![Akt Substrate of 160 kD Regulates Na+,K+-ATPase Trafficking in Response to Energy Depletion and Renal Ischemia | American Society of Nephrology Akt Substrate of 160 kD Regulates Na+,K+-ATPase Trafficking in Response to Energy Depletion and Renal Ischemia | American Society of Nephrology](https://jasn.asnjournals.org/content/26/11/2765/F1.large.jpg)
Akt Substrate of 160 kD Regulates Na+,K+-ATPase Trafficking in Response to Energy Depletion and Renal Ischemia | American Society of Nephrology
![IJMS | Free Full-Text | K+ and Rb+ Affinities of the Na,K-ATPase α1 and α2 Isozymes: An Application of ICP-MS for Quantification of Na+ Pump Kinetics in Myofibers | HTML IJMS | Free Full-Text | K+ and Rb+ Affinities of the Na,K-ATPase α1 and α2 Isozymes: An Application of ICP-MS for Quantification of Na+ Pump Kinetics in Myofibers | HTML](https://www.mdpi.com/ijms/ijms-19-02725/article_deploy/html/images/ijms-19-02725-g001b.png)
IJMS | Free Full-Text | K+ and Rb+ Affinities of the Na,K-ATPase α1 and α2 Isozymes: An Application of ICP-MS for Quantification of Na+ Pump Kinetics in Myofibers | HTML
![AKAPs-PKA disruptors increase AQP2 activity independently of vasopressin in a model of nephrogenic diabetes insipidus | Nature Communications AKAPs-PKA disruptors increase AQP2 activity independently of vasopressin in a model of nephrogenic diabetes insipidus | Nature Communications](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fs41467-018-03771-2/MediaObjects/41467_2018_3771_Fig1_HTML.jpg)
AKAPs-PKA disruptors increase AQP2 activity independently of vasopressin in a model of nephrogenic diabetes insipidus | Nature Communications
![IJMS | Free Full-Text | K+ and Rb+ Affinities of the Na,K-ATPase α1 and α2 Isozymes: An Application of ICP-MS for Quantification of Na+ Pump Kinetics in Myofibers | HTML IJMS | Free Full-Text | K+ and Rb+ Affinities of the Na,K-ATPase α1 and α2 Isozymes: An Application of ICP-MS for Quantification of Na+ Pump Kinetics in Myofibers | HTML](https://www.mdpi.com/ijms/ijms-19-02725/article_deploy/html/images/ijms-19-02725-g001a.png)
IJMS | Free Full-Text | K+ and Rb+ Affinities of the Na,K-ATPase α1 and α2 Isozymes: An Application of ICP-MS for Quantification of Na+ Pump Kinetics in Myofibers | HTML
![Characterization of a Urinary Bufodienolide Na+,K+-ATPase Inhibitor in Patients After Acute Myocardial Infarction | Hypertension Characterization of a Urinary Bufodienolide Na+,K+-ATPase Inhibitor in Patients After Acute Myocardial Infarction | Hypertension](https://www.ahajournals.org/cms/asset/6a346120-feb4-42ad-87b2-b22800283f49/hy0580507004.jpeg)
Characterization of a Urinary Bufodienolide Na+,K+-ATPase Inhibitor in Patients After Acute Myocardial Infarction | Hypertension
![Human neuromuscular fatigue is associated with altered Na+-K+-ATPase activity following isometric exercise | Journal of Applied Physiology Human neuromuscular fatigue is associated with altered Na+-K+-ATPase activity following isometric exercise | Journal of Applied Physiology](https://journals.physiology.org/cms/10.1152/japplphysiol.00668.2001/asset/images/medium/dg0421457003.jpeg)
Human neuromuscular fatigue is associated with altered Na+-K+-ATPase activity following isometric exercise | Journal of Applied Physiology
![Do H+ ions obscure electrogenic Na+ and K+ binding in the E1 state of the Na,K-ATPase? - ScienceDirect Do H+ ions obscure electrogenic Na+ and K+ binding in the E1 state of the Na,K-ATPase? - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S001457930203675X-gr1.gif)
Do H+ ions obscure electrogenic Na+ and K+ binding in the E1 state of the Na,K-ATPase? - ScienceDirect
![Human neuromuscular fatigue is associated with altered Na+-K+-ATPase activity following isometric exercise | Journal of Applied Physiology Human neuromuscular fatigue is associated with altered Na+-K+-ATPase activity following isometric exercise | Journal of Applied Physiology](https://journals.physiology.org/cms/10.1152/japplphysiol.00668.2001/asset/images/medium/dg0421457001.jpeg)
Human neuromuscular fatigue is associated with altered Na+-K+-ATPase activity following isometric exercise | Journal of Applied Physiology
![The selectivity of the Na+/K+-pump is controlled by binding site protonation and self-correcting occlusion | eLife The selectivity of the Na+/K+-pump is controlled by binding site protonation and self-correcting occlusion | eLife](https://iiif.elifesciences.org/lax/16616%2Felife-16616-fig4-v2.tif/full/1500,/0/default.jpg)
The selectivity of the Na+/K+-pump is controlled by binding site protonation and self-correcting occlusion | eLife
![Of channels and pumps: different ways to boost the aldosterone? - Bandulik - 2017 - Acta Physiologica - Wiley Online Library Of channels and pumps: different ways to boost the aldosterone? - Bandulik - 2017 - Acta Physiologica - Wiley Online Library](https://onlinelibrary.wiley.com/cms/asset/91b06f39-791d-4ef9-9ce1-1bcaecb0651f/apha12832-fig-0004-m.jpg)
Of channels and pumps: different ways to boost the aldosterone? - Bandulik - 2017 - Acta Physiologica - Wiley Online Library
![Aldosterone-induced protein kinase signalling and the control of electrolyte balance | Semantic Scholar Aldosterone-induced protein kinase signalling and the control of electrolyte balance | Semantic Scholar](https://d3i71xaburhd42.cloudfront.net/c9c3c254525463434f283488d2011b97c356886b/2-Figure1-1.png)
Aldosterone-induced protein kinase signalling and the control of electrolyte balance | Semantic Scholar
![The selectivity of the Na+/K+-pump is controlled by binding site protonation and self-correcting occlusion | eLife The selectivity of the Na+/K+-pump is controlled by binding site protonation and self-correcting occlusion | eLife](https://iiif.elifesciences.org/lax/16616%2Felife-16616-fig5-v2.tif/full/,1500/0/default.jpg)