Proton nuclear magnetic resonance studies of the conformation of an ATP analog at the active site of sodium-potassium ATPase from kidney medulla
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00413a039
Reference58 articles.
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3. Effect of monovalent cations on the ouabain inhibition of the sodium and potassium ion activated adenosine triphosphatase
4. Temperature Dependence of Proton Relaxation Times in Aqueous Solutions of Paramagnetic Ions
5. Proton Relaxation Times in Paramagnetic Solutions
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1. Catalytic Activity of an Isolated Domain of Na,K-ATPase Expressed in Escherichia coli;Biophysical Journal;1999-07
2. The ATP Binding Sites of P-Type ION Transport ATPases: Properties, Structure, Conformations, and Mechanism of Energy Coupling;Ion Pumps;1997
3. Ptilomycalin A, a novel Na+,K+- or Ca2+-ATPase inhibitor, competitively interacts with ATP at its binding site;European Journal of Pharmacology;1996-08
4. Role of magnesium ions in the conformational change reported by fluorescein 5'-isothiocyanate modification of sodium-potassium-ATPase;Biochemistry;1993-06-15
5. High-affinity calcium and substrate-binding sites on protein kinase C .alpha. as determined by nuclear magnetic resonance spectroscopy;Biochemistry;1992-08-25
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