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Functions of the Hsp90 chaperone system: lifting client proteins to new heights

Functions of the Hsp90 chaperone system: lifting client proteins to new heights

http://www.wikidata.org/entity/Q27024085

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Atypical Rho GTPases of the RhoBTB Subfamily: Roles in Vesicle Trafficking and Tumorigenesis Chaperones in hepatitis C virus infection Legal but lethal: functional protein aggregation at the verge of toxicity The activity of protein phosphatase 5 towards native clients is modulated by the middle- and C-terminal domains of Hsp90 Selective targeting of the stress chaperome as a therapeutic strategy A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.First Structural View of a Peptide Interacting with the Nucleotide Binding Domain of Heat Shock Protein 90 Quercetin-Induced Cell Death in Human Papillary Thyroid Cancer (B-CPAP) Cells.Regulation of the Tumor-Suppressor Function of the Class III Phosphatidylinositol 3-Kinase Complex by Ubiquitin and SUMO The Mechanism of Hsp90 ATPase Stimulation by Aha1 Hop/Sti1 phosphorylation inhibits its co-chaperone function.Regulation of the Tumor-Suppressor BECLIN 1 by Distinct Ubiquitination Cascades.Cooperative Nucleotide Binding in Hsp90 and Its Regulation by Aha1.Hsp90β knockdown in DIO mice reverses insulin resistance and improves glucose tolerance.The Molecular Chaperone HSP90 Promotes Notch Signaling in the Germline of Caenorhabditis elegans.Hsp83/Hsp90 Physically Associates with Insulin Receptor to Promote Neural Stem Cell Reactivation

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Functions of the Hsp90 chaperone system: lifting client proteins to new heights

http://www.wikidata.org/entity/Q27024085

description

2013 nî lūn-bûn

@nan

2013 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2013年の論文

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2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Functions of the Hsp90 chaperone system: lifting client proteins to new heights

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Functions of the Hsp90 chaperone system: lifting client proteins to new heights

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Functions of the Hsp90 chaperone system: lifting client proteins to new heights

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type

label

Functions of the Hsp90 chaperone system: lifting client proteins to new heights

@ast

Functions of the Hsp90 chaperone system: lifting client proteins to new heights

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Functions of the Hsp90 chaperone system: lifting client proteins to new heights

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prefLabel

Functions of the Hsp90 chaperone system: lifting client proteins to new heights

@ast

Functions of the Hsp90 chaperone system: lifting client proteins to new heights

@en

Functions of the Hsp90 chaperone system: lifting client proteins to new heights

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Functions of the Hsp90 chaperone system: lifting client proteins to new heights

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Eckl JM

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Richter K

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The Hallmarks of Cancer

Hsp90 regulates p50(cdc37) function during the biogenesis of the activeconformation of the heme-regulated eIF2 alpha kinase

Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition

Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function

A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein

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

Modulation of Akt kinase activity by binding to Hsp90

Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition

Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation

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

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157-65

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813870

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4

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4

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2013-12-15T00:00:00Z

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24380020

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molecular chaperones

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3867702

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