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Conserved Residues within the Putative S4?S5 Region Serve Distinct Functions among Thermosensitive Vanilloid Transient Receptor Potential (TRPV) Channels

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F10%3A00354172" target="_blank" >RIV/67985823:_____/10:00354172 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Conserved Residues within the Putative S4?S5 Region Serve Distinct Functions among Thermosensitive Vanilloid Transient Receptor Potential (TRPV) Channels

  • Original language description

    Based on the structural similarity to voltage-gated potassium channels, the voltage-sensing domain in the TRP channels is hypothesized to be comprised of positively charged amino acids distributed within the transmembrane segments S1-S4. Our data providethe first functional evidence that, despite the highly conserved nature of S4 and the S4-S5 linker, the mechanisms of temperature and chemical sensitivity in TRPV1 appear to utilize different residues from those in TRPV2 and TRPV3, which indicates thatthese mechanisms are not fully conserved throughout thermosensitive TRPV channels. This conclusion is further supported by our finding that one specific mode of chemical activation of TRPV1 is separable from other activation mechanisms and depends on onebasic residue in the S4/S4-S5 domain

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    FH - Neurology, neuro-surgery, nuero-sciences

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2010

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Journal of Biological Chemistry

  • ISSN

    0021-9258

  • e-ISSN

  • Volume of the periodical

    285

  • Issue of the periodical within the volume

    53

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    8

  • Pages from-to

  • UT code for WoS article

    285622600031

  • EID of the result in the Scopus database