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Items: 1 to 20 of 77

1.

Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle.

Siligardi G, Hu B, Panaretou B, Piper PW, Pearl LH, Prodromou C.

J Biol Chem. 2004 Dec 10;279(50):51989-98. Epub 2004 Oct 2.

2.

Structure and functional relationships of Hsp90.

Prodromou C, Pearl LH.

Curr Cancer Drug Targets. 2003 Oct;3(5):301-23. Review.

PMID:
14529383
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.

Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation.

Vickery LE, Cupp-Vickery JR.

Crit Rev Biochem Mol Biol. 2007 Mar-Apr;42(2):95-111. Review.

PMID:
17453917
5.

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. Epub 2011 Aug 4. Review.

6.

Hsp90: chaperoning signal transduction.

Richter K, Buchner J.

J Cell Physiol. 2001 Sep;188(3):281-90. Review.

PMID:
11473354
7.

The Hsp90 molecular chaperone: an open and shut case for treatment.

Pearl LH, Prodromou C, Workman P.

Biochem J. 2008 Mar 15;410(3):439-53. doi: 10.1042/BJ20071640. Review.

PMID:
18290764
8.

Evolutionary epitopes of Hsp90 and p23: implications for their interaction.

Zhu S, Tytgat J.

FASEB J. 2004 Jun;18(9):940-7. Review.

PMID:
15173105
9.

Molecular chaperones: physical and mechanistic properties.

Burston SG, Clarke AR.

Essays Biochem. 1995;29:125-36. Review.

PMID:
9189717
10.

Cdc37 regulation of the kinome: when to hold 'em and when to fold 'em.

Karnitz LM, Felts SJ.

Sci STKE. 2007 May 8;2007(385):pe22. Review.

PMID:
17488976
11.

Functional specificity of co-chaperone interactions with Hsp90 client proteins.

Riggs DL, Cox MB, Cheung-Flynn J, Prapapanich V, Carrigan PE, Smith DF.

Crit Rev Biochem Mol Biol. 2004 Sep-Dec;39(5-6):279-95. Review.

PMID:
15763706
12.

The Hsp90 chaperone machinery: from structure to drug development.

Hahn JS.

BMB Rep. 2009 Oct 31;42(10):623-30. Review.

13.

Heat-shock protein 90, a chaperone for folding and regulation.

Picard D.

Cell Mol Life Sci. 2002 Oct;59(10):1640-8. Review.

PMID:
12475174
14.

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. Epub 2011 Sep 16. Review.

15.

Constantly updated knowledge of Hsp90.

Terasawa K, Minami M, Minami Y.

J Biochem. 2005 Apr;137(4):443-7. Review.

PMID:
15858167
16.

A Grp on the Hsp90 mechanism.

Richter K, Reinstein J, Buchner J.

Mol Cell. 2007 Oct 26;28(2):177-9. Review.

17.

The chaperone Hsp90: changing partners for demanding clients.

Röhl A, Rohrberg J, Buchner J.

Trends Biochem Sci. 2013 May;38(5):253-62. doi: 10.1016/j.tibs.2013.02.003. Epub 2013 Mar 16. Review.

PMID:
23507089
18.

Hsp70 and Hsp90--a relay team for protein folding.

Wegele H, Müller L, Buchner J.

Rev Physiol Biochem Pharmacol. 2004;151:1-44. Epub 2004 Jan 23. Review.

PMID:
14740253
19.

Hsp90 structure and function studied by NMR spectroscopy.

Didenko T, Duarte AM, Karagöz GE, Rüdiger SG.

Biochim Biophys Acta. 2012 Mar;1823(3):636-47. doi: 10.1016/j.bbamcr.2011.11.009. Epub 2011 Dec 6. Review.

20.

ATPase switches controlling DNA replication initiation.

Lee DG, Bell SP.

Curr Opin Cell Biol. 2000 Jun;12(3):280-5. Review.

PMID:
10801458

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