Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death - Wikidata - thesis-toulmin - TriplyDB

Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death

Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death

http://www.wikidata.org/entity/Q28287762

about

Ubiquitin-proteasome system involvement in Huntington's disease Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeast Huntingtin interacting proteins are genetic modifiers of neurodegeneration Oligonucleotide therapeutic approaches for Huntington disease p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both The Guanine nucleotide exchange factor kalirin-7 is a novel synphilin-1 interacting protein and modifies synphilin-1 aggregate transport and formation The selective macroautophagic degradation of aggregated proteins requires the PI3P-binding protein Alfy SCAMP5 links endoplasmic reticulum stress to the accumulation of expanded polyglutamine protein aggregates via endocytosis inhibition Rhes, a striatal specific protein, mediates mutant-huntingtin cytotoxicity Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by increasing wild-type Ataxin1 levels HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity Clioquinol down-regulates mutant huntingtin expression in vitro and mitigates pathology in a Huntington's disease mouse model.Clarifying lysosomal storage diseases Improved activities of CREB binding protein, heterogeneous nuclear ribonucleoproteins and proteasome following downregulation of noncoding hsromega transcripts help suppress poly(Q) pathogenesis in fly models The ubiquitin proteasome system in neuropathology Palmitoylation of huntingtin by HIP14 is essential for its trafficking and function Autophagy and the ubiquitin-proteasome system: collaborators in neuroprotection Misfolded proteins partition between two distinct quality control compartments Amyloids: friend or foe?Pathogenic mechanisms of a polyglutamine-mediated neurodegenerative disease, spinocerebellar ataxia type 1 Hyperphosphorylation of microtubule-associated protein tau: a promising therapeutic target for Alzheimer disease Tau-Centric Targets and Drugs in Clinical Development for the Treatment of Alzheimer's Disease Precision medicine in spinocerebellar ataxias: treatment based on common mechanisms of disease Adaptive preconditioning in neurological diseases – therapeutic insights from proteostatic perturbations Metazoan Hsp70-based protein disaggregases: emergence and mechanisms Treatment of Huntington's disease.Disaggregases, molecular chaperones that resolubilize protein aggregates Regulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genes Protein Folding and Mechanisms of Proteostasis Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)RAN translation and frameshifting as translational challenges at simple repeats of human neurodegenerative disorders Cell biology of spinocerebellar ataxia Sorting out the trash: the spatial nature of eukaryotic protein quality control Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases Potential mechanisms of progranulin-deficient FTLD Longitudinal measures of proteostasis in live neurons: features that determine fate in models of neurodegenerative disease Autophagy and disease: always two sides to a problem Modeling Huntington's disease with induced pluripotent stem cells

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Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death

http://www.wikidata.org/entity/Q28287762

description

2004 nî lūn-bûn

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2004 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2004 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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Inclusion body formation reduc ...... and the risk of neuronal death

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Inclusion body formation reduc ...... and the risk of neuronal death

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Inclusion body formation reduc ...... and the risk of neuronal death

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Inclusion body formation reduc ...... and the risk of neuronal death

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Inclusion body formation reduc ...... and the risk of neuronal death

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Inclusion body formation reduc ...... and the risk of neuronal death

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Inclusion body formation reduc ...... and the risk of neuronal death

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Erik S Schweitzer

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Mark R Segal

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Montserrat Arrasate

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Siddhartha Mitra

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Steven Finkbeiner

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P2860

A monomeric red fluorescent protein

Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation

Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease

Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract

Impairment of the ubiquitin-proteasome system by protein aggregation

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10.1038/NATURE02998

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1016382609

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