Dynamic recruitment of active proteasomes into polyglutamine initiated inclusion bodies. - Test2 - elhamkhani - TriplyDB

Dynamic recruitment of active proteasomes into polyglutamine initiated inclusion bodies.

Dynamic recruitment of active proteasomes into polyglutamine initiated inclusion bodies.

http://www.wikidata.org/entity/Q39051836

about

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 Imaging complex protein metabolism in live organisms by stimulated Raman scattering microscopy with isotope labeling.The ubiquitin proteasome system in glia and its role in neurodegenerative diseases Protein misfolding specifies recruitment to cytoplasmic inclusion bodies The ubiquitin-proteasome system in neurodegenerative diseases: precipitating factor, yet part of the solution Both ubiquitin ligases FBXW8 and PARK2 are sequestrated into insolubility by ATXN2 PolyQ expansions, but only FBXW8 expression is dysregulated.Proteasome-mediated proteolysis of the polyglutamine-expanded androgen receptor is a late event in spinal and bulbar muscular atrophy (SBMA) pathogenesis.Reduced Levels of Proteasome Products in a Mouse Striatal Cell Model of Huntington's Disease.Distinguishing aggregate formation and aggregate clearance using cell-based assays.From pathways to targets: understanding the mechanisms behind polyglutamine disease.UPS Activation in the Battle Against Aging and Aggregation-Related Diseases: An Extended Review.Huntington's Disease: Mechanisms of Pathogenesis and Therapeutic Strategies.Effects of Exogenous NUB1 Expression in the Striatum of HDQ175/Q7 Mice.Polyglutamine aggregation in Huntington's disease and spinocerebellar ataxia type 3: similar mechanisms in aggregate formation.Profilin reduces aggregation and phase separation of huntingtin N-terminal fragments by preferentially binding to soluble monomers and oligomers.Dynamic recruitment of ubiquitin to mutant huntingtin inclusion bodies.Proteostasis in Huntington's disease: disease mechanisms and therapeutic opportunities.

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P2860

Dynamic recruitment of active proteasomes into polyglutamine initiated inclusion bodies.

http://www.wikidata.org/entity/Q39051836

description

2013 nî lūn-bûn

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name

Dynamic recruitment of active proteasomes into polyglutamine initiated inclusion bodies.

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Dynamic recruitment of active proteasomes into polyglutamine initiated inclusion bodies.

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type

label

Dynamic recruitment of active proteasomes into polyglutamine initiated inclusion bodies.

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Dynamic recruitment of active proteasomes into polyglutamine initiated inclusion bodies.

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prefLabel

Dynamic recruitment of active proteasomes into polyglutamine initiated inclusion bodies.

@en

Dynamic recruitment of active proteasomes into polyglutamine initiated inclusion bodies.

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J.FEBSLET.2013.11.023

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Dynamic recruitment of active proteasomes into polyglutamine initiated inclusion bodies.

@en

P2093

Anne H Jansen

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Anne Wiemhoefer

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Donna L Smith

http://www.w3.org/2001/XMLSchema#string

Eric Reits

http://www.w3.org/2001/XMLSchema#string

Hermen Overkleeft

http://www.w3.org/2001/XMLSchema#string

Katrin Juenemann

http://www.w3.org/2001/XMLSchema#string

Mark A Hink

http://www.w3.org/2001/XMLSchema#string

Rianne van den Nieuwendijk

http://www.w3.org/2001/XMLSchema#string

Sabine Schipper-Krom

http://www.w3.org/2001/XMLSchema#string

P2860

The DNAJB6 and DNAJB8 protein chaperones prevent intracellular aggregation of polyglutamine peptides

A proteolytic pathway that recognizes ubiquitin as a degradation signal.

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

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

Misfolding of proteins with a polyglutamine expansion is facilitated by proteasomal chaperones

Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice

Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain

Profiling proteasome activity in tissue with fluorescent probes.

The ubiquitin-proteasome reporter GFPu does not accumulate in neurons of the R6/2 transgenic mouse model of Huntington's disease.

Activity-based profiling reveals reactivity of the murine thymoproteasome-specific subunit beta5t

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