A Highly Conserved Aspartic Acid Residue in the Signature Disulfide Loop of the α1 Subunit Is a Determinant of Gating in the Glycine Receptor

This publication has 19 references indexed in Scilit:

• The Inhibitory Glycine Receptor—Simple Views of a Complicated Channel
  ChemBioChem, 2002
• The Startle Disease Mutation Q266H, in the Second Transmembrane Domain of the Human Glycine Receptor, Impairs Channel Gating
  Molecular Pharmacology, 1999
• Properties of human glycine receptors containing the hyperekplexia mutation α1(K276E), expressed in Xenopus oocytes
  The Journal of Physiology, 1998
• The glycine receptor
  Pharmacology & Therapeutics, 1997
• Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel
  The EMBO Journal, 1997
• Analysis of GLRA1 in hereditary and sporadic hyperekplexia: a novel mutation in a family cosegregating for hyperekplexia and spastic paraparesis.
  Journal of Medical Genetics, 1996
• Mutations in the α1 subunit of the inhibitory glycine receptor cause the dominant neurologic disorder, hyperekplexia
  Nature Genetics, 1993
• Distinct agonist- and antagonist-binding sites on the glycine receptor
  Neuron, 1992
• Modeling of agonist binding to the ligand‐gated ion channel superfamily of receptors
  Proteins-Structure Function and Bioinformatics, 1990
• Conserved quaternary structure of ligand-gated ion channels: the postsynaptic glycine receptor is a pentamer.
  Proceedings of the National Academy of Sciences, 1988