Evidence map›Paper›PMID 32210767›Full record

ReviewFrontiers in cellular neuroscience2020

Proteostasis of α-Synuclein and Its Role in the Pathogenesis of Parkinson's Disease.

Deqiang Han, Wei Zheng, Xueyao Wang, Zhiguo Chen

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in cellular neuroscience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.0field-weighted citation impact, top 11% 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

27 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
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  7. Organosulfur Compounds: Potential Therapeutics for Parkinson's Disease.CNS & neurological disorders drug targets · 2026
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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

4 authors at 2 institutions in 1 country.

Deqiang HanKey Laboratory of Neurodegenerative Diseases, Ministry of Education, Cell Therapy Center, National Clinical Research Center for Geriatric Diseases, Beijing Institute of Geriatrics, Xuanwu Hospital Capital Medical University, Beijing, China.
Wei ZhengKey Laboratory of Neurodegenerative Diseases, Ministry of Education, Cell Therapy Center, National Clinical Research Center for Geriatric Diseases, Beijing Institute of Geriatrics, Xuanwu Hospital Capital Medical University, Beijing, China.
Xueyao WangKey Laboratory of Neurodegenerative Diseases, Ministry of Education, Cell Therapy Center, National Clinical Research Center for Geriatric Diseases, Beijing Institute of Geriatrics, Xuanwu Hospital Capital Medical University, Beijing, China.
Zhiguo ChenKey Laboratory of Neurodegenerative Diseases, Ministry of Education, Cell Therapy Center, National Clinical Research Center for Geriatric Diseases, Beijing Institute of Geriatrics, Xuanwu Hospital Capital Medical University, Beijing, China.
Capital Medical University · CNChinese Institute for Brain Research · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aggregation of α-Synuclein, possibly caused by disturbance of proteostasis, has been identified as a common pathological feature of Parkinson's disease (PD). However, the initiating events of aggregation have not been fully illustrated, and this knowledge may be critical to understanding the disease mechanisms of PD. Proteostasis is essential in maintaining normal cellular metabolic functions, which regulate the synthesis, folding, trafficking, and degradation of proteins. The toxicity of the aggregating proteins is dramatically influenced by its physical and physiological status. Genetic mutations may also affect the metastable phase transition of proteins. In addition, neuroinflammation, as well as lipid metabolism and its interaction with α-Synuclein, are likely to contribute to the pathogenesis of PD. In this review article, we will highlight recent progress regarding α-Synuclein proteostasis in the context of PD. We will also discuss how the phase transition status of α-Synuclein could correlate with different functional consequences in PD.

Indexed as

genetic mutationsinflammationParkinson’s diseasephase transitionproteostasisα-synuclein

Identifiers

PMID32210767
PMCPMC7075857
OpenAlexW3011214836

What OpenQuestion holds

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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.