Proteasomal inhibition-induced inclusion formation and death in cortical neurons require transcription and ubiquitination
about
Protein degradation pathways in Parkinson's disease: curse or blessingLoss of β-glucocerebrosidase activity does not affect alpha-synuclein levels or lysosomal function in neuronal cellsThe ubiquitin-proteasome system in spongiform degenerative disordersProteomic characterization of an isolated fraction of synthetic proteasome inhibitor (PSI)-induced inclusions in PC12 cells might offer clues to aggresomes as a cellular defensive response against proteasome inhibition by PSI.Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagyThe WD40 domain is required for LRRK2 neurotoxicity.Role of the proteasome in excitotoxicity-induced cleavage of glutamic acid decarboxylase in cultured hippocampal neurons.Mitochondrial accumulation of polyubiquitinated proteins and differential regulation of apoptosis by polyubiquitination sites Lys-48 and -63Killer proteases and little strokes--how the things that do not kill you make you stronger.Heat shock protein defenses in the neocortex and allocortex of the telencephalon.Effect of lysosomal and ubiquitin-proteasome system dysfunction on the abnormal aggregation of α-synuclein in PC12 cells.Methamphetamine-induced neurotoxicity linked to ubiquitin-proteasome system dysfunction and autophagy-related changes that can be modulated by protein kinase C delta in dopaminergic neuronal cells.Complex Effects of the ZSCAN21 Transcription Factor on Transcriptional Regulation of α-Synuclein in Primary Neuronal Cultures and in VivoLoss of NEDD4 contributes to RTP801 elevation and neuron toxicity: implications for Parkinson's disease.Adaptation and sensitization to proteotoxic stress.Drug targets from genetics: α-synuclein.Targeting intracellular and extracellular alpha-synuclein as a therapeutic strategy in Parkinson's disease and other synucleinopathies.α-Synuclein and protein degradation systems: a reciprocal relationship.The function of α-synuclein.Astrocytes Surviving Severe Stress Can Still Protect Neighboring Neurons from Proteotoxic Injury.Regulation of α-synuclein expression in cultured cortical neurons.Phosphorylated alpha-synuclein at Ser-129 is targeted to the proteasome pathway in a ubiquitin-independent mannerDifferential effects of Parkin and its mutants on protein aggregation, the ubiquitin-proteasome system, and neuronal cell death in human neuroblastoma cells.Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function.Synergistic stress exacerbation in hippocampal neurons: Evidence favoring the dual-hit hypothesis of neurodegeneration.Characterization of Puma-dependent and Puma-independent neuronal cell death pathways following prolonged proteasomal inhibition.Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells.Differential expression patterns of Puma and Hsp70 following proteasomal stress in the hippocampus are key determinants of neuronal vulnerability.Selective neuroprotective effects of the S18Y polymorphic variant of UCH-L1 in the dopaminergic system.Ubiquitination of alpha-synuclein in Lewy bodies is a pathological event not associated with impairment of proteasome function.alpha-synuclein is required for the fibrillar nature of ubiquitinated inclusions induced by proteasomal inhibition in primary neurons.A novel cell death pathway that is partially caspase dependent, but morphologically non-apoptotic, elicited by proteasomal inhibition of rat sympathetic neurons.N-Acetyl-l-Cysteine Protects Astrocytes against Proteotoxicity without Recourse to Glutathione.Neuroprotective upregulation of endogenous α-synuclein precedes ubiquitination in cultured dopaminergic neurons.A motif within the armadillo repeat of Parkinson's-linked LRRK2 interacts with FADD to hijack the extrinsic death pathway.Bcl-2 homology domain 3-only proteins Puma and Bim mediate the vulnerability of CA1 hippocampal neurons to proteasome inhibition in vivo.Targeted disruption of neuronal 19S proteasome subunits induces the formation of ubiquitinated inclusions in the absence of cell death.Proteasome inhibition leads to early loss of synaptic proteins in neuronal culture
P2860
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P2860
Proteasomal inhibition-induced inclusion formation and death in cortical neurons require transcription and ubiquitination
description
2002 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2002
@ast
im Oktober 2002 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2002/10/01)
@sk
vědecký článek publikovaný v roce 2002
@cs
wetenschappelijk artikel (gepubliceerd op 2002/10/01)
@nl
наукова стаття, опублікована в жовтні 2002
@uk
مقالة علمية (نشرت في أكتوبر 2002)
@ar
name
Proteasomal inhibition-induced ...... anscription and ubiquitination
@ast
Proteasomal inhibition-induced ...... anscription and ubiquitination
@en
Proteasomal inhibition-induced ...... anscription and ubiquitination
@nl
type
label
Proteasomal inhibition-induced ...... anscription and ubiquitination
@ast
Proteasomal inhibition-induced ...... anscription and ubiquitination
@en
Proteasomal inhibition-induced ...... anscription and ubiquitination
@nl
prefLabel
Proteasomal inhibition-induced ...... anscription and ubiquitination
@ast
Proteasomal inhibition-induced ...... anscription and ubiquitination
@en
Proteasomal inhibition-induced ...... anscription and ubiquitination
@nl
P356
P1476
Proteasomal inhibition-induced ...... anscription and ubiquitination
@en
P2093
Hardy J. Rideout
Leonidas Stefanis
P304
P356
10.1006/MCNE.2002.1173
P577
2002-10-01T00:00:00Z