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Roles of conserved ectodomain cysteines of the rat P2X4 purinoreceptor in agonist binding and channel gating

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F10%3A00355715" target="_blank" >RIV/67985823:_____/10:00355715 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11310/10:10112343

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Roles of conserved ectodomain cysteines of the rat P2X4 purinoreceptor in agonist binding and channel gating

  • Original language description

    Mammalian P2X receptors contain ten conserved cysteine residues in their ectodomains, which form five disulfide bonds. Replacement of cysteine pairs with threonines resulted in decreased sensitivity of P2X4 receptor to ATP. Three bonds contribute substantially to the structure of the ligand binding pocket, while the bond located towards the transmembrane domain contributes to receptor gating

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    ED - Physiology

  • 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

    Physiological Research

  • ISSN

    0862-8408

  • e-ISSN

  • Volume of the periodical

    59

  • Issue of the periodical within the volume

    6

  • Country of publishing house

    CZ - CZECH REPUBLIC

  • Number of pages

    9

  • Pages from-to

  • UT code for WoS article

    285711400010

  • EID of the result in the Scopus database