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

The role of alpha-synuclein oligomerization and aggregation in cellular and animal models of Parkinson's disease.

PloS one - 1 Jan 2012

Wan Oi Wan, Chung Kenny K K

Abstract excerpt

α-Synuclein (α-syn) is a synaptic protein in which four mutations (A53T, A30P, E46K and gene triplication) have been found to cause an autosomal dominant form of Parkinson's disease (PD). It is also the major component of intraneuronal protein aggregates, designated as Lewy bodies (LBs), a prominent pathological hallmark of PD. How α-syn contributes to LB formation and PD is still not well-understood. It has been...

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 Chromatography, Gel
Share to Lewy Bodies

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microscopy, Atomic Force

Share to Microscopy, Electron, Transmission

Share to Models, Animal

Share to Polymerization

Share to Substantia Nigra

Source

Open in PubMed Open full text

Identifiers

PMID: 22701661
DOI: 10.1371/journal.pone.0038545
PMCID: PMC3373518

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

The role of alpha-synuclein oligomerization and aggregation in cellular and animal models of Parkinson's disease.PMID 22701661Read ↗

Alteration of Structure and Aggregation of α-Synuclein by Familial Parkinson's Disease Associated Mutations.Semantic proximity Read ↗

In vitro models of synucleinopathies: informing on molecular mechanisms and protective strategiesSemantic proximity Read ↗

Alpha-synuclein at the intracellular and the extracellular side: functional and dysfunctional implications.Semantic proximity Read ↗

Loss of functional alpha-synuclein: a toxic event in Parkinson's disease?Semantic proximity Read ↗

Cellular models of alpha‐synuclein toxicity and aggregationSemantic proximity Read ↗

Alpha-synuclein dysfunction in Lewy body diseases.Semantic proximity Read ↗

Structure, function and toxicity of alpha-synuclein: the Bermuda triangle in synucleinopathies.Semantic proximity Read ↗

Molecular mechanisms of alpha-synuclein neurodegeneration.Semantic proximity Read ↗

Alpha-synuclein: its biological function and role in neurodegenerative diseases.Semantic proximity Read ↗

Seeking a mechanism for the toxicity of oligomeric α-synuclein.Semantic proximity Read ↗

Parkinson's disease and alpha synuclein: is Parkinson's disease a prion-like disorder?Semantic proximity Read ↗

Alpha-Synuclein in Parkinson’s Disease: From Pathogenetic Dysfunction to Potential Clinical ApplicationSemantic proximity Read ↗

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