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

Parkin reverses intracellular beta-amyloid accumulation and its negative effects on proteasome function.

Journal of neuroscience research - 1 Jan 2010

Rosen Kenneth M, Moussa Charbel E-H, Lee Han-Kyu, Kumar Pravir, Kitada Tohru, Qin Gangjian, Fu Qinghao, Querfurth Henry W

Abstract excerpt

The significance of intracellular beta-amyloid (Abeta(42)) accumulation is increasingly recognized in Alzheimer's disease (AD) pathogenesis. Abeta removal mechanisms that have attracted attention include IDE/neprilysin degradation and antibody-mediated uptake by immune cells. However, the role of the ubiquitin-proteasome system (UPS) in the disposal of cellular Abeta has not been fully explored. The E3 ubiquitin...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid beta-Peptides
Share to Cerebral Cortex

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytoprotection

Share to Fluorescent Antibody Technique

Share to Immunoprecipitation

Share to Proteasome Endopeptidase Complex

Share to Ubiquitin

Share to Ubiquitination

Source

Open in PubMed Open full text

Identifiers

PMID: 19610108
DOI: 10.1002/jnr.22178
PMCID: PMC2844439

Genes

IDE

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

Parkin reverses intracellular beta-amyloid accumulation and its negative effects on proteasome function.PMID 19610108Read ↗

Parkin promotes intracellular Abeta1-42 clearance.Semantic proximity Read ↗

Parkin mediates beclin-dependent autophagic clearance of defective mitochondria and ubiquitinated Abeta in AD models.Semantic proximity Read ↗

Pathogenic mutations inactivate parkin by distinct mechanismsSemantic proximity Read ↗

Wild type and mutant amyloid precursor proteins influence downstream effects of proteasome and autophagy inhibition.Semantic proximity Read ↗

Intracellular biology of Alzheimer's disease amyloid beta peptide.Semantic proximity Read ↗

Inclusion-body myositis: a myodegenerative conformational disorder associated with Abeta, protein misfolding, and proteasome inhibition.Semantic proximity Read ↗

The p38 subunit of the aminoacyl-tRNA synthetase complex is a Parkin substrate: linking protein biosynthesis and neurodegeneration.Semantic proximity Read ↗

Intracellular amyloid beta-protein as a therapeutic target for treating Alzheimer's disease.Semantic proximity Read ↗

Differential effects of Parkin and its mutants on protein aggregation, the ubiquitin-proteasome system, and neuronal cell death in human neuroblastoma cells.Semantic proximity Read ↗

β-Amyloid Protein Induces Mitophagy-Dependent Ferroptosis Through the CD36/PINK/PARKIN Pathway Leading to Blood-Brain Barrier Destruction in Alzheimer's DiseaseSemantic proximity Read ↗

Interleukin-1β drives NEDD8 nuclear-to-cytoplasmic translocation, fostering parkin activation via NEDD8 binding to the P-ubiquitin activating siteSemantic proximity Read ↗

In vitro Pb exposure disturbs the balance between Aβ production and elimination: The role of AβPP and neprilysinSemantic proximity Read ↗

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