Evidence map›Paper›PMID 41123993›Full record

ArticleACS chemical neuroscience2025

The Effect of SARS-COV-2 Protein Fragments on the Dimerization of α-Synuclein.

Lucy M Coleman, Ulrich H E Hansmann

Abstract read
In one paragraph

Article in ACS chemical neuroscience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Lucy M ColemanDepartment of Chemistry & Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.
Ulrich H E HansmannDepartment of Chemistry & Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.ORCID 0000-0002-0700-4835

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There is evidence that amyloidogenic segments in SARS-COV-2 proteins can induce aggregation of α-synuclein (αS), the main component of brain-located amyloids whose presence is connected with Parkinson's Disease (PD). Using molecular dynamics simulations, we showed in earlier work that SARS-COV-2 protein fragments shift the ensemble of αS chains toward more aggregation-prone conformations. However, the mechanism by which these chains assemble into fibrils, the presumed neurotoxic agents in PD, is not clear. The first step on that route is the formation of dimers. For this reason, we have now, using again molecular dynamics simulations, studied how the fragment

Indexed as

alpha-SynucleinPeptide FragmentsSARS-CoV-2Spike Glycoprotein, CoronavirusCOVID-19HumansMolecular Dynamics SimulationProtein Multimerizationalpha-SynucleinPeptide FragmentsSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2amyloid aggregationdimersmolecular dynamics simulationsParkinson’s diseaseSARS-CoV-2α-synuclein

Identifiers

PMID41123993
PMCPMC12593392

What OpenQuestion holds

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Registered trials

None linked

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.