Indirect inhibition of 26S proteasome activity in a cellular model of Huntington's disease. - Wikidata - wikimedia - TriplyDB

Indirect inhibition of 26S proteasome activity in a cellular model of Huntington's disease.

Indirect inhibition of 26S proteasome activity in a cellular model of Huntington's disease.

http://www.wikidata.org/entity/Q35839766

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Ubiquitin-proteasome system involvement in Huntington's disease The life cycle of the 26S proteasome: from birth, through regulation and function, and onto its death The many faces of autophagy dysfunction in Huntington's disease: from mechanism to therapy Huntington's disease: underlying molecular mechanisms and emerging concepts Regulation of proteasome activity in health and disease Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting.Distinct partitioning of ALS associated TDP-43, FUS and SOD1 mutants into cellular inclusions Protein misfolding specifies recruitment to cytoplasmic inclusion bodies The aggregation and inheritance of damaged proteins determines cell fate during mitosis.The ubiquitin-proteasome system in neurodegenerative diseases: precipitating factor, yet part of the solution Proteostasis in striatal cells and selective neurodegeneration in Huntington's disease.Chaperone-mediated autophagy: roles in disease and aging.The biology of proteostasis in aging and disease.Proteotoxic stress and ageing triggers the loss of redox homeostasis across cellular compartments.Natural genetic variation determines susceptibility to aggregation or toxicity in a C. elegans model for polyglutamine disease.PaCS is a novel cytoplasmic structure containing functional proteasome and inducible by cytokines/trophic factors.Trehalose reverses cell malfunction in fibroblasts from normal and Huntington's disease patients caused by proteosome inhibition.ER stress-induced eIF2-alpha phosphorylation underlies sensitivity of striatal neurons to pathogenic huntingtin Inducible HSP70 is critical in preventing the aggregation and enhancing the processing of PMP22.Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies.PiZ mouse liver accumulates polyubiquitin conjugates that associate with catalytically active 26S proteasomes Differential effect of HDAC3 on cytoplasmic and nuclear huntingtin aggregates.Reduced Levels of Proteasome Products in a Mouse Striatal Cell Model of Huntington's Disease.Prion-like transmission of neuronal huntingtin aggregates to phagocytic glia in the Drosophila brain.Ubiquitin Accumulation on Disease Associated Protein Aggregates Is Correlated with Nuclear Ubiquitin Depletion, Histone De-Ubiquitination and Impaired DNA Damage Response Proteasome function is not impaired in healthy aging of the lung.Potential for therapeutic manipulation of the UPR in disease.Heat shock response activation exacerbates inclusion body formation in a cellular model of Huntington disease.Ubiquilin-1 overexpression increases the lifespan and delays accumulation of Huntingtin aggregates in the R6/2 mouse model of Huntington's disease.De novo prion aggregates trigger autophagy in skeletal muscle.The Mechanistic Links Between Proteasome Activity, Aging and Age-related Diseases.Protein misfolding in neurodegenerative diseases: implications and strategies.Pharmacological protein targets in polyglutamine diseases: mutant polypeptides and their interactors.Endoplasmic reticulum stress response in yeast and humans.The role of protein clearance mechanisms in organismal ageing and age-related diseases.Primary cilia and autophagic dysfunction in Huntington's disease.Proteasome properties of hemocytes differ between the whiteleg shrimp Penaeus vannamei and the brown shrimp Crangon crangon (Crustacea, Decapoda).Nuclear inclusion bodies of mutant and wild-type p53 in cancer: a hallmark of p53 inactivation and proteostasis remodelling by p53 aggregation.Walking the tightrope: proteostasis and neurodegenerative disease.Modulation of Molecular Chaperones in Huntington's Disease and Other Polyglutamine Disorders.

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P2860

Indirect inhibition of 26S proteasome activity in a cellular model of Huntington's disease.

http://www.wikidata.org/entity/Q35839766

description

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Indirect inhibition of 26S pro ...... model of Huntington's disease.

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Indirect inhibition of 26S pro ...... model of Huntington's disease.

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Indirect inhibition of 26S pro ...... model of Huntington's disease.

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Indirect inhibition of 26S pro ...... model of Huntington's disease.

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Indirect inhibition of 26S pro ...... model of Huntington's disease.

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Indirect inhibition of 26S pro ...... model of Huntington's disease.

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Indirect inhibition of 26S pro ...... model of Huntington's disease.

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Brigit E Riley

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Chetan N Patel

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Kirill Bersuker

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Mark S Hipp

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Michael Brandeis

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Ron R Kopito

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Stephen E Kaiser

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Thomas A Shaler

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P2860

MAD2B is an inhibitor of the anaphase-promoting complex

SUMO modification of Huntingtin and Huntington's disease pathology

Recognition of the polyubiquitin proteolytic signal

Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging

The ubiquitin proteasome system in neuropathology

One step at a time: endoplasmic reticulum-associated degradation

Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS

Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate

Destabilizing protein polymorphisms in the genetic background direct phenotypic expression of mutant SOD1 toxicity

A proteolytic pathway that recognizes ubiquitin as a degradation signal.

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196

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Huntington disease

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3307690

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