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REF 1 |
A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways. Cell. 2014 Jul 17;158(2):434-448.
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REF 2 |
USP49 negatively regulates tumorigenesis and chemoresistance through FKBP51-AKT signaling. EMBO J. 2017 May 15;36(10):1434-1446.
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REF 3 |
Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor. Mol Cell Biol. 1997 Feb;17(2):594-603.
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REF 4 |
A high-throughput approach for measuring temporal changes in the interactome. Nat Methods. 2012 Sep;9(9):907-9.
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REF 5 |
Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle. Nat Struct Mol Biol. 2011 Jan;18(1):61-6.
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REF 6 |
Quantitative assessment of complex formation of nuclear-receptor accessory proteins. Biochem J. 2000 Feb 1;345 Pt 3:627-36.
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REF 7 |
Designed hybrid TPR peptide targeting Hsp90 as a novel anticancer agent. J Transl Med. 2011 Jan 14;9:8.
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REF 8 |
Purinergic receptor-mediated rapid depletion of nuclear phosphorylated Akt depends on pleckstrin homology domain leucine-rich repeat phosphatase, calcineurin, protein phosphatase 2A, and PTEN phosphatases. J Biol Chem. 2010 Sep 3;285(36):27900-10.
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Systematic Proteomic Identification of the Heat Shock Proteins (Hsp) that Interact with Estrogen Receptor Alpha (ER) and Biochemical Characterization of the ER-Hsp70 Interaction. PLoS One. 2016 Aug 2;11(8):e0160312.
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A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor. Cell Stress Chaperones. 1996 Dec;1(4):237-50.
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