Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation - Wikidata - awgldk - TriplyDB

Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation

Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation

http://www.wikidata.org/entity/Q36553586

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Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity Precision medicine in spinocerebellar ataxias: treatment based on common mechanisms of disease The nucleotide exchange factors of Hsp70 molecular chaperones Direct and Propagated Effects of Small Molecules on Protein-Protein Interaction Networks Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle The struggle by Caenorhabditis elegans to maintain proteostasis during aging and disease Engineering enhanced protein disaggregases for neurodegenerative disease A small-molecule Nrf1 and Nrf2 activator mitigates polyglutamine toxicity in spinal and bulbar muscular atrophy Hsp70-Bag3 interactions regulate cancer-related signaling networks HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.Peripheral androgen receptor gene suppression rescues disease in mouse models of spinal and bulbar muscular atrophy.Disrupting SUMOylation enhances transcriptional function and ameliorates polyglutamine androgen receptor-mediated disease.Inhibitors of difficult protein-protein interactions identified by high-throughput screening of multiprotein complexes.The ubiquitin-proteasome system in neurodegenerative diseases: precipitating factor, yet part of the solution Small-molecule inhibitors of protein-protein interactions: progressing toward the reality.Sequestration of cellular interacting partners by protein aggregates: implication in a loss-of-function pathology.Synergic prodegradative activity of Bicalutamide and trehalose on the mutant androgen receptor responsible for spinal and bulbar muscular atrophy.Hsp104 suppresses polyglutamine-induced degeneration post onset in a drosophila MJD/SCA3 model.A model in which heat shock protein 90 targets protein-folding clefts: rationale for a new approach to neuroprotective treatment of protein folding diseases Down-regulation of mortalin exacerbates Aβ-mediated mitochondrial fragmentation and dysfunction.An RNA aptamer specific to Hsp70-ATP conformation inhibits its ATPase activity independent of Hsp40.pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers Alleviating neurodegeneration in Drosophila models of PolyQ diseases.The Chemical Biology of Molecular Chaperones--Implications for Modulation of Proteostasis Targeting protein aggregation for the treatment of degenerative diseases Fluorescence Turn-On Folding Sensor To Monitor Proteome Stress in Live Cells.Chemical Tools to Investigate Mechanisms Associated with HSP90 and HSP70 in Disease.Allosteric heat shock protein 70 inhibitors block hepatitis C virus assembly Mechanisms mediating spinal and bulbar muscular atrophy: investigations into polyglutamine-expanded androgen receptor function and dysfunction.Engineering therapeutic protein disaggregases.Synthesis and initial evaluation of YM-08, a blood-brain barrier permeable derivative of the heat shock protein 70 (Hsp70) inhibitor MKT-077, which reduces tau levels.A current pharmacologic agent versus the promise of next generation therapeutics to ameliorate protein misfolding and/or aggregation diseases.Clearance of the mutant androgen receptor in motoneuronal models of spinal and bulbar muscular atrophy.New hope for therapy in neurodegenerative diseases.The Aqueous Extract of Rhizome of Gastrodia elata Protected Drosophila and PC12 Cells against Beta-Amyloid-Induced Neurotoxicity.Trinucleotide repeats and protein folding and disease: the perspective from studies with the androgen receptor.Transcriptional activation of TFEB/ZKSCAN3 target genes underlies enhanced autophagy in spinobulbar muscular atrophy.The Ubiquitination, Disaggregation and Proteasomal Degradation Machineries in Polyglutamine Disease Association of heat-shock proteins in various neurodegenerative disorders: is it a master key to open the therapeutic door?

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Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation

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Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation

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Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation

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Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation

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Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation

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Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation

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Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation

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Nature Chemical Biology

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Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation

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Adrienne M Wang

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Andrew P Lieberman

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Catherine A Collins

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Diane E Merry

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Hwei-Ming Peng

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Jason E Gestwicki

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Jason P Chua

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Susan Klinedinst

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Tomoko Komiyama

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William B Pratt

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P2860

Ubiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-dependent E3 ligase

Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by Hip

CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation

Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle

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

Novobiocin: redesigning a DNA gyrase inhibitor for selective inhibition of hsp90.

Inhibition of hsp70 by methylene blue affects signaling protein function and ubiquitination and modulates polyglutamine protein degradation

Glutamine repeats and neurodegeneration.

Heat shock protein 70 (hsp70) as an emerging drug target.

Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK)

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112-118

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10.1038/NCHEMBIO.1140

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2

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9

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2012-12-09T00:00:00Z

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233880849

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23222885

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3552084

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