Inhibition of proteasomal activity causes inclusion formation in neuronal and non-neuronal cells overexpressing Parkin. - Wikidata - wikimedia - TriplyDB

Inhibition of proteasomal activity causes inclusion formation in neuronal and non-neuronal cells overexpressing Parkin.

Inhibition of proteasomal activity causes inclusion formation in neuronal and non-neuronal cells overexpressing Parkin.

http://www.wikidata.org/entity/Q40195899

about

Human homologue of ariadne promotes the ubiquitylation of translation initiation factor 4E homologous protein, 4EHP The Parkinson's disease-linked proteins Fbxo7 and Parkin interact to mediate mitophagy Trapping of normal EB1 ligands in aggresomes formed by an EB1 deletion mutant.Parkin Regulation and Neurodegenerative Disorders Molecular chaperone-mediated rescue of mitophagy by a Parkin RING1 domain mutant The parkin-like human homolog of Drosophila ariadne-1 (HHARI) can induce aggresome formation in mammalian cells and is immunologically detectable in Lewy bodies alpha-Synuclein aggregates interfere with Parkin solubility and distribution: role in the pathogenesis of Parkinson disease Aggresome formation and neurodegenerative diseases: therapeutic implications Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6 BAG-6 is essential for selective elimination of defective proteasomal substrates The effects of oxidative stress on parkin and other E3 ligases.Focal distortion of the nuclear envelope by huntingtin aggregates revealed by lamin immunostaining Co-chaperone CHIP stabilizes aggregate-prone malin, a ubiquitin ligase mutated in Lafora disease.Lysine 27 ubiquitination of the mitochondrial transport protein Miro is dependent on serine 65 of the Parkin ubiquitin ligase Parkin reverses intracellular beta-amyloid accumulation and its negative effects on proteasome function.Biochemical analysis of Parkinson's disease-causing variants of Parkin, an E3 ubiquitin-protein ligase with monoubiquitylation capacity.Functional genetic analysis of mutations implicated in a human speech and language disorder.Post-translational modifications of tubulin: pathways to functional diversity of microtubules.The Copper Metabolism MURR1 domain protein 1 (COMMD1) modulates the aggregation of misfolded protein species in a client-specific manner N-terminal truncated UCH-L1 prevents Parkinson's disease associated damage.The aggravating role of the ubiquitin-proteasome system in neurodegeneration.Misfolded Gβ is recruited to cytoplasmic dynein by Nudel for efficient clearance.The role of ubiquitin-protein ligases in neurodegenerative disease.Signaling, polyubiquitination, trafficking, and inclusions: sequestosome 1/p62's role in neurodegenerative disease.Genome-wide RNAi screen and in vivo protein aggregation reporters identify degradation of damaged proteins as an essential hypertonic stress response.The two faces of protein misfolding: gain- and loss-of-function in neurodegenerative diseases.Direct binding with histone deacetylase 6 mediates the reversible recruitment of parkin to the centrosome.A sporadic Parkinson disease model via silencing of the ubiquitin-proteasome/E3 ligase component SKP1A Cross-functional E3 ligases Parkin and C-terminus Hsp70-interacting protein in neurodegenerative disorders.Aggrephagy: selective disposal of protein aggregates by macroautophagy.E3 ubiquitin ligases in protein quality control mechanism.Pneumocyte injury and ubiquitin-positive pneumocytes in interstitial lung diseases.Postmortem studies in Parkinson's disease.Antagonism of proteasome inhibitor-induced heme oxygenase-1 expression by PINK1 mutation.Intracellular pH Modulates Autophagy and Mitophagy.Expression pattern of parkin isoforms in lung adenocarcinomas.Versatile members of the DNAJ family show Hsp70 dependent anti-aggregation activity on RING1 mutant parkin C289G.Methamphetamine oxidatively damages parkin and decreases the activity of 26S proteasome in vivo.A simple cell based assay to measure Parkin activity.Parkin promotes intracellular Abeta1-42 clearance.

P2860

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P2860

Inhibition of proteasomal activity causes inclusion formation in neuronal and non-neuronal cells overexpressing Parkin.

http://www.wikidata.org/entity/Q40195899

description

2003 nî lūn-bûn

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

@zh-tw

2003年论文

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2003年论文

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2003年论文

@zh-cn

name

Inhibition of proteasomal acti ...... l cells overexpressing Parkin.

@en

Inhibition of proteasomal acti ...... l cells overexpressing Parkin.

@en-gb

type

label

Inhibition of proteasomal acti ...... l cells overexpressing Parkin.

@en

Inhibition of proteasomal acti ...... l cells overexpressing Parkin.

@en-gb

prefLabel

Inhibition of proteasomal acti ...... l cells overexpressing Parkin.

@en

Inhibition of proteasomal acti ...... l cells overexpressing Parkin.

@en-gb

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MBC.E03-02-0078

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Molecular Biology of the Cell

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Inhibition of proteasomal acti ...... l cells overexpressing Parkin.

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Gina B Scott

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Helen C Ardley

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Nancy G S Tan

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Philip A Robinson

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Stephen A Rose

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P2860

The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1

Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase

Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity

Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1

Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7

An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin

Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease

Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity

CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity

Parkin accumulation in aggresomes due to proteasome impairment

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4541-4556

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11

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14

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12937272

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