Recombinant Pig Sodium/potassium-transporting ATPase subunit alpha-1 (ATP1A1), partial

1. This study determined the specificity of the interaction between the N-terminus of the alpha-subunit of the Na+,K+-ATPase and the surrounding membrane. PMID: 29522705
2. The findings are consistent with previous studies that indicate a link between Na,K-ATPase activity and SFK signaling. PMID: 27748508
3. Uroguanylin modulates (Na++K+)ATPase in a proximal tubule cells via cGMP/protein kinase G, cAMP/protein kinase A, and mTOR pathways. PMID: 27102282
4. Data indicate that magnesium fluoride, magnesium fluoride and Na,K-ATPase form a very stable complex in the E2 conformation. PMID: 25838127
5. Data indicate that Rb(+) can be occluded through Na(+)/K(+)-ATPase cycling mode that takes place in the absence of Na(+) ions. PMID: 23357355
6. Expression of mutant alpha1 Na/K-ATPase defective in conformational transition attenuates Src-mediated signal transduction PMID: 23288841
7. re-arrangements of the Na+,K+-ATPase stabilized by cardiotonic steroids may affect protein-protein interactions within the intracellular signal transduction networks PMID: 21182963
8. Data indicate that the transmembrane domain of the Na+/K+ -ATPase in the E1 state is less exposed to the lipids than in E2. PMID: 21419126
9. The plasma membrane Na/K-ATPase-caveolin-1 interaction may represent an important sensing mechanism by which the cells regulate the sterol regulatory element-binding protein pathway. PMID: 19363037
10. Investigations of K(+)-occlusion by the phosphoenzyme of Na(+),K(+)-ATPase from shark rectal gland and pig kidney by stopped-flow fluorimetry reveal major differences in the kinetics of the two enzymes. PMID: 21190658
11. The results indicate that PKC could be the final target and an integrator molecule of different signaling pathways triggered by angiotensin II (Ang II), which could explain the sustained activation of Na(+)-ATPase by Ang II. PMID: 19958748
12. Na,K-ATPase is a new target of TGF-beta(1)-mediated Epithelial-to-mesenchymal transition in renal epithelial cells, a model system used in studies of both cancer progression and fibrosis. PMID: 20501797
13. Adenosine triphosphate binding to the E2P (intermediate) stage of the enzyme pump cycle causes a deceleration in its dephosphorylation when acting in the sodium ion (Na)+-ATPase mode, i.e., in the absence of monovalent potassium (K+) ions. PMID: 20063899
14. Results provide evidence for interaction of aspartic acid 443 in the N domain of Na(+),K(+)-ATPase with a magnesium ion. PMID: 16331955
15. addressed the question of how modification of the cholesterol content could affect the ATPase activity via changes in the membrane lipid phase and in the protein structure and dynamics PMID: 17105204
16. Neutralization of the charge on Asp 369 of Na+,K+-ATPase triggers conformational changes. PMID: 19726667

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KEGG: ssc:397481

STRING: 9823.ENSSSCP00000007190

UniGene: Ssc.12630