Increase in affinity for ATP and change in E1-E2 conformational equilibrium after mutations to the phosphorylation site (Asp369) of the alpha subunit of Na,K-ATPase
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Veröffentlicht in: | Annals of the New York Academy of Sciences 1997-11, Vol.834, p.454 |
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container_start_page | 454 |
container_title | Annals of the New York Academy of Sciences |
container_volume | 834 |
creator | Pedersen, P A Rasmussen, J H Jørgensen, P L |
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doi_str_mv | 10.1111/j.1749-6632.1997.tb52298.x |
format | Article |
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ispartof | Annals of the New York Academy of Sciences, 1997-11, Vol.834, p.454 |
issn | 0077-8923 |
language | eng |
recordid | cdi_pubmed_primary_9405843 |
source | MEDLINE; Wiley Online Library All Journals |
subjects | Adenosine Triphosphate - metabolism Aspartic Acid Binding Sites Kinetics Macromolecular Substances Mutagenesis, Site-Directed Ouabain - metabolism Phosphorylation Point Mutation Protein Conformation Recombinant Proteins - chemistry Recombinant Proteins - metabolism Saccharomyces cerevisiae Sodium-Potassium-Exchanging ATPase - chemistry Sodium-Potassium-Exchanging ATPase - metabolism |
title | Increase in affinity for ATP and change in E1-E2 conformational equilibrium after mutations to the phosphorylation site (Asp369) of the alpha subunit of Na,K-ATPase |
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