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

Early α-Synuclein Heterodimerization Kinetics Predict Parkinson's Disease Onset.

The journal of physical chemistry. B - 11 Jun 2026

Chaudhary Sachin, Tammara Vaishnavi, Choudhary Bhargavi, Das Atanu

Abstract excerpt

Identifying physicochemical predictors that connect protein aggregation to clinical phenotypes remains challenging. Here, we examine whether simulated aggregation descriptors of the intrinsically disordered protein α-synuclein (αS) relate to the clinical age of onset in Parkinson's disease. Using a multiscale simulation framework, we combine coarse-grained (CG) models to quantify the kinetics of early...

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 Dimerization
Share to Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Parkinson Disease

Share to Protein Multimerization

Share to Thermodynamics

Source

Identifiers

PMID: 42207861
DOI: 10.1021/acs.jpcb.6c00859

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

Early α-Synuclein Heterodimerization Kinetics Predict Parkinson's Disease Onset.PMID 42207861Read ↗

Deciphering the mechanism of protein aggregation and effects of inhibitors using single-molecule mass photometrySemantic proximity Read ↗

Combined Effects of Mutation and Ionic Strength on α-Synuclein Reveal Generic Features of Aggregation-Prone Monomeric States.Semantic proximity Read ↗

Energetic profiling reveals thermodynamic principles underlying amyloid fibril maturationSemantic proximity Read ↗

Beyond Co-Existence: Early α-Synuclein-Amyloid-β42 Association from Molecular Dynamics SimulationsSemantic proximity Read ↗

Missense Mutations Modify the Conformational Ensemble of the α-Synuclein Monomer Which Exhibits a Two-Phase CharacteristicSemantic proximity Read ↗

Aggregation landscapes of Huntingtin exon 1 protein fragments and the critical repeat length for the onset of Huntington’s diseaseSemantic proximity Read ↗

Effects of Mutations and Post-Translational Modifications on α-Synuclein In Vitro Aggregation.Semantic proximity Read ↗

Conformational equilibria in monomeric alpha-synuclein at the single-molecule level.Semantic proximity Read ↗

Distinct Mechanisms Determine α-Synuclein Fibril Morphology during Growth and Maturation.Semantic proximity Read ↗

Aggregation of α-synuclein is kinetically controlled by intramolecular diffusion.Semantic proximity Read ↗

Amyloid assembly is dominated by misregistered kinetic traps on an unbiased energy landscape.Semantic proximity Read ↗

Effects of Mutations on the Reconfiguration Rate of α-Synuclein.Semantic proximity Read ↗

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