Hsp90 and co-chaperones twist the functions of diverse client proteins. - Wikidata - awgldk - TriplyDB

Hsp90 and co-chaperones twist the functions of diverse client proteins.

Hsp90 and co-chaperones twist the functions of diverse client proteins.

http://www.wikidata.org/entity/Q33607477

about

Discovery and validation of small-molecule heat-shock protein 90 inhibitors through multimodality molecular imaging in living subjects Advances in the clinical development of heat shock protein 90 (Hsp90) inhibitors in cancers mTOR: An attractive therapeutic target for osteosarcoma?Distinct roles of molecular chaperones HSP90α and HSP90β in the biogenesis of KCNQ4 channels Approaches for defining the Hsp90-dependent proteome.Affinity-based proteomics reveal cancer-specific networks coordinated by Hsp90 Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis The Hsp90 co-chaperone Sgt1 governs Candida albicans morphogenesis and drug resistance Oxidative Stress Mediates the Antiproliferative Effects of Nelfinavir in Breast Cancer Cells Sgt1 acts via an LKB1/AMPK pathway to establish cortical polarity in larval neuroblasts.Hsp90 in the continuum of breast ductal carcinogenesis: Evaluation in precursors, preinvasive and ductal carcinoma lesions The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases Identification of in vivo HSP90-interacting proteins reveals modularity of HSP90 complexes is dependent on the environment in psychrophilic bacteria.An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans Destabilization of Bcr-Abl/Jak2 Network by a Jak2/Abl Kinase Inhibitor ON044580 Overcomes Drug Resistance in Blast Crisis Chronic Myelogenous Leukemia (CML)Heat shock protein 90 inhibitors in the treatment of cancer: current status and future directions Hsp90 is required for transfer of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol.Thermodynamics of aryl-dihydroxyphenyl-thiadiazole binding to human Hsp90 Heat shock protein 90 in Alzheimer's disease Suberoylanilide hydroxamic acid induces ROS-mediated cleavage of HSP90 in leukemia cells.An increase in integrin-linked kinase non-canonically confers NF-κB-mediated growth advantages to gastric cancer cells by activating ERK1/2.A first in human, safety, pharmacokinetics, and clinical activity phase I study of once weekly administration of the Hsp90 inhibitor ganetespib (STA-9090) in patients with solid malignancies.Heat shock protein 90-mediated inactivation of nuclear factor-κB switches autophagy to apoptosis through becn1 transcriptional inhibition in selenite-induced NB4 cells.Targeting heat-shock-protein 90 (Hsp90) by natural products: geldanamycin, a show case in cancer therapy.17-allyamino-17-demethoxygeldanamycin treatment results in a magnetic resonance spectroscopy-detectable elevation in choline-containing metabolites associated with increased expression of choline transporter SLC44A1 and phospholipase A2 Assessment and reconstruction of novel HSP90 genes: duplications, gains and losses in fungal and animal lineages.Topically applied Hsp90 inhibitor 17AAG inhibits UVR-induced cutaneous squamous cell carcinomas HSP90 functions in the circadian clock through stabilization of the client F-box protein ZEITLUPE.Molecular chaperone Hsp90 is a therapeutic target for noroviruses Expression and purification of Src-family kinases for solution NMR studies.Temperature desynchronizes sugar and organic acid metabolism in ripening grapevine fruits and remodels their transcriptome Correlation between mitochondrial TRAP-1 expression and lymph node metastasis in colorectal cancer Novel role of HAX-1 in ischemic injury protection involvement of heat shock protein 90 Heat shock protein 90 in plants: molecular mechanisms and roles in stress responses.ER stress stimulates production of the key antimicrobial peptide, cathelicidin, by forming a previously unidentified intracellular S1P signaling complex HSP90 inhibition blocks ERBB3 and RET phosphorylation in myxoid/round cell liposarcoma and causes massive cell death in vitro and in vivo.Developmental mechanisms underlying variable, invariant and plastic phenotypes.Clients Place Unique Functional Constraints on Hsp90.Targeting the Hsp90-associated viral oncoproteome in gammaherpesvirus-associated malignancies.Alternate strategies of Hsp90 modulation for the treatment of cancer and other diseases.

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P2860

Hsp90 and co-chaperones twist the functions of diverse client proteins.

http://www.wikidata.org/entity/Q33607477

description

2010 nî lūn-bûn

@nan

2010 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի մարտին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

@zh-hk

2010年論文

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2010年論文

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2010年论文

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name

Hsp90 and co-chaperones twist the functions of diverse client proteins.

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Hsp90 and co-chaperones twist the functions of diverse client proteins.

@en

type

label

Hsp90 and co-chaperones twist the functions of diverse client proteins.

@ast

Hsp90 and co-chaperones twist the functions of diverse client proteins.

@en

prefLabel

Hsp90 and co-chaperones twist the functions of diverse client proteins.

@ast

Hsp90 and co-chaperones twist the functions of diverse client proteins.

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Hsp90 and co-chaperones twist the functions of diverse client proteins.

@en

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Abbey Zuehlke

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Jill L Johnson

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

P2860

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

Role of the cochaperone Tpr2 in Hsp90 chaperoning

OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD

Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis

Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes

GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.

The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor

Chaperone ligand-discrimination by the TPR-domain protein Tah1.

Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone.

Cns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cells

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211-217

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scholarly article

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10.1002/BIP.21292

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3

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93

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2010-03-01T00:00:00Z

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26757733

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19697319

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molecular chaperones

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2810645

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