Retinoic acid inhibits calmodulin binding to human erythrocyte membranes and reduces membrane Ca2(+)-adenosine triphosphatase activity.

Eitemau Tebyg

• Structure-activity relationships of retinoids as inhibitors of calmodulin-dependent human erythrocyte Ca(2+)-ATPase activity and calmodulin binding to membranes.
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  Cyhoeddwyd: (1991)
• The effect of calmodulin on the phosphoprotein intermediate of Mg2+-dependent Ca2+-stimulated adenosine triphosphatase in human erythrocyte membranes.
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  Cyhoeddwyd: (1981)
• Stereochemical requirements for the modulation by retinoic acid of thyroid hormone activation of Ca(2+)-ATPase and binding at the human erythrocyte membrane.
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  Cyhoeddwyd: (1992)
• Vectorial aspects of adenosine-triphosphatase activity in erythrocyte membranes
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  Cyhoeddwyd: (1964)
• Calmodulin affinity chromatography yields a functional purified erythrocyte (Ca+ + Mg2+)-dependent adenosine triphosphatase.
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  Cyhoeddwyd: (1980)