| References |
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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 |
Architecture of the human interactome defines protein communities and disease networks. Nature. 2017 May 25;545(7655):505-509.
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| REF 3 |
Role of FAP48 in HIV-associated lipodystrophy. J Cell Biochem. 2012 Nov;113(11):3446-54.
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| REF 4 |
S100 proteins regulate the interaction of Hsp90 with Cyclophilin 40 and FKBP52 through their tetratricopeptide repeats. FEBS Lett. 2010 Mar 19;584(6):1119-25.
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| REF 5 |
A high-throughput approach for measuring temporal changes in the interactome. Nat Methods. 2012 Sep;9(9):907-9.
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| REF 6 |
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 7 |
Characterization of the interaction of Aha1 with components of the Hsp90 chaperone machine and client proteins. Biochim Biophys Acta. 2012 Jun;1823(6):1092-101.
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| REF 8 |
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 9 |
Ligand-specific glucocorticoid receptor activation in human platelets. Blood. 2005 Dec 15;106(13):4167-75.
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| REF 10 |
Overexpression, characterization, and purification of a recombinant mouse immunophilin FKBP-52 and identification of an associated phosphoprotein. Proc Natl Acad Sci U S A. 1993 Jul 15;90(14):6839-43.
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| REF 11 |
The FKBP-associated protein FAP48 is an antiproliferative molecule and a player in T cell activation that increases IL2 synthesis. Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2444-9.
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| REF 12 |
Mutation of FKBP associated protein 48 (FAP48) at proline 219 disrupts the interaction with FKBP12 and FKBP52. Regul Pept. 2001 Mar 2;97(2-3):147-52.
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| REF 13 |
Immunophilins, Refsum disease, and lupus nephritis: the peroxisomal enzyme phytanoyl-COA alpha-hydroxylase is a new FKBP-associated protein. Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):2104-9.
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