Front Cover: Activation, Structure, Biosynthesis and Bioactivity of Glidobactin‐like Proteasome Inhibitors from Photorhabdus laumondii (ChemBioChem 9/2021)

Glidobactin‐like proteasome inhibitors are regarded as promising candidates for anticancer drug development. We report the largest subset of glidobactin‐like proteasome inhibitors, which were produced and identified after the silent biosynthetic gene cluster plu1881–1877 had been activated in the na...

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Veröffentlicht in:	Chembiochem : a European journal of chemical biology 2021-05, Vol.22 (9), p.1494-1494
Hauptverfasser:	Zhao, Lei, Le Chapelain, Camille, Brachmann, Alexander O., Kaiser, Marcel, Groll, Michael, Bode, Helge B.
Format:	Artikel
Sprache:	eng
Schlagworte:	biosynthesis drug design glidobactins proteasome inhibitors structure–activity relationships
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creator	Zhao, Lei Le Chapelain, Camille Brachmann, Alexander O. Kaiser, Marcel Groll, Michael Bode, Helge B.
description	Glidobactin‐like proteasome inhibitors are regarded as promising candidates for anticancer drug development. We report the largest subset of glidobactin‐like proteasome inhibitors, which were produced and identified after the silent biosynthetic gene cluster plu1881–1877 had been activated in the native host Photorhabdus laumondii. Crystal‐structure analysis of the new glidobactin derivatives in complex with yeast proteasome core particle (yCP) suggests that the inhibition occurs primarily by covalent and irreversible binding of the inhibitors to the β5 subunit of the yCP. More information can be found in the full paper by H. B. Bode et al.
doi_str_mv	10.1002/cbic.202100174
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subjects	biosynthesis drug design glidobactins proteasome inhibitors structure–activity relationships
title	Front Cover: Activation, Structure, Biosynthesis and Bioactivity of Glidobactin‐like Proteasome Inhibitors from Photorhabdus laumondii (ChemBioChem 9/2021)
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