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Transient receptor potential ankyrin 1 channel: an evolutionarily tuned thermosensor

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F21%3A00544563" target="_blank" >RIV/67985823:_____/21:00544563 - isvavai.cz</a>

  • Result on the web

    <a href="https://www.biomed.cas.cz/physiolres/pdf/2021/70_363.pdf" target="_blank" >https://www.biomed.cas.cz/physiolres/pdf/2021/70_363.pdf</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.33549/physiolres.934697" target="_blank" >10.33549/physiolres.934697</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Transient receptor potential ankyrin 1 channel: an evolutionarily tuned thermosensor

  • Original language description

    The discovery of the role of the transient receptor potential ankyrin 1 (TRPA1) channel as a polymodal detector of cold and pain-producing stimuli almost two decades ago catalyzed the consequent identification of various vertebrate and invertebrate orthologues. In different species, the role of TRPA1 has been implicated in numerous physiological functions, indicating that the molecular structure of the channel exhibits evolutionary flexibility. Until very recently, information about the critical elements of the temperature-sensing molecular machinery of thermosensitive ion channels such as TRPA1 had lagged far behind information obtained from mutational and functional analysis. Current developments in single-particle cryo-electron microscopy are revealing precisely how the thermosensitive channels operate, how they might be targeted with drugs, and at which sites they can be critically regulated by membrane lipids. This means that it is now possible to resolve a huge number of very important pharmacological, biophysical and physiological questions in a way we have never had before. In this review, we aim at providing some of the recent knowledge on the molecular mechanisms underlying the temperature sensitivity of TRPA1. We also demonstrate how the search for differences in temperature and chemical sensitivity between human and mouse TRPA1 orthologues can be a useful approach to identifying important domains with a key role in channel activation.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    30103 - Neurosciences (including psychophysiology)

Result continuities

  • Project

    <a href="/en/project/GA19-03777S" target="_blank" >GA19-03777S: Molecular Basis of Thermosensitive TRP Ion Channel Regulation in Nociceptive Neurons</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2021

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Physiological Research

  • ISSN

    0862-8408

  • e-ISSN

    1802-9973

  • Volume of the periodical

    70

  • Issue of the periodical within the volume

    3

  • Country of publishing house

    CZ - CZECH REPUBLIC

  • Number of pages

    19

  • Pages from-to

    363-381

  • UT code for WoS article

    000675528500005

  • EID of the result in the Scopus database

    2-s2.0-85112123925