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GABAA Receptor α and γ Subunits Shape Synaptic Currents via Different Mechanisms
57/57 checkable references clean · checked 2026-07-23
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The 57 checked references that resolve
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Benzodiazepines Modulate GABA<sub>A</sub>Receptors by Regulating the Preactivation Step after GABA Binding
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Key Amino Acids in the γ Subunit of the γ-Aminobutyric AcidA Receptor that Determine Ligand Binding and Modulation at the Benzodiazepine Site
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A point mutation in the γ
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Subtle Changes in Residue 77 of the γ Subunit of α1β2γ2 GABAA Receptors Drastically Alter the Affinity for Ligands of the Benzodiazepine Binding Site
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Structural Mechanisms Underlying Benzodiazepine Modulation of the GABA<sub>A</sub>Receptor
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Pathway-Specific Targeting of GABA<sub>A</sub>Receptor Subtypes to Somatic and Dendritic Synapses in the Central Amygdala
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Activated radixin is essential for GABAA receptor α5 subunit anchoring at the actin cytoskeleton
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Mechanisms underlying synapse‐specific clustering of GABA<sub>A</sub>receptors
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Segregation of Different GABA<sub>A</sub>Receptors to Synaptic and Extrasynaptic Membranes of Cerebellar Granule Cells
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Decreased GABAA-receptor clustering results in enhanced anxiety and a bias for threat cues
The 2 references without a DOI — listed, not checked
no DOI — not checkedDifferences in affinity and efficacy of benzodiazepine receptor ligands at recombinant γ-aminobutyric acidA receptor subtypes
no DOI — not checkedFitting and statistical analysis of single-channel records
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