Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Proteasomal inhibition hypersensitizes differentiated neuroblastoma cells to oxidative damage.

Neuroscience letters - 15 May 2006

Lev Nirit, Melamed Eldad, Offen Daniel

Abstract excerpt

Parkinson's disease (PD) is a multifactorial disease caused by both genetic and environmental factors. Alpha-synuclein is of particular interest in PD since it is a major component of Lewy bodies and mutations in the alpha-synuclein gene were identified in familial PD. Oxidative stress and proteasomal dysfunction are implicated in the pathogenesis of PD but their interactions as well as their effect on aggregates...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to alpha-Synuclein
Share to Benzothiazoles
Share to Ferrous Compounds

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Neuroblastoma

Share to Proteasome Inhibitors

Share to Rotenone

Share to Thiazoles

Share to Ubiquitin

Source

Identifiers

PMID: 16584840
DOI: 10.1016/j.neulet.2005.09.086

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Proteasomal inhibition hypersensitizes differentiated neuroblastoma cells to oxidative damage.PMID 16584840Read ↗

Parkinson's disease genetic mutations increase cell susceptibility to stress: mutant alpha-synuclein enhances H2O2- and Sin-1-induced cell death.Semantic proximity Read ↗

Dopamine Cytotoxicity Involves Both Oxidative and Nonoxidative Pathways in SH-SY5Y Cells: Potential Role of Alpha-Synuclein Overexpression and Proteasomal Inhibition in the Etiopathogenesis of Parkinson's DiseaseSemantic proximity Read ↗

β-synuclein aggregates and induces neurodegeneration in dopaminergic neurons.Semantic proximity Read ↗

A precipitating role for truncated alpha-synuclein and the proteasome in alpha-synuclein aggregation: implications for pathogenesis of Parkinson disease.Semantic proximity Read ↗

The Parkinson disease-associated A30P mutation stabilizes alpha-synuclein against proteasomal degradation triggered by heme oxygenase-1 over-expression in human neuroblastoma cells.Semantic proximity Read ↗

Alpha-synuclein-induced oxidative stress correlates with altered superoxide dismutase and glutathione synthesis in human neuroblastoma SH-SY5Y cellsSemantic proximity Read ↗

Reciprocal effects of alpha-synuclein overexpression and proteasome inhibition in neuronal cells and tissue.Semantic proximity Read ↗

Prolyl oligopeptidase inhibition attenuates the toxicity of a proteasomal inhibitor, lactacystin, in the alpha-synuclein overexpressing cell culture.Semantic proximity Read ↗

α-Synuclein overexpression increases dopamine toxicity in BE(2)-M17 cellsSemantic proximity Read ↗

alpha-synuclein is required for the fibrillar nature of ubiquitinated inclusions induced by proteasomal inhibition in primary neurons.Semantic proximity Read ↗

The <i>SNCA</i> A53T mutation sensitizes human neurons and microglia to ferroptosisSemantic proximity Read ↗

Alpha synuclein aggregation: is it the toxic gain of function responsible for neurodegeneration in Parkinson's disease?Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.