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9. Hsp90 is regulated by a switch point in the C-terminal domain. Retzlaff M; Stahl M; Eberl HC; Lagleder S; Beck J; Kessler H; Buchner J EMBO Rep; 2009 Oct; 10(10):1147-53. PubMed ID: 19696785 [TBL] [Abstract][Full Text] [Related]
10. Stimulation of the weak ATPase activity of human hsp90 by a client protein. McLaughlin SH; Smith HW; Jackson SE J Mol Biol; 2002 Jan; 315(4):787-98. PubMed ID: 11812147 [TBL] [Abstract][Full Text] [Related]
11. Cdc37-Hsp90 complexes are responsive to nucleotide-induced conformational changes and binding of further cofactors. Gaiser AM; Kretzschmar A; Richter K J Biol Chem; 2010 Dec; 285(52):40921-32. PubMed ID: 20880838 [TBL] [Abstract][Full Text] [Related]
12. The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. Richter K; Walter S; Buchner J J Mol Biol; 2004 Oct; 342(5):1403-13. PubMed ID: 15364569 [TBL] [Abstract][Full Text] [Related]
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14. C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle. Weikl T; Muschler P; Richter K; Veit T; Reinstein J; Buchner J J Mol Biol; 2000 Nov; 303(4):583-92. PubMed ID: 11054293 [TBL] [Abstract][Full Text] [Related]
15. Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1. Xu W; Beebe K; Chavez JD; Boysen M; Lu Y; Zuehlke AD; Keramisanou D; Trepel JB; Prodromou C; Mayer MP; Bruce JE; Gelis I; Neckers L Nat Commun; 2019 Jun; 10(1):2574. PubMed ID: 31189925 [TBL] [Abstract][Full Text] [Related]
16. Structure and mechanism of the Hsp90 molecular chaperone machinery. Pearl LH; Prodromou C Annu Rev Biochem; 2006; 75():271-94. PubMed ID: 16756493 [TBL] [Abstract][Full Text] [Related]
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18. Structure and functional relationships of Hsp90. Prodromou C; Pearl LH Curr Cancer Drug Targets; 2003 Oct; 3(5):301-23. PubMed ID: 14529383 [TBL] [Abstract][Full Text] [Related]
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