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 emerging role of α-synuclein truncation in aggregation and disease

19 May 2020

Abstract excerpt

α-Synuclein (αsyn) is an abundant brain neuronal protein that can misfold and polymerize to form toxic fibrils coalescing into pathologic inclusions in neurodegenerative diseases, including Parkinson's disease, Lewy body dementia, and multiple system atrophy. These fibrils may induce further αsyn misfolding and propagation of pathologic fibrils in a prion-like process. It is unclear why αsyn initially misfolds,...

Read the complete abstract on PubMed

Topics

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

Share to Alzheimer's disease research and treatments
Share to Neurological disorders and treatments
Share to Parkinson's Disease Mechanisms and Treatments

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 32424039
DOI: 10.1074/jbc.rev120.011743

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The emerging role of α-synuclein truncation in aggregation and diseasePMID 32424039Read ↗

A Facile Method to Produce N-Terminally Truncated α-SynucleinSemantic proximity Read ↗

Carboxy‐terminal truncations of mouse α‐synuclein alter aggregation and prion‐like seedingSemantic proximity Read ↗

Carboxyl truncation of α-synuclein occurs early and is influenced by human APOE genotype in transgenic mouse models of α-synuclein pathogenesisSemantic proximity Read ↗

A precipitating role for truncated alpha-synuclein and the proteasome in alpha-synuclein aggregation: implications for pathogenesis of Parkinson disease.Semantic proximity Read ↗

Alpha-Synuclein in Neurodegeneration: From Shared Biology to Disease-Specific Phenotypes.Semantic proximity Read ↗

Alpha-Synuclein in Neurodegeneration: From Shared Biology to Disease-Specific PhenotypesSemantic proximity Read ↗

The good and bad of therapeutic strategies that directly target α‐synucleinSemantic proximity Read ↗

Navigating the Neurobiology of Parkinson’s: The Impact and Potential of α-SynucleinSemantic proximity Read ↗

Alpha-Synuclein Aggregation and Spread: Implications for the Pathology and Progression of Neurodegenerative DiseasesSemantic proximity Read ↗

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

Alpha-synuclein Toxicity in the Early Secretory Pathway: How It Drives Neurodegeneration in Parkinsons DiseaseSemantic proximity Read ↗

Alpha-Synuclein Post-translational Modifications: Implications for Pathogenesis of Lewy Body DisordersSemantic proximity Read ↗

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