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• W2143156516 abstract "To identify previously unknown small molecules that inhibit cell cycle machinery, we performed a chemical genetic screen in Xenopus extracts. One class of inhibitors, termed ubistatins, blocked cell cycle progression by inhibiting cyclin B proteolysis and inhibited degradation of ubiquitinated Sic1 by purified proteasomes. Ubistatins blocked the binding of ubiquitinated substrates to the proteasome by targeting the ubiquitin-ubiquitin interface of Lys 48 -linked chains. The same interface is recognized by ubiquitin-chain receptors of the proteasome, indicating that ubistatins act by disrupting a critical protein-protein interaction in the ubiquitin-proteasome system." @default.
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• W2143156516 date "2004-10-01" @default.
• W2143156516 modified "2023-10-16" @default.
• W2143156516 title "Ubistatins Inhibit Proteasome-Dependent Degradation by Binding the Ubiquitin Chain" @default.
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• W2143156516 doi "https://doi.org/10.1126/science.1100946" @default.
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