Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A single point mutation of the GABA(A) receptor alpha5-subunit confers fluoxetine sensitivity.

Neuropharmacology - 1 Feb 2007

Derry Jason M C, Paulsen Isabelle M, Davies Martin, Dunn Susan M J

Abstract excerpt

Fluoxetine has been reported to be a novel allosteric modulator of GABA(A) receptors with the notable exception of receptors that contain the alpha5-subunit isoform [Robinson, R.T., Drafts, B.C., Fisher, J.L., 2003. Fluoxetine increases GABA(A) receptor activity through a novel modulatory site. J...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Drug Interactions
Share to Electric Stimulation
Share to Fluoxetine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to gamma-Aminobutyric Acid

Share to Isoxazoles

Share to Receptors, GABA-A

Share to Selective Serotonin Reuptake Inhibitors

Share to Xenopus laevis

Source

Identifiers

PMID: 17045313
DOI: 10.1016/j.neuropharm.2006.07.036

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17045313-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A single point mutation of the GABA(A) receptor alpha5-subunit confers fluoxetine sensitivity.PMID 17045313Read ↗

A mutation in the GABAA receptor alpha 1 subunit linked to human epilepsy affects channel gating properties.Semantic proximity Read ↗

The alpha5(H105R) mutation impairs alpha5 selective binding properties by altered positioning of the alpha5 subunit in GABAA receptors containing two distinct types of alpha subunits.Semantic proximity Read ↗

Tricyclic antipsychotics and antidepressants can inhibit α5-containing GABA A receptors by two distinct mechanismsSemantic proximity Read ↗

Mutation of glutamate 155 of the GABAA receptor beta2 subunit produces a spontaneously open channel: a trigger for channel activation.Semantic proximity Read ↗

Mutations of the GABA-A receptor alpha1 subunit M1 domain reveal unexpected complexity for modulation by neuroactive steroids.Semantic proximity Read ↗

Role of the histidine residue at position 105 in the human alpha 5 containing GABA(A) receptor on the affinity and efficacy of benzodiazepine site ligands.Semantic proximity Read ↗

Mutations of α1F45 residue of GABAA receptor loop G reveal its involvement in agonist binding and channel opening/closing transitions.Semantic proximity Read ↗

Mutation at the putative GABA(A) ion-channel gate reveals changes in allosteric modulation.Semantic proximity Read ↗

An isoflurane- and alcohol-insensitive mutant GABA(A) receptor alpha(1) subunit with near-normal apparent affinity for GABA: characterization in heterologous systems and production of knockin mice.Semantic proximity Read ↗

Structural analysis of the positive AMPA receptor modulators CX516 and Me-CX516 in complex with the GluA2 ligand-binding domain.Semantic proximity Read ↗

Loop F of the GABAA receptor alpha subunit governs GABA potency.Semantic proximity Read ↗

Enhancement of α5-containing γ-aminobutyric acid type A receptors by the nonimmobilizer 1,2-dichlorohexafluorocyclobutane (F6) is abolished by the β3(N265M) mutation.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.