Evidence map›Paper›PMID 41507378›Full record

ArticleCommunications biology2026

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

Sneha Jos, Niharika Shivanandaswamy, Akshya Sharma, Thazhe Kootteri Prasad, Rachana Kashyap, Neelagandan Kamariah, M M Srinivas Bharath, Deepak Sharma, Sangeeta Nath, Balasundaram Padmanabhan and 1 more

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Article in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

11 authors.

Sneha JosDepartment of Biophysics, National Institute of Mental Health and Neurosciences, Bengaluru, India.
Niharika ShivanandaswamyDepartment of Biophysics, National Institute of Mental Health and Neurosciences, Bengaluru, India.
Akshya SharmaCSIR-Institute of Microbial Technology, Chandigarh, India.
Thazhe Kootteri PrasadCentre for Chemical Biology and Therapeutics, Institute for Stem Cell Science and Regenerative Medicine, Bengaluru, India.ORCID http://orcid.org/0000-0002-0524-8000
Rachana KashyapManipal Institute of Regenerative Medicine, Bengaluru, Manipal Academy of Higher Education, Manipal, India.
Neelagandan KamariahCentre for Chemical Biology and Therapeutics, Institute for Stem Cell Science and Regenerative Medicine, Bengaluru, India.
M M Srinivas BharathDepartment of Clinical Psychopharmacology and Neurotoxicology, National Institute of Mental Health and Neurosciences, Bengaluru, India.
Deepak SharmaCSIR-Institute of Microbial Technology, Chandigarh, India.
Sangeeta NathManipal Institute of Regenerative Medicine, Bengaluru, Manipal Academy of Higher Education, Manipal, India.ORCID http://orcid.org/0000-0003-0050-0606
Balasundaram PadmanabhanDepartment of Biophysics, National Institute of Mental Health and Neurosciences, Bengaluru, India.ORCID http://orcid.org/0000-0001-8434-828X
Sivaraman PadavattanDepartment of Biophysics, National Institute of Mental Health and Neurosciences, Bengaluru, India. s.padavattan@gmail.com.ORCID http://orcid.org/0000-0002-1732-5421

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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, proteins constantly encounter one another, but functional protein-protein interactions must outweigh disease-causing 'hydrophobicity' driven non-functional interactions. Although αSyn wild-type (

Indexed as

alpha-SynucleinLewy BodiesParkinson DiseaseHumansHydrophobic and Hydrophilic InteractionsMutationPhosphorylationProtein Aggregation, PathologicalProtein Bindingalpha-Synuclein

Identifiers

PMID41507378
PMCPMC12877186

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.