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

Alpha-Synuclein conformation affects its tyrosine-dependent oxidative aggregation.

Biochemistry - 23 Dec 2008

Ruf Rebecca A S, Lutz Evan A, Zigoneanu Imola G, Pielak Gary J

Abstract excerpt

Oxidative stress and aggregation of the protein alpha-synuclein are thought to be key factors in Parkinson's disease. Previous work shows that cytochrome c with H(2)O(2) causes tyrosine-dependent in vitro peroxidative aggregation of proteins, including alpha-synuclein. Here, we examine the role of each of alpha-synuclein's four tyrosine residues and how the protein's conformation affects covalent oxidative...

Read the complete abstract on PubMed

Topics

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

Share to Cytochromes c
Share to alpha-Synuclein
Share to Hydrogen Peroxide

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Conformation

Share to Oxygen

Share to Parkinson Disease

Share to Protein Denaturation

Share to Tyrosine

Source

Open in PubMed Open full text

Identifiers

PMID: 19049426
DOI: 10.1021/bi801884z
PMCID: PMC2645542

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

Alpha-Synuclein conformation affects its tyrosine-dependent oxidative aggregation.PMID 19049426Read ↗

Post-aggregation oxidation of mutant huntingtin controls the interactions between aggregates.Semantic proximity Read ↗

Unfolding Sequence-Specific Enigma in Monomeric α-Synuclein: Implications for Parkinson's Disease.Semantic proximity Read ↗

Tyrosine-to-cysteine modification of human alpha-synuclein enhances protein aggregation and cellular toxicity.Semantic proximity Read ↗

Increased Oxidative Stress Exacerbates α-Synuclein Aggregation In VivoSemantic proximity Read ↗

Methionine oxidation stabilizes non-toxic oligomers of alpha-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions.Semantic proximity Read ↗

Allostery in a disordered protein: oxidative modifications to α-synuclein act distally to regulate membrane binding.Semantic proximity Read ↗

Alpha-synuclein facilitates the toxicity of oxidized catechol metabolites: implications for selective neurodegeneration in Parkinson's disease.Semantic proximity Read ↗

Cross-talk between redox signalling and protein aggregationSemantic proximity Read ↗

The effect of tyrosine residues on α-synuclein fibrillation.Semantic proximity Read ↗

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

Effect of single amino acid substitution on oxidative modifications of the Parkinson's disease-related protein, DJ-1.Semantic proximity Read ↗

Human SOD2 modification by dopamine quinones affects enzymatic activity by promoting its aggregation: possible implications for Parkinson's disease.Semantic proximity Read ↗

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