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Titlebook: Calcium in Drug Actions; Peter F. Baker (Professor Sc. D., F.R.S.) Book 1988 Springer-Verlag Berlin Heidelberg 1988 ATP.ATPase.Calcium.bon

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Pascal D. König,Sebastian Jäckle 1985) and Ca. transport (C. 1984 a, b, c, d, 1985; S. 1983, 1985). Because relatively more is known about the Ca. pump in human red blood cells (RBCs) than in other types and species of cells, most of our concern has been with this type of cell. Ca. transport in the heart has been reviewed by L. (1984) and C. (1985).
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Drug Effects on Plasma Membrane Calcium Transport 1985) and Ca. transport (C. 1984 a, b, c, d, 1985; S. 1983, 1985). Because relatively more is known about the Ca. pump in human red blood cells (RBCs) than in other types and species of cells, most of our concern has been with this type of cell. Ca. transport in the heart has been reviewed by L. (1984) and C. (1985).
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Ligand-Binding Sites on Calmodulin 10.. (R. 1983). This situation is schematically depicted in Fig. 1. As a second step, the transient increase in intracellular Ca. needs to be translated into metabolic or contractile responses. To this end, nature has deployed a unique class of calcium-binding proteins. Upon binding Ca. they underg
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The Apamin-Sensitive Ca2+-Dependent K+ Channel: Molecular Properties, Differentiation, Involvement it (C. and M. 1977; G. et al. 1978). This approach has confirmed that the active site of apamin comprises the two residues Arg-13 and Arg-14. The exact three-dimensional structure of the toxin remains unknown. However, recent solution analysis of apamin by NMR techniques has suggested that the toxin
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