Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion - Wikidata - awgldk - TriplyDB

Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion

Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion

http://www.wikidata.org/entity/Q34388870

about

Protein homeostasis at the plasma membrane Contribution of chaperones to STAT pathway signaling.Targeting highly expressed extracellular HSP90 in breast cancer stem cells inhibits tumor growth in vitro and in vivo.Cytosolic Hsp90α and its mitochondrial isoform Trap1 are differentially required in a breast cancer model.Evidence of a Cell Surface Role for Hsp90 Complex Proteins Mediating Neuroblast Migration in the Subventricular Zone.Screening of multiple myeloma by polyclonal rabbit anti-human plasmacytoma cell immunoglobulin.Extracellular molecules involved in cancer cell invasion Patient-derived heavy chain antibody targets cell surface HSP90 on breast tumors.Evolutionarily conserved dual lysine motif determines the non-chaperone function of secreted Hsp90alpha in tumour progression.The significance of heat shock proteins in breast cancer therapy.The double-edged sword: conserved functions of extracellular hsp90 in wound healing and cancer.The Mysterious Ways of ErbB2/HER2 Trafficking Unconventional Secretion of Heat Shock Proteins in Cancer.Reactivation of ERK and Akt confers resistance of mutant BRAF colon cancer cells to the HSP90 inhibitor AUY922

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P2860

Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion

http://www.wikidata.org/entity/Q34388870

description

2012 nî lūn-bûn

@nan

2012 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion

@ast

Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion

@en

Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion

@nl

type

label

Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion

@ast

Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion

@en

Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion

@nl

prefLabel

Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion

@ast

Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion

@en

Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion

@nl

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JOURNAL.PONE.0042722

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Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion

@en

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Avraam El Hamidieh

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

Evangelia Patsavoudi

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

Nicholas Grammatikakis

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

P2860

Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4

p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function

The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)

Cdc37 is a molecular chaperone with specific functions in signal transduction.

Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness

p50(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 site

Extracellular heat shock protein (Hsp)70 and Hsp90α assist in matrix metalloproteinase-2 activation and breast cancer cell migration and invasion

Involvement of cell surface HSP90 in cell migration reveals a novel role in the developing nervous system

HSP90 and the chaperoning of cancer

Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery

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e42722

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scholarly article

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10.1371/JOURNAL.PONE.0042722

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8

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2012-08-17T00:00:00Z

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22912728

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3422348

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