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

Decrypting the Heat Activation Mechanism of TRPV1 Channel by Molecular Dynamics Simulation.

Biophysical journal - 9 Jan 2018

Wen Han, Zheng Wenjun

Abstract excerpt

As a prototype cellular sensor, the TRPV1 cation channel undergoes a closed-to-open gating transition in response to various physical and chemical stimuli including noxious heat. Despite recent progress, the molecular mechanism of heat activation of TRPV1 gating remains enigmatic. Toward decrypting the structural basis of TRPV1 heat activation, we performed extensive molecular dynamics simulations (with...

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 Hot Temperature
Share to Hydrogen Bonding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ion Channel Gating

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Protein Domains

Share to TRPV Cation Channels

Source

Open in PubMed Open full text

Identifiers

PMID: 29320695
DOI: 10.1016/j.bpj.2017.10.034
PMCID: PMC5773748

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

Decrypting the Heat Activation Mechanism of TRPV1 Channel by Molecular Dynamics Simulation.PMID 29320695Read ↗

Toward elucidating the heat activation mechanism of the TRPV1 channel gating by molecular dynamics simulation.Semantic proximity Read ↗

Conformational ensemble of the human TRPV3 ion channelSemantic proximity Read ↗

TRPV1 temperature activation is specifically sensitive to strong decreases in amino acid hydrophobicity.Semantic proximity Read ↗

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

Cold unfolding of heat-responsive TRPV3Semantic proximity Read ↗

Voltage-dependent structural models of the human Hv1 proton channel from long-timescale molecular dynamics simulations.Semantic proximity Read ↗

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

Deep mutational scan of the pore of the cold-sensing TRPM8 channelSemantic proximity Read ↗

A negative-hydrated constriction zone is revealed in the active state of the Hv1 channel.Semantic proximity Read ↗

Protons stabilize the closed conformation of gain-of-function mutants of the TRPV1 channel.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 ↗

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 ↗

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