Determinants of the Therapeutic Efficacy of Thymidylate Synthase Inhibitors View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1998

AUTHORS

G. J. Peters , C. M. Kuiper , B. van Triest , H. Backus , C. L. van der Wilt , J. A. M. van Laar , G. Jansen , C. J. van Groeningen , H. M. Pinedo

ABSTRACT

Thymidylate synthase (TS) catalyses a critical step in the pathway of DNA synthesis.1,2 Using the co-substrate 5,10-methylene tetrahydrofolate (CH2-THF) as a methyl donor, thymidylate synthase converts dUMP by methylation to dTMP (Fig. 1). This process is the only de novo source of dTMP which is subsequently metabolized to dTTP, exclusively for incorporation into DNA during synthesis and repair. The other source for dTMP is thymidine kinase, which uses thymidine as its precursor.2 TS inhibition results in a thymineless state, which is lethal to most actively dividing cells. In addition, the circulating thymidine concentrations in humans may not be adequate to prevent the lethal thymineless state. TS is therefore an ideal target for anticancer therapy.1,2 More... »

PAGES

699-704

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4615-5381-6_135

DOI

http://dx.doi.org/10.1007/978-1-4615-5381-6_135

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1034035636

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9598155


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