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

Structural and Functional Insights into α-Synuclein Fibril Polymorphism

28 Sept 2021

Abstract excerpt

Abnormal accumulation of aggregated α-synuclein (α-Syn) is seen in a variety of neurodegenerative diseases, including Parkinson's disease (PD), multiple system atrophy (MSA), dementia with Lewy body (DLB), Parkinson's disease dementia (PDD), and even subsets of Alzheimer's disease (AD) showing Lewy-body-like pathology. These synucleinopathies exhibit differences in their clinical and pathological representations,...

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 diseases and metabolism
Share to Parkinson's Disease Mechanisms and Treatments

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 34680054
DOI: 10.3390/biom11101419

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and Functional Insights into α-Synuclein Fibril PolymorphismPMID 34680054Read ↗

ɑ-Synuclein strains and the variable pathologies of synucleinopathies.Semantic proximity Read ↗

α-Synuclein strains that cause distinct pathologies differentially inhibit proteasomeSemantic proximity Read ↗

α-Synuclein strains cause distinct synucleinopathies after local and systemic administration.Semantic proximity Read ↗

Stochastic misfolding drives the emergence of distinct α-synuclein strains.Semantic proximity Read ↗

Stochastic Misfolding Drives the Emergence of Distinct α-Synuclein StrainsSemantic proximity Read ↗

Initiation and progression of α-synuclein pathology in Parkinson’s diseaseSemantic proximity Read ↗

Phenotypic manifestation of α-synuclein strains derived from Parkinson's disease and multiple system atrophy in human dopaminergic neurons.Semantic proximity Read ↗

Distinct α-Synuclein strains and implications for heterogeneity among α-SynucleinopathiesSemantic proximity Read ↗

Structural heterogeneity of α-synuclein fibrils amplified from patient brain extractsSemantic proximity Read ↗

α-Synuclein Conformational Strains as Drivers of Phenotypic Heterogeneity in Neurodegenerative DiseasesSemantic proximity Read ↗

Pre‐fibrillar α‐synuclein variants with impaired β‐structure increase neurotoxicity in Parkinson's disease modelsSemantic proximity Read ↗

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

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