Evidence map›Paper›PMID 29064079›Full record

ReviewCell and tissue research2018

Molecular mechanisms of α-synuclein and GBA1 in Parkinson's disease.

Iva Stojkovska, Dimitri Krainc, Joseph R Mazzulli

Abstract readReview
In one paragraph

Review in Cell and tissue research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
6.3field-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

58 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
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  7. Article
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  9. Review
  10. Article
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  12. 2024 Alzheimer's disease facts and figures.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2024
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Polygenic Parkinson's Disease Genetic Risk Score as Risk Modifier of Parkinsonism in Gaucher Disease.Movement disorders : official journal of the Movement Disorder Society · 2023
    Article
  19. Article
  20. Mesoporous silica nanoparticles: Their potential as drug delivery carriers and nanoscavengers in Alzheimer's and Parkinson's diseases.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2023
    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.

Iva StojkovskaThe Ken and Ruth Davee Department of Neurology, Northwestern University Feinberg School of Medicine, 303 E. Chicago Ave, Ward 12-369, Chicago, IL, 60611, USA.
Dimitri KraincThe Ken and Ruth Davee Department of Neurology, Northwestern University Feinberg School of Medicine, 303 E. Chicago Ave, Ward 12-369, Chicago, IL, 60611, USA.
Joseph R MazzulliThe Ken and Ruth Davee Department of Neurology, Northwestern University Feinberg School of Medicine, 303 E. Chicago Ave, Ward 12-369, Chicago, IL, 60611, USA. jmazzulli@northwestern.edu.
Northwestern University · US

Funding

The role of a-synuclein accumulation in lysosomal hydrolase trafficking and functionR01NS092823 · NINDS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Joseph R Mazzulli · 2015 to 2026
$4.8M
The Role of Lysosomal Glucocerebrosidase in SynucleinopathiesR01NS076054 · NINDS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI KRAINC, DIMITRI · 2011 to 2020
$4.1M
NINDS NIH HHS R01 NS076054NINDS NIH HHS R01 NS092823
6 · The paper itself

Abstract

Parkinson's disease (PD) is a neurodegenerative movement disorder characterized pathologically by the presence of Lewy bodies comprised of insoluble alpha (α)-synuclein. Pathological, clinical and genetic studies demonstrate that mutations in the GBA1 gene, which encodes the lysosomal enzyme glucocerebrosidase (GCase) that is deficient in Gaucher's disease, are important risk factors for the development of PD. The molecular mechanism for the association between these two diseases is not completely understood. We discuss several possible mechanisms that may lead to GBA1-related neuronal death and α-synuclein accumulation including disruptions in lipid metabolism, protein trafficking and impaired protein quality control mechanisms. Elucidating the mechanism between GCase and α-synuclein may provide insight into potential therapeutic pathways for PD and related synucleinopathies.

Indexed as

alpha-SynucleinAnimalsGlucosylceramidaseHumansLysosomesModels, BiologicalMutationParkinson Diseasealpha-SynucleinGlucosylceramidaseAlpha (α)-synucleinGlucosylceramideLysosomal dysfunctionNeurodegenerationProtein aggregation

Identifiers

PMID29064079
PMCPMC5916529
OpenAlexW2765638828

What OpenQuestion holds

Textmetadata
LicenceTDM
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.