Conformational Analysis of a Model for the trans-Fused FGH Ether Rings in Brevetoxin A
Author:
Affiliation:
1. Department of Chemistry, Gottwald Center for the Sciences, University of Richmond, Richmond, Virginia 23173
Publisher
American Chemical Society (ACS)
Subject
Organic Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/jo902558h
Reference26 articles.
1. Structure of brevetoxin A (GB-1 toxin), the most potent toxin in the Florida red tide organism Gymnodinium breve (Ptychodiscus brevis)
2. Brevetoxin B: Chemical Modifications, Synaptosome Binding, Toxicity, and an Unexpected Conformational Effect
3. Conformational Analysis of the Sodium Channel Modulator, Brevetoxin A, Comparison with Brevetoxin B Conformations, and a Hypothesis about the Common Pharmacophore of the "Site 5" Toxins
4. Binding of brevetoxins and ciguatoxin to the voltage-sensitive sodium channel and conformational analysis of brevetoxin B
5. X-ray Crystallographic Studies of Marine Toxins
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