Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones - Test2 - elhamkhani - TriplyDB

Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones

Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones

http://www.wikidata.org/entity/Q34352138

about

Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity Targeting heat shock proteins to modulate α-synuclein toxicity Molecular chaperones and co-chaperones in Parkinson disease Legal but lethal: functional protein aggregation at the verge of toxicity Synergism between a foldase and an unfoldase: reciprocal dependence between the thioredoxin-like activity of DnaJ and the polypeptide-unfolding activity of DnaK.Molecular chaperones and protein folding as therapeutic targets in Parkinson's disease and other synucleinopathies Structure of CbpA J-domain bound to the regulatory protein Cbpm explains its specificity and suggests evolutionary link between Cbpm and transcriptional regulators.Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.The stress of protein misfolding: from single cells to multicellular organisms The novel hydroxylamine derivative NG-094 suppresses polyglutamine protein toxicity in Caenorhabditis elegans.Natural genetic variation determines susceptibility to aggregation or toxicity in a C. elegans model for polyglutamine disease.Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperones Molecular chaperones in Parkinson's disease--present and future Quantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPs Enhanced J-protein interaction and compromised protein stability of mtHsp70 variants lead to mitochondrial dysfunction in Parkinson's disease α-Synuclein oligomers and clinical implications for Parkinson disease.Structural and functional properties of prefibrillar α-synuclein oligomers GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATP Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates.AFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species.Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation.Physical interaction between bacterial heat shock protein (Hsp) 90 and Hsp70 chaperones mediates their cooperative action to refold denatured proteins Molecular chaperones and associated cellular clearance mechanisms against toxic protein conformers in Parkinson's disease.Drug targets from genetics: α-synuclein.The elusive middle domain of Hsp104 and ClpB: location and function.Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides.α-Synuclein and Parkinsonism: Updates and Future Perspectives.Expanding role of molecular chaperones in regulating α-synuclein misfolding; implications in Parkinson's disease.Designer protein disaggregases to counter neurodegenerative disease.Reactivation of protein aggregates by mortalin and Tid1--the human mitochondrial Hsp70 chaperone system.Purification of hsp104, a protein disaggregase.Animal models of α-synucleinopathy for Parkinson disease drug development.Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate.Alpha-synuclein, proteotoxicity and Parkinson's disease: Search for neuroprotective therapy.

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P2860

Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones

http://www.wikidata.org/entity/Q34352138

description

2010 nî lūn-bûn

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2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2010 թվականի սեպտեմբերին 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

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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

Stable alpha-synuclein oligome ...... ns with J-domain co-chaperones

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Stable alpha-synuclein oligome ...... ns with J-domain co-chaperones

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Stable alpha-synuclein oligome ...... ns with J-domain co-chaperones

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Stable alpha-synuclein oligome ...... ns with J-domain co-chaperones

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Stable alpha-synuclein oligome ...... ns with J-domain co-chaperones

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Stable alpha-synuclein oligome ...... ns with J-domain co-chaperones

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Stable alpha-synuclein oligome ...... ns with J-domain co-chaperones

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Stable alpha-synuclein oligome ...... ns with J-domain co-chaperones

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Stable alpha-synuclein oligome ...... ns with J-domain co-chaperones

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Stable alpha-synuclein oligome ...... ns with J-domain co-chaperones

@en

P2093

America Farina Henriquez Cuendet

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Giovanni Dietler

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Marie-Pierre Hinault

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Mounir Mensi

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Pierre Goloubinoff

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Rayees U H Mattoo

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P2860

Mutation in the alpha-synuclein gene identified in families with Parkinson's disease

Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.

Adapting proteostasis for disease intervention

Principles that govern the folding of protein chains

Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.

Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons

Heat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar species

The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia

Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease

Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy

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10.1074/JBC.M110.127753

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49

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285

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20847048

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molecular chaperones

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2992251

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