Mutant human α1β1(T262Q) GABAA receptors are directly activated but not modulated by pentobarbital

This publication has 14 references indexed in Scilit:

• Propofol and Other Intravenous Anesthetics Have Sites of Action on the γ-Aminobutyric Acid Type A Receptor Distinct from That for Isoflurane
  Molecular Pharmacology, 1998
• The interaction of the general anesthetic etomidate with the γ-aminobutyric acid type A receptor is influenced by a single amino acid
  Proceedings of the National Academy of Sciences, 1997
• Sites of alcohol and volatile anaesthetic action on GABAA and glycine receptors
  Nature, 1997
• Insensitivity to anaesthetic agents conferred by a class of GABAA receptor subunit
  Nature, 1997
• A Structural Determinant of Desensitization and Allosteric Regulation by Pentobarbitone of the GABA A Receptor
  The Journal of Membrane Biology, 1997
• The agonistic action of pentobarbital on GABAA β-subunit homomeric receptors
  NeuroReport, 1996
• Rapid desensitization of ?1?1 GABAA receptors expressed in Sf9 cells under optimized conditions
  The Journal of Membrane Biology, 1995
• GABAA receptor needs two homologous domains of the & beta;-subunit for activation by GABA but not by pentobarbital
  Nature, 1993
• Functional characteristics and sites of gene expression of the alpha 1, beta 1, gamma 2-isoform of the rat GABAA receptor
  Journal of Neuroscience, 1990
• Kinetic properties of the pentobarbitone‐gated chloride current in frog sensory neurones.
  The Journal of Physiology, 1987