Structures of the mono- and divalent metal nucleotide complexes in the myosin ATPase.

This publication has 58 references indexed in Scilit:

• Structure of the metal‐nucleotide chelate in the myosin‐product complex
  FEBS Letters, 1980
• Mechanistic studies on deoxyribonucleic acid dependent ribonucleic acid polymerase from Escherichia coli using phosphorothioate analogs. 2. The elongation reaction
  Biochemistry, 1979
• Mechanistic studies on deoxyribonucleic acid dependent ribonucleic acid polymerase from Escherichia coli using phosphorothioate analog. 1. Initiation and pyrophosphate exchange reactions
  Biochemistry, 1979
• Phosphorothioate analogs of nucleotides
  Accounts of Chemical Research, 1979
• X-ray crystal and molecular structure and absolute configuration of (dihydrogen tripolyphosphato)tetraamminecobalt(III) monohydrate, Co(NH₃)₄H₂P₃O₁₀·H₂O. A model for a metal-nucleoside polyphosphate complex
  Biochemistry, 1978
• Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility
  Journal of Molecular Biology, 1977
• The kinetic mechanism of the manganous ion‐dependent adenosine triphosphatase of myosin subfragment 1
  FEBS Letters, 1975
• Chemistry of Muscle Contraction
  Annual Review of Biochemistry, 1972
• The effects of monovalent and divalent cations on the ATPase activity of myosin
  Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1969
• Hard and Soft Acids and Bases
  Journal of the American Chemical Society, 1963