Evidence map›Paper›PMID 34360787›Full record

ReviewInternational journal of molecular sciences2021

Parkinson's Disease: A Prionopathy?

Sarah Vascellari, Aldo Manzin

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Synucleinopathies: Intrinsic and Extrinsic Factors.Cell biochemistry and biophysics · 2023
    Article
  7. Neurobiology of Parkinson's Disease.International journal of molecular sciences · 2023
    Article
  8. Article
  9. Review
  10. Prion Protein: The Molecule of Many Forms and Faces.International journal of molecular sciences · 2022
    Review
  11. Article
  12. 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

2 authors at 1 institution in 1 country.

Sarah VascellariMicrobiology and Virology Unit, Department of Biomedical Sciences, University of Cagliari, 09042 Cagliari, Italy.
Aldo ManzinMicrobiology and Virology Unit, Department of Biomedical Sciences, University of Cagliari, 09042 Cagliari, Italy.ORCID 0000-0003-2961-3428
University of Cagliari · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The principal pathogenic event in Parkinson's disease is characterized by the conformational change of α-synuclein, which form pathological aggregates of misfolded proteins, and then accumulate in intraneuronal inclusions causing dopaminergic neuronal loss in specific brain regions. Over the last few years, a revolutionary theory has correlated Parkinson's disease and other neurological disorders with a shared mechanism, which determines α-synuclein aggregates and progresses in the host in a prion-like manner. In this review, the main characteristics shared between α-synuclein and prion protein are compared and the cofactors that influence the remodeling of native protein structures and pathogenetic mechanisms underlying neurodegeneration are discussed.

Indexed as

Parkinson DiseasePrion DiseasesProtein Aggregatesalpha-SynucleinAnimalsDopaminergic NeuronsHumanstau Proteinsalpha-SynucleinMAPT protein, humanProtein AggregatesSNCA protein, humantau Proteinsgut microbiotaParkinson’s diseaseprion-like mechanismprotein misfolding co-factorsα-synuclein

Identifiers

PMID34360787
PMCPMC8347681
OpenAlexW3183514940

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.