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pro vyhledávání: '"Käthi Geering"'
Publikováno v:
Journal of Membrane Biology, vol. 213, no. 1, pp. 1-9
Sodium- and potassium-activated adenosine triphosphatases (Na,K-ATPase) is the ubiquitous active transport system that maintains the Na(+) and K(+) gradients across the plasma membrane by exchanging three intracellular Na(+) ions against two extracel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a24eaaf833cecd8886ea5c6f7401890
http://doc.rero.ch/record/319660/files/232_2006_Article_35.pdf
http://doc.rero.ch/record/319660/files/232_2006_Article_35.pdf
Autor:
Solange Kharoubi-Hess, Sophie Roy, Käthi Geering, Stéphanie Bibert, Jean-Daniel Horisberger, David Aebischer, Florian Desgranges, Danièle Schaer
Publikováno v:
Molecular Biology of the Cell. 20:1132-1140
FXYD3 (Mat-8) proteins are regulators of Na,K-ATPase. In normal tissue, FXYD3 is mainly expressed in stomach and colon, but it is also overexpressed in cancer cells, suggesting a role in tumorogenesis. We show that FXYD3 silencing has no effect on ce
Autor:
Käthi Geering
Publikováno v:
Current Opinion in Nephrology and Hypertension. 17:526-532
Na,K-ATPase is an oligomeric protein composed of alpha subunits, beta subunits and FXYD proteins. The catalytic alpha subunit hydrolyzes ATP and transports the cations. Increasing experimental evidence suggest that beta subunits and FXYD proteins ess
Autor:
Tatiana V. Korneenko, Rossen Radkov, Danièle Schaer, Nikolai N. Modyanov, Stéphanie Bibert, Nikolay B. Pestov, Nisar Ahmad, Käthi Geering, Hao Zhao, Sophie Roy
Publikováno v:
Proceedings of the National Academy of Sciences. 104:11215-11220
Change in gene functions (gene cooption) is one of the key mechanisms of molecular evolution. Genes can acquire new functions via alteration in properties of encoded proteins and/or via changes in temporal or spatial regulation of expression. Here we
Autor:
Rossen Radkov, Solange Kharoubi-Hess, Danièle Schaer, Käthi Geering, Jean-Daniel Horisberger, Nikolai N. Modyanov
Publikováno v:
Biochemical and Biophysical Research Communications, vol. 356, no. 1, pp. 142-6
Cardiac steroids inhibit Na,K-ATPase and the related non-gastric H,K-ATPase, while they do not interact with gastric H,K-ATPase. Introducing an arginine, the residue present in the gastric H,K-ATPase, in the second extracellular loop at the correspon
Publikováno v:
Developmental Dynamics
Developmental Dynamics, Wiley, 2007, 236 (9), pp.2534-40. ⟨10.1002/dvdy.21269⟩
Developmental Dynamics, Wiley, 2007, 236 (9), pp.2534-40. ⟨10.1002/dvdy.21269⟩
A key protein in the production and in the maintenance of the endocochlear potential is the Na,K-ATPase. Previously, we have shown that FXYD6 is a modulator of the Na,K-ATPase expressed in the inner ear (Delprat et al. [2007] J Biol Chem 282:7450-745
Publikováno v:
Journal of Biological Chemistry. 281:39142-39151
Six of 7 FXYD proteins have been shown to be tissue-specific modulators of Na,K-ATPase. In this study, we have identified two splice variants of human FXYD3, or Mat-8, in CaCo-2 cells. Short human FXYD3 has 72% sequence identity with mouse FXYD3, whe
Autor:
Käthi Geering
Publikováno v:
American Journal of Physiology-Renal Physiology. 290:F241-F250
FXYD proteins belong to a family of small-membrane proteins. Recent experimental evidence suggests that at least five of the seven members of this family, FXYD1 (phospholemman), FXYD2 (γ-subunit of Na-K-ATPase), FXYD3 (Mat-8), FXYD4 (CHIF), and FXYD
Role of the Transmembrane Domain of FXYD7 in Structural and Functional Interactions with Na,K-ATPase
Publikováno v:
Journal of Biological Chemistry. 280:42738-42743
Members of the FXYD family are tissue-specific regulators of the Na,K-ATPase. Here, we have investigated the contribution of amino acids in the transmembrane (TM) domain of FXYD7 to the interaction with Na,K-ATPase. Twenty amino acids of the TM domai
Autor:
Käthi Geering
Publikováno v:
Journal of Bioenergetics and Biomembranes. 37:387-392
In this short review, we summarize our work on the role of members of the FXYD protein family as tissue-specific modulators of Na, K-ATPase. FXYD1 or phospholemman, mainly expressed in heart and skeletal muscle increases the apparent affinity for int