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

Reduced anti-oxidative stress activities of DJ-1 mutants found in Parkinson's disease patients.

Biochemical and biophysical research communications - 23 Jul 2004

Takahashi-Niki Kazuko, Niki Takeshi, Taira Takahiro, Iguchi-Ariga Sanae M M, Ariga Hiroyoshi

Abstract excerpt

DJ-1 is a multi-functional protein that plays roles in transcriptional regulation and anti-oxidative stress, and loss of its function is thought to result in onset of Parkinson's disease. We have previously reported that L166P, a mutant DJ-1 found in Parkinson's disease patients, had no activity to prevent hydrogen peroxide (H2O2)-induced cell death. In this study, we analyzed other mutants of DJ-1 found in...

Read the complete abstract on PubMed

Topics

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

Share to 3T3 Cells
Share to Cell Death

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to Hydrogen Peroxide

Share to Oncogene Proteins

Share to Oxidative Stress

Share to Parkinson Disease

Share to Protein Deglycase DJ-1

Source

Identifiers

PMID: 15219840
DOI: 10.1016/j.bbrc.2004.05.187

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Reduced anti-oxidative stress activities of DJ-1 mutants found in Parkinson's disease patients.PMID 15219840Read ↗

Familial Parkinson's disease-associated L166P mutation disrupts DJ-1 protein folding and function.Semantic proximity Read ↗

DJ-1 has a role in antioxidative stress to prevent cell death.Semantic proximity Read ↗

Loss of function of DJ-1 triggered by Parkinson's disease-associated mutation is due to proteolytic resistance to caspase-6.Semantic proximity Read ↗

Monomer DJ-1 and its N-terminal sequence are necessary for mitochondrial localization of DJ-1 mutants.Semantic proximity Read ↗

Parkinson disease protein DJ-1 converts from a zymogen to a protease by carboxyl-terminal cleavage.Semantic proximity Read ↗

Differential effects of Parkinson's disease-associated mutations on stability and folding of DJ-1.Semantic proximity Read ↗

Mutational analysis of DJ-1 in <i>Drosophila</i> implicates functional inactivation by oxidative damage and agingSemantic proximity Read ↗

Down regulation of DJ-1 enhances cell death by oxidative stress, ER stress, and proteasome inhibition.Semantic proximity Read ↗

L10p and P158DEL DJ-1 mutations cause protein instability, aggregation, and dimerization impairments.Semantic proximity Read ↗

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

L166P mutant DJ-1 promotes cell death by dissociating Bax from mitochondrial Bcl-XL.Semantic proximity Read ↗

L166P mutant DJ-1, causative for recessive Parkinson's disease, is degraded through the ubiquitin-proteasome system.Semantic proximity Read ↗

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