The oncoprotein kinase chaperone CDC37 functions as an oncogene in mice and collaborates with both c-myc and cyclin D1 in transformation of multiple tissues
about
Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 functionThe role of the ubiquitination-proteasome pathway in breast cancer: use of mouse models for analyzing ubiquitination processesGene expression profile of HIV-1 Tat expressing cells: a close interplay between proliferative and differentiation signalsThe C-terminal domain of human Cdc37 studied by solution NMRCdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturationA mouse homologue of the Drosophila tumor suppressor l(2)tid gene defines a novel Ras GTPase-activating protein (RasGAP)-binding proteinIdentification and characterization of Harc, a novel Hsp90-associating relative of Cdc37Canonical and kinase activity-independent mechanisms for extracellular signal-regulated kinase 5 (ERK5) nuclear translocation require dissociation of Hsp90 from the ERK5-Cdc37 complexSplit Renilla luciferase protein fragment-assisted complementation (SRL-PFAC) to characterize Hsp90-Cdc37 complex and identify critical residues in protein/protein interactions.Small molecule activators of the heat shock response: chemical properties, molecular targets, and therapeutic promise.Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasionStructure of an Hsp90-Cdc37-Cdk4 complex.HSP90 inhibition downregulates thymidylate synthase and sensitizes colorectal cancer cell lines to the effect of 5FU-based chemotherapy.Cell cycle dysregulation in oral cancer.Withaferin A targets heat shock protein 90 in pancreatic cancer cells.Cdc37 goes beyond Hsp90 and kinasesThe oncogenic role of the cochaperone Sgt1Expression of β-catenin and REG Iα in relation to cell proliferative ability in salivary gland tumorsThe Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability.Delta N89 beta-catenin induces precocious development, differentiation, and neoplasia in mammary gland.Silencing the cochaperone CDC37 destabilizes kinase clients and sensitizes cancer cells to HSP90 inhibitorsTargeting the oncogene and kinome chaperone CDC37.Genetic and epigenetic control of molecular alterations in hepatocellular carcinoma.Molecular cochaperones: tumor growth and cancer treatment.Role and Regulation of Myeloid Zinc Finger Protein 1 in Cancer.Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteinsComputational Discovery of Niclosamide Ethanolamine, a Repurposed Drug Candidate That Reduces Growth of Hepatocellular Carcinoma Cells In Vitro and in Mice by Inhibiting Cell Division Cycle 37 Signaling.Mechanisms of Resistance to Hsp90 Inhibitor Drugs: A Complex Mosaic Emerges.Proteome analysis and morphological studies reveal multiple effects of the immunosuppressive drug mycophenolic acid specifically resulting from guanylic nucleotide depletion.Cdc37 is essential for chromosome segregation and cytokinesis in higher eukaryotes.Identification of Cdc37 as a novel regulator of the stress-responsive mitogen-activated protein kinaseAkt shows variable sensitivity to an Hsp90 inhibitor depending on cell context.Interaction of Hsp90 with the nascent form of the mutant epidermal growth factor receptor EGFRvIII.Insulin-like growth factor I triggers nuclear accumulation of cyclin D1 in MCF-7S breast cancer cells.CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37.Suppressing the CDC37 cochaperone in hepatocellular carcinoma cells inhibits cell cycle progression and cell growth.Alteration of the protein kinase binding domain enhances function of the Saccharomyces cerevisiae molecular chaperone Cdc37.Structural bioinformatics and protein docking analysis of the molecular chaperone-kinase interactions: towards allosteric inhibition of protein kinases by targeting the hsp90-cdc37 chaperone machinery.Cellular turnover in the mammary gland is correlated with systemic levels of progesterone and not 17beta-estradiol during the estrous cycle.A positive feedback loop between protein kinase CKII and Cdc37 promotes the activity of multiple protein kinases.
P2860
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P2860
The oncoprotein kinase chaperone CDC37 functions as an oncogene in mice and collaborates with both c-myc and cyclin D1 in transformation of multiple tissues
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
The oncoprotein kinase chapero ...... sformation of multiple tissues
@ast
The oncoprotein kinase chapero ...... sformation of multiple tissues
@en
type
label
The oncoprotein kinase chapero ...... sformation of multiple tissues
@ast
The oncoprotein kinase chapero ...... sformation of multiple tissues
@en
prefLabel
The oncoprotein kinase chapero ...... sformation of multiple tissues
@ast
The oncoprotein kinase chapero ...... sformation of multiple tissues
@en
P2093
P2860
P1476
The oncoprotein kinase chapero ...... sformation of multiple tissues
@en
P2093
E V Schmidt
J W Harper
L Stepanova
M Finegold
P2860
P304
P356
10.1128/MCB.20.12.4462-4473.2000
P407
P577
2000-06-01T00:00:00Z