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Nature Structural Biology  9, 640 - 642 (2002)
doi:10.1038/nsb0902-640

Chaperones and transcriptional regulation by nuclear receptors

Jason C. Young & F. Ulrich Hartl

Jason C. Young and F. Ulrich Hartl are in the Department of Cellular Biochemistry, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18a, D-82152 Martinsried, Germany. uhartl@biochem.mpg.de

Molecular chaperones generally assist in the folding of proteins, and the cytoplasmic chaperone Hsp90, with its cofactors, additionally aids the activation of signaling proteins, including nuclear receptors. New evidence suggests that these chaperones also act to disassemble and down-regulate transcriptionally active nuclear receptor complexes.

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REFERENCE
Heat Shock Response
Nature Encyclopaedia of Life Sciences

REVIEWS
Molecular chaperones and the stress of oncogenesis
Oncogene Reviews (12 Apr 2004)
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RESEARCH
Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system
The EMBO Journal Article (15 Jul 2003)
Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23
The EMBO Journal Article (01 Nov 2000)
The Hsp90-binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo
The EMBO Journal Article (03 Mar 2003)
 See all 15 matches for Research

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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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