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Thiostrepton exhibits antibiotic activity through blockade of ribosome turnover after an elongation step in protein synthesis by inhibiting both the dissociation of elongation factor G (EF-G) from the ribosome and the release of inorganic phosphate from EF-G following GTP hydrolysis. Thiostrepton is also described to show efficacy against cancer cell growth through downregulation of the forkhead box M1 (FOXM1) transcription factor, commonly overexpressed in many malignancies. Thiostrepton is an inhibitor of FOXM1. Thiostrepton has been used as a selectable marker for recombinant Streptomyces cultures.
Ursula Mocek.; Zhaopie Zeng.; David O'Hagan.; Pei Zho.; Lai Duen G. Fan.; John M. Beale.; Heinz G. Floss. Biosynthesis of the modified peptide antibiotic thiostrepton in Streptomyces azureus and Streptomyces laurentii.J. Am. Chem. Soc. 1993, 115 (18),7992-8001 .
Takahiro Suzuki.; Tsuneo Yamane.; Shoichi Shimizu. Mass production of thiostrepton by fed-batch culture of Streptomyces laurentii with pH-stat modal feeding of multi-substrate. . 1987, 25 (6),526-531 .
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