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Items: 1 to 20 of 133

1.

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.

2.

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.

PMID:
18485364
3.

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.

PMID:
11812147
4.

Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery.

Pratt WB, Toft DO.

Exp Biol Med (Maywood). 2003 Feb;228(2):111-33. Review.

PMID:
12563018
5.

The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex.

Hernández MP, Sullivan WP, Toft DO.

J Biol Chem. 2002 Oct 11;277(41):38294-304. Epub 2002 Aug 2.

6.

Importance of the C-terminal domain of Harc for binding to Hsp70 and Hop as well as its response to heat shock.

Cartledge K, Elsegood C, Roiniotis J, Hamilton JA, Scholz GM.

Biochemistry. 2007 Dec 25;46(51):15144-52. Epub 2007 Dec 1.

PMID:
18052042
7.

ATPase activity and ATP-dependent conformational change in the co-chaperone HSP70/HSP90-organizing protein (HOP).

Yamamoto S, Subedi GP, Hanashima S, Satoh T, Otaka M, Wakui H, Sawada K, Yokota S, Yamaguchi Y, Kubota H, Itoh H.

J Biol Chem. 2014 Apr 4;289(14):9880-6. doi: 10.1074/jbc.M114.553255. Epub 2014 Feb 17.

8.

A primate specific extra domain in the molecular chaperone Hsp90.

Tripathi V, Obermann WM.

PLoS One. 2013 Aug 9;8(8):e71856. doi: 10.1371/journal.pone.0071856. eCollection 2013.

9.

Balance between folding and degradation for Hsp90-dependent client proteins: a key role for CHIP.

Kundrat L, Regan L.

Biochemistry. 2010 Sep 7;49(35):7428-38. doi: 10.1021/bi100386w.

10.

Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70.

Carrello A, Allan RK, Morgan SL, Owen BA, Mok D, Ward BK, Minchin RF, Toft DO, Ratajczak T.

Cell Stress Chaperones. 2004 Summer;9(2):167-81.

11.

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions.

Meyer P, Prodromou C, Hu B, Vaughan C, Roe SM, Panaretou B, Piper PW, Pearl LH.

Mol Cell. 2003 Mar;11(3):647-58.

12.

Structure and mechanism of the Hsp90 molecular chaperone machinery.

Pearl LH, Prodromou C.

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

PMID:
16756493
13.

Modeling signal propagation mechanisms and ligand-based conformational dynamics of the Hsp90 molecular chaperone full-length dimer.

Morra G, Verkhivker G, Colombo G.

PLoS Comput Biol. 2009 Mar;5(3):e1000323. doi: 10.1371/journal.pcbi.1000323. Epub 2009 Mar 20.

14.

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.

16.

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.

PMID:
16403523
17.

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.

18.

Structure of an Hsp90-Cdc37-Cdk4 complex.

Vaughan CK, Gohlke U, Sobott F, Good VM, Ali MM, Prodromou C, Robinson CV, Saibil HR, Pearl LH.

Mol Cell. 2006 Sep 1;23(5):697-707.

19.
20.

Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles.

Kirschke E, Goswami D, Southworth D, Griffin PR, Agard DA.

Cell. 2014 Jun 19;157(7):1685-97. doi: 10.1016/j.cell.2014.04.038.

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