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

DJ-1 interactions with α-synuclein attenuate aggregation and cellular toxicity in models of Parkinson's disease.

Cell death & disease - 24 Jul 2014

Zondler L, Miller-Fleming L, Repici M, Gonçalves S, Tenreiro S, Rosado-Ramos R, Betzer C, Straatman K R, Jensen P H, Giorgini F, Outeiro T F

Abstract excerpt

Parkinson's disease (PD) is a devastating neurodegenerative disorder characterized by the loss of neurons in the substantia nigra pars compacta and the presence of Lewy bodies in surviving neurons. These intracellular protein inclusions are primarily composed of misfolded α-synuclein (aSyn), which has also been genetically linked to familial and sporadic forms of PD. DJ-1 is a small ubiquitously expressed protein...

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 Brain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Intracellular Signaling Peptides and Proteins

Share to Oncogene Proteins

Share to Parkinson Disease

Share to Peroxiredoxins

Share to Protein Aggregates

Share to Protein Deglycase DJ-1

Source

Open in PubMed Open full text

Identifiers

PMID: 25058424
DOI: 10.1038/cddis.2014.307
PMCID: PMC4123098

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

DJ-1 interactions with α-synuclein attenuate aggregation and cellular toxicity in models of Parkinson's disease.PMID 25058424Read ↗

Pathogenesis of DJ-1/PARK7-Mediated Parkinson’s DiseaseSemantic proximity Read ↗

DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation.Semantic proximity Read ↗

DJ‐1 is present in a large molecular complex in human brain tissue and interacts with α‐synucleinSemantic proximity Read ↗

Parkinson's disease-associated mutations in DJ-1 modulate its dimerization in living cells.Semantic proximity Read ↗

Association of DJ-1 and parkin mediated by pathogenic DJ-1 mutations and oxidative stress.Semantic proximity Read ↗

Limelight on Alpha-Synuclein: Pathological and Mechanistic Implications in NeurodegenerationSemantic proximity Read ↗

Role of DJ-1 in Parkinson's disease.Semantic proximity Read ↗

α-synuclein interacts with SOD1 and promotes its oligomerization.Semantic proximity Read ↗

The Parkinson's disease-related protein DJ-1 protects dopaminergic neurons in vivo and cultured cells from alpha-synuclein and 6-hydroxydopamine toxicity.Semantic proximity Read ↗

Linking DJ-1 to neurodegeneration offers novel insights for understanding the pathogenesis of Parkinson's disease.Semantic proximity Read ↗

Interaction of α-synuclein with DJ-1 in homodimer and L166P mutant monomer forms in Parkinson's disease: a molecular dynamics study.Semantic proximity Read ↗

DJ‐1 colocalizes with tau inclusions: A link between parkinsonism and dementiaSemantic proximity Read ↗

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