The pore domain of the nicotinic acetylcholine receptor: molecular modeling, pore dimensions, and electrostatics

This publication has 64 references indexed in Scilit:

• Acetylcholine Receptors: Too Many Channels, Too Few Functions
  Science, 1995
• Design of Molecular Function: Channels of Communication
  Annual Review of Biophysics, 1995
• Conductance mutations of the nicotinic acetylcholine receptor do not act by a simple electrostatic mechanism
  Biophysical Journal, 1994
• The pore dimensions of gramicidin A
  Biophysical Journal, 1993
• Hydrophilic surface maps of channel-forming peptides: analysis of amphipathic helices
  European Biophysics Journal, 1993
• Stratification of the channel domain in neurotransmitter receptors
  Current Opinion in Cell Biology, 1993
• An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase.
  Proceedings of the National Academy of Sciences, 1993
• Successful prediction of the coiled coil geometry of the GCN4 leucine zipper domain by simulated annealing: Comparison to the X‐ray structure
  Proteins-Structure Function and Bioinformatics, 1993
• Nicotinic Acetylcholine Receptor an 9 Å Resolution
  Journal of Molecular Biology, 1993
• The functional architecture of the acetylcholine nicotinic receptor explored by affinity labelling and site-directed mutagenesis
  Quarterly Reviews of Biophysics, 1992