The Hsp90-binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo
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Hsp90 cochaperones p23 and FKBP4 physically interact with hAgo2 and activate RNA interference-mediated silencing in mammalian cellsA role for FKBP52 in Tau protein functionXAP2 inhibits glucocorticoid receptor activity in mammalian cellsAdipogenesis is under surveillance of Hsp90 and the high molecular weight Immunophilin FKBP51Steroid Receptor-Associated Immunophilins: A Gateway to Steroid SignallingFKBP51 and FKBP52 in signaling and diseaseChaperoning steroidal physiology: lessons from mouse genetic models of Hsp90 and its cochaperonesStructural and functional analysis of Nro1/Ett1: a protein involved in translation termination in S. cerevisiae and in O2-mediated gene control in S. pombeSmall molecule Plasmodium FKBP35 inhibitor as a potential antimalaria agentCrystal structure and conformational flexibility of the unligated FK506-binding protein FKBP12.6Structure and function of Hip, an attenuator of the Hsp70 chaperone cycleCrystal structure of Plasmodium vivax FK506-binding protein 25 reveals conformational changes responsible for its noncanonical activityTwo crystal structures of the FK506-binding domain of Plasmodium falciparum FKBP35 in complex with rapamycin at high resolutionProteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasisThe aryl hydrocarbon receptor complex and the control of gene expressionFKBP51 reciprocally regulates GRα and PPARγ activation via the Akt-p38 pathwayThe roles of co-chaperone CCRP/DNAJC7 in Cyp2b10 gene activation and steatosis development in mouse liversFKBP51 promotes assembly of the Hsp90 chaperone complex and regulates androgen receptor signaling in prostate cancer cells.FKBP52 deficiency-conferred uterine progesterone resistance is genetic background and pregnancy stage specificPeptidyl-prolyl cis/trans isomerase-independent functional NifH mutant of Azotobacter vinelandii.Noncatalytic role of the FKBP52 peptidyl-prolyl isomerase domain in the regulation of steroid hormone signaling.The helix 1-3 loop in the glucocorticoid receptor LBD is a regulatory element for FKBP cochaperones.Intronic hormone response elements mediate regulation of FKBP5 by progestins and glucocorticoids.A four-hour yeast bioassay for the direct measure of estrogenic activity in wastewater without sample extraction, concentration, or sterilizationTargeting the regulation of androgen receptor signaling by the heat shock protein 90 cochaperone FKBP52 in prostate cancer cells.Susceptibility to diet-induced hepatic steatosis and glucocorticoid resistance in FK506-binding protein 52-deficient mice.Differential impact of tetratricopeptide repeat proteins on the steroid hormone receptorsDose- and time-dependent glucocorticoid receptor signaling in podocytes.NF-κB transcriptional activity is modulated by FK506-binding proteins FKBP51 and FKBP52: a role for peptidyl-prolyl isomerase activity.Independent regulation of Hsp70 and Hsp90 chaperones by Hsp70/Hsp90-organizing protein Sti1 (Hop1).The heat shock protein-90 co-chaperone, Cyclophilin 40, promotes ALK-positive, anaplastic large cell lymphoma viability and its expression is regulated by the NPM-ALK oncoprotein.Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperoneNoncanonical mechanisms to regulate nuclear receptor signaling.3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex.Tetratricopeptide repeat domain 9A negatively regulates estrogen receptor alpha activityThe chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains.FKBP51 and Cyp40 are positive regulators of androgen-dependent prostate cancer cell growth and the targets of FK506 and cyclosporin A.InterAKTions with FKBPs--mutational and pharmacological exploration.Versatile TPR domains accommodate different modes of target protein recognition and functionDealing with misfolded proteins: examining the neuroprotective role of molecular chaperones in neurodegeneration.
P2860
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P2860
The Hsp90-binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh
2003年學術文章
@zh-hant
name
The Hsp90-binding peptidylprol ...... ucocorticoid signaling in vivo
@en
The Hsp90-binding peptidylprol ...... cocorticoid signaling in vivo.
@nl
type
label
The Hsp90-binding peptidylprol ...... ucocorticoid signaling in vivo
@en
The Hsp90-binding peptidylprol ...... cocorticoid signaling in vivo.
@nl
prefLabel
The Hsp90-binding peptidylprol ...... ucocorticoid signaling in vivo
@en
The Hsp90-binding peptidylprol ...... cocorticoid signaling in vivo.
@nl
P2093
P2860
P356
P1433
P1476
The Hsp90-binding peptidylprol ...... ucocorticoid signaling in vivo
@en
P2093
Daniel L Riggs
David F Smith
Didier Picard
Joyce Cheung-Flynn
Patricia J Roberts
Richard Gaber
Samantha C Chirillo
Thomas Ratajczak
Viravan Prapapanich
P2860
P304
P356
10.1093/EMBOJ/CDG108
P407
P577
2003-03-01T00:00:00Z