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

Single-Molecule Fingerprinting Reveals Different Growth Mechanisms in Seed Amplification Assays for Different Polymorphs of α-Synuclein Fibrils

28 Aug 2024

Abstract excerpt

High Resolution Image Download MS PowerPoint Slide α-Synuclein (αSyn) aggregates, detected in the biofluids of patients with Parkinson’s disease (PD), have the ability to catalyze their own aggregation, leading to an increase in the number and size of aggregates. This self-templated amplification is used by newly developed assays to diagnose Parkinson’s disease and turns the presence of αSyn aggregates into a...

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 Biotin and Related Studies
Share to Parkinson's Disease Mechanisms and Treatments

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 39197832
DOI: 10.1021/acschemneuro.4c00185

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 10 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Single-Molecule Fingerprinting Reveals Different Growth Mechanisms in Seed Amplification Assays for Different Polymorphs of α-Synuclein FibrilsPMID 39197832Read ↗

Single molecule fingerprinting reveals different growth mechanisms in seed amplification assays for different polymorphs of αSynuclein fibrilsSemantic proximity Read ↗

Brain-derived and in vitro-seeded alpha-synuclein fibrils exhibit distinct biophysical profilesSemantic proximity Read ↗

Distinct alpha-synuclein strains derived from Parkinson’s disease patient tissues trigger differential inclusion pathology in a novel biosensor cell modelSemantic proximity Read ↗

Emergence of stealth polymorphs that escape α-synuclein amyloid monitoring, take over and acutely spread in neuronsSemantic proximity Read ↗

α-Synuclein: A Promising Biomarker for Parkinson’s Disease and Related DisordersSemantic proximity Read ↗

The α-Synuclein Seeding Amplification Assay for Parkinson’s DiseaseSemantic proximity Read ↗

An automated workflow for quantifying the formation of synuclein aggregates in human dopaminergic neuronsSemantic proximity Read ↗

Secondary nucleation of α-Synuclein drives Mitochondria dysfunctions and Lewy body formation in Parkinson’s DiseaseSemantic proximity Read ↗

A novel approach to evaluate alpha-synuclein seeding shows a wide heterogeneity in multiple system atrophySemantic proximity Read ↗

Kinetic control in amyloid polymorphism: Different agitation and solution conditions promote distinct amyloid polymorphs of alpha-synucleinSemantic proximity Read ↗

Association of Misfolded α-Synuclein Derived from Neuronal Exosomes in Blood with Parkinson’s Disease Diagnosis and DurationSemantic proximity Read ↗

Secondary nucleation of α-Synuclein drives Mitochondria dysfunctions and Lewy body formation in Parkinson’s DiseaseSemantic proximity Read ↗

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