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Items: 1 to 20 of 304

1.

Analysis of Hsp90 cochaperone interactions reveals a novel mechanism for TPR protein recognition.

Chadli A, Bruinsma ES, Stensgard B, Toft D.

Biochemistry. 2008 Mar 4;47(9):2850-7. doi: 10.1021/bi7023332. Epub 2008 Jan 23.

PMID:
18211007
2.

C-terminal sequences outside the tetratricopeptide repeat domain of FKBP51 and FKBP52 cause differential binding to Hsp90.

Cheung-Flynn J, Roberts PJ, Riggs DL, Smith DF.

J Biol Chem. 2003 May 9;278(19):17388-94. Epub 2003 Feb 27.

3.

Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity.

Odunuga OO, Hornby JA, Bies C, Zimmermann R, Pugh DJ, Blatch GL.

J Biol Chem. 2003 Feb 28;278(9):6896-904. Epub 2002 Dec 13.

4.
5.

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
6.

GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.

Chadli A, Graham JD, Abel MG, Jackson TA, Gordon DF, Wood WM, Felts SJ, Horwitz KB, Toft D.

Mol Cell Biol. 2006 Mar;26(5):1722-30.

7.

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.

8.

Role of the cochaperone Tpr2 in Hsp90 chaperoning.

Moffatt NS, Bruinsma E, Uhl C, Obermann WM, Toft D.

Biochemistry. 2008 Aug 5;47(31):8203-13. doi: 10.1021/bi800770g. Epub 2008 Jul 12.

PMID:
18620420
9.

A structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90.

Ward BK, Allan RK, Mok D, Temple SE, Taylor P, Dornan J, Mark PJ, Shaw DJ, Kumar P, Walkinshaw MD, Ratajczak T.

J Biol Chem. 2002 Oct 25;277(43):40799-809. Epub 2002 Jul 26.

10.

Two structures of cyclophilin 40: folding and fidelity in the TPR domains.

Taylor P, Dornan J, Carrello A, Minchin RF, Ratajczak T, Walkinshaw MD.

Structure. 2001 May 9;9(5):431-8.

11.

Hsp104 interacts with Hsp90 cochaperones in respiring yeast.

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

Mol Cell Biol. 2001 Nov;21(22):7569-75.

12.

A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains.

Owens-Grillo JK, Czar MJ, Hutchison KA, Hoffmann K, Perdew GH, Pratt WB.

J Biol Chem. 1996 Jun 7;271(23):13468-75.

13.

Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90.

Young JC, Obermann WM, Hartl FU.

J Biol Chem. 1998 Jul 17;273(29):18007-10.

14.

Defining the requirements for Hsp40 and Hsp70 in the Hsp90 chaperone pathway.

Cintron NS, Toft D.

J Biol Chem. 2006 Sep 8;281(36):26235-44. Epub 2006 Jul 19.

15.

Crystal structure of a designed tetratricopeptide repeat module in complex with its peptide ligand.

Cortajarena AL, Wang J, Regan L.

FEBS J. 2010 Feb;277(4):1058-66. doi: 10.1111/j.1742-4658.2009.07549.x. Epub 2010 Jan 18.

16.

The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains.

Mok D, Allan RK, Carrello A, Wangoo K, Walkinshaw MD, Ratajczak T.

FEBS Lett. 2006 May 15;580(11):2761-8. Epub 2006 Apr 24.

17.

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.

18.
19.

Overlapping sites of tetratricopeptide repeat protein binding and chaperone activity in heat shock protein 90.

Ramsey AJ, Russell LC, Whitt SR, Chinkers M.

J Biol Chem. 2000 Jun 9;275(23):17857-62.

20.

Chaperone-interacting TPR proteins in Caenorhabditis elegans.

Haslbeck V, Eckl JM, Kaiser CJ, Papsdorf K, Hessling M, Richter K.

J Mol Biol. 2013 Aug 23;425(16):2922-39. doi: 10.1016/j.jmb.2013.05.019. Epub 2013 May 29.

PMID:
23727266

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