Block of nicotinic acetylcholine receptors by philanthotoxins is strongly dependent on their subunit composition
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/srep38116.pdf
Reference23 articles.
1. Eldefrawi, A. T. et al. Structure and synthesis of a potent glutamate receptor antagonist in wasp venom. Proc Natl Acad Sci USA 85, 4910–4913 (1988).
2. Piek, T. delta-Philanthotoxin, a semi-irreversible blocker of ion-channels. Comp Biochem Physiol C 72, 311–315 (1982).
3. Bahring, R. & Mayer, M. L. An analysis of philanthotoxin block for recombinant rat GluR6(Q) glutamate receptor channels. J Physiol 509 (Pt 3), 635–650 (1998).
4. McClymont, D. W., Harris, J. & Mellor, I. R. Open-channel blockade is less effective on GluN3B than GluN3A subunit-containing NMDA receptors. Eur J Pharmacol 686, 22–31, doi: 10.1016/j.ejphar.2012.04.036 (2012).
5. Mellor, I. R. et al. Modification of the philanthotoxin-343 polyamine moiety results in different structure-activity profiles at muscle nicotinic ACh, NMDA and AMPA receptors. Neuropharmacology 44, 70–80 (2003).
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