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The Hsp90 independence of the interaction between p23 and p53 DNA-binding domain, together with the competition of p23 versus DNA for p53, raises the intriguing possibility that p23, like other small charged proteins, may affect p53 in hitherto unknown ways.
dysregulation of GR, MR, FKBP5, and PTGES3 in autistic spectrum disorder (ASD) and suggest a possible role of inflammation in altered GR function in ASD.
increased p23 expression may allow cells to acquire a more aggressive phenotype, contributing to disease progression
Even if p23 predominantly binds the Hsp90 dimer, p23 is also able to interact with Hsp90 oligomers, shifting the Hsp90 dimer-oligomers equilibrium toward dimer.
FKBP4, p23, and Aha1 cooperatively regulate the progression of hAgo2 through the chaperone cycle.
p23 recruits PHD2 to the HSP90 machinery to facilitate HIF-1alpha hydroxylation
The effects of p23 on androgen receptor (AR) activity are at least partly HSP90 independent, a mutant form of p23, unable to bind HSP90, increases AR activity.
p23 co-chaperone protects the aryl hydrocarbon receptor 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.
a small increase in the expression of p23 amplifies ER-binding genome wide and, in combination with ER, elicits an invasive phenotype in breast cancer
In cytosol only one protein called p23 hsp90 binds to Bax but the binding protein does not affect the subcellular localization and pro-apoptotic activity of Bax.
Data show that cytosolic prostaglandin E synthase 2 is found in microglia, neurons, and endothelium of control human middle frontal gyrus and that its levels decrease in pyramidal cells of Alzheimer's disease brains.
The p23 cochaperone of Hsp90, which plays a major role in glucocorticoid receptor folding and function, associates with influenza virus polymerase.
the N-terminal domain of human Hsp90 triggers binding to the cochaperone p23
High levels of Hsp90 cochaperone p23 promote tumor progression in breast cancer by increasing lymph node metastases and drug resistance.
the interaction of the Hsp90-p23 complex with hTERT is critical for regulation of the nuclear localization of telomerase
Data show that the small molecule celastrol inhibits the Hsp90 chaperoning machinery by inactivating the co-chaperone p23, resulting in a more selective destabilization of steroid receptors.
localizes in vivo to genomic response elements in a hormone-dependent manner, disrupting receptor-mediated transcriptional activation in vivo and in vitro
TEP1, hTR, hsp90, p23, and dyskerin remained at high and unchanged levels throughout up- or down regulation of telomerase activity.
Skin differentiation is impaired, and both apoptosis and cell proliferation are augmented in the absence of p23; the consequences are a severe thinning of the stratum corneum and reduced numbers of hair follicles. Since the phenotype of p23-null embryos is strikingly similar to that of embryos lacking the glucocorticoid receptor, a paradigmatic Hsp90-p23 client protein, we investigated glucocorticoid signaling.
Results identified two proteins P23 and HCLS1, 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 or uncleavable p23
Data support a model in which p23 and GCN5 regulate diverse multistep pathways by controlling the longevity of protein-DNA complexes.
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.
Overexpression of p23 contributes to the development of hydronephrosis through the upregulation of the aryl hydrocarbon receptor pathway in vivo.
prostaglandin E synthase (cPGES/p23) acts as a regulatory factor for expression of a PGE2-inactivating enzyme, 15-PGDH
cPGES is required for glucocorticoid receptor function and embryonic growth but not dinoprostone biosynthesis.
Embryos homozygous for cPGES/p23-null had lower body weights than wild-type embryos, and abnormal morphology of skin and lungs.
CPGES1 is not the only prostaglandin synthase present in the bovine endometrium but is the main enzyme associated with increased prostaglandin E production in vitro.
Zebrafish cytosolic (c) PGES-1 and COX-1 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