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Items: 19

1.

Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones.

Prodromou C, Siligardi G, O'Brien R, Woolfson DN, Regan L, Panaretou B, Ladbury JE, Piper PW, Pearl LH.

EMBO J. 1999 Feb 1;18(3):754-62.

2.

The 'active life' of Hsp90 complexes.

Prodromou C.

Biochim Biophys Acta. 2012 Mar;1823(3):614-23. doi: 10.1016/j.bbamcr.2011.07.020. Review.

3.

Structure and mechanism of the Hsp90 molecular chaperone machinery.

Pearl LH, Prodromou C.

Annu Rev Biochem. 2006;75:271-94. Review.

PMID:
16756493
4.

The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones.

Li J, Soroka J, Buchner J.

Biochim Biophys Acta. 2012 Mar;1823(3):624-35. doi: 10.1016/j.bbamcr.2011.09.003. Review.

5.

Hsp90 and co-chaperones twist the functions of diverse client proteins.

Zuehlke A, Johnson JL.

Biopolymers. 2010 Mar;93(3):211-7. doi: 10.1002/bip.21292. Review.

6.

Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket.

Donnelly A, Blagg BS.

Curr Med Chem. 2008;15(26):2702-17. Review.

7.

Mechanistic Asymmetry in Hsp90 Dimers.

Flynn JM, Mishra P, Bolon DN.

J Mol Biol. 2015 Sep 11;427(18):2904-11. doi: 10.1016/j.jmb.2015.03.017. Review.

8.

Proposal for a role of the Hsp90/Hsp70-based chaperone machinery in making triage decisions when proteins undergo oxidative and toxic damage.

Pratt WB, Morishima Y, Peng HM, Osawa Y.

Exp Biol Med (Maywood). 2010 Mar;235(3):278-89. doi: 10.1258/ebm.2009.009250. Review.

9.

Post-translational modifications of Hsp90 and their contributions to chaperone regulation.

Mollapour M, Neckers L.

Biochim Biophys Acta. 2012 Mar;1823(3):648-55. doi: 10.1016/j.bbamcr.2011.07.018. Review.

10.

Heat Shock Protein 90 Inhibition in Cancer Drug Discovery: From Chemistry to Futural Clinical Applications.

Özgür A, Tutar Y.

Anticancer Agents Med Chem. 2016;16(3):280-90. Review.

PMID:
26295332
11.

Function of cytosolic chaperones in Tom70-mediated mitochondrial import.

Fan AC, Young JC.

Protein Pept Lett. 2011 Feb;18(2):122-31. Review.

12.

Conformational dynamics of the molecular chaperone Hsp90.

Krukenberg KA, Street TO, Lavery LA, Agard DA.

Q Rev Biophys. 2011 May;44(2):229-55. doi: 10.1017/S0033583510000314. Review.

13.

Molecular interaction network of the Hsp90 chaperone system.

Zhao R, Houry WA.

Adv Exp Med Biol. 2007;594:27-36. Review.

PMID:
17205672
14.

Targeting Hsp90 and its co-chaperones to treat Alzheimer's disease.

Blair LJ, Sabbagh JJ, Dickey CA.

Expert Opin Ther Targets. 2014 Oct;18(10):1219-32. doi: 10.1517/14728222.2014.943185. Review.

15.

The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts.

Pratt WB, Morishima Y, Osawa Y.

J Biol Chem. 2008 Aug 22;283(34):22885-9. doi: 10.1074/jbc.R800023200. Review. No abstract available.

16.

HSP90 manages the ends.

DeZwaan DC, Freeman BC.

Trends Biochem Sci. 2010 Jul;35(7):384-91. doi: 10.1016/j.tibs.2010.02.005. Review.

17.

Tetratricopeptide repeat cochaperones in steroid receptor complexes.

Smith DF.

Cell Stress Chaperones. 2004 Summer;9(2):109-21. Review.

18.

TRAP-1, the mitochondrial Hsp90.

Altieri DC, Stein GS, Lian JB, Languino LR.

Biochim Biophys Acta. 2012 Mar;1823(3):767-73. doi: 10.1016/j.bbamcr.2011.08.007. Review.

19.

Sculpting the proteome with AAA(+) proteases and disassembly machines.

Sauer RT, Bolon DN, Burton BM, Burton RE, Flynn JM, Grant RA, Hersch GL, Joshi SA, Kenniston JA, Levchenko I, Neher SB, Oakes ES, Siddiqui SM, Wah DA, Baker TA.

Cell. 2004 Oct 1;119(1):9-18. Review.

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