Ontology highlight
ABSTRACT:
SUBMITTER: Paiardini A
PROVIDER: S-EPMC5438088 | biostudies-literature | 2015 Mar
REPOSITORIES: biostudies-literature
Paiardini Alessandro A Fiascarelli Alessio A Rinaldo Serena S Daidone Frederick F Giardina Giorgio G Koes David R DR Parroni Alessia A Montini Giulia G Marani Marina M Paone Alessio A McDermott Lee A LA Contestabile Roberto R Cutruzzolà Francesca F
ChemMedChem 20150210 3
Metabolic reprogramming of tumor cells toward serine catabolism is now recognized as a hallmark of cancer. Serine hydroxymethyltransferase (SHMT), the enzyme providing one-carbon units by converting serine and tetrahydrofolate (H4 PteGlu) to glycine and 5,10-CH2 -H4 PteGlu, therefore represents a target of interest in developing new chemotherapeutic drugs. In this study, 13 folate analogues under clinical evaluation or in therapeutic use were in silico screened against SHMT, ultimately identifyi ...[more]