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Journal of Enzyme Inhibition|January 1, 1996
Modeling of the three-dimensional structure of the digitalis intercalating matrix in Na+/K(+)-ATPase protodimerK R Repke, J Weiland, R Megges, et al.
Naunyn-Schmiedeberg'S Archives of Pharmacology|March 1, 1995
Differentiation between isoforms of Na+/K+-transporting atpase from human and guinea-pig muscle through use of digitalis derivatives as analytical probesR Schön, J Weiland, R Megges, et al.
FEBS Letters|February 13, 1995
Location and properties of the digitalis receptor site in Na+/K(+)-ATPaseK R Repke, R Megges, J Weiland, et al.
Journal of Enzyme Inhibition|January 1, 1987
5 Beta,14 beta-androstane-3 beta,14-diol binds to the digitalis receptor site on Na/K-ATPaseW Schönfeld, K H Menke, R Schönfeld, et al.
Biochimica Et Biophysica Acta|March 14, 1984
Evidence against parallel operation of sodium/calcium antiport and ATP-driven calcium transport in plasma membrane vesicles from kidney tubule cellsW Schönfeld, K H Menke, R Schönfeld, et al.
Pharmacological Research|January 1, 1991
Interaction of progesterone derivatives with the digitalis target enzyme: impact of glycosidation on inhibitory potencyJ Weiland, W Schönfeld, K H Menke, et al.
Biochimica Et Biophysica Acta|November 1, 1977
Electron microscopic visualization of the arrangement of the two protein components of (Na+ + K+)-ATPaseF Vogel, H W Meyer, R Grosse, et al.
Biochemical and Biophysical Research Communications|February 29, 1984
Kinetic studies on interaction of (Na,K)-ATPase with Cibacron Blue F3GA as probe of the nucleotide foldW Schönfeld, K H Menke, R Schönfeld, et al.
European Journal of Biochemistry|April 15, 1977
Spectroscopic studies on effector-induced and substrate-induced conformation changes of phosphofructokinaseR Grosse, K Eckert, M Otto, et al.
Journal of Enzyme Inhibition|January 1, 1987
Glycosidation of chlormadinol acetate alters its actions on Na+/K+-transporting ATPase and cardiac contractility: a contribution to the endogenous digitalis problemJ Weiland, K Schwabe, D Hübler, et al.
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