3H-n.m.r. studies of multiple conformations and dynamic processes in complexes of folate and methotrexate with Lactobacillus casei dihydrofolate reductase.

Eitemau Tebyg

• A 1H n.m.r. study of the role of the glutamate moiety in the binding of methotrexate to Lactobacillus casei dihydrofolate reductase.
  gan: Antonjuk, D. J., et al.
  Cyhoeddwyd: (1984)
• 19F-n.m.r. studies of 3',5'-difluoromethotrexate binding to Lactobacillus casei dihydrofolate reductase. Molecular motion and coenzyme-induced conformational changes.
  gan: Clore, G M, et al.
  Cyhoeddwyd: (1984)
• Structure and dynamics in solution of the complex of Lactobacillus casei dihydrofolate reductase with the new lipophilic antifolate drug trimetrexate.
  gan: Polshakov, V. I., et al.
  Cyhoeddwyd: (1999)
• Conformational Changes Induced in Dihydrofolate Reductase by Folates, Pyridine Nucleotide Coenzymes, and Methotrexate
  gan: Pastore, Edward J., et al.
  Cyhoeddwyd: (1974)
• Proceedings: NMR studies of the binding of substrate analogues to L. casei dihydrofolate reductase.
  gan: Burgen, A S, et al.
  Cyhoeddwyd: (1974)