Determination of the subunit stoichiometry of a voltage-activated potassium channel (Q28270398)

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Language	Label	Description	Also known as
English	Determination of the subunit stoichiometry of a voltage-activated potassium channel	scientific article

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Determination of the subunit stoichiometry of a voltage-activated potassium channel (English)

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author name string

R MacKinnon

1

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publication date

21 March 1991

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350

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232-5

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6315

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Heteropolymeric potassium channels expressed in Xenopus oocytes from cloned subunits.

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Evidence for the formation of heteromultimeric potassium channels in Xenopus oocytes

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Heteromultimeric channels formed by rat brain potassium-channel proteins.

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Sequence of a probable potassium channel component encoded at Shaker locus of Drosophila

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Structure and function of voltage-sensitive ion channels

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A Rosetta stone for K channels.

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Charybdotoxin, a protein inhibitor of single Ca2+-activated K+ channels from mammalian skeletal muscle

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Charybdotoxin block of single Ca2+-activated K+ channels. Effects of channel gating, voltage, and ionic strength

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Mechanism of charybdotoxin block of the high-conductance, Ca2+-activated K+ channel

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Charybdotoxin block of Shaker K+ channels suggests that different types of K+ channels share common structural features

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Mutant potassium channels with altered binding of charybdotoxin, a pore-blocking peptide inhibitor

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Mapping the receptor site for charybdotoxin, a pore-blocking potassium channel inhibitor

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Single-channel currents of an intercellular junction

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Gap junction structures. V. Structural chemistry inferred from X-ray diffraction measurements on sucrose accessibility and trypsin susceptibility

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The structure of ion channels in membranes of excitable cells

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Multiple products of the Drosophila Shaker gene may contribute to potassium channel diversity

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Rapid and efficient site-specific mutagenesis without phenotypic selection

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DNA sequencing with chain-terminating inhibitors

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Inactivation of the sodium channel. I. Sodium current experiments

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Molecular Structure of Charybdotoxin, a Pore-Directed Inhibitor of Potassium Ion Channels

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11 February 2024

https://opencitations.net/index/api/v1/citations/10.1126/SCIENCE.1696395

Identifiers

10.1038/350232A0

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Dimensions Publication ID

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release_5aqqw6igyjdr7pajy5v6kwrfqi

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https://api.fatcat.wiki/v0/release/5aqqw6igyjdr7pajy5v6kwrfqi

24 November 2022

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mapped directly with Wikidata item

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Springer Nature article ID

10.1038/350232a0

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