Evidence map›Paper›PMID 29941855›Full record

ReviewMolecules (Basel, Switzerland)2018

α-Synuclein and Polyunsaturated Fatty Acids: Molecular Basis of the Interaction and Implication in Neurodegeneration.

Chiara Fecchio, Luana Palazzi, Patrizia Polverino de Laureto

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed, 1 pooled it
5.3field-weighted citation impact, top 4% 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

47 citing papers in PubMed, 1 synthesis or guideline pooled it, 68 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Parkinson disease is a fatty acidopathy.Nature reviews. Neurology · 2025
    Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. The Contribution of Type 2 Diabetes to Parkinson's Disease Aetiology.International journal of molecular sciences · 2024
    Review
  17. Liquid-liquid phase separation and conformational strains ofFrontiers in molecular neuroscience · 2024
    Review
  18. Review
  19. Lipid-induced polymorphic amyloid fibril formation by α-synuclein.Protein science : a publication of the Protein Society · 2023
    Article
  20. Review
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

3 authors at 1 institution in 1 country.

Chiara FecchioDepartment of Biomedical Sciences, University of Padova; Padova 35131, Italy. chiara.fecchio@bio.unipd.it.
Luana PalazziDepartment of Pharmaceutical and Pharmacological Sciences, CRIBI, University of Padova; Padova 35131, Italy. luana.palazzi@unipd.it.
Patrizia Polverino de LauretoDepartment of Pharmaceutical and Pharmacological Sciences, CRIBI, University of Padova; Padova 35131, Italy. patrizia.polverinodelaureto@unipd.it.ORCID 0000-0002-0367-6781
University of Padua · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Synuclein (α-syn) is a 140-amino acid protein, the physiological function of which has yet to be clarified. It is involved in several neurodegenerative disorders, and the interaction of the protein with brain lipids plays an important role in the pathogenesis of Parkinson's disease (PD). Polyunsaturated fatty acids (PUFA) are highly abundant in the brain where they play critical roles in neuronal membrane fluidity and permeability, serve as energy reserves and function as second messengers in cell signaling. PUFA concentration and composition in the brain are altered with age when also an increase of lipid peroxidation is observed. Considering that PD is clearly correlated with oxidative stress, PUFA abundance and composition became of great interest in neurodegeneration studies because of PUFA's high propensity to oxidize. The high levels of the PUFA docosahexaenoic acid (DHA) in brain areas containing α-syn inclusions in patients with PD further support the hypothesis of possible interactions between α-syn and DHA. Additionally, a possible functional role of α-syn in sequestering the early peroxidation products of fatty acids was recently proposed. Here, we provide an overview of the current knowledge regarding the molecular interactions between α-syn and fatty acids and the effect exerted by the protein on their oxidative state. We highlight recent findings supporting a neuroprotective role of the protein, linking α-syn, altered lipid composition in neurodegenerative disorders and PD development.

Indexed as

alpha-SynucleinAnimalsFatty Acids, UnsaturatedHumansNeurodegenerative DiseasesParkinson Diseasealpha-SynucleinFatty Acids, Unsaturatedalpha-synucleinneurodegenerationParkinson’s diseasepolyunsaturated fatty acids

Identifiers

PMID29941855
PMCPMC6099649
OpenAlexW2809493245

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.