Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus.
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Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 functionThe hsp90 chaperone complex regulates intracellular localization of the dioxin receptorIdentification of the nuclear receptor CAR:HSP90 complex in mouse liver and recruitment of protein phosphatase 2A in response to phenobarbitalNucleotide binding states of hsp70 and hsp90 during sequential steps in the process of glucocorticoid receptor.hsp90 heterocomplex assemblyThe hsp90 Co-chaperone XAP2 alters importin beta recognition of the bipartite nuclear localization signal of the Ah receptor and represses transcriptional activityMutations at positions 547-553 of rat glucocorticoid receptors reveal that hsp90 binding requires the presence, but not defined composition, of a seven-amino acid sequence at the amino terminus of the ligand binding domainNuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin betaGeldanamycin disrupts platelet-membrane structure, leading to membrane permeabilization and inhibition of platelet aggregation.Development and validation of a high-content screening assay to identify inhibitors of cytoplasmic dynein-mediated transport of glucocorticoid receptor to the nucleus.Sequence of the gene encoding hsp90e from Cryptosporidium parvum.Heat-shock factor-1, steroid hormones, and regulation of heat-shock protein expression in the heart.Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha subunit of eukaryotic translation initiation factor 2 [corrected]Characterization of inhibitors of glucocorticoid receptor nuclear translocation: a model of cytoplasmic dynein-mediated cargo transport.Hsp10 and Hsp60 suppress ubiquitination of insulin-like growth factor-1 receptor and augment insulin-like growth factor-1 receptor signaling in cardiac muscle: implications on decreased myocardial protection in diabetic cardiomyopathy.Steroid receptor and molecular chaperone encounters in the nucleus.Unliganded and hormone-bound glucocorticoid receptors interact with distinct hydrophobic sites in the Hsp90 C-terminal domain.Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2.The multifaceted mineralocorticoid receptorHSP60 plays a regulatory role in IL-1β-induced microglial inflammation via TLR4-p38 MAPK axis.Hsp90 is required for pheromone signaling in yeast.Minireview: the intersection of steroid receptors with molecular chaperones: observations and questionsA conformational switch in the ligand-binding domain regulates the dependence of the glucocorticoid receptor on Hsp90.Rapid glucocorticoid receptor exchange at a promoter is coupled to transcription and regulated by chaperones and proteasomesInduction of angiogenesis by heat shock protein 90 mediated by protein kinase Akt and endothelial nitric oxide synthaseHsp90 is essential for the synthesis and subsequent membrane association, but not the maintenance, of the Src-kinase p56(lck).HSP90AB1: Helping the good and the bad.Nuclear transport of Epstein-Barr virus DNA polymerase is dependent on the BMRF1 polymerase processivity factor and molecular chaperone Hsp90The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events.HSP90: a promising broad-spectrum antiviral drug target.Geldanamycin, an inhibitor of Hsp90, blocks cytoplasmic retention of progesterone receptors and glucocorticoid receptors via their respective ligand binding domains.The Hsp90-specific inhibitor geldanamycin selectively disrupts kinase-mediated signaling events of T-lymphocyte activation.Effects of 17-allylamino-17-demethoxygeldanamycin (17-AAG) on pediatric acute lymphoblastic leukemia (ALL) with respect to Bcr-Abl status and imatinib mesylate sensitivity.The role of DnaJ-like proteins in glucocorticoid receptor.hsp90 heterocomplex assembly by the reconstituted hsp90.p60.hsp70 foldosome complex.Herpes simplex virus type 1 DNA polymerase requires the mammalian chaperone hsp90 for proper localization to the nucleus.Inhibition of glucocorticoid receptor nucleocytoplasmic shuttling by okadaic acid requires intact cytoskeleton.Aldosterone resistance in kidney transplantation is in part induced by a down-regulation of mineralocorticoid receptor expression.Luminal flow induces eNOS activation and translocation in the rat thick ascending limb. II. Role of PI3-kinase and Hsp90.A conserved proline in the hsp90 binding region of the glucocorticoid receptor is required for hsp90 heterocomplex stabilization and receptor signaling.Aldosterone Blocks Rat Stem Leydig Cell Development In Vitro.
P2860
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P2860
Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Geldanamycin, a heat shock pro ...... the cytoplasm to the nucleus.
@en
type
label
Geldanamycin, a heat shock pro ...... the cytoplasm to the nucleus.
@en
prefLabel
Geldanamycin, a heat shock pro ...... the cytoplasm to the nucleus.
@en
P2093
P356
P1433
P1476
Geldanamycin, a heat shock pro ...... the cytoplasm to the nucleus.
@en
P2093
Galigniana MD
Silverstein AM
P304
P356
10.1021/BI970648X
P407
P577
1997-06-01T00:00:00Z