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Cited by 347

The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.

Mutant Potassium Channels with Altered Binding of Charybdotoxin, a Pore-Blocking Peptide Inhibitor

MacKinnon, Roderick, Miller, Christopher·1989·Science

Abstract

The inhibition by charybdotoxin of A-type potassium channels expressed in Xenopus oocytes was studied for several splicing variants of the Drosophila Shaker gene and for several site-directed mutants of this channel. Charybdotoxin blocking affinity is lowered by a factor of 3.5 upon replacing glutamate-422 with glutamine, and by a factor of about 12 upon substituting lysine in this position. Replacement of glutamate-422 by aspartate had no effect on toxin affinity. Thus, the glutamate residue at position 422 of this potassium channel is near or in the externally facing mouth of the potassium conduction pathway, and the positively charged toxin is electrostatically focused toward its blocking site by the negative potential set up by glutamate-422.

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Metadata

Authors
MacKinnon, R., & Miller, C.
Venue
Science
Published
1989-09-22
Volume
245
Issue
4924
Pages
1382-1385
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1972116208
Cited by
347
References
22
FWCI
8.31
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Mutant Potassium Channels with Altered Binding of Charybdotoxin, a Pore-Blocking Peptide Inhibitor. https://app.cochat.ai/papers/10.1126/science.2476850
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MacKinnon, R., & Miller, C. (1989). Mutant Potassium Channels with Altered Binding of Charybdotoxin, a Pore-Blocking Peptide Inhibitor. Science. https://doi.org/10.1126/science.2476850

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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.