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

TRPV1 structures in distinct conformations reveal activation mechanisms.

Nature - 5 Dec 2013

Cao Erhu, Liao Maofu, Cheng Yifan, Julius David

Abstract excerpt

Transient receptor potential (TRP) channels are polymodal signal detectors that respond to a wide range of physical and chemical stimuli. Elucidating how these channels integrate and convert physiological signals into channel opening is essential to understanding how they regulate cell excitability under normal and pathophysiological conditions. Here we exploit pharmacological probes (a peptide toxin and small...

Read the complete abstract on PubMed

Topics

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

Share to TRPV1 gene
Share to Models, Molecular
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Structure, Tertiary

Share to TRPV Cation Channels

Source

Open in PubMed Open full text

Identifiers

PMID: 24305161
DOI: 10.1038/nature12823
PMCID: PMC4023639

Genes

TRPV1

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

TRPV1 structures in distinct conformations reveal activation mechanisms.PMID 24305161Read ↗

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

TRPV1.Semantic proximity Read ↗

Polymodal Transient Receptor Potential Vanilloid Type 1 Nocisensor: Structure, Modulators, and Therapeutic Applications.Semantic proximity Read ↗

The TRPV4 channel.Semantic proximity Read ↗

TRPing to the Point of Clarity: Understanding the Function of the Complex TRPV4 Ion Channel.Semantic proximity Read ↗

Conformational dynamics in TRPV1 channels reported by an encoded coumarin amino acidSemantic proximity Read ↗

A tyrosine residue in TM6 of the Vanilloid Receptor TRPV1 involved in desensitization and calcium permeability of capsaicin-activated currents.Semantic proximity Read ↗

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

Structural origins of species-specific differences in TRPV2 activation.Semantic proximity Read ↗

Cryo-EM and X-ray structures of TRPV4 reveal insight into ion permeation and gating mechanisms.Semantic proximity Read ↗

Detailed Analysis of the Binding Mode of Vanilloids to Transient Receptor Potential Vanilloid Type I (TRPV1) by a Mutational and Computational Study.Semantic proximity Read ↗

Identification of molecular determinants of channel gating in the transient receptor potential box of vanilloid receptor I.Semantic proximity Read ↗

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