Evidence map›Paper›PMID 37781241›Full record

ReviewFrontiers in neuroscience2023

Liquid-liquid phase separation regulates alpha-synuclein aggregate and mitophagy in Parkinson's disease.

Kaiying Hou, Tingting Liu, Jingwen Li, Meiyan Xian, Lin Sun, Jianshe Wei

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in neuroscience, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

13 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Roles of mitophagy and immune infiltration in Parkinson's disease: new perspectives from bioinformatics analysis and A53T transgenic mice.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
    Article
  5. Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Liquid-liquid phase separation and conformational strains ofFrontiers in molecular neuroscience · 2024
    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

6 authors at 1 institution in 1 country.

Kaiying HouSchool of Life Sciences, Henan University, Kaifeng, China.
Tingting LiuSchool of Life Sciences, Henan University, Kaifeng, China.
Jingwen LiSchool of Life Sciences, Henan University, Kaifeng, China.
Meiyan XianSchool of Life Sciences, Henan University, Kaifeng, China.
Lin SunCollege of Chemistry and Molecular Sciences, Henan University, Kaifeng, China.
Jianshe WeiSchool of Life Sciences, Henan University, Kaifeng, China.
Henan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Parkinson's disease (PD) is the second most common neurodegenerative disease in the world, and alpha-synuclein (α-syn) abnormal aggregate and mitochondrial dysfunction play a crucial role in its pathological development. Recent studies have revealed that proteins can form condensates through liquid-liquid phase separation (LLPS), and LLPS has been found to be widely present in α-syn aberrant aggregate and mitophagy-related protein physiological processes. This review summarizes the occurrence of α-syn LLPS and its influencing factors, introduces the production and transformation of the related protein LLPS during PINK1-Parkin-mediated mitophagy, hoping to provide new ideas and methods for the study of PD pathology.

Indexed as

alpha-synucleinliquid-liquid phase separationmitophagyParkinson’s diseasePINK1-Parkin

Identifiers

PMID37781241
PMCPMC10536155
OpenAlexW4386751298

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.