The stereochemical course of phosphoric residue transfer during the myosin ATPase reaction.

This publication has 21 references indexed in Scilit:

• Enzyme-Catalyzed Phosphoryl Transfer Reactions
  Annual Review of Biochemistry, 1980
• Stereochemical course of a phosphokinase using a chiral [18O]phosphorothioate. Comparison with the transfer of a chiral [16O,17O,18O] phosphoryl group
  Biochemistry, 1980
• Use of phosphorus-31 nuclear magnetic resonance to distinguish bridge and nonbridge oxygens of oxygen-17-enriched nucleoside triphosphates. Stereochemistry of acetate activation by acetyl coenzyme A synthetase
  Biochemistry, 1979
• Stereochemical course of thiophosphoryl group transfer catalyzed by adenylate kinase
  Journal of the American Chemical Society, 1978
• ³¹P nuclear magnetic resonance spectra of the thiophosphate analogs of adenine nucleotides; effects of pH and Mg²⁺ binding
  Biochemistry, 1978
• Kinetic Analysis of ATPase Mechanisms
  Quarterly Reviews of Biophysics, 1976
• Synthesis and properties of diastereoisomers of adenosine 5'-(O-1-thiotriphosphate) and adenosine 5'-(O-2-thiotriphosphate)
  Biochemistry, 1976
• Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin
  Nature, 1975
• Investigation of Enzyme Mechanisms with Nucleoside Phosphorothioates
  Angewandte Chemie International Edition in English, 1975
• On the nature of p-nitrothiophenylated myosin
  Biochimica et Biophysica Acta (BBA) - Protein Structure, 1973