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Structural determinants of the pharmacological properties of the GABAA receptor alpha6 subunit.
A mutation in the GABAA receptor alpha 1 subunit linked to human epilepsy affects channel gating properties.
The alpha 1 and alpha 6 subunit subtypes of the mammalian GABA(A) receptor confer distinct channel gating kinetics.
Identification of structures within GABAA receptor alpha subunits that regulate the agonist action of pentobarbital.
Effect of the alpha subunit subtype on the macroscopic kinetic properties of recombinant GABA(A) receptors.
The anti-convulsant stiripentol acts directly on the GABA(A) receptor as a positive allosteric modulator.
RNA editing of the GABA(A) receptor alpha3 subunit alters the functional properties of recombinant receptors.
Activation of alpha6-containing GABAA receptors by pentobarbital occurs through a different mechanism than activation by GABA.
The wake-promoting transmitter histamine preferentially enhances a-4 subunit-containing GABAA receptors.
Amiloride inhibition of gamma-aminobutyric acid(A) receptors depends upon the alpha subunit subtype.
A lysine residue in the beta3 subunit contributes to the regulation of GABA(A) receptor activity by voltage.
Fluoxetine increases GABA(A) receptor activity through a novel modulatory site.