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Article

Dimerization of Parkinson's disease-causing DJ-1 and formation of high molecular weight complexes in human brain

28 Sept 2004

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Share to Neurological diseases and metabolism
Share to Nuclear Receptors and Signaling
Share to Parkinson's Disease Mechanisms and Treatments

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 15519239
DOI: 10.1016/j.mcn.2004.06.014

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Related research

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Dimerization of Parkinson's disease-causing DJ-1 and formation of high molecular weight complexes in human brainPMID 15519239Read ↗

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

Role of DJ-1 in parkinson’s diseaseSemantic proximity Read ↗

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

Structural Biology of the DJ-1 Superfamily.Semantic proximity Read ↗

The Tale of DJ-1 (PARK7): A Swiss Army Knife in Biomedical and Psychological ResearchSemantic proximity Read ↗

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

Plasma levels of DJ-1 as a possible marker for progression of sporadic Parkinson's diseaseSemantic proximity Read ↗

On the oligomeric state of DJ-1 protein and its mutants associated with Parkinson Disease. A combined computational and in vitro study.Semantic proximity Read ↗

Aggresome-forming TTRAP mediates pro-apoptotic properties of Parkinson's disease-associated DJ-1 missense mutationsSemantic proximity Read ↗

DJ-1 binds to mitochondrial complex I and maintains its activitySemantic proximity Read ↗

The DJ-1L166P mutant protein associated with early onset Parkinson's disease is unstable and forms higher-order protein complexes.Semantic proximity Read ↗

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

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