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Items: 1 to 20 of 290

1.

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.

2.

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.

3.

The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37).

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

Cell. 2004 Jan 9;116(1):87-98.

4.

Biochemical and structural studies of the interaction of Cdc37 with Hsp90.

Zhang W, Hirshberg M, McLaughlin SH, Lazar GA, Grossmann JG, Nielsen PR, Sobott F, Robinson CV, Jackson SE, Laue ED.

J Mol Biol. 2004 Jul 16;340(4):891-907.

PMID:
15223329
5.

Hsp90 regulates p50(cdc37) function during the biogenesis of the activeconformation of the heme-regulated eIF2 alpha kinase.

Shao J, Grammatikakis N, Scroggins BT, Uma S, Huang W, Chen JJ, Hartson SD, Matts RL.

J Biol Chem. 2001 Jan 5;276(1):206-14.

6.

Hop modulates Hsp70/Hsp90 interactions in protein folding.

Johnson BD, Schumacher RJ, Ross ED, Toft DO.

J Biol Chem. 1998 Feb 6;273(6):3679-86.

7.

The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.

Abbas-Terki T, Briand PA, Donzé O, Picard D.

Biol Chem. 2002 Sep;383(9):1335-42.

PMID:
12437126
8.

p50(cdc37) is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules.

Hartson SD, Irwin AD, Shao J, Scroggins BT, Volk L, Huang W, Matts RL.

Biochemistry. 2000 Jun 27;39(25):7631-44.

PMID:
10858314
9.

Functional specificity of co-chaperone interactions with Hsp90 client proteins.

Riggs DL, Cox MB, Cheung-Flynn J, Prapapanich V, Carrigan PE, Smith DF.

Crit Rev Biochem Mol Biol. 2004 Sep-Dec;39(5-6):279-95. Review.

PMID:
15763706
10.

Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37.

Shao J, Prince T, Hartson SD, Matts RL.

J Biol Chem. 2003 Oct 3;278(40):38117-20. Epub 2003 Aug 20.

11.

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.

12.

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.

PMID:
15364569
13.

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
14.

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
15.

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.

16.

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.

17.

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.

18.

Protein kinase CK2 in health and disease: CK2: the kinase controlling the Hsp90 chaperone machinery.

Miyata Y.

Cell Mol Life Sci. 2009 Jun;66(11-12):1840-9. doi: 10.1007/s00018-009-9152-0. Review.

PMID:
19387550
19.

A client-binding site of Cdc37.

Terasawa K, Minami Y.

FEBS J. 2005 Sep;272(18):4684-90.

20.

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