For immunochemical analysis of FKBP52
Hsp90 is crucial to cellular signaling by its regulation of the folding, activity, and stability of a wide range of client proteins. These client protein complexes may also contain one or more co-
1.Cheung-Flynn, J., Roberts, P.J., Riggs, D.L., et al.C-terminal sequences outside the tetratricopeptide repeat domain of FKBP51 and FKBP52 cause differential binding to Hsp90The Journal of Biological Chemisty278(19)17388-17394(2003) 2.Davies, T.H., Ning, Y.M., and Sánchez, E.R.A new first step in activation of steroid receptors. Hormone-induced switching of FKBP51 and FKBP52 immunophilinsThe Journal of Biological Chemisty277(7)4597-4600(2002) 3.Wu, B., Li, P., Liu, Y., et al.3D structure of human FK506-binding protein 52: Implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin hetrocomplexThe Journal of Biological Chemisty101(22)8348-8353(2004) 4.Denny, W.B., Prapapanich, V., Smith, D.F., et al.Structure-function analysis of squirrel monkey FK506-binding protein 51, a potent inhibitor of glucocorticoid receptor activityEndocrinology146(7)3194-3201(2005) 5.Cox, M.B., Riggs, D.L., Hessling, M., et al.FK506-binding protein 52 phosphorylation: A potential mechanism for regulating steroid hormone receptor activityMol. Endocrinol.21(12)2956-2967(2007)
动态评分
0.0