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Substitution of glutamic 779 with alanine in the Na,K-ATPase α subunit removes voltage dependence of ion transport
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Koster JC, Blanco G, Mills PB, Mercer RW: Substitutions of glutamate 781 in the Na,K-aATPase α subunit demonstrate reduced cation selectivity and an increased affinity for ATP. J Biol Chem 1996, 271:2413-2421.
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0029658484
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Kuntzweiler TA, Argüello JM, Lingrel JB: ASP(804) and ASP(808) in the transmembrane domain of the Na,K-ATPase α subunit are cation coordinating residues. J Biol Chem 1996, 271:29682-29687.
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15844371622
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Ouabain interactions with the H5-H6 hairpin of the Na,K-ATPase reveal a possible inhibition mechanism via the cation binding
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Palasis M, Kuntzweiler TA, Argüello JM, Lingrel JB: Ouabain interactions with the H5-H6 hairpin of the Na,K-ATPase reveal a possible inhibition mechanism via the cation binding. J Biol Chem 1996, 271:14176-14182. By using random mutagenesis the authors identified new sites for ouabain inhibition in the energy transduction and cation transport domains of the α subunit of Na,K-ATPase.
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+ ions. J Biol Chem 1996, 271:10309-10316. Controlled proteolysis of '19 kDa membranes' provides evidence that the N-terminus of the β subunit controls access of Rb ions into or out of the occlusion site.
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Only the first and the last hydrophobic segments in the COOH-terminal third of Na,K-ATPase α subunit initiate and halt, respectively, membrane translocation of the newly synthesized polypeptide: Implications for the membrane topology
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Xie YH. Langhansrajasekaran SA, Bellovino D, Morimoto T: Only the first and the last hydrophobic segments in the COOH-terminal third of Na,K-ATPase α subunit initiate and halt, respectively, membrane translocation of the newly synthesized polypeptide: implications for the membrane topology. J Biol Chem 1996, 271:2563-2573.
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