C-terminus of a long α-neurotoxin is highly mobile when bound to the nicotinic acetylcholine receptor: A time-resolved fluorescence anisotropy approach-Reference-Cited by-同舟云学术

C-terminus of a long α-neurotoxin is highly mobile when bound to the nicotinic acetylcholine receptor: A time-resolved fluorescence anisotropy approach

Published:2005-08 Issue:3 Volume:116 Page:213-218
ISSN:0301-4622
Container-title:Biophysical Chemistry
language:en
Short-container-title:Biophysical Chemistry

Author:

Johnson David A.

Publisher

Elsevier BV

Subject

Organic Chemistry,Biochemistry,Biophysics

Reference20 articles.

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3. Distinct protein components from Torpedo marmorata membranes carry the acetylcholine receptor site and the binding site for local anesthetics and histrionicotoxin;Sobel;Proc. Natl. Acad. Sci. U. S. A.,1979

4. Direct structural localization of two toxin-recognition sites on an ACh receptor protein;Zingsheim;Nature,1982

5. Fluorescence energy transfer between α-toxins bound to the acetylcholine receptors;Johnson;J. Biol. Chem.,1984

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3. Structural answers and persistent questions about how nicotinic receptors work;Frontiers in Bioscience;2008

4. Bacterial Expression, NMR, and Electrophysiology Analysis of Chimeric Short/Long-chain α-Neurotoxins Acting on Neuronal Nicotinic Receptors;Journal of Biological Chemistry;2007-08

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