Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90 - Test2 - elhamkhani - TriplyDB

Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90

Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90

http://www.wikidata.org/entity/Q28143497

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The heat shock protein 90-CDC37 chaperone complex is required for signaling by types I and II interferons Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function Integrin alphavbeta3, requirement for VEGFR2-mediated activation of SAPK2/p38 and for Hsp90-dependent phosphorylation of focal adhesion kinase in endothelial cells activated by VEGF Calreticulin and Hsp90 stabilize the human insulin receptor and promote its mobility in the endoplasmic reticulum Heat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha.Heat shock protein 90: role in enterovirus 71 entry and assembly and potential target for therapy Quercetin-induced ubiquitination and down-regulation of Her-2/neu The role of the ubiquitination-proteasome pathway in breast cancer: ubiquitin mediated degradation of growth factor receptors in the pathogenesis and treatment of cancer Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases Different Poses for Ligand and Chaperone in Inhibitor-Bound Hsp90 and GRP94: Implications for Paralog-Specific Drug Design Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2 Contribution of chaperones to STAT pathway signaling.UDP glucuronosyltransferase 1A expression levels determine the response of colorectal cancer cells to the heat shock protein 90 inhibitor ganetespib.ErbB2 degradation mediated by the co-chaperone protein CHIP Amplification and high-level expression of heat shock protein 90 marks aggressive phenotypes of human epidermal growth factor receptor 2 negative breast cancer Phase I trial of 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), a heat shock protein inhibitor, administered twice weekly in patients with advanced malignancies A phase I study of the heat shock protein 90 inhibitor alvespimycin (17-DMAG) given intravenously to patients with advanced solid tumors Modulation of α(2C) adrenergic receptor temperature-sensitive trafficking by HSP90 Induction of premature senescence by hsp90 inhibition in small cell lung cancer Targeting oncoprotein stability overcomes drug resistance caused by FLT3 kinase domain mutations Heat shock protein 90 stabilization of ErbB2 expression is disrupted by ATP depletion in myocytes Regulation of the Src family kinase Lck by Hsp90 and ubiquitination The C terminus of c-Src inhibits breast tumor cell growth by a kinase-independent mechanism.Heat shock protein 90 inhibition: rationale and clinical potential.Clathrin-independent endocytosis of ErbB2 in geldanamycin-treated human breast cancer cells.Hsp90 inhibition transiently activates Src kinase and promotes Src-dependent Akt and Erk activation.Endocytic down-regulation of ErbB2 is stimulated by cleavage of its C-terminus.Heat shock protein expression in canine malignant mammary tumours.Divergent synthesis of a pochonin library targeting HSP90 and in vivo efficacy of an identified inhibitor Degradation of HER2/neu by ANT2 shRNA suppresses migration and invasiveness of breast cancer cells.Antiviral chemotherapy facilitates control of poxvirus infections through inhibition of cellular signal transduction.FW-04-806 inhibits proliferation and induces apoptosis in human breast cancer cells by binding to N-terminus of Hsp90 and disrupting Hsp90-Cdc37 complex formation.Targeted inhibition of the molecular chaperone Hsp90 overcomes ALK inhibitor resistance in non-small cell lung cancer.Drug-induced ubiquitylation and degradation of ErbB receptor tyrosine kinases: implications for cancer therapy.Hsp90 restrains ErbB-2/HER2 signalling by limiting heterodimer formation.Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu.HILI inhibits TGF-β signaling by interacting with Hsp90 and promoting TβR degradation.Prognostic implications of carboxyl-terminus of Hsc70 interacting protein and lysyl-oxidase expression in human breast cancer.Hsp90 (heat shock protein 90) inhibitor occupancy is a direct determinant of client protein degradation and tumor growth arrest in vivo

P2860

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P2860

Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90

http://www.wikidata.org/entity/Q28143497

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2001 nî lūn-bûn

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2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2001 թվականի փետրվարին հրատարակված գիտական հոդված

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2001年の論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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Sensitivity of mature Erbb2 to ...... by the chaperone protein Hsp90

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Sensitivity of mature Erbb2 to ...... by the chaperone protein Hsp90

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Sensitivity of mature Erbb2 to ...... by the chaperone protein Hsp90

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Sensitivity of mature Erbb2 to ...... by the chaperone protein Hsp90

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Sensitivity of mature Erbb2 to ...... by the chaperone protein Hsp90

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Sensitivity of mature Erbb2 to ...... by the chaperone protein Hsp90

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Sensitivity of mature Erbb2 to ...... by the chaperone protein Hsp90

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Sensitivity of mature Erbb2 to ...... by the chaperone protein Hsp90

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Sensitivity of mature Erbb2 to ...... by the chaperone protein Hsp90

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C Nicchitta

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P2860

Ligand-specific activation of HER4/p180erbB4, a fourth member of the epidermal growth factor receptor family

Isolation and characterization of ERBB3, a third member of the ERBB/epidermal growth factor receptor family: evidence for overexpression in a subset of human mammary tumors

Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.

A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor

Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase

The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation

Hsp90 as a capacitor for morphological evolution

Controlled dimerization of ErbB receptors provides evidence for differential signaling by homo- and heterodimers

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10.1074/JBC.M006864200

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11071886

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molecular chaperones