Evidence map›Paper›PMID 35733294›Full record

ReviewBMB reports2022

Role of post-translational modifications on the alpha-synuclein aggregation-related pathogenesis of Parkinson's disease.

Hajung Yoo, Jeongmin Lee, Bokwang Kim, Heechang Moon, Huisu Jeong, Kyungmi Lee, Woo Jeung Song, Junho K Hur, Yohan Oh

Open access · goldAbstract readReview
PubMed Full text at PMC
In one paragraph

Review in BMB reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  14. Article
  15. Review
  16. Liquid-liquid phase separation and conformational strains ofFrontiers in molecular neuroscience · 2024
    Review
  17. Alpha Synuclein: Neurodegeneration and Inflammation.International journal of molecular sciences · 2023
    Review
  18. Disease-relevant βNature communications · 2023
    Article
  19. 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

9 authors at 1 institution in 1 country.

Hajung YooDepartment of Biomedical Science, Graduate School of Biomedical Science and Engineering, Hanyang University, Seoul 04763, Korea.
Jeongmin LeeDepartment of Biomedical Science, Graduate School of Biomedical Science and Engineering, Hanyang University, Seoul 04763, Korea.
Bokwang KimDepartment of Biomedical Science, Graduate School of Biomedical Science and Engineering, Hanyang University, Seoul 04763, Korea.
Heechang MoonDepartment of Biomedical Science, Graduate School of Biomedical Science and Engineering, Hanyang University, Seoul 04763, Korea.
Huisu JeongDepartment of Biomedical Science, Graduate School of Biomedical Science and Engineering, Hanyang University, Seoul 04763, Korea.
Kyungmi LeeDepartment of Medicine, College of Medicine, Hanyang University, Seoul 04763, Korea.
Woo Jeung SongDepartment of Medical Genetics, College of Medicine, Hanyang University, Seoul 04763, Korea.
Junho K HurDepartment of Biomedical Science, Graduate School of Biomedical Science and Engineering, Hanyang University, Seoul 04763; Department of Medical Genetics, College of Medicine, Hanyang University, Seoul 04763; Hanyang Institute of Bioscience and Biotechnology, Hanyang University, Seoul 04763, Korea.
Yohan OhDepartment of Biomedical Science, Graduate School of Biomedical Science and Engineering, Hanyang University, Seoul 04763; Hanyang Institute of Bioscience and Biotechnology, Hanyang University, Seoul 04763; Department of Biochemistry and Molecular Biology, College of Medicine, Hanyang University, Seoul 04763, Korea.
Hanyang University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Together with neuronal loss, the existence of insoluble inclusions of alpha-synuclein (α-syn) in the brain is widely accepted as a hallmark of synucleinopathies including Parkinson's disease (PD), multiple system atrophy, and dementia with Lewy body. Because the α-syn aggregates are deeply involved in the pathogenesis, there have been many attempts to demonstrate the mechanism of the aggregation and its potential causative factors including post-translational modifications (PTMs). Although no concrete conclusions have been made based on the previous study results, growing evidence suggests that modifications such as phosphorylation and ubiquitination can alter α-syn characteristics to have certain effects on the aggregation process in PD; either facilitating or inhibiting fibrillization. In the present work, we reviewed studies showing the significant impacts of PTMs on α-syn aggregation. Furthermore, the PTMs modulating α-syn aggregation-induced cell death have been discussed. [BMB Reports 2022; 55(7): 323-335].

Indexed as

alpha-SynucleinParkinson DiseaseHumansLewy BodiesPhosphorylationProtein Processing, Post-Translationalalpha-Synuclein

Identifiers

PMID35733294
PMCPMC9340086
OpenAlexW4283362867

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.