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

Lack of constitutive activation or inactivation of the platelet-activating factor receptor by glutamate substitution of alanine 230.

Receptors & signal transduction - 1 Jan 1996

Carlson S A, Chatterjee T K, Fisher R A

Abstract excerpt

The platelet-activating factor (PAF) receptor (PAFR) is a G protein-coupled receptor (GPCR) that mediates a diverse array of biological responses to PAF. Recently, we provided evidence that the third intracellular domain (3i) of the rat PAFR (rPAFR) is a critical determinant in its coupling to phosphoinositide phospholipase C (PI PLC)-activating G proteins. In the present study, we assessed the potential role of...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Conserved Sequence

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

Share to Dose-Response Relationship, Drug

Share to Enzyme Activation

Share to GTP-Binding Proteins

Share to Mutagenesis, Site-Directed

Share to Mutation

Source

Identifiers

PMID: 9015866

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

Lack of constitutive activation or inactivation of the platelet-activating factor receptor by glutamate substitution of alanine 230.PMID 9015866Read ↗

Mutation of a putative amphipathic alpha-helix in the third intracellular domain of the platelet-activating factor receptor disrupts receptor/G protein coupling and signaling.Semantic proximity Read ↗

Single nucleotide polymorphism of human platelet-activating factor receptor impairs G-protein activation.Semantic proximity Read ↗

Substitution of the cysteine 438 residue in the cytoplasmic tail of the glucagon-like peptide-1 receptor alters signal transduction activity.Semantic proximity Read ↗

An asn to lys polymorphism in the third intracellular loop of the human alpha 2A-adrenergic receptor imparts enhanced agonist-promoted Gi coupling.Semantic proximity Read ↗

Platelet-activating factor (PAF) receptor and genetically engineered PAF receptor mutant mice.Semantic proximity Read ↗

Phenotypic classification of mutants: a tool for understanding ligand binding and activation of muscarinic acetylcholine receptors.Semantic proximity Read ↗

Platelet-activating factor receptor.Semantic proximity Read ↗

Loss of receptor regulation by a phospholipase D1 mutant unresponsive to protein kinase C.Semantic proximity Read ↗

Lipid raft association and cholesterol sensitivity of P2X1-4 receptors for ATP: chimeras and point mutants identify intracellular amino-terminal residues involved in lipid regulation of P2X1 receptors.Semantic proximity Read ↗

Functional characterization of lysophosphatidic acid receptor 1 mutants identified in rat cancer tissues.Semantic proximity Read ↗

Inverse agonism and neutral antagonism at a constitutively active alpha-1a adrenoceptor.Semantic proximity Read ↗

Regulatory properties of alpha(1B)-adrenergic receptors defective in coupling to phosphoinositide hydrolysis.Semantic proximity Read ↗

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