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Results: 1 to 20 of 35

References for PMC Articles for PubMed (Select 19554567)

1.

The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis.

Mickler M, Hessling M, Ratzke C, Buchner J, Hugel T.

Nat Struct Mol Biol. 2009 Mar;16(3):281-6. doi: 10.1038/nsmb.1557. Epub 2009 Feb 22.

PMID:
19234469
2.

Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90.

Hessling M, Richter K, Buchner J.

Nat Struct Mol Biol. 2009 Mar;16(3):287-93. doi: 10.1038/nsmb.1565. Epub 2009 Feb 22.

PMID:
19234467
3.

New developments in Hsp90 inhibitors as anti-cancer therapeutics: mechanisms, clinical perspective and more potential.

Li Y, Zhang T, Schwartz SJ, Sun D.

Drug Resist Updat. 2009 Feb-Apr;12(1-2):17-27. doi: 10.1016/j.drup.2008.12.002. Review.

4.

Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine.

Graf C, Stankiewicz M, Kramer G, Mayer MP.

EMBO J. 2009 Mar 4;28(5):602-13. doi: 10.1038/emboj.2008.306. Epub 2009 Jan 22.

5.

Phase II trial of 17-allylamino-17-demethoxygeldanamycin in patients with metastatic melanoma.

Solit DB, Osman I, Polsky D, Panageas KS, Daud A, Goydos JS, Teitcher J, Wolchok JD, Germino FJ, Krown SE, Coit D, Rosen N, Chapman PB.

Clin Cancer Res. 2008 Dec 15;14(24):8302-7. doi: 10.1158/1078-0432.CCR-08-1002.

6.

Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle.

Southworth DR, Agard DA.

Mol Cell. 2008 Dec 5;32(5):631-40. doi: 10.1016/j.molcel.2008.10.024.

7.

Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90.

Cunningham CN, Krukenberg KA, Agard DA.

J Biol Chem. 2008 Jul 25;283(30):21170-8. doi: 10.1074/jbc.M800046200. Epub 2008 May 20.

8.

Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90.

Krukenberg KA, Förster F, Rice LM, Sali A, Agard DA.

Structure. 2008 May;16(5):755-65. doi: 10.1016/j.str.2008.01.021.

9.

Apo-Hsp90 coexists in two open conformational states in solution.

Bron P, Giudice E, Rolland JP, Buey RM, Barbier P, Díaz JF, Peyrot V, Thomas D, Garnier C.

Biol Cell. 2008 Jul;100(7):413-25. doi: 10.1042/BC20070149.

PMID:
18215117
10.

Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones.

Dollins DE, Warren JJ, Immormino RM, Gewirth DT.

Mol Cell. 2007 Oct 12;28(1):41-56.

11.

The ATPase cycle of the endoplasmic chaperone Grp94.

Frey S, Leskovar A, Reinstein J, Buchner J.

J Biol Chem. 2007 Dec 7;282(49):35612-20. Epub 2007 Oct 9.

12.

Hsp90--from signal transduction to cell transformation.

Brown MA, Zhu L, Schmidt C, Tucker PW.

Biochem Biophys Res Commun. 2007 Nov 16;363(2):241-6. Epub 2007 Aug 20. Review.

13.

The peptide-binding activity of GRP94 is regulated by calcium.

Biswas C, Ostrovsky O, Makarewich CA, Wanderling S, Gidalevitz T, Argon Y.

Biochem J. 2007 Jul 15;405(2):233-41.

14.

Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements.

Shiau AK, Harris SF, Southworth DR, Agard DA.

Cell. 2006 Oct 20;127(2):329-40.

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.

Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex.

Ali MM, Roe SM, Vaughan CK, Meyer P, Panaretou B, Piper PW, Prodromou C, Pearl LH.

Nature. 2006 Apr 20;440(7087):1013-7.

PMID:
16625188
17.

Effect of hsp70 chaperone on the folding and misfolding of polypeptides modeling an elongating protein chain.

Kurt N, Rajagopalan S, Cavagnero S.

J Mol Biol. 2006 Jan 27;355(4):809-20. Epub 2005 Nov 8.

18.

Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone.

Zhao R, Davey M, Hsu YC, Kaplanek P, Tong A, Parsons AB, Krogan N, Cagney G, Mai D, Greenblatt J, Boone C, Emili A, Houry WA.

Cell. 2005 Mar 11;120(5):715-27.

19.

Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform.

McLaughlin SH, Ventouras LA, Lobbezoo B, Jackson SE.

J Mol Biol. 2004 Nov 26;344(3):813-26.

PMID:
15533447
20.

Pathways of chaperone-mediated protein folding in the cytosol.

Young JC, Agashe VR, Siegers K, Hartl FU.

Nat Rev Mol Cell Biol. 2004 Oct;5(10):781-91. Review.

PMID:
15459659
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