Using the deadly μ-conotoxins as probes of voltage-gated sodium channels

This publication has 30 references indexed in Scilit:

• Charge conversion enables quantification of the proximity between a normally‐neutral μ‐conotoxin (GIIIA) site and the Na⁺ channel pore
  FEBS Letters, 2002
• Latent Specificity of Molecular Recognition in Sodium Channels Engineered To Discriminate between Two “Indistinguishable” μ-Conotoxins
  Biochemistry, 2001
• The Structure of the Potassium Channel: Molecular Basis of K ⁺ Conduction and Selectivity
  Science, 1998
• Predominant Interactions between μ-Conotoxin Arg-13 and the Skeletal Muscle Na⁺Channel Localized by Mutant Cycle Analysis
  Biochemistry, 1998
• Ion channels as enzymes: analogy or homology?
  Trends in Neurosciences, 1997
• Three-Dimensional Solution Structure of μ-Conotoxin GIIIB, a Specific Blocker of Skeletal Muscle Sodium Channels^,
  Biochemistry, 1996
• Electrostatic distance geometry in a K+ channel vestibule.
  Proceedings of the National Academy of Sciences, 1994
• Structure-activity relationships of .mu.-conotoxin GIIIA: structure determination of active and inactive sodium channel blocker peptides by NMR and simulated annealing calculations
  Biochemistry, 1992
• Action of derivatives of .mu.-conotoxin GIIIA on sodium channels. Single amino acid substitutions in the toxin separately affect association and dissociation rates
  Biochemistry, 1992
• Disulfide pairings in geographutoxin I, a peptide neurotoxin from Conus geographus
  FEBS Letters, 1990