Evidence map›Paper›PMID 23800232›Full record

ReviewMolecular pain2013

Functionally important amino acid residues in the transient receptor potential vanilloid 1 (TRPV1) ion channel--an overview of the current mutational data.

Zoltán Winter, Andrea Buhala, Ferenc Ötvös, Katalin Jósvay, Csaba Vizler, György Dombi, Gerda Szakonyi, Zoltán Oláh

Open access · goldAbstract readReview
In one paragraph

Review in Molecular pain, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

50 citing papers in PubMed, 76 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Sonogenetics in the Treatment of Chronic Diseases: A New Method for Cell Regulation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Nociception and pain in humans lacking a functional TRPV1 channel.The Journal of clinical investigation · 2023
    Article
  10. Efficiency of cutaneous heat diffusion after local hyperthermia for the treatment of itch.Skin research and technology : official journal of International Society for Bioengineering and the Skin (ISBS) [and] International Society for Digital Imaging of Skin (ISDIS) [and] International Society for Skin Imaging (ISSI) · 2023
    Article
  11. Review
  12. Article
  13. Centipede Venom: A Potential Source of Ion Channel Modulators.International journal of molecular sciences · 2022
    Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. The role of TRPV1 ion channels in the suppression of gastric cancer development.Journal of experimental & clinical cancer research : CR · 2020
    Article
  19. Article
  20. Review
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

8 authors at 3 institutions in 1 country.

Zoltán WinterInstitute of Pharmaceutical Analysis, Faculty of Pharmacy, University of Szeged, Szeged, Hungary. winter.zoltan@brc.mta.hu
Andrea Buhala
Ferenc Ötvös
Katalin Jósvay
Csaba Vizler
György Dombi
Gerda Szakonyi
Zoltán Oláh
University of Szeged · HUInstitute of Biochemistry · HUHungarian Academy of Sciences · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This review aims to create an overview of the currently available results of site-directed mutagenesis studies on transient receptor potential vanilloid type 1 (TRPV1) receptor. Systematization of the vast number of data on the functionally important amino acid mutations of TRPV1 may provide a clearer picture of this field, and may promote a better understanding of the relationship between the structure and function of TRPV1. The review summarizes information on 112 unique mutated sites along the TRPV1, exchanged to multiple different residues in many cases. These mutations influence the effect or binding of different agonists, antagonists, and channel blockers, alter the responsiveness to heat, acid, and voltage dependence, affect the channel pore characteristics, and influence the regulation of the receptor function by phosphorylation, glycosylation, calmodulin, PIP2, ATP, and lipid binding. The main goal of this paper is to publish the above mentioned data in a form that facilitates in silico molecular modelling of the receptor by promoting easier establishment of boundary conditions. The better understanding of the structure-function relationship of TRPV1 may promote discovery of new, promising, more effective and safe drugs for treatment of neurogenic inflammation and pain-related diseases and may offer new opportunities for therapeutic interventions.

Indexed as

MutationAmino Acid SequenceAnimalsBinding SitesHumansModels, BiologicalMutagenesis, Site-DirectedRatsTRPV Cation ChannelsTrpv1 protein, ratTRPV1 receptorTRPV Cation Channels

Identifiers

PMID23800232
PMCPMC3707783
OpenAlexW2163830012

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.