作者: Sarah Shaikho , Christine C. Dobson , Thet Naing , Bahram Samanfar , Houman Moteshareie
DOI: 10.1080/21690731.2016.1244395
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摘要: ABSTRACTMammalian 90 kDa heat shock protein (Hsp90) is a ubiquitous molecular chaperone whose expression selectively upregulated during stress, although the precise control mechanism of this increase yet to be fully elucidated. We used polysome profiling show that Hsp90α mRNA translated, while global translation inhibited stress. Furthermore, we have identified 2 ribosomal proteins, eL36 and eL42 modulate under both normal conditions. Importantly, noted elevated in panel human rhabdomyosarcomas where it drives high Hsp90 modulates sensitivity these cells an inhibitor 17-AAG.