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Items: 1 to 20 of 42


Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex.

Southworth DR, Agard DA.

Mol Cell. 2011 Jun 24;42(6):771-81. doi: 10.1016/j.molcel.2011.04.023.


Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone.

Street TO, Lavery LA, Agard DA.

Mol Cell. 2011 Apr 8;42(1):96-105. doi: 10.1016/j.molcel.2011.01.029.


Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity.

Motojima-Miyazaki Y, Yoshida M, Motojima F.

Biochem Biophys Res Commun. 2010 Sep 17;400(2):241-5. doi: 10.1016/j.bbrc.2010.08.047. Epub 2010 Aug 19.


Charge-rich regions modulate the anti-aggregation activity of Hsp90.

Wayne N, Bolon DN.

J Mol Biol. 2010 Sep 3;401(5):931-9. doi: 10.1016/j.jmb.2010.06.066. Epub 2010 Jul 6.


Asymmetric activation of the hsp90 dimer by its cochaperone aha1.

Retzlaff M, Hagn F, Mitschke L, Hessling M, Gugel F, Kessler H, Richter K, Buchner J.

Mol Cell. 2010 Feb 12;37(3):344-54. doi: 10.1016/j.molcel.2010.01.006.


DANGLE: A Bayesian inferential method for predicting protein backbone dihedral angles and secondary structure.

Cheung MS, Maguire ML, Stevens TJ, Broadhurst RW.

J Magn Reson. 2010 Feb;202(2):223-33. doi: 10.1016/j.jmr.2009.11.008. Epub 2009 Dec 16.


Osmolyte-induced conformational changes in the Hsp90 molecular chaperone.

Street TO, Krukenberg KA, Rosgen J, Bolen DW, Agard DA.

Protein Sci. 2010 Jan;19(1):57-65. doi: 10.1002/pro.282.


Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide.

Krukenberg KA, Böttcher UM, Southworth DR, Agard DA.

Protein Sci. 2009 Sep;18(9):1815-27. doi: 10.1002/pro.191.


pH-dependent conformational changes in bacterial Hsp90 reveal a Grp94-like conformation at pH 6 that is highly active in suppression of citrate synthase aggregation.

Krukenberg KA, Southworth DR, Street TO, Agard DA.

J Mol Biol. 2009 Jul 10;390(2):278-91. doi: 10.1016/j.jmb.2009.04.080. Epub 2009 May 7.


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.


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.


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.


A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s.

Vaughan CK, Piper PW, Pearl LH, Prodromou C.

FEBS J. 2009 Jan;276(1):199-209. doi: 10.1111/j.1742-4658.2008.06773.x. Epub 2008 Nov 20.


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.


Structural studies on the co-chaperone Hop and its complexes with Hsp90.

Onuoha SC, Coulstock ET, Grossmann JG, Jackson SE.

J Mol Biol. 2008 Jun 13;379(4):732-44. doi: 10.1016/j.jmb.2008.02.013. Epub 2008 Feb 14.


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.


Conserved conformational changes in the ATPase cycle of human Hsp90.

Richter K, Soroka J, Skalniak L, Leskovar A, Hessling M, Reinstein J, Buchner J.

J Biol Chem. 2008 Jun 27;283(26):17757-65. doi: 10.1074/jbc.M800540200. Epub 2008 Apr 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.


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.


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.

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