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Items: 1 to 20 of 261

1.

C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances.

Muller P, Ruckova E, Halada P, Coates PJ, Hrstka R, Lane DP, Vojtesek B.

Oncogene. 2013 Jun 20;32(25):3101-10. doi: 10.1038/onc.2012.314. Epub 2012 Jul 23.

PMID:
22824801
2.

Alterations of the Hsp70/Hsp90 chaperone and the HOP/CHIP co-chaperone system in cancer.

Ruckova E, Muller P, Nenutil R, Vojtesek B.

Cell Mol Biol Lett. 2012 Sep;17(3):446-58. doi: 10.2478/s11658-012-0021-8. Epub 2012 Jun 5.

PMID:
22669480
3.

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.

4.

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.

5.

Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation.

Assimon VA, Southworth DR, Gestwicki JE.

Biochemistry. 2015 Dec 8;54(48):7120-31. doi: 10.1021/acs.biochem.5b00801. Epub 2015 Nov 25.

6.

Domain:domain interactions within Hop, the Hsp70/Hsp90 organizing protein, are required for protein stability and structure.

Carrigan PE, Sikkink LA, Smith DF, Ramirez-Alvarado M.

Protein Sci. 2006 Mar;15(3):522-32. Epub 2006 Feb 1.

7.

Increased expression of co-chaperone HOP with HSP90 and HSC70 and complex formation in human colonic carcinoma.

Kubota H, Yamamoto S, Itoh E, Abe Y, Nakamura A, Izumi Y, Okada H, Iida M, Nanjo H, Itoh H, Yamamoto Y.

Cell Stress Chaperones. 2010 Nov;15(6):1003-11. doi: 10.1007/s12192-010-0211-0. Epub 2010 Jul 9.

8.

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
9.

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.

10.
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.

Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop.

Alvira S, Cuéllar J, Röhl A, Yamamoto S, Itoh H, Alfonso C, Rivas G, Buchner J, Valpuesta JM.

Nat Commun. 2014 Nov 19;5:5484. doi: 10.1038/ncomms6484.

PMID:
25407331
13.
14.

The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins.

Connell P, Ballinger CA, Jiang J, Wu Y, Thompson LJ, Höhfeld J, Patterson C.

Nat Cell Biol. 2001 Jan;3(1):93-6.

PMID:
11146632
15.

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.

16.

Chaperone-mediated hierarchical control in targeting misfolded proteins to aggresomes.

Zhang X, Qian SB.

Mol Biol Cell. 2011 Sep;22(18):3277-88. doi: 10.1091/mbc.E11-05-0388. Epub 2011 Jul 20.

17.

Nox5 stability and superoxide production is regulated by C-terminal binding of Hsp90 and CO-chaperones.

Chen F, Haigh S, Yu Y, Benson T, Wang Y, Li X, Dou H, Bagi Z, Verin AD, Stepp DW, Csanyi G, Chadli A, Weintraub NL, Smith SM, Fulton DJ.

Free Radic Biol Med. 2015 Dec;89:793-805. doi: 10.1016/j.freeradbiomed.2015.09.019. Epub 2015 Oct 9.

18.

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.

19.

Differential effects of the hsp70-binding protein BAG-1 on glucocorticoid receptor folding by the hsp90-based chaperone machinery.

Kanelakis KC, Morishima Y, Dittmar KD, Galigniana MD, Takayama S, Reed JC, Pratt WB.

J Biol Chem. 1999 Nov 26;274(48):34134-40.

20.

Hsp70 and Hsp90 multichaperone complexes sequentially regulate thiazide-sensitive cotransporter endoplasmic reticulum-associated degradation and biogenesis.

Donnelly BF, Needham PG, Snyder AC, Roy A, Khadem S, Brodsky JL, Subramanya AR.

J Biol Chem. 2013 May 3;288(18):13124-35. doi: 10.1074/jbc.M113.455394. Epub 2013 Mar 12.

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