Evidence map›Paper›PMID 28852163›Full record

ArticleScientific reports2017

Expression and Purification of the Pain Receptor TRPV1 for Spectroscopic Analysis.

Phanindra Velisetty, Richard A Stein, Francisco J Sierra-Valdez, Valeria Vásquez, Julio F Cordero-Morales

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.6field-weighted citation impact, top 36% of its field
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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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

10 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. TRPV1 pore turret dictates distinct DkTx and capsaicin gating.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Article
  10. Purification and Reconstitution of TRPV1 for Spectroscopic Analysis.Journal of visualized experiments : JoVE · 2018
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Phanindra VelisettyDepartment of Physiology, University of Tennessee Health Science Center, 71S. Manassas St., Memphis, TN, 38163, USA.
Richard A SteinDepartment of Molecular Physiology and Biophysics, Vanderbilt University Medical Center, Nashville, TN, 37232, USA.
Francisco J Sierra-ValdezDepartment of Physiology, University of Tennessee Health Science Center, 71S. Manassas St., Memphis, TN, 38163, USA.
Valeria VásquezDepartment of Physiology, University of Tennessee Health Science Center, 71S. Manassas St., Memphis, TN, 38163, USA.
Julio F Cordero-MoralesDepartment of Physiology, University of Tennessee Health Science Center, 71S. Manassas St., Memphis, TN, 38163, USA. jcordero@uthsc.edu.
University of Tennessee Health Science Center · USVanderbilt University Medical Center · US

Funding

The Role of Bioactive Lipids in Transient Receptor Potential Channels GatingR01GM125629 · NIGMS · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI CORDERO-MORALES, JULIO F · 2018 to 2022
$1.5M
NIGMS NIH HHS R01 GM125629
6 · The paper itself

Abstract

The transient receptor potential vanilloid 1 (TRPV1) channel is an essential component of the cellular mechanism through which noxious stimuli evoke pain. Functional and structural characterizations of TRPV1 shed light on vanilloid activation, yet the mechanisms for temperature and proton gating remain largely unknown. Spectroscopic approaches are needed to understand the mechanisms by which TRPV1 translates diverse stimuli into channel opening. Here, we have engineered a minimal cysteine-less rat TRPV1 construct (eTRPV1) that can be stably purified and reconstituted for spectroscopic studies. Biophysical analyses of TRPV1 constructs reveal that the S5-pore helix loop influences protein stability and vanilloid and proton responses, but not thermal sensitivity. Cysteine mutants retain function and stability for double electron-electron resonance (DEER) and electron paramagnetic resonance (EPR) spectroscopies. DEER measurements in the closed state demonstrate that eTRPV1 reports distances in the extracellular vestibule, equivalent to those observed in the apo TRPV1 structure. EPR measurements show a distinct pattern of mobilities and spectral features, in detergent and liposomes, for residues at the pore domain that agree with their location in the TRPV1 structure. Our results set the stage for a systematic characterization of TRPV1 using spectroscopic approaches to reveal conformational changes compatible with thermal- and ligand-dependent gating.

Indexed as

Gene ExpressionAmino Acid SequenceAnimalsCysteineMolecular Dynamics SimulationMutationPhosphorylationProtein ConformationProtein StabilityProtonsRatsRecombinant ProteinsSpectrum AnalysisTRPV Cation ChannelsXenopusCysteineProtonsRecombinant ProteinsTRPV1 receptorTRPV Cation Channels

Identifiers

PMID28852163
PMCPMC5575240
OpenAlexW2747172031

What OpenQuestion holds

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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.