Alterations of the Hsp70/Hsp90 chaperone and the HOP/CHIP co-chaperone system in cancer. - Wikidata - awgldk - TriplyDB

Alterations of the Hsp70/Hsp90 chaperone and the HOP/CHIP co-chaperone system in cancer.

Alterations of the Hsp70/Hsp90 chaperone and the HOP/CHIP co-chaperone system in cancer.

http://www.wikidata.org/entity/Q43463170

about

Selective targeting of the stress chaperome as a therapeutic strategy Regulation and function of the human HSP90AA1 gene Aurora Kinase A Promotes AR Degradation via the E3 Ligase CHIP.Engagement of cellular prion protein with the co-chaperone Hsp70/90 organizing protein regulates the proliferation of glioblastoma stem-like cells.MiR-1178 promotes the proliferation, G1/S transition, migration and invasion of pancreatic cancer cells by targeting CHIP.Identification of novel putative-binding proteins for cellular prion protein and a specific interaction with the STIP1 homology and U-Box-containing protein 1.Heat Shock Protein (HSP) Drug Discovery and Development: Targeting Heat Shock Proteins in Disease.Cancer stem-like cell related protein CD166 degrades through E3 ubiquitin ligase CHIP in head and neck cancer.Oncogene and non-oncogene addiction in inflammation-associated cancers.The E3 ligase CHIP: insights into its structure and regulation.Computational genomic analysis of PARK7 interactome reveals high BBS1 gene expression as a prognostic factor favoring survival in malignant pleural mesothelioma.Disruption of prion protein-HOP engagement impairs glioblastoma growth and cognitive decline and improves overall survival.VER-155008, a small molecule inhibitor of HSP70 with potent anti-cancer activity on lung cancer cell lines.HOP expression is regulated by p53 and RAS and characteristic of a cancer gene signature.Prion protein binding to HOP modulates the migration and invasion of colorectal cancer cells.Hop/Sti1 phosphorylation inhibits its co-chaperone function.A heat shock protein 90 inhibitor that modulates the immunophilins and regulates hormone receptors without inducing the heat shock response Molecular chaperones in the acquisition of cancer cell chemoresistance with mutated TP53 and MDM2 up-regulation.Andrographolide Induces Cell Cycle Arrest and Apoptosis of Chondrosarcoma by Targeting TCF-1/SOX9 Axis.Identification of novel response and predictive biomarkers to Hsp90 inhibitors through mass spectrometry-based proteomic profiling of patient-derived prostate tumor explants.Intrinsic proteotoxic stress levels vary and act as a predictive marker for sensitivity of cancer cells to Hsp90 inhibition UBXN2A enhances CHIP-mediated proteasomal degradation of oncoprotein mortalin-2 in cancer cells

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P2860

Alterations of the Hsp70/Hsp90 chaperone and the HOP/CHIP co-chaperone system in cancer.

http://www.wikidata.org/entity/Q43463170

description

2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

@zh-cn

2012年学术文章

@zh-hans

2012年学术文章

@zh-my

2012年学术文章

@zh-sg

2012年學術文章

@yue

2012年學術文章

@zh-hant

name

Alterations of the Hsp70/Hsp90 chaperone and the HOP/CHIP co-chaperone system in cancer.

@en

Alterations of the Hsp70/Hsp90 chaperone and the HOP/CHIP co-chaperone system in cancer.

@nl

type

label

Alterations of the Hsp70/Hsp90 chaperone and the HOP/CHIP co-chaperone system in cancer.

@en

Alterations of the Hsp70/Hsp90 chaperone and the HOP/CHIP co-chaperone system in cancer.

@nl

prefLabel

Alterations of the Hsp70/Hsp90 chaperone and the HOP/CHIP co-chaperone system in cancer.

@en

Alterations of the Hsp70/Hsp90 chaperone and the HOP/CHIP co-chaperone system in cancer.

@nl

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S11658-012-0021-8

P1433

Cellular & Molecular Biology Letters

P1476

Alterations of the Hsp70/Hsp90 chaperone and the HOP/CHIP co-chaperone system in cancer

@en

P2093

Borivoj Vojtesek

http://www.w3.org/2001/XMLSchema#string

Eva Ruckova

http://www.w3.org/2001/XMLSchema#string

Rudolf Nenutil

http://www.w3.org/2001/XMLSchema#string

P2860

CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates

Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine

Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1

Targeting the dynamic HSP90 complex in cancer

Proteome analysis of hepatocellular carcinoma by two-dimensional difference gel electrophoresis: novel protein markers in hepatocellular carcinoma tissues.

Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications

The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex.

Balance between folding and degradation for Hsp90-dependent client proteins: a key role for CHIP.

High levels of nuclear heat-shock factor 1 (HSF1) are associated with poor prognosis in breast cancer.

Altered states: selectively drugging the Hsp90 cancer chaperone.

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s11658-012-0021-8

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446-458

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scholarly article

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10.2478/S11658-012-0021-8

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3

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22669480

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molecular chaperones

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6275590

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