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What we know about ST13, a co-factor of heat shock protein, or a tumor suppressor?

Shi ZZ, Zhang JW, Zheng S.

J Zhejiang Univ Sci B. 2007 Mar;8(3):170-6. Review.


hsp70 interacting protein Hip does not affect glucocorticoid receptor folding by the hsp90-based chaperone machinery except to oppose the effect of BAG-1.

Kanelakis KC, Murphy PJ, Galigniana MD, Morishima Y, Takayama S, Reed JC, Toft DO, Pratt WB.

Biochemistry. 2000 Nov 21;39(46):14314-21.


Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by Hip.

Roodveldt C, Bertoncini CW, Andersson A, van der Goot AT, Hsu ST, Fernández-Montesinos R, de Jong J, van Ham TJ, Nollen EA, Pozo D, Christodoulou J, Dobson CM.

EMBO J. 2009 Dec 2;28(23):3758-70. doi: 10.1038/emboj.2009.298. Epub 2009 Oct 29.


Modulation of in vivo HSP70 chaperone activity by Hip and Bag-1.

Nollen EA, Kabakov AE, Brunsting JF, Kanon B, Höhfeld J, Kampinga HH.

J Biol Chem. 2001 Feb 16;276(7):4677-82. Epub 2000 Nov 13.


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.


The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system.

Morishima Y, Kanelakis KC, Silverstein AM, Dittmar KD, Estrada L, Pratt WB.

J Biol Chem. 2000 Mar 10;275(10):6894-900.


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.


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.


Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53.

King FW, Wawrzynow A, Höhfeld J, Zylicz M.

EMBO J. 2001 Nov 15;20(22):6297-305.


Bag1 functions in vivo as a negative regulator of Hsp70 chaperone activity.

Nollen EA, Brunsting JF, Song J, Kampinga HH, Morimoto RI.

Mol Cell Biol. 2000 Feb;20(3):1083-8.


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.


Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system.

Brychzy A, Rein T, Winklhofer KF, Hartl FU, Young JC, Obermann WM.

EMBO J. 2003 Jul 15;22(14):3613-23.


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.


Overexpression of the cochaperone CHIP enhances Hsp70-dependent folding activity in mammalian cells.

Kampinga HH, Kanon B, Salomons FA, Kabakov AE, Patterson C.

Mol Cell Biol. 2003 Jul;23(14):4948-58.


Hsp70 molecular chaperones are required to support p53 tumor suppressor activity under stress conditions.

Walerych D, Olszewski MB, Gutkowska M, Helwak A, Zylicz M, Zylicz A.

Oncogene. 2009 Dec 3;28(48):4284-94. doi: 10.1038/onc.2009.281. Epub 2009 Sep 14.


Human Fas-associated factor 1 interacts with heat shock protein 70 and negatively regulates chaperone activity.

Kim HJ, Song EJ, Lee YS, Kim E, Lee KJ.

J Biol Chem. 2005 Mar 4;280(9):8125-33. Epub 2004 Dec 13.


Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle.

Li Z, Hartl FU, Bracher A.

Nat Struct Mol Biol. 2013 Aug;20(8):929-35. doi: 10.1038/nsmb.2608. Epub 2013 Jun 30.


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