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- W17045731 abstract "EGFR and ErbB2 proteins are highly homologous in their amino acid sequence, yet they differ in their dependence on the molecular chaperone Hsp90. While both newly synthesized and mature ErbB2 proteins rely on Hsp90 for their stability, only the nascent form of the EGFR requires association with Hsp90 (, , ). Thus, blocking Hsp90 function with pharmacologic inhibitors, such as the benzoquinone ansamycin antibiotic geldanamycin (GA) and its derivatives, induces a rapid and dramatic decrease in the level of ErbB2 expression, but causes a much slower decline in the steady-state level of EGFR (Fig. 5.1). Open image in new window Fig. 5.1 EGFR and ErbB2 proteins are differentially sensitive to GA-induced down-regulation. A431 (lower panel) and SKBR3 (upper panel) cells were treated with 3 μM GA for increasing times. Cell lysates were separated by SDS-PAGE and Western-blotted for either EGFR (A431 lysates) or ErbB2 (SKBR3 lysates)." @default.
- W17045731 created "2016-06-24" @default.
- W17045731 creator A5018089497 @default.
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- W17045731 date "2008-01-01" @default.
- W17045731 modified "2023-10-11" @default.
- W17045731 title "Differential dependence of EGFR and ErbB2 on the molecular chaperone Hsp90" @default.
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- W17045731 doi "https://doi.org/10.1007/978-1-59745-356-1_5" @default.
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