Quality control and fate determination of Hsp90 client proteins - Wikidata - awgldk - TriplyDB

Quality control and fate determination of Hsp90 client proteins

Quality control and fate determination of Hsp90 client proteins

http://www.wikidata.org/entity/Q26853052

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Hsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cells Chaperone machines for protein folding, unfolding and disaggregation A Decade of Boon or Burden: What Has the CHIP Ever Done for Cellular Protein Quality Control Mechanism Implicated in Neurodegeneration and Aging?Distinct roles of molecular chaperones HSP90α and HSP90β in the biogenesis of KCNQ4 channels Hsp90 inhibitors exhibit resistance-free antiviral activity against respiratory syncytial virus A novel pulse-chase SILAC strategy measures changes in protein decay and synthesis rates induced by perturbation of proteostasis with an Hsp90 inhibitor Differential modulation of functional dynamics and allosteric interactions in the Hsp90-cochaperone complexes with p23 and Aha1: a computational study.Identification and characterization of novel ER-based hsp90 gene in the red flour beetle, Tribolium castaneum.Targeting heat-shock-protein 90 (Hsp90) by natural products: geldanamycin, a show case in cancer therapy.LPS-induced delayed preconditioning is mediated by Hsp90 and involves the heat shock response in mouse kidney.High-throughput screen of natural product libraries for hsp90 inhibitors.Molecular chaperone Hsp90 is a therapeutic target for noroviruses Kelch Domain of Gigaxonin Interacts with Intermediate Filament Proteins Affected in Giant Axonal Neuropathy A network of ubiquitin ligases is important for the dynamics of misfolded protein aggregates in yeast.Soluble guanylyl cyclase requires heat shock protein 90 for heme insertion during maturation of the NO-active enzyme.Opposing actions of heat shock protein 90 and 70 regulate nicotinamide adenine dinucleotide phosphate oxidase stability and reactive oxygen species production.HSP90 activity is required for MLKL oligomerisation and membrane translocation and the induction of necroptotic cell death.Specificity in the actions of the UBR1 ubiquitin ligase in the degradation of nuclear receptors.Proteomic analysis of saliva in HIV-positive heroin addicts reveals proteins correlated with cognition.Broad action of Hsp90 as a host chaperone required for viral replication.Targeting the Hsp90 C-terminal domain by the chemically accessible dihydropyrimidinone scaffold.PU-H71 effectively induces degradation of IκB kinase β in the presence of TNF-α.Combined effects of 17-DMAG and TNF on cells through a mechanism related to the NF-kappaB pathway Hsp70 - a master regulator in protein degradation.The first report of direct inhibitors that target the C-terminal MEEVD region on heat shock protein 90.CD24 induces changes to the surface receptors of B cell microvesicles with variable effects on their RNA and protein cargo.The anticancer drug AUY922 generates a proteomics fingerprint that is highly conserved among structurally diverse Hsp90 inhibitors.Effects of 17-DMAG on diffuse large B-cell lymphoma cell apoptosis.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.Fibronectin is a stress responsive gene regulated by HSF1 in response to geldanamycin.The ubiquitin E3 ligase CHIP promotes proteasomal degradation of the serine/threonine protein kinase PINK1 during staurosporine-induced cell death.Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding.Computational Modeling of the Hsp90 Interactions with Cochaperones and Small-Molecule Inhibitors.Inhibition of Heat Shock proteins HSP90 and HSP70 induce oxidative stress, suppressing cotton fiber development.CHIP buffers heterogeneous Bcl-2 expression levels to prevent augmentation of anticancer drug-resistant cell population.The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease

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P2860

Quality control and fate determination of Hsp90 client proteins

http://www.wikidata.org/entity/Q26853052

description

2012 nî lūn-bûn

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2012 թուականի Մարտին հրատարակուած գիտական յօդուած

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2012 թվականի մարտին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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Quality control and fate determination of Hsp90 client proteins

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Quality control and fate determination of Hsp90 client proteins

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Quality control and fate determination of Hsp90 client proteins

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type

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Quality control and fate determination of Hsp90 client proteins

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Quality control and fate determination of Hsp90 client proteins

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Quality control and fate determination of Hsp90 client proteins

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Quality control and fate determination of Hsp90 client proteins

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Quality control and fate determination of Hsp90 client proteins

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Quality control and fate determination of Hsp90 client proteins

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J.BBAMCR.2011.08.006

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Biochimica et Biophysica Acta

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Quality control and fate determination of Hsp90 client proteins

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Avrom J. Caplan

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Maria A. Theodoraki

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P2860

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

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

The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction

Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis

Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome

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

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

The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

Global analysis of protein expression in yeast

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10.1016/J.BBAMCR.2011.08.006

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quality control

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