description of gating of the human cardiac ryanodine receptor in a regulated minimal environment.The Journal of general physiology · 2012Article
- Ryanodol action on calcium sparks in ventricular myocytes.Pflugers Archiv : European journal of physiology · 2010Article
- Flecainide inhibits arrhythmogenic Ca2+ waves by open state block of ryanodine receptor Ca2+ release channels and reduction of Ca2+ spark mass.Journal of molecular and cellular cardiology · 2010Article
- Article
- Ca2+-calmodulin increases RyR2 open probability yet reduces ryanoid association with RyR2.Biophysical journal · 2009Article
- Amitriptyline activates cardiac ryanodine channels and causes spontaneous sarcoplasmic reticulum calcium release.Molecular pharmacology · 2009Article
- Ryanoids and imperatoxin affect the modulation of cardiac ryanodine receptors by dihydropyridine receptor Peptide A.Biochimica et biophysica acta · 2008Article
- Voltage-sensitive equilibrium between two states within a ryanoid-modified conductance state of the ryanodine receptor channel.Biophysical journal · 2005Article
- Effects of ryanoids on spontaneous and depolarization-evoked calcium release events in frog muscle.Biophysical journal · 2004Article
- An anionic ryanoid, 10-O-succinoylryanodol, provides insights into the mechanisms governing the interaction of ryanoids and the subsequent altered function of ryanodine-receptor channels.The Journal of general physiology · 2003Article
- Role of the proposed pore-forming segment of the Ca2+ release channel (ryanodine receptor) in ryanodine interaction.Biophysical journal · 2002Article
- Ryanodine-induced structural alterations in the RyR channel suggested by neomycin block.Biophysical journal · 2002Article
- Ryanoid modification of the cardiac muscle ryanodine receptor channel results in relocation of the tetraethylammonium binding site.The Journal of general physiology · 2001Article
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5 authors.
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Abstract
In an earlier investigation, we demonstrated that the likelihood of interaction of a positively charged ryanoid, 21-amino-9alpha-hydroxyryanodine, with the sarcoplasmic reticulum Ca(2+)-release channel (ryanodine receptor, RyR) is dependent on holding potential (Tanna, B., W. Welch, L. Ruest, J.L. Sutko, and A. J. Williams. 1998. J. Gen. Physiol. 112:55-69) and suggested that voltage dependence could result from either the translocation of the charged ligand to a site within the voltage drop across the channel or a voltage-driven alteration in receptor affinity. We now report experiments that allow us to assess the validity of these alternate mechanisms. Ryanodol is a neutral ryanoid that binds to RyR and induces modification of channel function. By determining the influence of transmembrane potential on the probability of channel modification by ryanodol and the rate constants of ryanodol association and dissociation, we demonstrate that the influence of voltage is qualitatively the same for both the neutral and positively charged ryanoids. These experiments establish that most, if not all, of the modification of ryanoid interaction with RyR by transmembrane holding potential results from a voltage-driven alteration in receptor affinity.
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