Krupka RM, Deves R (1980) <br />The electrostatic contribution to binding in the choline transport system of erythrocytes<br /><i>Journal of Biological Chemistry</i> <b>255</b>: 8546<br /><br />Hellenbrand K, Krupka RM (1975) <br />The comparative biochemistry of mammalian and insect acetylcholinesterase with reference to the selective inhibition by organophosphates and carbamates<br /><i>Croatica Chemica Acta</i> <b>47</b>: 345<br /><br />Krupka RM (1975) <br />Methanesulphonyl fluoride : A probe of substrate interactions in the catalytic site of acetylcholinesterase<br /><i>Croatica Chemica Acta</i> <b>47</b>: 299<br /><br />Reiner E, Aldridge WN, Hopff WH, Taylor P, Krupka RM, Rosenberry TL, Augustinsson KB, Mooser G, O'Brien RD, Brodbeck U, Massoulie J, Maricic S, Eldefrawi ME, Silman I (1975) <br />General discussion on models for the ligand binding sites of cholinesterase<br /><i>Croatica Chemica Acta</i> <b>47</b>: 499<br /><br />Krupka RM, Hellenbrand K (1974) <br />Specific versus non-specific interactions of mammalian and insect acetylcholinesterase with substrates and reversible inhibitors<br /><i>Biochimica & Biophysica Acta</i> <b>370</b>: 208<br /><br />Hellenbrand K, Krupka RM (1970) <br />Kinetic studies on the mechanism of insect acetylcholinesterase<br /><i>Biochemistry</i> <b>9</b>: 4665<br /><br />Krupka RM (1967) <br />Evidence for an intermediate in the acetylation reaction of acetylcholinesterase<br /><i>Biochemical Journal</i> <b>6</b>: 1183<br /><br />Krupka RM (1966) <br />Chemical structure and function of the active center of acetylcholinesterase<br /><i>Biochemistry</i> <b>5</b>: 1988<br /><br />Krupka RM (1966) <br />Fluoride inhibition of acetylcholinesterase<br /><i>Molecular Pharmacology</i> <b>2</b>: 558<br /><br />Krupka RM (1966) <br />Hydrolysis of neutral substrates by acetylcholinesterase<br /><i>Biochemistry</i> <b>5</b>: 1983<br /><br />Krupka RM (1965) <br />Are identical catalytic groups involved in the acetylation and the deacetylation steps of acetylcholinesterase reactions?<br /><i>Biochemical & Biophysical Research Communications</i> <b>19</b>: 531<br /><br />Krupka RM (1965) <br />Acetylcholinesterase: structural requirements for blocking deacetylation<br /><i>Biochemistry</i> <b>4</b>: 429<br /><br />Krupka RM (1964) <br />Acetylcholinesterase<br /><i>Canadian Journal of Biochemistry</i> <b>42</b>: 677<br /><br />Krupka RM (1964) <br />Acetylcholinesterase: trimethylammonium ion inhibition of deacetylation<br /><i>Biochemistry</i> <b>3</b>: 1749<br /><br />Krupka RM (1963) <br />The mechanism of action of acetylcholinesterase, substrats inhibition and the binding of inhibitors<br /><i>Biochemistry</i> <b>2</b>: 76<br /><br />Hein GE, Krupka RM, Laidler KJ (1962) <br />Multi-step mechanisms for cholinesterase activity<br /><i>Nature</i> <b>193</b>: 1155<br /><br />Krupka RM, Laidler KJ (1961) <br />Molecular mechanisms for hydrolytic enzyme action. I. Apparent non-competitive inhibition, with special reference to acetylcholinesterase. II. Inhibition of acetylcholinesterase by excess substrats. III. A general mechanism for the inhibition of acetylcholinesterase. IV. The structure of the active center and the reaction mechanism<br /><i>Journal of the American Chemical Society</i> <b>83</b>: 1445<br /><br />Krupka RM, Laidler KJ (1960) <br />The influence of pH on the rates of enzyme reactions. 6. Reactions catalyzed by acetylcholinesterase<br /><i>Discussions of the Faraday Society</i> <b>56</b>: 1477<br /><br />