Functional Coupling of Phosphorylation and Nucleotide Binding Sites in the Proteolytic Fragments of Na+/K+-ATPase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference47 articles.
1. [27] Proteolytic cleavage as a tool for studying structure and conformation of pure membrane-bound Na+,K+-ATPase
2. Chemical modification as an approach to elucidation of sodium pump structure-function relations
3. STRUCTURE OF THE Na, K PUMP: CRYSTALLIZATION OF PURE MEMBRANE-BOUND Na, K-ATPase AND IDENTIFICATION OF FUNCTIONAL DOMAINS OF THE ?-SUBUNIT
4. Chymotryptic cleavage of α-subunit in E1-forms of renal (Na+ + K +)-ATPase: effects on enzymatic properties, ligand binding and cation exchange
5. Autoregulation of the phosphointermediate of Na+/K+-ATPase by the amino-terminal domain of the α-subunit
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1. Identification of a Potential Receptor That Couples Ion Transport to Protein Kinase Activity;Journal of Biological Chemistry;2011-02
2. A structural overview of the plasma membrane Na+,K+-ATPase and H+-ATPase ion pumps;Nature Reviews Molecular Cell Biology;2010-12-22
3. Interaction of SDS with Na+/K+-ATPase;Journal of Biological Chemistry;2004-07
4. Structural analysis of the products of chymotryptic cleavage of the E1 form of Na,K-ATPase α-subunit: identification of the N-terminal fragments containing the transmembrane H1-H2domain;FEBS Letters;1997-12-22
5. 2′-O-Dansyl Analogs of ATP Bind with High Affinity to the Low Affinity ATP Site of Na+/K+-ATPase and Reveal the Interaction of Two ATP Sites during Catalysis;Journal of Biological Chemistry;1997-06
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