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Titlebook: Nicotinic Acetylcholine Receptor; Structure and Functi Alfred Maelicke Conference proceedings 1986 Springer-Verlag Berlin Heidelberg 1986 c

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Topography of the Acetylcholine Receptor Revealed by Fluorescence Energy Transfered to overall receptor structure. The approach carries the inherent advantage that conformation can be monitored on a functional receptor. Also, fluorescence polarization, lifetimes, quantum yields, and spectral characteristics all yield information on molecular motion, the environment of the site o
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Monoclonal Antibodies as Probes of Acetylcholine Receptor Functionl., Fuchs, et al., Tzartos et al., Barkas et al., Froehner, et al. in this volume; Young et al. 1985). The existence of only a few reports on functional studies (Moshly-Rosen and Fuchs, 1981; Watters and Maelicke, 1983; Mikovilovic and Richman, 1984; Lindstrom, 1984) is mainly due to the fact that a
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Tertiary Structure of the Nicotinic Acetylcholine Receptor Probed by Photolabeling and Protein Chemive four chains of the Ach-receptor have been cloned and sequenced in . (Ballivet .., 1982, Noda .., 1982, 1983a,b, Claudio .., 1983), in . (for the a chain: Giraudat .., 1982, Sumikawa .., 1982, Devillers-Thiéry .., 1983) and in several vertebrate species, including humans (ref. in Kubo .., 1985 and
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A Structural Model of the Ion Channel of the Nicotinic Acetylcholine Receptorhe ion channel. Both are integral parts of the heteropentameric receptor protein and appear not to be separable as molecular entities. Their interaction has been described in analogy to other allosteric proteins (1) as mediated by conformational changes of the protein conveyed from the ligand bindin
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A General Treatment of Ligand Binding to the Acetylcholine Receptorontrolled cation channel (For review see: Maelicke 1984, Changeux et al. 1984). When plotted versus the agonist concentration, the response (depolarisation of the membrane) follows a sigmoid curve. Half-maximal response is observed at 28μM acetylcholine (Dreyer et al. 1978), whereas equilibrium bind
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Lipid-Protein Interactions and Acetylcholine Receptor Function in Reconstituted Membranesariety of biophysical techniques (1). The lipids in direct contact with membrane proteins are usually exchangeable with bulk lipids, although the two different types of lipid environments can be readily detected using electron spin resonance techniques (2–4). There is some selectivity in the apparen
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Regulation of Intercellular Signal Transmission. New Approaches to Chemical Kinetic Measurementsr-rich membrane vesicles. More recently we have begun to develop techniques for making similar chemical kinetic measurements of receptor function directly on cell surfaces. We are using the information we have already obtained about the mechanism of action of the acetylcholine receptor to calibrate
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