Structural Domain Organization of Gastric H+,K+-ATPase and Its Rearrangement during the Catalytic Cycle
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference58 articles.
1. Amino-acid sequence of a Ca2+ + Mg2+ -dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence
2. Amino-acid sequence of the catalytic subunit of the (Na+ + K+)ATPase deduced from a complementary DNA
3. ATP/ADP exchange activity of gastric (H+ + K+)-ATPase
4. Conformational states of (K+ + H+)-ATPase studied using tryptic digestion as a tool
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1. The transported cations impose differences in the thermostability of the gastric H,K-ATPase. A kinetic analysis;Biochimica et Biophysica Acta (BBA) - Biomembranes;2022-11
2. Different domain organization of two main conformational states of Na+/K+-ATPase;Biophysics;2009-12
3. Stabilization of Na,K–ATPase by ionic interactions;Biochimica et Biophysica Acta (BBA) - Biomembranes;2008-04
4. Conformational changes in gastric H+/K+-ATPase monitored by difference Fourier-transform infrared spectroscopy and hydrogen/deuterium exchange;Biochemical Journal;2004-08-10
5. Hydrogen-deuterium exchange in membrane proteins monitored by IR spectroscopy: A new tool to resolve protein structure and dynamics;Biopolymers;2004
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