Evidence map›Paper›PMID 29844450›Full record

ArticleScientific reports2018

Oleuropein aglycone stabilizes the monomeric α-synuclein and favours the growth of non-toxic aggregates.

Luana Palazzi, Elena Bruzzone, Giovanni Bisello, Manuela Leri, Massimo Stefani, Monica Bucciantini, Patrizia Polverino de Laureto

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
7.0field-weighted citation impact, top 3% of its field
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

35 citing papers in PubMed, 78 citations in OpenAlex.

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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

7 authors at 2 institutions in 1 country.

Luana PalazziDepartment of Pharmaceutical Sciences, CRIBI Biotechnology Centre, University of Padova, Padova, Italy.
Elena BruzzoneDepartment of Biomedical, Experimental and Clinical Sciences, University of Firenze, Firenze, Italy.
Giovanni BiselloDepartment of Pharmaceutical Sciences, CRIBI Biotechnology Centre, University of Padova, Padova, Italy.
Manuela LeriDepartment of Biomedical, Experimental and Clinical Sciences, University of Firenze, Firenze, Italy.
Massimo StefaniDepartment of Biomedical, Experimental and Clinical Sciences, University of Firenze, Firenze, Italy.
Monica BucciantiniDepartment of Biomedical, Experimental and Clinical Sciences, University of Firenze, Firenze, Italy. monica.bucciantini@unifi.it.
Patrizia Polverino de LauretoDepartment of Pharmaceutical Sciences, CRIBI Biotechnology Centre, University of Padova, Padova, Italy. patrizia.polverinodelaureto@unipd.it.
University of Florence · ITUniversity of Padua · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-synuclein plays a key role in the pathogenesis of Parkinson's disease (PD); its deposits are found as amyloid fibrils in Lewy bodies and Lewy neurites, the histopathological hallmarks of PD. Amyloid fibrillation is a progressive polymerization path starting from peptide/protein misfolding and proceeding through the transient growth of oligomeric intermediates widely considered as the most toxic species. Consequently, a promising approach of intervention against PD might be preventing α-synuclein build-up, misfolding and aggregation. A possible strategy involves the use of small molecules able to slow down the aggregation process or to alter oligomer conformation favouring the growth of non-pathogenic species. Here, we show that oleuropein aglycone (OleA), the main olive oil polyphenol, exhibits anti-amyloidogenic power in vitro by interacting with, and stabilizing, α-synuclein monomers thus hampering the growth of on-pathway oligomers and favouring the growth of stable and harmless aggregates with no tendency to evolve into other cytotoxic amyloids. We investigated the molecular basis of such interference by both biophysical techniques and limited proteolysis; aggregate morphology was monitored by electron microscopy. We also found that OleA reduces the cytotoxicity of α-synuclein aggregates by hindering their binding to cell membrane components and preventing the resulting oxidative damage to cells.

Identifiers

PMID29844450
PMCPMC5974307
OpenAlexW2805550368

What OpenQuestion holds

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LicenceCC BY
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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.