Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity
about
Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independentlyChaperone-like activity of high-mobility group box 1 protein and its role in reducing the formation of polyglutamine aggregatesThe diverse members of the mammalian HSP70 machine show distinct chaperone-like activitiesExome sequencing reveals a homozygous SYT14 mutation in adult-onset, autosomal-recessive spinocerebellar ataxia with psychomotor retardationTherapeutic potential of mood stabilizers lithium and valproic acid: beyond bipolar disorderHuman single-chain Fv intrabodies counteract in situ huntingtin aggregation in cellular models of Huntington's diseaseCytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregatesPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseasesMammalian, yeast, bacterial, and chemical chaperones reduce aggregate formation and death in a cell model of oculopharyngeal muscular dystrophyA chaperome subnetwork safeguards proteostasis in aging and neurodegenerative diseasePaeoniflorin, a novel heat shock protein-inducing compound.Huntington's diseaseDysregulation of C/EBPalpha by mutant Huntingtin causes the urea cycle deficiency in Huntington's diseaseRevisiting and revising the purinosomeHSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.Heat shock proteins: cellular and molecular mechanisms in the central nervous system.Elongation kinetics of polyglutamine peptide fibrils: a quartz crystal microbalance with dissipation study.Altered chromatin architecture underlies progressive impairment of the heat shock response in mouse models of Huntington disease.Mouse models of Huntington's disease and methodological considerations for therapeutic trials.Alterations in the mouse and human proteome caused by Huntington's disease.SGNP: an essential Stress Granule/Nucleolar Protein potentially involved in 5.8s rRNA processing/transport.Hsp40 couples with the CSPalpha chaperone complex upon induction of the heat shock response.Complexity and heterogeneity: what drives the ever-changing brain in Huntington's disease?Prevention of UVB radiation-induced epidermal damage by expression of heat shock protein 70.The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative DiseasesThe chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions.Hsp70 interacts with the retroviral restriction factor TRIM5alpha and assists the folding of TRIM5alphaDose-dependent neuroprotection of VEGF₁₆₅ in Huntington's disease striatumTherapeutic Strategies in Huntington's DiseaseHeat shock protein 70 (hsp70) as an emerging drug target.Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool.Interaction of intracellular beta amyloid peptide with chaperone proteins.Hsp70 and its molecular role in nervous system diseasesThe selective vulnerability of nerve cells in Huntington's disease.Preclinical and clinical investigations of mood stabilizers for Huntington's disease: what have we learned?Hsp70 and Hsp40 functionally interact with soluble mutant huntingtin oligomers in a classic ATP-dependent reaction cycleProtein aggregation can inhibit clathrin-mediated endocytosis by chaperone competition.Heteromeric complexes of heat shock protein 70 (HSP70) family members, including Hsp70B', in differentiated human neuronal cells.Molecular chaperone dysfunction in neurodegenerative diseases and effects of curcumin.
P2860
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P2860
Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity
description
2000 nî lūn-bûn
@nan
2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Polyglutamine length-dependent ...... regation and cellular toxicity
@ast
Polyglutamine length-dependent ...... regation and cellular toxicity
@en
Polyglutamine length-dependent ...... regation and cellular toxicity
@nl
type
label
Polyglutamine length-dependent ...... regation and cellular toxicity
@ast
Polyglutamine length-dependent ...... regation and cellular toxicity
@en
Polyglutamine length-dependent ...... regation and cellular toxicity
@nl
prefLabel
Polyglutamine length-dependent ...... regation and cellular toxicity
@ast
Polyglutamine length-dependent ...... regation and cellular toxicity
@en
Polyglutamine length-dependent ...... regation and cellular toxicity
@nl
P2093
P356
P1476
Polyglutamine length-dependent ...... regation and cellular toxicity
@en
P2093
P304
P356
10.1093/HMG/9.13.2009
P407
P577
2000-08-12T00:00:00Z