PML clastosomes prevent nuclear accumulation of mutant ataxin-7 and other polyglutamine proteins - Wikidata - wikimedia - TriplyDB

PML clastosomes prevent nuclear accumulation of mutant ataxin-7 and other polyglutamine proteins

PML clastosomes prevent nuclear accumulation of mutant ataxin-7 and other polyglutamine proteins

http://www.wikidata.org/entity/Q24683226

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Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradation 3D reconstruction of VZV infected cell nuclei and PML nuclear cages by serial section array scanning electron microscopy and electron tomography SUMOylation of the Forkhead transcription factor FOXL2 promotes its stabilization/activation through transient recruitment to PML bodies Pondering the puzzle of PML (promyelocytic leukemia) nuclear bodies: can we fit the pieces together using an RNA regulon?Ataxin-1 fusion partners alter polyQ lethality and aggregation.Design of RNAi hairpins for mutation-specific silencing of ataxin-7 and correction of a SCA7 phenotype.Molecular mechanisms of varicella zoster virus pathogenesis.Entrapment of viral capsids in nuclear PML cages is an intrinsic antiviral host defense against varicella-zoster virus.How the nucleus copes with proteotoxic stress.Comparative ultrastructure of CRM1-Nucleolar bodies (CNoBs), Intranucleolar bodies (INBs) and hybrid PML/p62 bodies uncovers new facets of nuclear body dynamic and diversity Sequestration of cellular interacting partners by protein aggregates: implication in a loss-of-function pathology.Does Huntingtin play a role in selective macroautophagy?Exposed hydrophobicity is a key determinant of nuclear quality control degradation.A cellular system that degrades misfolded proteins and protects against neurodegeneration PML nuclear bodies: assembly and oxidative stress-sensitive sumoylation.FBXO25-associated nuclear domains: a novel subnuclear structure.Substrate recognition in nuclear protein quality control degradation is governed by exposed hydrophobicity that correlates with aggregation and insolubility.New insights into the role of PML in tumour suppression.PML in the Brain: From Development to Degeneration.Polyglutamine diseases: where does toxicity come from? what is toxicity? where are we going?Progressive multifocal leukoencephalopathy and promyelocytic leukemia nuclear bodies: a review of clinical, neuropathological, and virological aspects of JC virus-induced demyelinating disease Orphan nuclear bodies.The role of PML in the nervous system.How a disordered ubiquitin ligase maintains order in nuclear protein homeostasis Cellular maintenance of nuclear protein homeostasis Allele-selective suppression of mutant genes in polyglutamine diseases.Proteostasis and aging.Protein quality control in the nucleus.The autophagy/lysosome pathway is impaired in SCA7 patients and SCA7 knock-in mice.Deficit of heat shock transcription factor 1-heat shock 70 kDa protein 1A axis determines the cell death vulnerability in a model of spinocerebellar ataxia type 6.Nuclear polyglutamine-containing protein aggregates as active proteolytic centers.Herpes simplex virus type 1 genomes are associated with ND10 nuclear substructures in quiescently infected human fibroblasts.N-terminal hydrophobic amino acids of activating transcription factor 5 (ATF5) protein confer interleukin 1β (IL-1β)-induced stabilization.Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates.Nucleocytoplasmic shuttling of p62/SQSTM1 and its role in recruitment of nuclear polyubiquitinated proteins to promyelocytic leukemia bodies.SUMOylation attenuates the aggregation propensity and cellular toxicity of the polyglutamine expanded ataxin-7.PML has a predictive role in tumor cell permissiveness to interferon-sensitive oncolytic viruses.Interferon β induces clearance of mutant ataxin 7 and improves locomotion in SCA7 knock-in mice.Localization and regulation of PML bodies in the adult mouse brain.PML: Regulation and multifaceted function beyond tumor suppression.

P2860

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P2860

PML clastosomes prevent nuclear accumulation of mutant ataxin-7 and other polyglutamine proteins

http://www.wikidata.org/entity/Q24683226

description

2006 nî lūn-bûn

@nan

2006 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հուլիսին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

PML clastosomes prevent nuclea ...... d other polyglutamine proteins

@ast

PML clastosomes prevent nuclea ...... d other polyglutamine proteins

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PML clastosomes prevent nuclea ...... d other polyglutamine proteins

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type

label

PML clastosomes prevent nuclea ...... d other polyglutamine proteins

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PML clastosomes prevent nuclea ...... d other polyglutamine proteins

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PML clastosomes prevent nuclea ...... d other polyglutamine proteins

@nl

prefLabel

PML clastosomes prevent nuclea ...... d other polyglutamine proteins

@ast

PML clastosomes prevent nuclea ...... d other polyglutamine proteins

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PML clastosomes prevent nuclea ...... d other polyglutamine proteins

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P1433

Journal of Cell Biology

P1476

PML clastosomes prevent nuclea ...... d other polyglutamine proteins

@en

P2093

Alexandre Janer

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

Annie Sittler

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Elodie Martin

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

Hiroto Fujigasaki

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

Marie-Paule Muriel

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Merle Ruberg

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

Morwena Latouche

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Yvon Trottier

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

P2860

Nuclear localization of the spinocerebellar ataxia type 7 protein, ataxin-7

Regulation of p53 activity in nuclear bodies by a specific PML isoform

Cloning of the SCA7 gene reveals a highly unstable CAG repeat expansion

Ataxin-1 with an expanded glutamine tract alters nuclear matrix-associated structures

Ataxin-7 is a subunit of GCN5 histone acetyltransferase-containing complexes

Structure, localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL): structural similarities with a new family of oncoproteins

A novel GTPase, CRAG, mediates promyelocytic leukemia protein-associated nuclear body formation and degradation of expanded polyglutamine protein

Glutamine-expanded ataxin-7 alters TFTC/STAGA recruitment and chromatin structure leading to photoreceptor dysfunction.

Polyglutamine-expanded spinocerebellar ataxia-7 protein disrupts normal SAGA and SLIK histone acetyltransferase activity.

The transcriptional role of PML and the nuclear body

P304

65-76

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scholarly article

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10.1083/JCB.200511045

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P433

1

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174

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2006-07-01T00:00:00Z

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6965684

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16818720

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P932

2064165

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