The inhibition of dihydrofolate reductase by folate analogues: Structural requirements for slow- and tight-binding inhibition
- 1 February 1980
- journal article
- research article
- Published by Elsevier BV in Biochemical Pharmacology
- Vol. 29 (4), 589-595
- https://doi.org/10.1016/0006-2952(80)90381-0
Abstract
No abstract availableThis publication has 19 references indexed in Scilit:
- Methotrexate, a high-affinity pseudosubstrate of dihydrofolate reductaseBiochemistry, 1979
- Cooperativity in ligand binding to dihydrofolate reductaseBiochemistry, 1978
- Reactivation of dihydrofolate reductase inhibited by methotrexate or aminopterinArchives of Biochemistry and Biophysics, 1977
- Tight-binding inhibitors—IIIBiochemical Pharmacology, 1976
- Correlation analysis of Baker's studies on enzyme inhibition. 2. Chymotrypsin, trypsin, thymidine phosphorylase, uridine phosphorylase, thymidilate synthetase, cytosine nucleoside deaminase, dihydrofolate reductase, malate, glutamate, lactate, and glyceraldehyde-phosphate dehydrogenaseJournal of Medicinal Chemistry, 1976
- Tight-binding inhibitors—IBiochemical Pharmacology, 1975
- Relationship between the inhibition constant (KI) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reactionBiochemical Pharmacology, 1973
- A program for efficient integration of rate equations and least-squares fitting of chemical reaction dataComputers and Biomedical Research, 1972
- Crystalline Dihydropteroylglutamic AcidNature, 1960
- Analogs of Pteroylglutamic Acid. III. 4-Amino DerivativesJournal of the American Chemical Society, 1949