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

Mechanisms of enhanced aggregation and fibril formation of Parkinson's disease-related variants of α-synuclein.

Scientific reports - 26 Apr 2022

Ohgita Takashi, Namba Norihiro, Kono Hiroki, Shimanouchi Toshinori, Saito Hiroyuki

Abstract excerpt

Aggregation of α-synuclein (α-syn) into amyloid fibrils is closely associated with Parkinson's disease (PD). Familial mutations or posttranslational truncations in α-syn are known as risk factor for PD. Here, we examined the effects of the PD-related A30P or A53T point mutation and C-terminal 123-140 or 104-140 truncation on the aggregating property of α-syn based on the kinetic and thermodynamic analyses....

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 Amyloid
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Parkinson Disease

Share to Point Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 35474118
DOI: 10.1038/s41598-022-10789-6
PMCID: PMC9043213

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mechanisms of enhanced aggregation and fibril formation of Parkinson's disease-related variants of α-synuclein.PMID 35474118Read ↗

Multiplicity of α-Synuclein Aggregated Species and Their Possible Roles in DiseaseSemantic proximity Read ↗

Role of α-Synuclein Regions in Nucleation and Elongation of Amyloid Fiber Assembly.Semantic proximity Read ↗

Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy.Semantic proximity Read ↗

Comparison of Kinetics, Toxicity, Oligomer Formation, and Membrane Binding Capacity of α-Synuclein Familial Mutations at the A53 Site, Including the Newly Discovered A53V Mutation.Semantic proximity Read ↗

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

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

Amyloidogenic 60-71 deletion/ValThr insertion mutation of apolipoprotein A-I generates a new aggregation-prone segment that promotes nucleation through entropic effects.Semantic proximity Read ↗

Divergent effects of the H50Q and G51D SNCA mutations on the aggregation of α-synuclein.Semantic proximity Read ↗

Controlling aggregation propensity in A53T mutant of alpha-synuclein causing Parkinson's disease.Semantic proximity Read ↗

Effect of Disease-Associated P123H and V70M Mutations on β-Synuclein Fibrillation.Semantic proximity Read ↗

Distinct microscopic mechanisms for the accelerated aggregation of pathogenic Tau mutants revealed by kinetic analysis.Semantic proximity Read ↗

The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization.Semantic proximity Read ↗

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