Evidence map›Paper›PMID 37214999›Full record

ArticlebioRxiv : the preprint server for biology2023

SARS-COV-2 Spike Protein Fragment eases Amyloidogenesis of α-Synuclein.

Andrew D Chesney, Buddhadev Maiti, Ulrich H E Hansmann

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. 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, 0 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Andrew D ChesneyDepartment of Chemistry & Biochemistry, University of Oklahoma, Norman, OK 73019, USA.
Buddhadev MaitiDepartment of Chemistry & Biochemistry, University of Oklahoma, Norman, OK 73019, USA.
Ulrich H E HansmannDepartment of Chemistry & Biochemistry, University of Oklahoma, Norman, OK 73019, USA.
University of Oklahoma · US

Funding

Structural Transitions in Proteins and Protein AssembliesR01GM120634 · NIGMS · UNIVERSITY OF OKLAHOMA · PI HANSMANN, ULRICH H.E. · 2017 to 2020
$1.2M
NIGMS NIH HHS R01 GM120634
6 · The paper itself

Abstract

Parkinson's Disease is accompanied by presence of amyloids in the brain formed of α-synuclein chains. Correlation between COVID-19 and the onset of Parkinson's disease let to the idea that amyloidogenic segments in SARS-COV-2 proteins can induce aggregation of α-synuclein. Using molecular dynamic simulations, we show that the fragment FKNIDGYFKI of the spike protein, which is unique for SARS-COV-2, shifts preferentially the ensemble of α-synuclein monomer towards rod-like fibril seeding conformations, and at the same time stabilizes differentially this polymorph over the competing twister-like structure. Our results are compared with earlier work relying on a different protein fragment that is not specific for SARS-COV-2.

Identifiers

PMID37214999
PMCPMC10197603
OpenAlexW4375951479

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

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.