The α5(H105R) mutation impairs α5 selective binding properties by altered positioning of the α5 subunit in GABAAreceptors containing two distinct types of α subunits

Author:

Balic Ela,Rudolph Uwe,Fritschy Jean-Marc,Mohler Hanns,Benke Dietmar

Publisher

Wiley

Subject

Cellular and Molecular Neuroscience,Biochemistry

Reference24 articles.

1. Native γ-aminobutyric acid type A receptors from rat hippocampus, containing both α1 and α5 subunits, exhibit a single benzodiazepine binding site with α5 pharmacological properties;Araujo;J. Pharmacol. Exp. Therap,1999

2. International Union of Pharmacology. XV. Subtypes of γ-aminobutyric acidA receptors: classification of the basis of subunit structure and receptor function;Barnard;Pharmacol. Rev.,1998

3. Influence of the pointmutation alpha-1-H101R on the assembly of gamma-aminobutyric acid type A receptors;Baur;Neuroreport,2005

4. Immunochemical identification of the α1- and α3-subunits of the GABAA-receptor in rat brain;Benke;J. Recept. Res,1991

5. GABAA-receptors display association of γ2-subunit with α1-subunit and β2/3-subunits;Benke;J. Biol. Chem.,1991

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