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

A folding reaction at the C-terminal domain drives temperature sensing in TRPM8 channels.

Proceedings of the National Academy of Sciences of the United States of America - 18 Aug 2020

Díaz-Franulic Ignacio, Raddatz Natalia, Castillo Karen, González-Nilo Fernando D, Latorre Ramon

Abstract excerpt

In mammals, temperature-sensitive TRP channels make membrane conductance of cells extremely temperature dependent, allowing the detection of temperature ranging from noxious cold to noxious heat. We progressively deleted the distal carboxyl terminus domain (CTD) of the cold-activated melastatin receptor channel, TRPM8. We found that the enthalpy change associated with channel gating is proportional to the length...

Read the complete abstract on PubMed

Topics

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

Share to Cold Temperature
Share to Cryoelectron Microscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ion Channel Gating

Share to Oocytes

Share to Protein Domains

Share to Thermodynamics

Share to TRPM Cation Channels

Share to Xenopus laevis

Source

Open in PubMed Open full text

Identifiers

PMID: 32747539
DOI: 10.1073/pnas.2004303117
PMCID: PMC7443914

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A folding reaction at the C-terminal domain drives temperature sensing in TRPM8 channels.PMID 32747539Read ↗

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

Coiled coils direct assembly of a cold-activated TRP channel.Semantic proximity Read ↗

Cold unfolding of heat-responsive TRPV3Semantic proximity Read ↗

TRPM8 voltage sensor mutants reveal a mechanism for integrating thermal and chemical stimuli.Semantic proximity Read ↗

Mutations of TRPM8 channels: Unraveling the molecular basis of activation by cold and ligands.Semantic proximity Read ↗

Critical role of the pore domain in the cold response of TRPM8 channels identified by ortholog functional comparison.Semantic proximity Read ↗

Ion permeation through a narrow cavity constriction in KCNQ1 channels: Mechanism and implications for pathogenic variants.Semantic proximity Read ↗

ATP-dependent thermoring basis for the heat unfolding of the first nucleotide-binding domain isolated from human CFTRSemantic proximity Read ↗

The desensitization gating of the MthK K+ channel is governed by its cytoplasmic amino terminus.Semantic proximity Read ↗

Residues in the pore region of Drosophila transient receptor potential A1 dictate sensitivity to thermal stimuli.Semantic proximity Read ↗

Cryo-EM structure of the cytoplasmic domain of murine transient receptor potential cation channel subfamily C member 6 (TRPC6).Semantic proximity Read ↗

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

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