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The Hsp90 (show HSP90 Proteins) independence of the interaction between p23 and p53 (show TP53 Proteins) DNA-binding domain, together with the competition of p23 versus DNA for p53 (show TP53 Proteins), raises the intriguing possibility that p23, like other small charged proteins, may affect p53 (show TP53 Proteins) in hitherto unknown ways.
dysregulation of GR, MR, FKBP5 (show FKBP5 Proteins), and PTGES3 in autistic spectrum disorder (ASD (show ARSD Proteins)) and suggest a possible role of inflammation in altered GR function in ASD (show ARSD Proteins).
increased p23 expression may allow cells to acquire a more aggressive phenotype, contributing to disease progression
Even if p23 predominantly binds the Hsp90 (show HSP90 Proteins) dimer, p23 is also able to interact with Hsp90 (show HSP90 Proteins) oligomers, shifting the Hsp90 (show HSP90 Proteins) dimer-oligomers equilibrium toward dimer.
FKBP4 (show FKBP4 Proteins), p23, and Aha1 (show AHSA1 Proteins) cooperatively regulate the progression of hAgo2 (show EIF2C2 Proteins) through the chaperone cycle.
p23 recruits PHD2 (show EGLN1 Proteins) to the HSP90 (show HSP90 Proteins) machinery to facilitate HIF-1alpha (show HIF1A Proteins) hydroxylation
The effects of p23 on androgen receptor (AR (show AR Proteins)) activity are at least partly HSP90 (show HSP90 Proteins) independent, a mutant form of p23, unable to bind HSP90 (show HSP90 Proteins), increases AR activity.
p23 co-chaperone protects the aryl hydrocarbon receptor (show AHR Proteins) from degradation
As an anti-apoptotic factor, p23 is able to be a potential target for anti-leukemic therapy.
Patients with severe Alzheimer disease displayed a consistent reduction in brain p23 levels. Cleavage product p19 was not seen in AD brain samples.
Skin differentiation is impaired, and both apoptosis and cell proliferation are augmented in the absence of p23 (show CDK5R1 Proteins); the consequences are a severe thinning of the stratum corneum and reduced numbers of hair follicles. Since the phenotype of p23 (show CDK5R1 Proteins)-null embryos is strikingly similar to that of embryos lacking the glucocorticoid receptor (show NR3C1 Proteins), a paradigmatic Hsp90 (show HSP90 Proteins)-p23 (show CDK5R1 Proteins) client protein, we investigated glucocorticoid signaling.
Results identified two proteins P23 (show CDK5R1 Proteins) and HCLS1 (show HCLS1 Proteins), which were not known as RNA-binding proteins, exhibiting RNA-binding activity.
we report the generation of transgenic mouse lines that overexpress wild-type p23 (show CDK5R1 Proteins) or uncleavable p23 (show CDK5R1 Proteins)
Data support a model in which p23 and GCN5 regulate diverse multistep pathways by controlling the longevity of protein-DNA complexes.
p23 (show CDK5R1 Proteins) co-chaperone protects the aryl hydrocarbon receptor (show AHR Proteins) from degradation
Cleavage product p19 was not seen in brain samples from a mouse model of Alzheimer disease, but p23 and p19 were seen in hypoxic cultured cells experienceing endoplasmic reticulum stress.
In cytosol only one protein called p23 (show CDK5R1 Proteins) hsp90 (show HSP90 Proteins) binds to Bax (show BAX Proteins) but the binding protein does not affect the subcellular localization and pro-apoptotic activity of Bax (show BAX Proteins).
The p23 cochaperone of Hsp90, which plays a major role in glucocorticoid receptor folding and function, associates with influenza virus polymerase.
Overexpression of p23 (show CDK5R1 Proteins) contributes to the development of hydronephrosis through the upregulation of the aryl hydrocarbon receptor (show AHR Proteins) pathway in vivo.
prostaglandin E synthase (show PTGES Proteins) (cPGES/p23) acts as a regulatory factor for expression of a PGE2-inactivating enzyme, 15-PGDH (show HPGD Proteins)
Zebrafish cytosolic (c) PGES (show PTGES Proteins)-1 and COX-1 (show PTGS1 Proteins) were coordinately expressed in the inner ear, the pronephros, and intestine.
Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor- mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes (By similarity).
, cytosolic prostaglandin E synthase
, cytosolic prostaglandin E2 synthase
, progesterone receptor complex p23
, prostaglandin E synthase 3
, telomerase-binding protein p23
, unactive progesterone receptor, 23 kD
, prostaglandin E synthase 3 (cytosolic)
, hsp90 co-chaperone
, p23 cochaperone
, sid 3177
, telomerase binding protein, p23
, prostaglandin-E synthase 3