Nuclear aggresomes form by fusion of PML-associated aggregates. - Wikidata - awgldk - TriplyDB

Nuclear aggresomes form by fusion of PML-associated aggregates.

Nuclear aggresomes form by fusion of PML-associated aggregates.

http://www.wikidata.org/entity/Q30476220

about

The nuclear RhoA exchange factor Net1 interacts with proteins of the Dlg family, affects their localization, and influences their tumor suppressor activity Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradation Recruitment of the oncoprotein v-ErbA to aggresomes.3D reconstruction of VZV infected cell nuclei and PML nuclear cages by serial section array scanning electron microscopy and electron tomography ER-associated complexes (ERACs) containing aggregated cystic fibrosis transmembrane conductance regulator (CFTR) are degraded by autophagy.Puromycin-based vectors promote a ROS-dependent recruitment of PML to nuclear inclusions enriched with HSP70 and Proteasomes.Herpes simplex virus type I disrupts the ATR-dependent DNA-damage response during lytic infection.Ataxin-1 fusion partners alter polyQ lethality and aggregation.Virus-Induced Chaperone-Enriched (VICE) domains function as nuclear protein quality control centers during HSV-1 infection Misfolded polypeptides are selectively recognized and transported toward aggresomes by a CED complex The microtubule-associated histone deacetylase 6 (HDAC6) regulates epidermal growth factor receptor (EGFR) endocytic trafficking and degradation.Virus-induced aggregates in infected cells.Hsp70/Hsp90 chaperone machinery is involved in the assembly of the purinosome.Efficient induction of nuclear aggresomes by specific single missense mutations in the DNA-binding domain of a viral AP-1 homolog.Overexpression of the transcriptional repressor complex BCL-6/BCoR leads to nuclear aggregates distinct from classical aggresomes Exposed hydrophobicity is a key determinant of nuclear quality control degradation.Characterization of aggregate/aggresome structures formed by polyhedrin of Bombyx mori nucleopolyhedrovirus Human cytomegalovirus UL97 kinase activity is required for the hyperphosphorylation of retinoblastoma protein and inhibits the formation of nuclear aggresomes.Substrate recognition in nuclear protein quality control degradation is governed by exposed hydrophobicity that correlates with aggregation and insolubility.Oligomerization of ICP4 and rearrangement of heat shock proteins may be important for herpes simplex virus type 1 prereplicative site formation.Human cytomegalovirus UL97 kinase prevents the deposition of mutant protein aggregates in cellular models of Huntington's disease and ataxia How a disordered ubiquitin ligase maintains order in nuclear protein homeostasis Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies DNA virus replication compartments.Cellular maintenance of nuclear protein homeostasis Functional protein aggregates: just the tip of the iceberg.Nuclear inclusion bodies of mutant and wild-type p53 in cancer: a hallmark of p53 inactivation and proteostasis remodelling by p53 aggregation.Protein quality control in the nucleus.Herpes simplex virus 1 ubiquitin ligase ICP0 interacts with PML isoform I and induces its SUMO-independent degradation.Listeria monocytogenes ActA-mediated escape from autophagic recognition.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.Intrinsically disordered sequences enable modulation of protein phase separation through distributed tyrosine motifs.

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P2860

Nuclear aggresomes form by fusion of PML-associated aggregates.

http://www.wikidata.org/entity/Q30476220

description

2005 nî lūn-bûn

@nan

2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի հուլիսին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

@zh-tw

2005年论文

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name

Nuclear aggresomes form by fusion of PML-associated aggregates.

@ast

Nuclear aggresomes form by fusion of PML-associated aggregates.

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type

label

Nuclear aggresomes form by fusion of PML-associated aggregates.

@ast

Nuclear aggresomes form by fusion of PML-associated aggregates.

@en

prefLabel

Nuclear aggresomes form by fusion of PML-associated aggregates.

@ast

Nuclear aggresomes form by fusion of PML-associated aggregates.

@en

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MBC.E05-01-0019

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Molecular Biology of the Cell

P1476

Nuclear aggresomes form by fusion of PML-associated aggregates

@en

P2093

Albert Tousson

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

Anish Shah

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

Barbara M Vertel

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Elizabeth Sztul

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

Tung-Ling L Chen

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Ya-Sheng Gao

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P2860

The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription

Molecular characterization of two human autoantigens: unique cDNAs encoding 95- and 160-kD proteins of a putative family in the Golgi complex

Molecular characterization of GCP170, a 170-kDa protein associated with the cytoplasmic face of the Golgi membrane

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

Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis.

Interaction between neuronal intranuclear inclusions and promyelocytic leukemia protein nuclear and coiled bodies in CAG repeat diseases

The transcriptional role of PML and the nuclear body

The NH2-terminal domain of Golgin-160 contains both Golgi and nuclear targeting information

Folding proteins in fatal ways

Aggresomes: a cellular response to misfolded proteins

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4905-4917

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scholarly article

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10.1091/MBC.E05-01-0019

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10

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16

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1237092

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