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Literature summary for 2.1.1.45 extracted from

  • Cannazza, G.; Cazzato, A.S.; Marraccini, C.; Pavesi, G.; Pirondi, S.; Guerrini, R.; Pela, M.; Frassineti, C.; Ferrari, S.; Marverti, G.; Ponterini, G.; Costi, M.P.
    Internalization and stability of a thymidylate synthase peptide inhibitor in ovarian cancer cells (2014), J. Med. Chem., 57, 10551-10556.
    View publication on PubMed

Application

Application Comment Organism
medicine octapeptide inhibitor LSCQLYQR and derivatives are expected to work in combination with more aggressive chemotherapeutic agents in cancer cells to improve the efficacy, fight platinum-induced drug resistance, and reduce the overall drug combination toxicities. The cellular half-life observed for the peptide suggests that more chemical changes should be performed for an acceptable in vivo pharmacokinetics Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
LSCQLYQR octapeptide to specifically target the monomer-monomer interface of the enzyme. A fast-equilibrium mechanism exists that combines trafficking in/out of the cell and degradation pathways within cells Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Source Tissue

Source Tissue Comment Organism Textmining
ovary cancer cell line epithelial ovarian cancer cell line resistant to cisplatin Homo sapiens
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