Expression of an Active Na,K-ATPase with an α-Subunit Lacking All Twenty-three Native Cysteine Residues
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference30 articles.
1. Organization of P-type ATPases: significance of structural diversity
2. Isozymes of the Na+/K+-ATPase
3. Na+,K(+)-ATPase.
4. Characterization of the Fourth α Isoform of the Na,K-ATPase
5. Functional Characterization of a Testes-Specific α-Subunit Isoform of the Sodium/Potassium Adenosinetriphosphatase
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1. Displacement of the Na+/K+ pump’s transmembrane domains demonstrates conserved conformational changes in P-type 2 ATPases;Proceedings of the National Academy of Sciences;2021-02-17
2. A conserved, buried cysteine near the P-site is accessible to cysteine modifications and increases ROS stability in the P-type plasma membrane H+-ATPase;Biochemical Journal;2021-02-12
3. Enhancement of Na,K-ATPase Activity as a Result of Removal of Redox Modifications from Cysteine Residues of the α1 Subunit: the Effect of Reducing Agents;Molecular Biology;2018-03
4. Cysteine residues 244 and 458–459 within the catalytic subunit of Na,K-ATPase control the enzyme's hydrolytic and signaling function under hypoxic conditions;Redox Biology;2017-10
5. Effect of Reduction of Redox Modifications of Cys-Residues in the Na,K-ATPase α1-Subunit on Its Activity;Biomolecules;2017-02-21
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