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Synthesis, molecular docking study and biological evaluation of new pyrrole scaffolds as potential antitubercular agents for dual targeting of enoyl ACP reductase and dihydrofolate reductase. [PDF]
PLoS OneMahnashi MH +11 more
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TaqMan-quantitative PCR assays applied in <i>Neospora caninum</i> knock-outs generated through CRISPR-Cas9 allow to determine the copy numbers of integrated dihydrofolate reductase-thymidylate synthase <i>drug selectable markers</i>. [PDF]
Front Cell Infect MicrobiolRico-San Román L +6 more
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Dismutation of dihydrofolate by dihydrofolate reductase
Biochemistry, 1984Degradation of 7,8-dihydrofolate (H2folate) in the presence of dihydrofolate reductase (DHFR) has been shown due not to an oxygenase activity of the reductase as previously reported but to dismutation of H2folate to folate and 5,6,7,8-tetrahydrofolate (H4folate). The reaction can be followed spectrophotometrically or by analysis of the reaction mixture
R L, Blakley, L, Cocco
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Nature, 1958
THE enzymatic reduction of dihydrofolic acid (FH2) to tetrahydrofolic acid (FH4) has been reported by several investigators1–3. Futterman1 noted that dihydrofolic acid was reduced by chicken liver extracts when either reduced di- or tri-phospho-pyridine nucleotide served as the co-factor. We have found that the rate of reduction of dihydrofolic acid by
J M, PETERS, D M, GREENBERG
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THE enzymatic reduction of dihydrofolic acid (FH2) to tetrahydrofolic acid (FH4) has been reported by several investigators1–3. Futterman1 noted that dihydrofolic acid was reduced by chicken liver extracts when either reduced di- or tri-phospho-pyridine nucleotide served as the co-factor. We have found that the rate of reduction of dihydrofolic acid by
J M, PETERS, D M, GREENBERG
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How Dihydrofolate Reductase Facilitates Protonation of Dihydrofolate
Journal of the American Chemical Society, 2003Dihydrofolate Reductase (DHFR) catalyzes the reduction of dihydrofolate (H2F) to tetrahydrofolate. On the basis of 10-12.5 ns molecular dynamics simulations of two conformations (closed and occluded) of the ternary DHFR/NADPH/H2F complex from Escherichia coli and a free energy perturbation approach, we have calculated the pKa value for the N5 atom in ...
Thomas H, Rod, Charles L, Brooks
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Dihydrofolate reductase as a therapeutic target
The FASEB Journal, 1990The folate antagonists are an important class of therapeutic compounds, as evidenced by their use as antiinfective, antineoplastic, and antiinflammatory drugs. Thus far, all of the clinically useful drugs of this class have been inhibitors of dihydrofolate reductase (DHFR), a key enzyme in the synthesis of thymidylate, and ...
B I, Schweitzer +2 more
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A fluorometric assay for dihydrofolate reductase
Analytical Biochemistry, 1977Abstract A recording fluorometric assay for dihydrofolate reductase is described. The technique measures the appearance of product, tetrahydrofolate, as the reaction proceeds. The assay can be accomplished with as little as 2 pmol of enzyme and is sufficiently sensitive to allow accurate kinetic studies using very low concentrations of substrate ...
C A, Lindquist +2 more
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The mammalian dihydrofolate reductase locus
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1990Synthese de resultats relatifs au gene de la dihydrofolate reductase, en particulier: expression et replication, structure de la chromatine et organisation nucleaire, mutation, reparation et recombinaison du gene; role de ce gene dans la division des cellules tumorales et applications en chimiotherapie et genie ...
J L, Hamlin, C, Ma
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A Gene for Dihydrofolate Reductase in a Herpesvirus
Science, 1988The enzyme dihydrofolate reductase (DHFR) is found ubiquitously in both prokaryotes and eukaryotes. It is essential for de novo synthesis of purines and of deoxythymidine monophosphate for DNA synthesis. Among viruses, however, only the T-even and T5 bacteriophage have been found to encode their own DHFR.
J J, Trimble +4 more
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A histochemical method for dihydrofolate reductase
The Histochemical Journal, 1970A histochemical method for the detection of dihydrofolate reductase (5,6,7,8-tetrahydrofolate: NADP oxidoreductase, E.C. 1.5.1.3) is described. With this method, the highest enzyme activity has been found in hepatocytes, nephrocytes, intestinal epithelium and connective tissue cells.
D, Onicescu, L, Taşcă, E, Trutza
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