BIOCHEMICAL MECHANISMS OF ACTION OF FLUORINATED PYRIMIDINES.

doi:10.1016/0014-4827(63)90286-6

Paper

DOI: 10.1016/0014-4827(63)90286-6

BIOCHEMICAL MECHANISMS OF ACTION OF FLUORINATED PYRIMIDINES.

Published 1963 · Charles Heidelberger

Experimental cell research

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Abstract

Abstract hidden due to publisher request; this does not indicate any issues with the research. Click the full text link above to read the abstract and view the original source.

Study Snapshot

Fluorinated pyrimidines inhibit DNA biosynthesis by inhibiting thymidylate synthetase and incorporating into RNA, replacing uracil with fluorouracil.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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Citations

DOI: 10.1016/j.abb.2021.109066

Mammalian dihydropyrimidine dehydrogenase.

DPD catalyzes the two-electron reduction of pyrimidine bases, uracil and thymine, as the first step in pyrimidine catabolism, using a complex cofactor set including two flavins and four Fe 4 S 4 centers.

2021·12citations·D. Forouzesh et al.·Archives of biochemistry and biophysics

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Perturbing the Movement of Hydrogens to Delineate and Assign Events in the Reductive Activation and Turnover of Porcine Dihydropyrimidine Dehydrogenase.

The slow turnover of dihydropyrimidine dehydrogenase (DPD) is governed by the movement of a mobile structural feature that carries the C671 residue, rather than the protonation state of cysteine 671.

2021·5citations·B. Beaupre et al.·Biochemistry

Biochemistry

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Clinical development of retroviral replicating vector Toca 511 for gene therapy of cancer

Toca 511 shows promising results in early-stage clinical trials, but negative overall results in a registrational Phase III trial suggest further clinical investigation and development of other retroviral vectors.

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Transient State Analysis of Porcine Dihydropyrimidine Dehydrogenase Reveals Reductive Activation by NADPH.

Porcine dihydropyrimidine dehydrogenase undergoes reductive activation by NADPH, with the enzyme acting as a wire to rapidly transmit electrons from NADPH to the pyrimidine substrate.

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Biochemistry

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An improved method for the expression and purification of porcine dihydropyrimidine dehydrogenase.

This study presents a 4-fold improvement in the yield of active porcine dihydropyrimidine dehydrogenase when expressed in E. coli cells, enabling rapid quantitation and evaluation of purified samples.

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