Protons stabilize the closed conformation of gain-of-function mutants of the TRPV1 channel

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F13%3A00394052" target="_blank" >RIV/67985823:_____/13:00394052 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.bbamcr.2012.11.017" target="_blank" >http://dx.doi.org/10.1016/j.bbamcr.2012.11.017</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.bbamcr.2012.11.017" target="_blank" >10.1016/j.bbamcr.2012.11.017</a>

Result language
angličtina
Original language name
Protons stabilize the closed conformation of gain-of-function mutants of the TRPV1 channel
Original language description
The vanilloid transient receptor potential channel TRPV1 is a molecular integrator of noxious stimuli, including capsaicin, heat and protons. To explore the function of S1 in TRPV1, we used tryptophan-scanning mutagenesis and characterized the responsesto capsaicin and protons. We propose that the S1 domain contains a functionally important region that may be specifically involved in TRPV1 channel gating, and thus be important for the energetic coupling between S1-S4 sensor activation and gate opening
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
ED - Physiology
OECD FORD branch
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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