Structure, Function and Regulation of the Hsp90 Machinery
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...Post-translational modifications of Hsp90 include acetylation, nitrosylation, phosphorylation, and methylation, which has been elegantly reviewed by Li and Buchner (2013)....
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...S‐nitrosylation is a reversible covalent modification of reactive cysteine thiols in proteins by nitric oxide (NO).([109,110]) Mammalian Hsp90 is a target of S‐nitrosylation mediated by NO produced by its client protein, endothelial nitric oxide synthase (eNOS)....
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...To date, more than 20 co‐chaper‐ ones have been identified.([1,31]) They regulate the function of Hsp90 in different ways such as inhibition and activation of the ATPase of Hsp90 as well as recruitment of specific client...
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...Heat shock protein 90 (Hsp90), one of the most abundant and conserved molecular chaperones, is essential in eukaryotic cells.([1,2]) Different from other well‐known mo‐ lecular chaperone like Hsp70 and GroEL/ES, Hsp90 is not required for de novo folding of most proteins but facilitates the final maturation of a selected clientele of proteins....
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...Hsp90—DISEASES As one of themost abundant proteins in the cell, Hsp90 is known to counter different types of stresses (Borkovich et al. 1989; Taipale et al. 2010; Schopf et al. 2017)....
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...Early work on Hsp90 mainly focused on the co‐chap‐ erone requirement for the activation of SHRs.([32,33]) The maturation of most SHRs strictly depends on the interaction with Hsp90....
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...Archaea lackHsp90 (Chen et al. 2006), although most bacteria harbor one copy of Hsp90....
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...The most prominent examples of amino-terminal inhibitors are RD and the ansamycin GA (Whitesell et al. 1994; Roe et al. 1999)....
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...Bacterial HtpG hydrolyzes ATP at a rate between that of Hsp82 and Hsp90....
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...TRAP1 shares 50% amino acid similarity with Hsp90β....
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...A largely open issue is why Sti1/Hop harbors three Hsp90/Hsp70-binding sites and how the different TPR and DP modules modulate the interaction with Hsp70 and Hsp90....
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