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Items: 1 to 20 of 286


Dynamics of the regulation of Hsp90 by the co-chaperone Sti1.

Lee CT, Graf C, Mayer FJ, Richter SM, Mayer MP.

EMBO J. 2012 Mar 21;31(6):1518-28. doi: 10.1038/emboj.2012.37. Epub 2012 Feb 21.


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.


The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop.

Schmid AB, Lagleder S, Gräwert MA, Röhl A, Hagn F, Wandinger SK, Cox MB, Demmer O, Richter K, Groll M, Kessler H, Buchner J.

EMBO J. 2012 Mar 21;31(6):1506-17. doi: 10.1038/emboj.2011.472. Epub 2012 Jan 6.


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.


The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle.

Richter K, Walter S, Buchner J.

J Mol Biol. 2004 Oct 1;342(5):1403-13.


Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle.

Richter K, Muschler P, Hainzl O, Reinstein J, Buchner J.

J Biol Chem. 2003 Mar 21;278(12):10328-33. Epub 2003 Jan 13.


Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules.

Röhl A, Wengler D, Madl T, Lagleder S, Tippel F, Herrmann M, Hendrix J, Richter K, Hack G, Schmid AB, Kessler H, Lamb DC, Buchner J.

Nat Commun. 2015 Apr 8;6:6655. doi: 10.1038/ncomms7655.


N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.

Richter K, Reinstein J, Buchner J.

J Biol Chem. 2002 Nov 22;277(47):44905-10. Epub 2002 Sep 13.


Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.

Siligardi G, Panaretou B, Meyer P, Singh S, Woolfson DN, Piper PW, Pearl LH, Prodromou C.

J Biol Chem. 2002 Jun 7;277(23):20151-9. Epub 2002 Mar 26.


Cns1 is an activator of the Ssa1 ATPase activity.

Hainzl O, Wegele H, Richter K, Buchner J.

J Biol Chem. 2004 May 28;279(22):23267-73. Epub 2004 Mar 25.


Hop/Sti1 phosphorylation inhibits its co-chaperone function.

Röhl A, Tippel F, Bender E, Schmid AB, Richter K, Madl T, Buchner J.

EMBO Rep. 2015 Feb;16(2):240-9. doi: 10.15252/embr.201439198. Epub 2014 Dec 12.


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.


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.


Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites.

Eckl JM, Rutz DA, Haslbeck V, Zierer BK, Reinstein J, Richter K.

J Biol Chem. 2013 May 31;288(22):16032-42. doi: 10.1074/jbc.M112.439257. Epub 2013 Apr 8.


Sti1 is a novel activator of the Ssa proteins.

Wegele H, Haslbeck M, Reinstein J, Buchner J.

J Biol Chem. 2003 Jul 11;278(28):25970-6. Epub 2003 Apr 25.


Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90.

Wegele H, Muschler P, Bunck M, Reinstein J, Buchner J.

J Biol Chem. 2003 Oct 10;278(41):39303-10. Epub 2003 Jul 30.


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.


Stimulation of the weak ATPase activity of human hsp90 by a client protein.

McLaughlin SH, Smith HW, Jackson SE.

J Mol Biol. 2002 Jan 25;315(4):787-98.


Substrate transfer from the chaperone Hsp70 to Hsp90.

Wegele H, Wandinger SK, Schmid AB, Reinstein J, Buchner J.

J Mol Biol. 2006 Feb 24;356(3):802-11. Epub 2005 Dec 20.


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