A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom (Q34331989)

1 August 2017

A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom (English)

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1 August 2017

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2

Roderick MacKinnon

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1 August 2017

Seok-Yong Lee

1

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PubMed ID

15241419

1 August 2017

language of work or name

English

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publication date

1 July 2004

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1 August 2017

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1 August 2017

430

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1 August 2017

6996

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1 August 2017

232-235

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https://scigraph.springernature.com/pub.10.1038/nature02632

1 August 2017

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How to measure and analyze tryptophan fluorescence in membranes properly, and why bother?

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Apamin as a selective blocker of the calcium-dependent potassium channel in neuroblastoma cells: voltage-clamp and biochemical characterization of the toxin receptor

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Diffusion-controlled binding of a peptide neurotoxin to its potassium channel receptor

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Influence of protein surface charge on the bimolecular kinetics of a potassium channel peptide inhibitor

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Three-dimensional structure in solution of neurotoxin III from the sea anemone Anemonia sulcata

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Purification and characterization of three inhibitors of voltage-dependent K+ channels from Leiurus quinquestriatus var. hebraeus venom

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The Role of Diffusion in Enzyme Kinetics

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Effects of phrixotoxins on the Kv4 family of potassium channels and implications for the role of Ito1 in cardiac electrogenesis

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1038/NATURE02632

Identifiers

DOI

10.1038/NATURE02632

1 reference

PubMed ID

15241419

Dimensions Publication ID

1 August 2017

0 references

1 reference

PubMed ID

15241419