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Cited by 218

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The Ca channel in skeletal muscle is a large pore.

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McCleskey, E W, Almers, W·1985·Proceedings of the National Academy of Sciences

Abstract

The permeability of Ca channels to various foreign cations has been investigated in the absence of external Ca2+. All physiological metal cations are clearly permeant, including Mg2+. The large organic cation n-butylamine+ is sparingly permeant or impermeant, but its larger derivative 1,4-diaminobutane2+ is highly permeant. Among the cations of the methylated ammonium series, permeability diminishes in a graded fashion as ion size increases. Tetramethylammonium, the largest cation found to be permeant, has a diameter of about 6 A; hence, the aqueous pore of the Ca channel at its narrowest point can be no smaller. That the pore is so large strengthens our view that, under physiologic conditions, the high selectivity of Ca channels is due to selective binding of Ca2+ rather than to rejection of other cations by, for example, a sieving mechanism.

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Metadata

Authors
McCleskey, E. W., & Almers, W.
Venue
Proceedings of the National Academy of Sciences
Published
1985-10
Volume
82
Issue
20
Pages
7149-7153
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1970288191
Cited by
218
References
0
FWCI
3.36
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: The Ca channel in skeletal muscle is a large pore. https://app.cochat.ai/papers/10.1073/pnas.82.20.7149
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McCleskey, E. W., & Almers, W. (1985). The Ca channel in skeletal muscle is a large pore. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.82.20.7149

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.