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

Acid potentiation of the capsaicin receptor determined by a key extracellular site.

Proceedings of the National Academy of Sciences of the United States of America - 5 Jul 2000

Jordt S E, Tominaga M, Julius D

Abstract excerpt

The capsaicin (vanilloid) receptor, VR1, is a sensory neuron-specific ion channel that serves as a polymodal detector of pain-producing chemical and physical stimuli. The response of VR1 to capsaicin or noxious heat is dynamically potentiated by extracellular protons within a pH range encountered during tissue acidosis, such as that associated with arthritis, infarction, tumor growth, and other forms of injury. A...

Read the complete abstract on PubMed

Topics

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

Share to Acids
Share to Cell Death
Share to Nociceptors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protons

Share to Receptors, Drug

Share to Selection, Genetic

Share to Titrimetry

Share to TRPV Cation Channels

Source

Open in PubMed Open full text

Identifiers

PMID: 10859346
DOI: 10.1073/pnas.100129497
PMCID: PMC16682

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Acid potentiation of the capsaicin receptor determined by a key extracellular site.PMID 10859346Read ↗

Distinct modulations of human capsaicin receptor by protons and magnesium through different domains.Semantic proximity Read ↗

cAMP-dependent protein kinase regulates desensitization of the capsaicin receptor (VR1) by direct phosphorylation.Semantic proximity Read ↗

The molecular basis for species-specific activation of human TRPA1 protein by protons involves poorly conserved residues within transmembrane domains 5 and 6.Semantic proximity Read ↗

Direct phosphorylation of capsaicin receptor VR1 by protein kinase Cepsilon and identification of two target serine residues.Semantic proximity Read ↗

TRPV1.Semantic proximity Read ↗

Functionally important amino acid residues in the transient receptor potential vanilloid 1 (TRPV1) ion channel--an overview of the current mutational data.Semantic proximity Read ↗

Functional characterisation of the S512Y mutant vanilloid human TRPV1 receptor.Semantic proximity Read ↗

Temperature-induced opening of TRPV1 ion channel is stabilized by the pore domain.Semantic proximity Read ↗

Identification of species-specific determinants of the action of the antagonist capsazepine and the agonist PPAHV on TRPV1.Semantic proximity Read ↗

TRPV1 corneal neuralgia mutation: Enhanced pH response, bradykinin sensitization, and capsaicin desensitization.Semantic proximity Read ↗

Agonist-dependence of functional properties for common nonsynonymous variants of human transient receptor potential vanilloid 1.Semantic proximity Read ↗

Tunable calcium current through TRPV1 receptor channels.Semantic proximity Read ↗

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