Thymidylate synthase (TS) takes part in the folate pathway and is a dimeric enzyme that catalyzes the conversion from dUMP to dTMP. This reaction step is essential for all cells, but especially for fast growing cancer cells, making TS an important target for cancer treatment. Most of the clinical drugs for inhibiting TS are substrate or cofactor analogues that give rise to resistance after a certain time. The aim of the LIGHTS EU project is to overcome such resistance to inhibitors by interfering with TS dimerizationusing low molecular weight compounds and peptides binding to allosteric sites.
Allosteric Inhibition of human Thymidylate Synthase / S., Henrich; O., Salo Ahen; D., Garg; Cardinale, Daniela; Ferrari, Stefania; Franchini, Silvia; Genovese, Filippo; Guaitoli, Giambattista; Lazzari, Sandra; Venturelli, Alberto; S., Mangani; Costi, Maria Paola; R. C., Wade. - STAMPA. - ...:(2010), pp. ...-.... (Intervento presentato al convegno Biomolecular Interaction Networks: Function and Disease. tenutosi a Fairmont Le Château Frontenac, Québec, QC, Canada nel March 7 - 12, 2010).
Allosteric Inhibition of human Thymidylate Synthase.
CARDINALE, Daniela;FERRARI, Stefania;FRANCHINI, Silvia;GENOVESE, Filippo;GUAITOLI, GIAMBATTISTA;LAZZARI, Sandra;VENTURELLI, Alberto;COSTI, Maria Paola;
2010
Abstract
Thymidylate synthase (TS) takes part in the folate pathway and is a dimeric enzyme that catalyzes the conversion from dUMP to dTMP. This reaction step is essential for all cells, but especially for fast growing cancer cells, making TS an important target for cancer treatment. Most of the clinical drugs for inhibiting TS are substrate or cofactor analogues that give rise to resistance after a certain time. The aim of the LIGHTS EU project is to overcome such resistance to inhibitors by interfering with TS dimerizationusing low molecular weight compounds and peptides binding to allosteric sites.
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