Steady-state levels of phosphorylated intermediates of (Na,K)-ATPase monitored with oligomycin and anthroylouabain.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference23 articles.
1. Inhibition of sodium and potassium adenosine triphosphatase by 2‘,3‘-O-(2,4,6-trinitrocyclohexadienylidene) adenine nucleotides. Implications for the structure and mechanism of the Na:K pump.
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3. Conformational transitions between Na+-bound and K+-bound forms of (Na+ + K+)-ATPase, studied with formycin nucleotides
4. The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain III. A minimal model
5. Kinetics of Na-ATPase activity by the Na,K pump. Interactions of the phosphorylated intermediates with Na+, Tris+, and K+.
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2. Chlorpromazine Binding to Na+, K+-ATPase and Photolabeling: Involvement of the Ouabain Site Monitored by Fluorescence;Photochemistry and Photobiology;2007-04-19
3. The modulation of action potential generation by calcium-induced calcium release is enhanced by mitochondrial inhibitors in mudpuppy parasympathetic neurons;Neuroscience;2004-01
4. Transient kinetics and thermodynamics of anthroylouabain binding to Na/K-ATPase;Biophysical Chemistry;1998-04
5. Transient kinetics of substrate binding to measured by fluorescence quenching;Biophysical Chemistry;1997-12
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