ArticleBiophysical journal2002
Ryanodine-induced structural alterations in the RyR channel suggested by neomycin block.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Article
- CapZ integrates several signaling pathways in response to mechanical stiffness.The Journal of general physiology · 2019Article
- Protecting Mammalian Hair Cells from Aminoglycoside-Toxicity: Assessing Phenoxybenzamine's Potential.Frontiers in cellular neuroscience · 2017Article
- Insights into the gating mechanism of the ryanodine-modified human cardiac Ca2+-release channel (ryanodine receptor 2).Molecular pharmacology · 2014Article
- The ryanodine receptor pore blocker neomycin also inhibits channel activity via a previously undescribed high-affinity Ca(2+) binding site.The Journal of membrane biology · 2007Article
- Two rings of negative charges in the cytosolic vestibule of type-1 ryanodine receptor modulate ion fluxes.Biophysical journal · 2006Article
- Electrostatic mechanisms underlie neomycin block of the cardiac ryanodine receptor channel (RyR2).Biophysical journal · 2004Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Mead and Williams, (Biophys. J. 82:1953-1963, 2002) we have reported that neomycin is a potent partial blocker of single purified sheep cardiac SR calcium release channels. Neomycin is unusual in that it is capable of blocking when applied to either the cytosolic or the luminal face of the channel. Block at either aspect of the channel is both concentration- and voltage-dependent, but exhibits different blocking parameters. In this study we have investigated the actions of neomycin on ion handling in the ryanodine-modified channel. Neomycin is more effective at the cytosolic face, having a Kb(0) value of 534.9 +/- 35.17 nM compared with a Kb(0) value of 971.5 +/- 66.62 nM for the luminal face. The voltage dependence also differs at the two sites. Values of zdelta for cytosolic and luminal neomycin are 1.09 +/- 0.04 and -0.57 +/- 0.03, respectively. The interaction of neomycin with the ryanodine-modified channel differs notably from that in the unmodified channel. Voltage-dependent relief of block is not observed after ryanodine modification, and the luminal blocking characteristics are altered. This suggests that ryanodine induces changes at the luminal mouth of the channel and may confer increased rigidity to the channel protein.
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