Hsp90 is an essential regulator of EphA2 receptor stability and signaling: implications for cancer cell migration and metastasis. - Wikidata - awgldk - TriplyDB

Hsp90 is an essential regulator of EphA2 receptor stability and signaling: implications for cancer cell migration and metastasis.

Hsp90 is an essential regulator of EphA2 receptor stability and signaling: implications for cancer cell migration and metastasis.

http://www.wikidata.org/entity/Q35161906

about

Hsp90 cochaperones p23 and FKBP4 physically interact with hAgo2 and activate RNA interference-mediated silencing in mammalian cells Identification of PDCL3 as a novel chaperone protein involved in the generation of functional VEGF receptor 2 Extracellular HSPs: The Complicated Roles of Extracellular HSPs in Immunity Hsp90: A New Player in DNA Repair?A novel extracellular Hsp90 mediated co-receptor function for LRP1 regulates EphA2 dependent glioblastoma cell invasion Hsp90 inhibitors are efficacious against Kaposi Sarcoma by enhancing the degradation of the essential viral gene LANA, of the viral co-receptor EphA2 as well as other client proteins Protein Signatures in Human MDA-MB-231 Breast Cancer Cells Indicating a More Invasive Phenotype Following Knockdown of Human Endometase/Matrilysin-2 by siRNA.Eph receptors and ephrins in cancer: bidirectional signalling and beyond.Quantitative proteomics reveals that Hsp90 inhibition preferentially targets kinases and the DNA damage response.Hsp90 molecular chaperone inhibitors: are we there yet?The receptor tyrosine kinase EphA2 is a direct target gene of hypermethylated in cancer 1 (HIC1).Extracellular Hsp90 and TGFβ regulate adhesion, migration and anchorage independent growth in a paired colon cancer cell line model.Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.The status of intercellular junctions in established lens epithelial cell lines.A novel HSP90 inhibitor with reduced hepatotoxicity synergizes with radiotherapy to induce apoptosis, abrogate clonogenic survival, and improve tumor control in models of colorectal cancer.Enhanced cytotoxic effect of radiation and temozolomide in malignant glioma cells: targeting PI3K-AKT-mTOR signaling, HSP90 and histone deacetylases.Hsp90 as a gatekeeper of tumor angiogenesis: clinical promise and potential pitfalls.Chlamydia-infected cells shed Gp96 to prevent chlamydial re-infection.miR-26b enhances radiosensitivity of hepatocellular carcinoma cells by targeting EphA2 Regulation of Nm23-H1 and cell invasiveness by Kaposi's sarcoma-associated herpesvirus.Siglecs take a TOLL on inflammation: deciphering the Hsp70 riddle.Elevated levels of ribosomal proteins eL36 and eL42 control expression of Hsp90 in rhabdomyosarcoma.Molecular and functional crosstalk between extracellular Hsp90 and ephrin A1 signaling.The Role of Hypoxia in Glioblastoma Invasion.Novel strategy for a bispecific antibody: induction of dual target internalization and degradation.

P2860

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P2860

Hsp90 is an essential regulator of EphA2 receptor stability and signaling: implications for cancer cell migration and metastasis.

http://www.wikidata.org/entity/Q35161906

description

2009 nî lūn-bûn

@nan

2009 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Hsp90 is an essential regulato ...... cell migration and metastasis.

@ast

Hsp90 is an essential regulato ...... cell migration and metastasis.

@en

type

label

Hsp90 is an essential regulato ...... cell migration and metastasis.

@ast

Hsp90 is an essential regulato ...... cell migration and metastasis.

@en

prefLabel

Hsp90 is an essential regulato ...... cell migration and metastasis.

@ast

Hsp90 is an essential regulato ...... cell migration and metastasis.

@en

P1433

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P356

1541-7786.MCR-08-0582

P1433

Molecular Cancer Research

P1476

Hsp90 is an essential regulato ...... cell migration and metastasis.

@en

P2093

Balasubramaniam Annamalai

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

Jennifer S Isaacs

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

Udhayakumar Gopal

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

Xueguang Liu

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

P2860

Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.

Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation

The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

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

Blockade of EphA receptor tyrosine kinase activation inhibits vascular endothelial cell growth factor-induced angiogenesis.

Structural characterization of a mutated, ADCC-enhanced human Fc fragment

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

Cell migration: a physically integrated molecular process

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

P304

1021-1032

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scholarly article

P356

10.1158/1541-7786.MCR-08-0582

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7

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7

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19567782

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3155284

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