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

Mutations in the extracellular amino-terminal domain of the NK2 neurokinin receptor abolish cAMP signaling but preserve intracellular calcium responses.

The Journal of biological chemistry - 1 Nov 2002

Lecat Sandra, Bucher Bernard, Mely Yves, Galzi Jean-Luc

Abstract excerpt

By combining real time measurements of agonist binding, by fluorescence resonance energy transfer, and of subsequent responses, we proposed previously that the neurokinin NK2 receptor preexists in equilibrium between three states: inactive, calcium-triggering, and cAMP-producing. Thr(24) and Phe(...

Read the complete abstract on PubMed

Topics

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

Share to Calcium
Share to Cyclic AMP
Share to Fluorescence Resonance Energy Transfer

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Kinetics

Share to Models, Theoretical

Share to Protein Conformation

Share to Structure-Activity Relationship

Share to Substance P

Source

Identifiers

PMID: 12185075
DOI: 10.1074/jbc.M203606200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-12185075-2026-09-02.2. 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

Mutations in the extracellular amino-terminal domain of the NK2 neurokinin receptor abolish cAMP signaling but preserve intracellular calcium responses.PMID 12185075Read ↗

C-terminal truncation of the neurokinin-2 receptor causes enhanced and sustained agonist-induced signaling. Role of receptor phosphorylation in signal attenuation.Semantic proximity Read ↗

NK1 receptor fused to beta-arrestin displays a single-component, high-affinity molecular phenotype.Semantic proximity Read ↗

Two active molecular phenotypes of the tachykinin NK1 receptor revealed by G-protein fusions and mutagenesis.Semantic proximity Read ↗

Truncated, desensitization-defective neurokinin receptors mediate sustained MAP kinase activation, cell growth and transformation by a Ras-independent mechanism.Semantic proximity Read ↗

Development of a BRET2 screening assay using beta-arrestin 2 mutants.Semantic proximity Read ↗

Alanine-(87)-threonine polymorphism impairs signaling and internalization of the human P2Y11 receptor, when co-expressed with the P2Y1 receptor.Semantic proximity Read ↗

Sequential phosphorylation mediates receptor- and kinase-induced inhibition of TREK-1 background potassium channels.Semantic proximity Read ↗

Conformational compatibility as a basis of differential affinities of tachykinins for the neurokinin-1 receptor.Semantic proximity Read ↗

Role of hydroxyl containing residues in the intracellular region of rat bradykinin B(2) receptor in signal transduction, receptor internalization, and resensitization.Semantic proximity Read ↗

Replacement of threonine 394 by alanine facilitates internalization and resensitization of the rat mu opioid receptor.Semantic proximity Read ↗

Interaction of Met297 in the seventh transmembrane segment of the tachykinin NK2 receptor with neurokinin A.Semantic proximity Read ↗

Occurrence and pharmacological characterization of four human tachykinin NK2 receptor variants.Semantic proximity Read ↗

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