ArticleBiophysical journal2003
Control of ion conduction in L-type Ca2+ channels by the concerted action of S5-6 regions.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- The Cav1.2 N terminus contains a CaM kinase site that modulates channel trafficking and function.Pflugers Archiv : European journal of physiology · 2015Article
- Voltage control of Ca²⁺ permeation through N-type calcium (Ca(V)2.2) channels.The Journal of general physiology · 2014Article
- Article
- How "Pharmacoresistant" is Cav2.3, the Major Component of Voltage-Gated R-type Ca2+ Channels?Pharmaceuticals (Basel, Switzerland) · 2013Article
- Molecular determinant for specific Ca/Ba selectivity profiles of low and high threshold Ca2+ channels.The Journal of general physiology · 2007Article
- Block of CaV1.2 channels by Gd3+ reveals preopening transitions in the selectivity filter.The Journal of general physiology · 2007Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Voltage-gated L-type Ca(2+) channels from cardiac (alpha(1C)) and skeletal (alpha(1S)) muscle differ from one another in ion selectivity and permeation properties, including unitary conductance. In 110 mM Ba(2+), unitary conductance of alpha(1S) is approximately half that of alpha(1C). As a step toward understanding the mechanism of rapid ion flux through these highly selective ion channels, we used chimeras constructed between alpha(1C) and alpha(1S) to identify structural features responsible for the difference in conductance. Combined replacement of the four pore-lining P-loops in alpha(1C) with P-loops from alpha(1S) reduced unitary conductance to a value intermediate between those of the two parent channels. Combined replacement of four larger regions that include sequences flanking the P-loops (S5 and S6 segments along with the P-loop-containing linker between these segments (S5-6)) conferred alpha(1S)-like conductance on alpha(1C). Likewise, substitution of the four S5-6 regions of alpha(1C) into alpha(1S) conferred alpha(1C)-like conductance on alpha(1S). These results indicate that, comparing alpha(1C) with alpha(1S), the differences in structure that are responsible for the difference in ion conduction are housed within the S5-6 regions. Moreover, the pattern of unitary conductance values obtained for chimeras in which a single P-loop or single S5-6 region was replaced suggest a concerted action of pore-lining regions in the control of ion conduction.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.