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September 1, 1990Journal of Biological ChemistryOpen Access

Characterization of high affinity binding sites for charybdotoxin in synaptic plasma membranes from rat brain. Evidence for a direct association with an inactivating, voltage-dependent, potassium channel.

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Authors

JVJesús VázquezCross-Cutting CardiologyPFP. FeigenbaumUniversity of Maryland, BaltimoreVKV. Frank KingMerck & Co., Inc., Rahway, NJ, USA (United States)

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Cite This Study

Vázquez et al. (1990) studied this question.

synapsesocial.com/papers/6a71a23635aa2c282ce2d9a6https://doi.org/10.1016/s0021-9258(18)55434-x
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Also Consider

Synapse has enriched 3 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Interaction of Tetraethylammonium Ion Derivatives with the Potassium Channels of Giant Axons1971 · 937 citations
  2. 2Charybdotoxin block of single Ca2+-activated K+ channels. Effects of channel gating, voltage, and ionic strength.1988 · 252 citations
  3. 3Characterization of High Affinity Binding Sites for Charybdotoxin in Sarcolemmal Membranes from Bovine Aortic Smooth Muscle1989 · 84 citations