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

Parkinson's disease-specific α-Synuclein variants potentially drive Lewy body formation by engaging in promiscuous and non-functional interactions.

Communications biology - 8 Jan 2026

Jos Sneha, Shivanandaswamy Niharika, Sharma Akshya, Prasad Thazhe Kootteri, Kashyap Rachana, Kamariah Neelagandan, Bharath M M Srinivas, Sharma Deepak, Nath Sangeeta, Padmanabhan Balasundaram, Padavattan Sivaraman

Abstract excerpt

Lewy bodies (LBs), a pathological hallmark of synucleinopathies, are heterogeneous inclusions that contain α-Synuclein (αSyn) alongside numerous proteins, lipids, and damaged organelles. Current αSyn-fibrillization centric aggregation/phase separation models fail to explain how diverse cellular components are sequestered by disease-specific αSyn variants during LB formation. In the crowded intracellular milieu,...

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 Hydrophobic and Hydrophilic Interactions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lewy Bodies

Share to Mutation

Share to Parkinson Disease

Share to Phosphorylation

Share to Protein Aggregation, Pathological

Share to Protein Binding

Source

Open in PubMed Open full text

Identifiers

PMID: 41507378
DOI: 10.1038/s42003-025-09395-9
PMCID: PMC12877186

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Parkinson's disease-specific α-Synuclein variants potentially drive Lewy body formation by engaging in promiscuous and non-functional interactions.PMID 41507378Read ↗

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

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

Combating deleterious phase transitions in neurodegenerative disease.Semantic proximity Read ↗

Heterotypic droplet formation by pro-inflammatory S100A9 and neurodegenerative disease-related alpha-synucleinSemantic proximity Read ↗

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

α-Synuclein acts as a cholesteryl-ester sensor on lipid droplets regulating organelle size and abundanceSemantic proximity Read ↗

Reconstitution of Helical Soluble α-Synuclein through Transient Interaction with Lipid InterfacesSemantic proximity Read ↗

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

Polyglutamine aggregation in Huntington and related diseases.Semantic proximity Read ↗

Rationally Designed Variants of α-Synuclein Illuminate Its in vivo Structural Properties in Health and DiseaseSemantic proximity Read ↗

Dual effect of α-synuclein disease variants on condensate formationSemantic proximity Read ↗

Distinct Effects of Familial Parkinson's Disease-Associated Mutations on α-Synuclein Phase Separation and Amyloid Aggregation.Semantic proximity Read ↗

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