The role of car☐yl groups of Na+/K+-ATPase in the interaction with divalent cations
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference17 articles.
1. Mechanism of the Na+, K+ pump protein structure and conformations of the pure
2. Structure and Mechanism of the (Na,K)-ATPase
3. Characterization of a Mg2+-stabilized state of the (Na+ and K+)–stimulated adenosine triphosphatase using a fluorescent reporter group.
4. The interaction of divalent cations with (Na,K)-ATPase. A lipid-bound fluorescence probe study.
5. Mg2+-induced changes of lipid order and conformation of (Na+ + K+)-ATPase
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1. Subcellular redistribution of trimeric G-proteins – potential mechanism of desensitization of hormone response; internalisation, solubilization, down-regulation;Physiological Research;2008
2. Biochemistry of transmembrane signaling mediated by trimeric G proteins;Physiological Research;2004
3. Photolabile Amiloride Derivatives as Cation Site Probes of the Na,K-ATPase;Journal of Biological Chemistry;1996-04
4. Cryptic na+, k+-atpase activity in rat liver canalicular plasma membranes: Evidence for its basolateral origin;Hepatology;1990-02
5. Chemical modification as an approach to elucidation of sodium pump structure-function relations;American Journal of Physiology-Cell Physiology;1990-01-01
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