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High- and low-affinity sites for sodium in delta-OR-G(i)1 alpha (Cys(351)-Ile(351)) fusion protein stably expressed in HEK293 cells; functional significance and correlation with biophysical state of plasma membrane
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SYSNO ASEP 0428435 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title High- and low-affinity sites for sodium in delta-OR-G(i)1 alpha (Cys(351)-Ile(351)) fusion protein stably expressed in HEK293 cells; functional significance and correlation with biophysical state of plasma membrane Author(s) Vošahlíková, Miroslava (FGU-C) RID, ORCID, SAI
Jurkiewicz, Piotr (UFCH-W) RID, ORCID
Roubalová, Lenka (FGU-C) RID, ORCID, SAI
Hof, Martin (UFCH-W) RID, ORCID
Svoboda, Petr (FGU-C) RID, ORCIDSource Title Naunyn-Schmiedeberg's Archives of Pharmacology. - : Springer - ISSN 0028-1298
Roč. 387, č. 5 (2014), s. 487-502Number of pages 16 s. Language eng - English Country DE - Germany Keywords delta - opioid receptor ; monovalent ions ; agonist and antagonist binding ; [35S]GTPγS binding ; membrane biophysics ; Laurdan fluorescence Subject RIV CE - Biochemistry R&D Projects GAP207/12/0919 GA ČR - Czech Science Foundation (CSF) GBP304/12/G069 GA ČR - Czech Science Foundation (CSF) Institutional support FGU-C - RVO:67985823 ; UFCH-W - RVO:61388955 UT WOS 000334512800010 EID SCOPUS 84899982061 DOI 10.1007/s00210-014-0962-8 Annotation The effect of monovalent cations on delta-opioid receptor ligand binding parameters and coupling with the cognate G protein was compared in model HEK293 cell line stably expressing PTX-insensitive delta OR Gi1alpha (Cys351-Ile351) fusion protein. The possible differences between individual ions when interacting with the polar membrane-water interface and the hydrophobic interior of membrane bilayer was studied with help of fluorescence probes Workplace Institute of Physiology Contact Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400 Year of Publishing 2015
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