Format
Sort by
Items per page

Send to

Choose Destination

Links from PubMed

Items: 1 to 20 of 25

1.

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. Epub 2011 Mar 18. Review.

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. Epub 2011 Aug 4. Review.

3.

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.

4.

Structure, function and regulation of the hsp90 machinery.

Li J, Buchner J.

Biomed J. 2013 May-Jun;36(3):106-17. doi: 10.4103/2319-4170.113230. Review.

5.

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
6.

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.

7.

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.

8.

The HSP90 complex of plants.

Kadota Y, Shirasu K.

Biochim Biophys Acta. 2012 Mar;1823(3):689-97. doi: 10.1016/j.bbamcr.2011.09.016. Epub 2011 Oct 6. Review.

9.

The Hsp90 chaperone machinery: from structure to drug development.

Hahn JS.

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

10.

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.

11.

Hsp90: structure and function.

Jackson SE.

Top Curr Chem. 2013;328:155-240. doi: 10.1007/128_2012_356. Review.

PMID:
22955504
12.

Hsp90: Friends, clients and natural foes.

Verma S, Goyal S, Jamal S, Singh A, Grover A.

Biochimie. 2016 Aug;127:227-40. doi: 10.1016/j.biochi.2016.05.018. Epub 2016 Jun 11. Review.

PMID:
27295069
13.

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
14.

Review: The HSP90 molecular chaperone-an enigmatic ATPase.

Pearl LH.

Biopolymers. 2016 Aug;105(8):594-607. doi: 10.1002/bip.22835. Review.

15.

Structure and mechanism of the Hsp90 molecular chaperone machinery.

Pearl LH, Prodromou C.

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

PMID:
16756493
16.

Hsp90's secrets unfold: new insights from structural and functional studies.

Caplan AJ.

Trends Cell Biol. 1999 Jul;9(7):262-8. Review.

PMID:
10370241
17.

The HSP90 chaperone machinery.

Schopf FH, Biebl MM, Buchner J.

Nat Rev Mol Cell Biol. 2017 Jun;18(6):345-360. doi: 10.1038/nrm.2017.20. Epub 2017 Apr 21. Review.

PMID:
28429788
18.

Hsp90: breaking the symmetry.

Mayer MP, Le Breton L.

Mol Cell. 2015 Apr 2;58(1):8-20. doi: 10.1016/j.molcel.2015.02.022. Review.

19.

Impact of Posttranslational Modifications on the Anticancer Activity of Hsp90 Inhibitors.

Woodford MR, Dunn D, Miller JB, Jamal S, Neckers L, Mollapour M.

Adv Cancer Res. 2016;129:31-50. doi: 10.1016/bs.acr.2015.09.002. Epub 2015 Oct 23. Review.

PMID:
26916000
20.

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. Epub 2015 Apr 3. Review.

Supplemental Content

Support Center