Binding of [3H]perhydrohistrionicotoxin and [3H]phencyclidine to the nicotinic receptor-ion channel complex of Torpedo electroplax. Inhibition by histrionicotoxins and derivatives.

@article{Aronstam1985BindingO,
  title={Binding of [3H]perhydrohistrionicotoxin and [3H]phencyclidine to the nicotinic receptor-ion channel complex of Torpedo electroplax. Inhibition by histrionicotoxins and derivatives.},
  author={Robert S. Aronstam and Chung Ta King and Edson X. Albuquerque and John William Daly and Dan Feigl},
  journal={Biochemical pharmacology},
  year={1985},
  volume={34 17},
  pages={
          3037-47
        }
}
Histrionicotoxin, a spiropiperidine alkaloid, and twenty-two analogs inhibited binding of [3H]perhydrohistrionicotoxin [( 3H]H12-HTX) and of [3H]phencyclidine [( 3H]PCP) to sites on the acetylcholine receptor-ion complex of Torpedo electroplax membranes. Structural alterations to the nitrogen (secondary amine) or oxygen (alcohol) functions or to the five carbon and four carbon side chain of histrionicotoxin altered the potency versus [3H]H12-HTX and [3H]PCP binding measured in the presence or… CONTINUE READING

Citations

Publications citing this paper.
SHOWING 1-9 OF 9 CITATIONS

Characterization of cembranoid interaction with the nicotinic acetylcholine receptor.

  • The Journal of pharmacology and experimental therapeutics
  • 1998
VIEW 1 EXCERPT
CITES RESULTS
HIGHLY INFLUENCED

Regulation of nicotinic acetylcholine receptor function by adenine nucleotides

Vesna A. Eterović, Lian Li, Andrew Palma, Mark G. McNamee
  • Cellular and Molecular Neurobiology
  • 1990
VIEW 1 EXCERPT
CITES BACKGROUND