Results 171 to 180 of about 45,192 (224)
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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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Directed Mutagenesis of Dihydrofolate Reductase
Science, 1983Three mutations of the enzyme dihydrofolate reductase were constructed by oligonucleotide-directed mutagenesis of the cloned Escherichia coli gene. The mutations—at residue 27, aspartic acid replaced with asparagine; at residue 39, proline replaced with cysteine; and at residue 95, glycine replaced with alanine—were
Villafranca, Jesus E. +6 more
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Dihydrofolate reductases as targets for inhibitors
Advances in Enzyme Regulation, 1980Abstract Species differences among dihydrofolate reductases were first detected and most strikingly illustrated by the selective binding of small molecule inhibitors. This led on the one hand to practical applications in the chemotherapy of microbial infections, and on the other hand to stimuli for sequence and conformation studies of representative ...
G H, Hitchings, S L, Smith
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The kinetics of the histochemical method for dihydrofolate dehydrogenase (dihydrofolate reductase)
Histochemistry, 1979The purpose of the present investigation is to report some histochemical and cytospectrophotometric observations providng more objective evidence for the specific activity of the histochemical method for dihydrofolate reductase activity (5.6.7.8-tetrahydrofolate: E.C. 1.5.1.3).
D, Onicescu, V, Atanasiu
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Structure of Dihydrofolate When Bound to Dihydrofolate Reductase
Journal of the American Chemical Society, 1998The Raman spectrum of dihydrofolate (H2folate) complexed with dihydrofolate reductase (DHFR) and NADP+, believed to be an accurate mimic of the productive DHFR/NADPH/H2folate complex involved in the reaction catalyzed by DHFR, contains bands associated with stretch motions of N5C6 of bound substrate.
Hua Deng, Robert Callender
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The interactions of dihydrofolate with M. tuberculosis dihydrofolate reductase
2016 Second Asian Conference on Defence Technology (ACDT), 2016The molecular dynamics (MD) simulation was used to determine the interactions and binding affinities of Mycobacterium tuberculosis dihydrofolate reductase (mtbDHFR) in complex with dihydrofolate (DHF), which is the natural substrate of the enzyme. The MD simulation approach can predict the ternary complexes of mtbDHFR with NADPH and DHF in the present ...
Pimonluck Sittikornpaiboon +2 more
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