Inefficient degradation of truncated polyglutamine proteins by the proteasome.
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Ubiquitin-proteasome system involvement in Huntington's diseaseThe DNAJB6 and DNAJB8 protein chaperones prevent intracellular aggregation of polyglutamine peptidesClioquinol down-regulates mutant huntingtin expression in vitro and mitigates pathology in a Huntington's disease mouse model.Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model miceRegulation of cellular protein quality control networks in a multicellular organismPolarised asymmetric inheritance of accumulated protein damage in higher eukaryotesAggresome formation and neurodegenerative diseases: therapeutic implicationsProteasomes activate aggresome disassembly and clearance by producing unanchored ubiquitin chainsThe requirement for Cdc48/p97 in nuclear protein quality control degradation depends on the substrate and correlates with substrate insolubilityThe ubiquitin proteasome system in glia and its role in neurodegenerative diseasesRegulation of proteasome activity in health and diseaseParkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6Misfolding of proteins with a polyglutamine expansion is facilitated by proteasomal chaperonesTransportable, Chemical Genetic Methodology for the Small Molecule-Mediated Inhibition of Heat Shock Factor 1Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and agingExtended polyglutamine tracts cause aggregation and structural perturbation of an adjacent beta barrel protein.ER-associated complexes (ERACs) containing aggregated cystic fibrosis transmembrane conductance regulator (CFTR) are degraded by autophagy.Systems biology analysis of Drosophila in vivo screen data elucidates core networks for DNA damage repair in SCA1.Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradationUbiquitin conjugating enzymes participate in polyglutamine protein aggregation.The ubiquitin proteasome system in Huntington's disease and the spinocerebellar ataxiasThe ubiquitin-proteasome reporter GFPu does not accumulate in neurons of the R6/2 transgenic mouse model of Huntington's disease.Modeling Huntington disease in yeast: perspectives and future directions.Decreased O-linked GlcNAcylation protects from cytotoxicity mediated by huntingtin exon1 protein fragmentHsp70 interacts with the retroviral restriction factor TRIM5alpha and assists the folding of TRIM5alphaAtomistic simulations of the effects of polyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerizationPhosphorylation of NBR1 by GSK3 modulates protein aggregation.Unraveling a role for dopamine in Huntington's disease: the dual role of reactive oxygen species and D2 receptor stimulationThe ubiquitin-proteasome system in neurodegenerative diseases: precipitating factor, yet part of the solutionThymopoiesis in mice depends on a Foxn1-positive thymic epithelial cell lineage.Assessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptidesPuromycin-sensitive aminopeptidase protects against aggregation-prone proteins via autophagyDysregulation of the proteasome increases the toxicity of ALS-linked mutant SOD1.The biology of proteostasis in aging and disease.Large-scale screen for modifiers of ataxin-3-derived polyglutamine-induced toxicity in Drosophila.Proteotoxic stress and ageing triggers the loss of redox homeostasis across cellular compartments.Pathogenic polyglutamine expansion length correlates with polarity of the flanking sequences.Pharmacological promotion of inclusion formation: a therapeutic approach for Huntington's and Parkinson's diseases.A cellular perspective on conformational disease: the role of genetic background and proteostasis networks.Proteins in aggregates functionally impact multiple neurodegenerative disease models by forming proteasome-blocking complexes.
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Inefficient degradation of truncated polyglutamine proteins by the proteasome.
description
article científic
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article scientifique
@fr
articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 07 October 2004
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Inefficient degradation of truncated polyglutamine proteins by the proteasome.
@en
Inefficient degradation of truncated polyglutamine proteins by the proteasome.
@nl
type
label
Inefficient degradation of truncated polyglutamine proteins by the proteasome.
@en
Inefficient degradation of truncated polyglutamine proteins by the proteasome.
@nl
prefLabel
Inefficient degradation of truncated polyglutamine proteins by the proteasome.
@en
Inefficient degradation of truncated polyglutamine proteins by the proteasome.
@nl
P2093
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P356
P1433
P1476
Inefficient degradation of truncated polyglutamine proteins by the proteasome.
@en
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Kristine E Staniszewski
Kwame N Mensah
Richard I Morimoto
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P304
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10.1038/SJ.EMBOJ.7600426
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P577
2004-10-07T00:00:00Z