Beneficent and Maleficent Effects of Cations on Bufadienolide Binding to Na+,K+-ATPase
Author:
Affiliation:
1. Department of Biomedicine, Aarhus University, Høegh-Guldbergsgade 10, 8000 Aarhus C, Denmark
2. Department of Chemistry, Aarhus University, Langelandsgade 140, 8000 Aarhus C, Denmark
Funder
Fonden til L?gevidenskabens Fremme
Natur og Univers, Det Frie Forskningsr?d
Novo Nordic Foundation
Publisher
American Chemical Society (ACS)
Subject
Library and Information Sciences,Computer Science Applications,General Chemical Engineering,General Chemistry
Link
http://pubs.acs.org/doi/pdf/10.1021/acs.jcim.0c01396
Reference38 articles.
1. Selectivity of Digitalis Glycosides for Isoforms of Human Na,K-ATPase
2. Na+,K+-ATPase Isoform Selectivity for Digitalis-Like Compounds Is Determined by Two Amino Acids in the First Extracellular Loop
3. Digoxin derivatives with selectivity for the α2β3 isoform of Na,K-ATPase potently reduce intraocular pressure
4. Structures and characterization of digoxin- and bufalin-bound Na+,K+-ATPase compared with the ouabain-bound complex
5. Crystal structure of the high-affinity Na+,K+-ATPase-ouabain complex with Mg2+ bound in the cation binding site
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