Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor.
about
Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteinsA subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.The hsp90 chaperone complex regulates intracellular localization of the dioxin receptorThe human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refoldingHsp70-RAP46 interaction in downregulation of DNA binding by glucocorticoid receptorThe cochaperone Bag-1L enhances androgen receptor action via interaction with the NH2-terminal region of the receptorCDC37 is required for p60v-src activity in yeastGlucocorticoid and growth factor synergism requirement for Notch4 chromatin domain activationChaperoning steroidal physiology: lessons from mouse genetic models of Hsp90 and its cochaperonesCns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cellsMutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase.In vivo analysis of the Hsp90 cochaperone Sti1 (p60)Substrate-binding characteristics of proteins in the 90 kDa heat shock protein familyHeat shock protein 90 and the nuclear transport of progesterone receptorHormone binding and co-regulator binding to the glucocorticoid receptor are allosterically coupled.Ribosomes as sensors of heat and cold shock in Escherichia coli.Selective cancer targeting via aberrant behavior of cancer cell-associated glucocorticoid receptor.Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23.Hsp90β inhibition modulates nitric oxide production and nitric oxide-induced apoptosis in human chondrocytesHeat shock proteins: molecular chaperones of protein biogenesis.A role for Hsp90 in retinoid receptor signal transductionThe molecular chaperone Hsp90 can negatively regulate the activity of a glucocorticosteroid-dependent promoter.Geldanamycin, an inhibitor of heat shock protein 90 (Hsp90) mediated signal transduction has anti-inflammatory effects and interacts with glucocorticoid receptor in vivo.A model in which heat shock protein 90 targets protein-folding clefts: rationale for a new approach to neuroprotective treatment of protein folding diseasesEffect of novobiocin on the viability of human gingival fibroblasts (HGF-1).Ubiquitylation of nuclear receptors: new linkages and therapeutic implications.Activation of the unliganded estrogen receptor by EGF involves the MAP kinase pathway and direct phosphorylationPhenobarbital induction of cytochrome P-450 gene expression.Subnuclear trafficking of glucocorticoid receptors in vitro: chromatin recycling and nuclear exportInteraction of glucocorticosteroid receptor and wild-type or mutated 90-kDa heat shock protein coexpressed in baculovirus-infected Sf9 cells.Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70Differential roles of heat shock protein 70 in the in vitro nuclear import of glucocorticoid receptor and simian virus 40 large tumor antigen.Functional evidence for ligand-dependent dissociation of thyroid hormone and retinoic acid receptors from an inhibitory cellular factorHsp90 Inhibition Results in Glucocorticoid Receptor Degradation in Association with Increased Sensitivity to Paclitaxel in Triple-Negative Breast CancerIsolation of Hsp90 mutants by screening for decreased steroid receptor function.Signal transduction by steroid hormones: nuclear localization is differentially regulated in estrogen and glucocorticoid receptors.The Hsp90-Sti1 interaction is critical for Leishmania donovani proliferation in both life cycle stages.A conformational switch in the ligand-binding domain regulates the dependence of the glucocorticoid receptor on Hsp90.Molecular characterization of SMILE as a novel corepressor of nuclear receptorsEffect of geldanamycin on androgen receptor function and stability.
P2860
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P2860
Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年学术文章
@wuu
1989年学术文章
@zh-cn
1989年学术文章
@zh-hans
1989年学术文章
@zh-my
1989年学术文章
@zh-sg
1989年學術文章
@yue
1989年學術文章
@zh
1989年學術文章
@zh-hant
name
Evidence that the 90-kDa heat ...... cell glucocorticoid receptor.
@en
Evidence that the 90-kDa heat ...... cell glucocorticoid receptor.
@nl
type
label
Evidence that the 90-kDa heat ...... cell glucocorticoid receptor.
@en
Evidence that the 90-kDa heat ...... cell glucocorticoid receptor.
@nl
prefLabel
Evidence that the 90-kDa heat ...... cell glucocorticoid receptor.
@en
Evidence that the 90-kDa heat ...... cell glucocorticoid receptor.
@nl
P2093
P1476
Evidence that the 90-kDa heat ...... cell glucocorticoid receptor.
@en
P2093
P304
P407
P577
1989-03-01T00:00:00Z