Identification of an essential sulfhydryl group in the ouabain binding site of (Na,K)-ATPase.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference20 articles.
1. Studies on (Na+ +K+ activated ATPase, XLI. Effects of N-ethylmaleimide on overall and partial reactions
2. Reaction of purified (Na,K)-ATPase with the fluorescent sulfhydryl probe 2-(4'-maleimidylanilino)naphthalene 6-sulfonic acid. Characterization and the effects of ligands.
3. Showdomycin, a nucleotide-site-directed inhibitor of (Na+ + K+)-ATPase
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5. Enzyme modifications that alter interactions of K + and cardioactive steroids with (Na + + K +)-dependent ATPase
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1. Urea-Induced Unfolding of Na,K-ATPase As Evaluated by Electron Paramagnetic Resonance Spectroscopy;Biochemistry;2009-09-02
2. Halenaquinol, a natural cardioactive pentacyclic hydroquinone, interacts with sulfhydryls on rat brain Na+,K+-ATPase;Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology;2001-04
3. Inhibition of Na+,K+-ATPase in Penaeus indicus postlarvae by lead;Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology;2000-08
4. Cardiac lysosomes and the mechanism of action of ouabain;Bulletin of Experimental Biology and Medicine;1998-04
5. Extensive Random Mutagenesis Analysis of the Na+/K+-ATPase alpha Subunit Identifies Known and Previously Unidentified Amino Acid Residues that Alter Ouabain Sensitivity Implications for Ouabain Binding;European Journal of Biochemistry;1997-09
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