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The Hsp90 (zeige HSP90 Proteine) independence of the interaction between p23 and p53 (zeige TP53 Proteine) DNA-binding domain, together with the competition of p23 versus DNA for p53 (zeige TP53 Proteine), raises the intriguing possibility that p23, like other small charged proteins, may affect p53 (zeige TP53 Proteine) in hitherto unknown ways.
dysregulation of GR, MR, FKBP5 (zeige FKBP5 Proteine), and PTGES3 in autistic spectrum disorder (ASD (zeige ARSD Proteine)) and suggest a possible role of inflammation in altered GR function in ASD (zeige ARSD Proteine).
increased p23 expression may allow cells to acquire a more aggressive phenotype, contributing to disease progression
Even if p23 predominantly binds the Hsp90 (zeige HSP90 Proteine) dimer, p23 is also able to interact with Hsp90 (zeige HSP90 Proteine) oligomers, shifting the Hsp90 (zeige HSP90 Proteine) dimer-oligomers equilibrium toward dimer.
FKBP4 (zeige FKBP4 Proteine), p23, and Aha1 (zeige AHSA1 Proteine) cooperatively regulate the progression of hAgo2 (zeige EIF2C2 Proteine) through the chaperone cycle.
p23 recruits PHD2 (zeige EGLN1 Proteine) to the HSP90 (zeige HSP90 Proteine) machinery to facilitate HIF-1alpha (zeige HIF1A Proteine) hydroxylation
The effects of p23 on androgen receptor (AR (zeige AR Proteine)) activity are at least partly HSP90 (zeige HSP90 Proteine) independent, a mutant form of p23, unable to bind HSP90 (zeige HSP90 Proteine), increases AR activity.
p23 co-chaperone protects the aryl hydrocarbon receptor (zeige AHR Proteine) 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 (zeige CDK5R1 Proteine); the consequences are a severe thinning of the stratum corneum and reduced numbers of hair follicles. Since the phenotype of p23 (zeige CDK5R1 Proteine)-null embryos is strikingly similar to that of embryos lacking the glucocorticoid receptor (zeige NR3C1 Proteine), a paradigmatic Hsp90 (zeige HSP90 Proteine)-p23 (zeige CDK5R1 Proteine) client protein, we investigated glucocorticoid signaling.
Results identified two proteins P23 (zeige CDK5R1 Proteine) and HCLS1 (zeige HCLS1 Proteine), 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 (zeige CDK5R1 Proteine) or uncleavable p23 (zeige CDK5R1 Proteine)
Data support a model in which p23 and GCN5 regulate diverse multistep pathways by controlling the longevity of protein-DNA complexes.
p23 (zeige CDK5R1 Proteine) co-chaperone protects the aryl hydrocarbon receptor (zeige AHR Proteine) 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 (zeige CDK5R1 Proteine) hsp90 (zeige HSP90 Proteine) binds to Bax (zeige BAX Proteine) but the binding protein does not affect the subcellular localization and pro-apoptotic activity of Bax (zeige BAX Proteine).
The p23 cochaperone of Hsp90, which plays a major role in glucocorticoid receptor folding and function, associates with influenza virus polymerase.
Overexpression of p23 (zeige CDK5R1 Proteine) contributes to the development of hydronephrosis through the upregulation of the aryl hydrocarbon receptor (zeige AHR Proteine) pathway in vivo.
prostaglandin E synthase (zeige PTGES Proteine) (cPGES/p23) acts as a regulatory factor for expression of a PGE2-inactivating enzyme, 15-PGDH (zeige HPGD Proteine)
Zebrafish cytosolic (c) PGES (zeige PTGES Proteine)-1 and COX-1 (zeige PTGS1 Proteine) 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