Spin‐labeled derivatives of cardiotonic steroids as tools for characterization of the extracellular entrance to the binding site on Na + ,K + ‐ ATP ase
Author:
Affiliation:
1. Guangdong Province Key Laboratory of Pharmacodynamic Constituents of TCM and New Drugs Research College of Pharmacy Jinan University Guangzhou City Guangdong Province China
2. Department of Biomedicine Aarhus University Denmark
Funder
National Natural Science Foundation of China
Det Frie Forskningsråd
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1111/febs.14480
Reference12 articles.
1. A Hundred Years of Sodium Pumping
2. Crystal structure of the high-affinity Na+,K+-ATPase-ouabain complex with Mg2+ bound in the cation binding site
3. Structures and characterization of digoxin- and bufalin-bound Na+,K+-ATPase compared with the ouabain-bound complex
4. Novel stereoselective bufadienolides reveal new insights into the requirements for Na+, K+-ATPase inhibition by cardiotonic steroids
5. Selectivity of Digitalis Glycosides for Isoforms of Human Na,K-ATPase
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