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

Modulation of 5-HT(1A) receptor activation by its interaction with wild-type and mutant g(alphai3) proteins.

Neuropharmacology - 1 Jan 2001

Dupuis D S, Wurch T, Tardif S, Colpaert F C, Pauwels P J

Abstract excerpt

Constitutive and agonist-dependent activation of the recombinant human 5-HT(1A) receptor (RC: 2.1.5HT.01A) was investigated by co-expression with a rat G(alphai3) protein in Cos-7 cells. The interaction between the 5-HT(1A) receptor and rat G(alphai3) protein was modulated by substitution of the G(alphai3) protein site for pertussis toxin-catalysed ADP-ribosylation (cysteine(351)) by each of the natural amino...

Read the complete abstract on PubMed

Topics

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

Share to COS Cells
Share to GTP-Binding Protein alpha Subunits, Gi-Go

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Guanosine 5'-O-(3-Thiotriphosphate)

Share to Pertussis Toxin

Share to Radioligand Assay

Share to Receptors, Serotonin

Share to Serotonin Receptor Agonists

Share to Virulence Factors, Bordetella

Source

Identifiers

PMID: 11077069
DOI: 10.1016/s0028-3908(00)00098-8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Modulation of 5-HT(1A) receptor activation by its interaction with wild-type and mutant g(alphai3) proteins.PMID 11077069Read ↗

Regulation of the avidity of ternary complexes containing the human 5-HT(1A) receptor by mutation of a receptor contact site on the interacting G protein alpha subunit.Semantic proximity Read ↗

Allosteric modulation and constitutive activity of fusion proteins between the adenosine A1 receptor and different 351Cys-mutated Gi alpha-subunits.Semantic proximity Read ↗

Interactions of the alpha2A-adrenoceptor with multiple Gi-family G-proteins: studies with pertussis toxin-resistant G-protein mutants.Semantic proximity Read ↗

A unique phenotype of 5-HT2C, agonist-induced GTPgamma35S binding, transferable to 5-HT2A and 5-HT2B, upon swapping intracellular regions.Semantic proximity Read ↗

The recombinant 5-HT1A receptor: G protein coupling and signalling pathways.Semantic proximity Read ↗

Modifying ligand-induced and constitutive signaling of the human 5-HT4 receptor.Semantic proximity Read ↗

Activation of constitutive 5-hydroxytryptamine(1B) receptor by a series of mutations in the BBXXB motif: positioning of the third intracellular loop distal junction and its G(o)alpha protein interactions.Semantic proximity Read ↗

Mutation in a protein kinase C phosphorylation site of the 5-HT1A receptor preferentially attenuates Ca2+ responses to partial as opposed to higher-efficacy 5-HT1A agonists.Semantic proximity Read ↗

Closely related G-protein-coupled receptors use multiple and distinct domains on G-protein alpha-subunits for selective coupling.Semantic proximity Read ↗

Site-directed mutagenesis of the 5-HT1B receptor increases the affinity of 5-HT for the agonist low-affinity conformation and reduces the intrinsic activity of 5-HT.Semantic proximity Read ↗

The 5-hydroxytryptamine(1A) receptor is stably palmitoylated, and acylation is critical for communication of receptor with Gi protein.Semantic proximity Read ↗

Localization of the mouse 5-hydroxytryptamine(1A) receptor in lipid microdomains depends on its palmitoylation and is involved in receptor-mediated signaling.Semantic proximity Read ↗

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