Results 241 to 250 of about 48,162 (258)
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Biochemistry, 1993
Dihydrofolate reductase (DHFR) is a critical enzyme in de novo purine and thymidylate biosynthesis. An RNA gel mobility shift assay was used to demonstrate a specific interaction between human recombinant DHFR protein and its corresponding DHFR mRNA.
Carmen J. Allegra +4 more
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Dihydrofolate reductase (DHFR) is a critical enzyme in de novo purine and thymidylate biosynthesis. An RNA gel mobility shift assay was used to demonstrate a specific interaction between human recombinant DHFR protein and its corresponding DHFR mRNA.
Carmen J. Allegra +4 more
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Dihydrofolate Reductase as a New “Affinity Handle”
The Journal of Biochemistry, 1992Dihydrofolate reductase (DHFR) has been demonstrated to be a versatile "affinity handle" for expression of recombinant proteins. The DHFR "handle" has advantages not only in terms of efficiency of expressing the fusion protein as a soluble form but also in stabilizing unstable polypeptides and facilitating purification of the expressed protein by means
Tomokuni Kokubu +6 more
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Life without dihydrofolate reductase FolA
Trends in Microbiology, 2003Reduced folate derivatives participate in numerous reactions of bacterial intermediary metabolism. Consequently, the well-characterized enzyme implicated in the formation of tetrahydrofolate--dihydrofolate reductase FolA--was considered to be essential for bacterial growth.
Myllykallio, H. +3 more
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Cytochemical Demonstration of Dihydrofolate Reductase Activity
British Journal of Haematology, 1974Summary. The enzyme dihydrofolate reductase plays an important role in the conversion of dietary folate to the active coenzymatic form, tetrahydrofolate, and during the synthesis of thymidylate from deoxyuridylate, when tetrahydrofolate is oxidized to dihydrofolate and the reductase re‐converts dihydro‐ to tetrahydrofolate.
Frank G. J. Hayhoe, Fotini Tzortzatou
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Mechanism of coenzyme a inhibition of dihydrofolate reductase
International Journal of Biochemistry, 19821. Coenzyme A was found to inhibit bovine liver dihydrofolate reductase. 2. The CoA inhibition types of dihydrofolate reductase were competitive with respect to NADPH and noncompetitive with respect to dihydrofolate. 3. The CoA inhibition is related to the number and the site of phosphoric residue in adenine nucleotide.
Ikuo Yasumasu, Masatoshi Mita
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1963
Publisher Summary This chapter discusses assay, purification, and properties of dihydrofolic reductase. Dihydrofolic reductase, also called “folic reductase,” catalyzes the reversible, TPNH-dependent reduction of dihydrofolate to tetrahydrofolate.
C.K. Mathews +2 more
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Publisher Summary This chapter discusses assay, purification, and properties of dihydrofolic reductase. Dihydrofolic reductase, also called “folic reductase,” catalyzes the reversible, TPNH-dependent reduction of dihydrofolate to tetrahydrofolate.
C.K. Mathews +2 more
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Lipophilic Inhibitors of Dihydrofolate Reductase
1984The evaluation of lipophilic inhibitors of dihydrofolate reductase (DHFR) as anticancer agents is a continuing effort because of the development of clinical resistance to methotrexate (MTX) and its limited spectrum of activity. The temperature-sensitive entry of MTX into cells is carrier-dependent and, in some tumors, MTX uptake is so slow that the ...
David S. Duch +2 more
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Multiple forms of dihydrofolate reductase
Biochemical and Biophysical Research Communications, 1968G.P. Mell +3 more
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Effect of amines on dihydrofolate reductase
Life Sciences, 1963D.K. Misra, Richard H. Adamson
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COMPARATIVE BIOCHEMISTRY OF DIHYDROFOLATE REDUCTASE
Annals of the New York Academy of Sciences, 1971openaire +3 more sources