Interaction of cardiac glycosides and Na,K-ATPase is regulated by effector-controlled equilibrium between two limit enzyme conformers (Q48652988)

13 February 2018

title

Interaction of cardiac glycosides and Na,K-ATPase is regulated by effector-controlled equilibrium between two limit enzyme conformers (English)

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https://api.crossref.org/works/10.1016/0006-2952(84)90578-1

30 September 2023

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A6331458

30 September 2023

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30 September 2023

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author name string

K. R. Repke

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A6331458

30 September 2023

I. Herrmann

2

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A6331458

30 September 2023

H. J. Portius

3

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30 September 2023

language of work or name

English

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publication date

1 July 1984

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13 February 2018

full work available at URL

https://api.elsevier.com/content/article/PII:0006295284905781?httpAccept=text/xml

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https://api.elsevier.com/content/article/PII:0006295284905781?httpAccept=text/plain

30 September 2023

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30 September 2023

published in

Biochemical Pharmacology

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13 February 2018

volume

33

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13 February 2018

issue

13

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13 February 2018

page(s)

2089-2099

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13 February 2018

Ouabain-receptor interactions in (Na+ + K−)-ATPase preparations. A contribution to the problem of nonlinear scatchard plots

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Membrane (Na+ + K+)-ATPase of canine brain, heart and kidney. Tissue-dependent differences in kinetic properties and the influence of purification procedures

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Two receptor forms for ouabain in sarcolemma-enriched preparations from canine ventricle

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An allosteric explanation for ouabain-induced time-dependent inhibition of sodium, potassium-adenosine triphosphatase

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Effects of sodium and potassium on the partial reactions of a highly purified (Na+ plus K+)-ATPase: modulation of the rate of ouabain interaction.

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Side-dependent effects of internal versus external Na and K on ouabain binding to reconstituted human red blood cell ghosts

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Interaction of ouabain with (Na+ + K+)ATPase from human heart and from guinea-pig heart

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Kinetics studies on the interaction between ouabain and (Na+,K+)-ATPase

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A heterogeneous ouabain-ATPase interaction in mouse brain

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Organ Specificity of Rat Sodium- and Potassium-Activated Adenosine Triphosphatase1

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Purification and properties of a highly active ouabain-sensitive Na+, K+-dependent adenosinetriphosphatase from cardiac tissue.

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Rates of dissociation of enzyme-ouabain complexes and K 0.5 values in (Na + + K + ) adenosine triphosphatase from different species

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Ligand interactions with membrane-bound porcine atrial muscarinic receptor(s).

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Glucocorticoid-receptor interactions. Discrimination between glucocorticoid agonists and antagonists by means of receptor-binding kinetics

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Binding of Ouabain to Na+, K+-Dependent ATPase during the ATPase Reaction: Evidence for a Dimer Structure of the ATPase1

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The K+-induced apparent heterogeneity of high-affinity nucleotide-binding sites in (Na+ + K+)-ATPase can only be due to the oligomeric structure of the enzyme

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Kinetics of cardiac glycoside binding to sodium, potassium adenosine triphosphatase studied with a fluorescent derivative of ouabain

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A study of the rate of chelation of magnesium by CDTA and EDTA in the ATP (NA+ + K+)-ATPase system.

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Thermodynamic Characterization of Conformational States of Biological Macromolecules using Differential Scanning Calorimetry

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Identifiers

1 reference

13 February 2018

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13 February 2018