Evidence map›Paper›PMID 32256340›Full record

ArticleFrontiers in aging neuroscience2020

Protein-Protein Interactions in Alpha-Synuclein Biogenesis: New Potential Targets in Parkinson's Disease.

Sarah M Hernandez, Elena B Tikhonova, Andrey L Karamyshev

Open access · goldAbstract read
In one paragraph

Article in Frontiers in aging neuroscience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.6field-weighted citation impact, top 8% 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

18 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  7. Synucleinopathies: Intrinsic and Extrinsic Factors.Cell biochemistry and biophysics · 2023
    Article
  8. Review
  9. SUMO1 hinders α-Synuclein fibrillation by inducing structural compaction.Protein science : a publication of the Protein Society · 2023
    Article
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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

3 authors at 2 institutions in 1 country.

Sarah M HernandezDepartment of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX, United States.
Elena B TikhonovaDepartment of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX, United States.
Andrey L KaramyshevDepartment of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX, United States.
Texas Tech University Health Sciences Center · USTexas Tech University · US

Funding

Regulation of Aberrant Protein ProductionR01GM135167 · NIGMS · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI KARAMYSHEV, ANDREY L · 2019 to 2022
$1.3M
Identification of Translational Regulators of alpha-Synuclein Folding and AggregationR03NS102645 · NINDS · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI KARAMYSHEV, ANDREY L · 2018 to 2019
$153k
NIGMS NIH HHS R01 GM135167NINDS NIH HHS R03 NS102645
6 · The paper itself

Abstract

Parkinson's disease (PD) is a debilitating neurodegenerative disorder defined by a loss of dopamine-producing neurons in the substantia nigra in the brain. It is associated with cytosolic inclusions known as Lewy bodies. The major component of Lewy bodies is aggregated alpha-synuclein. The molecular mechanism of alpha-synuclein aggregation is not known. Our conceptual model is that alpha-synuclein aggregates due to a dysregulation of its interactions with other protein partners that are required for its biogenesis. In this mini review article, we identified alpha-synuclein interactions using both current literature and predictive pathway analysis. Alterations of these interactions may be crucial elements for the molecular mechanism of the protein aggregation and related pathology in the disease. Identification of alpha-synuclein interactions provides valuable tools to understand PD pathology and find new pharmacological targets for disease treatment.

Indexed as

alpha-synucleindisease-causing mutationsneurodegenerative diseasesParkinson’s diseaseprotein misfoldingprotein-protein interactionsprotein quality controltranslational control

Identifiers

PMID32256340
PMCPMC7092629
OpenAlexW3011664285

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.