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- W2000604837 abstract "Since many Hsp90 client proteins are key players in tumour pathways, the ubiquitylation and subsequent degradation of Hsp90-substrates as a consequence of pharmacologically inhibiting Hsp90 represents an innovative approach for cancer therapy. We therefore identified Hsp90-binding proteins which accumulated as ubiquityl-tagged aggregates in the detergent insoluble fraction of HeLa cells as a consequence of simultaneously inhibiting Hsp90 and the proteasome. 2-DE followed by nanoLC-MS/MS of trypsinised protein spots provided the Hsp90-dependent ubiquitylated proteome which was finally annotated and functionally classified. The overall picture thus obtained emphasised the well-established role of Hsp90 in stabilising proteins involved in gene transcription and signal transduction. It also provided a novel Hsp90-related link to metabolic pathways as the inhibition of Hsp90 caused the ubiquitylation of a significant amount of metabolic enzymes. These findings serve to support cumulating indications which attribute Hsp90 to diverse stabilising functions beyond signal transduction and gene transcription." @default.
- W2000604837 created "2016-06-24" @default.
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- W2000604837 date "2007-07-01" @default.
- W2000604837 modified "2023-10-03" @default.
- W2000604837 title "A proteomic approach towards the Hsp90-dependent ubiquitinylated proteome" @default.
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- W2000604837 doi "https://doi.org/10.1002/pmic.200600996" @default.
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