[27] Proteolytic cleavage as a tool for studying structure and conformation of pure membrane-bound Na+,K+-ATPase
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Elsevier
Reference23 articles.
1. Asymmetric orientation of amino groups in the α-subunit and the β-subunit of (Na+ + K+)-ATPase in tight right-side-out vesicles of basolateral membranes from outer medulla
2. Identification of a membrane-embedded segment of the large polypeptide chain of (Na+, K+)ATPase
3. Proteolytic fragmentation of the catalytic subunit of the sodium and potassium adenosine triphosphatase. Alignment of tryptic and chymotryptic fragments and location of sites labeled with ATP and iodoacetate
4. Evidence for the organization of the transmembrane segments of (Na,K)-ATPase based on labeling lipid-embedded and surface domains of the alpha-subunit.
5. STRUCTURE OF THE Na, K PUMP: CRYSTALLIZATION OF PURE MEMBRANE-BOUND Na, K-ATPase AND IDENTIFICATION OF FUNCTIONAL DOMAINS OF THE ?-SUBUNIT
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2. Structural analysis of 2D crystals of gastric H+,K+-ATPase in different states of the transport cycle;Journal of Structural Biology;2008-05
3. Kinetic characterization of tetrapropylammonium inhibition reveals how ATP and Pialter access to the Na+-K+-ATPase transport site;American Journal of Physiology-Cell Physiology;2005-08
4. Covalent Cross-links between the γ Subunit (FXYD2) and α and β Subunits of Na,K-ATPase;Journal of Biological Chemistry;2005-05
5. Corroboration of Dahl S Q276L α1Na,K-ATPase protein sequence: impact on affinities for ligands and on E1 conformation;Journal of Hypertension;2005-04
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