N. Kovalevskaya

NMR Structures of Apo L. casei Dihydrofolate Reductase and Its Complexes with Trimethoprim and NADPH: Contributions to Positive Cooperative Binding from Ligand-Induced Refolding, Conformational Changes, and Interligand Hydrophobic Interactions

J. Feeney, B. Birdsall, V. Polshakov, 2011, Biochemistry.

Structural factors determining the binding selectivity of the antibacterial drug trimethoprim to dihydrofolate reductase

B. Birdsall, J. Feeney, J. Feeney, 2007, Pharmaceutical Chemistry Journal.

Solution Structure of Human Dihydrofolate Reductase in its Complex with Trimethoprim and NADPH

T. Frenkiel, J. Feeney, A. F. Bradbury, 2005, Journal of biomolecular NMR.

NMR Structures of Apo L. casei Dihydrofolate Reductase and Its Complexes with Trimethoprim and NADPH: Contributions to Positive Cooperative Binding from Ligand-Induced Refolding, Conformational Changes, and Interligand Hydrophobic Interactions

J. Feeney, B. Birdsall, V. Polshakov, 2011, Biochemistry.

NMR Structures of Apo L. casei Dihydrofolate Reductase and Its Complexes with Trimethoprim and NADPH: Contributions to Positive Cooperative Binding from Ligand-Induced Refolding, Conformational Changes, and Interligand Hydrophobic Interactions

J. Feeney, B. Birdsall, V. Polshakov, 2011, Biochemistry.