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

Our previous findings suggested that reversible thiol modifications of cysteine residues within the actuator (AD) and nucleotide binding domain (NBD) of the Na,K-ATPase may represent a powerful regulatory mechanism conveying redox- and oxygen-sensitivity of this multifunctional enzyme. S-glutathiony...

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Bibliographic Details
Main Authors: Irina Yu. Petrushanko, Vladimir A. Mitkevich, Valentina A. Lakunina, Anastasia A. Anashkina, Pavel V. Spirin, Peter M. Rubtsov, Vladimir S. Prassolov, Nikolay B. Bogdanov, Pascal Hänggi, William Fuller, Alexander A. Makarov, Anna Bogdanova
Format: Article
Language:English
Published: Elsevier 2017-10-01
Series:Redox Biology
Subjects:
Na
Online Access:http://www.sciencedirect.com/science/article/pii/S2213231717301143