The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase.
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In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysisHsp90: a specialized but essential protein-folding toolAkt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 functionThe Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKRCochaperone Activity of Human Butyrate-Induced Transcript 1 Facilitates Hepatitis C Virus Replication through an Hsp90-Dependent PathwayNovel complexes of guanylate cyclase with heat shock protein 90 and nitric oxide synthaseCalmodulin binds to K-Ras, but not to H- or N-Ras, and modulates its downstream signalingA comparison of Hsp90alpha and Hsp90beta interactions with cochaperones and substratesp50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding siteGeldanamycin: the prototype of a class of antitumor drugs targeting the heat shock protein 90 family of molecular chaperonesKinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localizationVascular endothelial growth factor (VEGF)-driven actin-based motility is mediated by VEGFR2 and requires concerted activation of stress-activated protein kinase 2 (SAPK2/p38) and geldanamycin-sensitive phosphorylation of focal adhesion kinaseEstradiol-induced phosphorylation of ERK1/2 in explants of the mouse cerebral cortex: the roles of heat shock protein 90 (Hsp90) and MEK2.Opposite effects of the Hsp90 inhibitor Geldanamycin: induction of apoptosis in PC12, and differentiation in N2A cells.H-Ras modulates N-methyl-D-aspartate receptor function via inhibition of Src tyrosine kinase activity.ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo.Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha subunit of eukaryotic translation initiation factor 2 [corrected]Novel strategies and therapeutics for the treatment of prostate carcinoma.Chaperones in cell cycle regulation and mitogenic signal transduction: a review.Hsp90: chaperoning signal transduction.Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone.Hsp90 (heat shock protein 90) inhibitor occupancy is a direct determinant of client protein degradation and tumor growth arrest in vivoFolding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70.Activity of the heat shock protein 90 inhibitor ganetespib in melanomaAnsamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2.Heat shock response and insulin-associated neurodegeneration.Chemical approaches to controlling intracellular protein degradation.Raf kinases: function, regulation and role in human cancer.Hsp90 regulates O-linked β-N-acetylglucosamine transferase: a novel mechanism of modulation of protein O-linked β-N-acetylglucosamine modification in endothelial cells.Role of phosphorylation sites and the C2 domain in regulation of cytosolic phospholipase A2.Heat-shock protein 90 inhibitors in cancer therapy: 17AAG and beyond.The 90-kDa heat shock protein stabilizes the polysomal ribonuclease 1 mRNA endonuclease to degradation by the 26S proteasome.Assays for pharmacodynamic analysis of histone deacetylase inhibitors.MEK-1 activates C-Raf through a Ras-independent mechanism.Hsp90 is required for pheromone signaling in yeast.Mitogen-activated protein kinase kinase 1/2 inhibitors and 17-allylamino-17-demethoxygeldanamycin synergize to kill human gastrointestinal tumor cells in vitro via suppression of c-FLIP-s levels and activation of CD95.Phase II trial of 17-allylamino-17-demethoxygeldanamycin in patients with metastatic melanoma.Stressing Out Hsp90 in Neurotoxic Proteinopathies.Oxidative stress plays a critical role in inactivating mutant BRAF by geldanamycin derivativesSmall-molecule control of intracellular protein levels through modulation of the ubiquitin proteasome system
P2860
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P2860
The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase.
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
The hsp90-binding antibiotic g ...... ymatic activity of Raf kinase.
@en
type
label
The hsp90-binding antibiotic g ...... ymatic activity of Raf kinase.
@en
prefLabel
The hsp90-binding antibiotic g ...... ymatic activity of Raf kinase.
@en
P2093
P356
P1476
The hsp90-binding antibiotic g ...... ymatic activity of Raf kinase.
@en
P2093
Owens-Grillo JK
Silverstein AM
Stancato LF
P304
P356
10.1074/JBC.272.7.4013
P407
P577
1997-02-01T00:00:00Z