Simultaneous Binding of Three Na+and Two K+ Ions to Na+, K+-Dependent ATPase and Changes in Its Affinities for the Ions Induced by the Formation of a Phosphorylated Intermediate1
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,General Medicine
Link
http://academic.oup.com/jb/article-pdf/86/2/509/2257754/86-2-509.pdf
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1. Ouabain-Induced Cell Death and Survival. Role of α1-Na,K-ATPase-Mediated Signaling and [Na+]i/[K+]i-Dependent Gene Expression;Frontiers in Physiology;2020-09-04
2. Gastric H/K-ATPase Liberates Two Moles of Pi from One Mole of Phosphoenzyme Formed from a High-Affinity ATP Binding Site and One Mole of Enzyme-Bound ATP at the Low-Affinity Site during Cross-Talk between Catalytic Subunits;Biochemistry;2002-01-25
3. Acid-labile ATP and/or ADP/Pi Binding to the Tetraprotomeric Form of Na/K-ATPase Accompanying Catalytic Phosphorylation-Dephosphorylation Cycle;Journal of Biological Chemistry;1999-11
4. Mechanism of the Conformational Change in Sodium Pump Reported by Eosin;Biochemistry;1995-10-10
5. An Equivalent Site Mechanism for Na+ and K+ Binding to Sodium Pump and Control of the Conformational Change Reported by Fluorescein 5'-Isothiocyanate Modification;Biochemistry;1995-07
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