Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Ciming Li"'
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
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
Publikováno v:
Molecular Biology of the Cell. 16:2363-2371
Four of the seven members of the FXYD protein family have been identified as specific regulators of Na,K-ATPase. In this study, we show that FXYD3, also known as Mat-8, is able to associate with and to modify the transport properties of Na,K-ATPase.
Publikováno v:
Annals of the New York Academy of Sciences. 986:226-228
The sodium pump, or Na,K-ATPase, exports three intracellular sodium ions in exchange for two extracellular potassium ions. In the high resolution structure of the related calcium pump, two cation-binding sites have been identified. The two correspond
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb72775e0490b8834f7962f8b718aff4
https://europepmc.org/articles/PMC1200292/
https://europepmc.org/articles/PMC1200292/
Autor:
Gilles Crambert, Jean-Daniel Horisberger, Ciming Li, Kaethi Geering, Aurélien Grosdidier, Olivier Michielin
Publikováno v:
The Journal of biological chemistry. 279(37)
Several members of the FXYD protein family are tissue-specific regulators of Na,K-ATPase that produce distinct effects on its apparent K(+) and Na(+) affinity. Little is known about the interaction sites between the Na,K-ATPase alpha subunit and FXYD
Publikováno v:
The Journal of biological chemistry. 279(29)
The brain-specific FXYD7 is a member of the recently defined FXYD family that associates with the alpha1-beta1 Na,K-ATPase isozyme and induces an about 2-fold decrease in its apparent K+ affinity. By using the Xenopus oocyte as an expression system,
Autor:
Ciming Li1, Crambert, Gilles1, Thuillard, Deiphine1, Roy, Sophie1, Schaer, Danièle1, Geering, Käthi1 kaethi.geering@unil.ch
Publikováno v:
Journal of Biological Chemistry. 12/30/2005, Vol. 280 Issue 52, p42738-42743. 6p. 2 Diagrams, 4 Graphs.
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America; 9/6/2005, Vol. 102 Issue 36, p12706-12711, 6p
Autor:
Ciming Li1, Grosdidier, Aurelien2, Crambert, Gilles1, Horisberger, Jean-Daniel1, Michielin, Olivier2, Geering, Käthi1 kaethi.geering@ipharm.unil.ch
Publikováno v:
Journal of Biological Chemistry. 9/10/2004, Vol. 279 Issue 37, p38895-38902. 8p. 4 Black and White Photographs, 3 Diagrams, 1 Chart, 29 Graphs.