Conformational change of sodium- and potassium-dependent adenosine triphosphatase. Conformational evidence for the Post-Albers mechanism in Na+- and K+-dependent hydrolysis of ATP.

This publication has 39 references indexed in Scilit:

• Kinetics of Na-ATPase activity by the Na,K pump. Interactions of the phosphorylated intermediates with Na+, Tris+, and K+.
  The Journal of general physiology, 1983
• ATP binding to solubilized (Na+ + K+)-ATPase
  Biochimica et Biophysica Acta (BBA) - Biomembranes, 1983
• THE (Na⁺+K⁺)‐ATPase: COUPLING OF THE REACTION WITH ATP TO THE REACTION WITH Na⁺ AND K⁺
  Annals of the New York Academy of Sciences, 1982
• ON THE MECHANISM OF ENERGY RELEASE, TRANSFER, AND UTILIZATION IN Na, K‐ATPase TRANSPORT WORK: OLD IDEAS AND NEW FINDINGS
  Annals of the New York Academy of Sciences, 1982
• Mechanism of the Na+, K+ pump protein structure and conformations of the pure
  Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1982
• The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain III. A minimal model
  Biochimica et Biophysica Acta (BBA) - Biomembranes, 1981
• Biochemical Mechanism of the Sodium Pump
  Annual Review of Physiology, 1979
• The (Na+ + K+)-activated ATPase Enzymatic and transport properties
  Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1979
• The reaction mechanism of the sodium pump
  Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1975
• Synthesis of adenosine triphosphate by way of potassium‐sensitive phosphoenzyme of sodium, potassium adenosine triphosphatase
  Journal of Supramolecular Structure, 1975