Evidence map›Paper›PMID 40321781›Full record

ArticleResearch square2025

Pathway-dependent cold activation of heat-responsive TRPV channels.

Guangyu Wang

Abstract readPreprint
In one paragraph

Article in Research square, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author.

Guangyu WangDepartment of Physiology and Membrane Biology, University of California School of Medicine, Davis, CA, USA.

Funding

CFTR--ION CONDUCTION AND GATING MECHANISMSR01DK045880 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI DAWSON, DAVID C · 1992 to 2010
$3.5M
New paradigms of CFTR regulationR56DK056796 · NIDDK · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI KIRK, KEVIN L · 2010 to 2010
$220k
CFTR-Ion Conduction and Gating MechanismsR56DK045880 · NIDDK · OREGON HEALTH & SCIENCE UNIVERSITY · PI DAWSON, DAVID C · 2007 to 2007
$57k
NIDDK NIH HHS R01 DK045880NIDDK NIH HHS R56 DK045880NIDDK NIH HHS R56 DK056796
6 · The paper itself

Abstract

The homotetrameric thermosensitive transient receptor potential vanilloid 1-4 (TRPV1-4) channels in sensory neurons are highly responsive to heat stimuli. However, their primary heat sensors or triggers for heat activation have not been examined for cold activation. In this study, cold activation of minimal TRPV1 without the pore turret was compared with that of full-length human TRPV3. The former followed a pathway from the putative heat activation starter, while the latter tracked a different pathway starting far from the assumed heat activation point. The results showed that the former shared temperature sensitivity with heat activation while the latter did not. Therefore, this mirrored thermosensitivity can be used to confirm the location of the primary thermal sensor for TRPV1 or TRPV3, and potentially define the primary thermal sensor of other thermosensitive proteins like TRPV2 or TRPV4 once the same heat capacity mechanism is applied.

Indexed as

noncovalent thermoring structureprotein unfolding thresholdsymmetric thermosensitivity

Identifiers

PMID40321781
PMCPMC12047967

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.