Evidence map›Paper›PMID 35692426›Full record

ArticleFrontiers in neuroscience2022

Quiescent Elongation of α-Synuclein Pre-form Fibrils Under Different Solution Conditions.

Hengxu Mao, Yongyi Ye, Xiang Sun, Chen Qian, Baoyan Wang, Linghai Xie, Shizhong Zhang

Open access · goldAbstract read
In one paragraph

Article in Frontiers in neuroscience, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Parkinson's Disease: A Tale of Many Players.Medical principles and practice : international journal of the Kuwait University, Health Science Centre · 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

7 authors at 3 institutions in 1 country.

Hengxu MaoGuangdong Provincial Key Laboratory on Brain Function Repair and Regeneration, Department of Neurosurgery, The Engineering Technology Research Center of Education Ministry of China, Zhujiang Hospital, Southern Medical University, Guangzhou, China.
Yongyi YeDepartment of Neurosurgery, The Second Affiliated Hospital of Guangzhou Medical University, Guangzhou, China.
Xiang SunGuangdong Provincial Key Laboratory on Brain Function Repair and Regeneration, Department of Neurosurgery, The Engineering Technology Research Center of Education Ministry of China, Zhujiang Hospital, Southern Medical University, Guangzhou, China.
Chen QianGuangdong Provincial Key Laboratory on Brain Function Repair and Regeneration, Department of Neurosurgery, The Engineering Technology Research Center of Education Ministry of China, Zhujiang Hospital, Southern Medical University, Guangzhou, China.
Baoyan WangGuangdong Provincial Key Laboratory on Brain Function Repair and Regeneration, Department of Neurosurgery, The Engineering Technology Research Center of Education Ministry of China, Zhujiang Hospital, Southern Medical University, Guangzhou, China.
Linghai XieGuangdong Provincial Key Laboratory on Brain Function Repair and Regeneration, Department of Neurosurgery, The Engineering Technology Research Center of Education Ministry of China, Zhujiang Hospital, Southern Medical University, Guangzhou, China.
Shizhong ZhangGuangdong Provincial Key Laboratory on Brain Function Repair and Regeneration, Department of Neurosurgery, The Engineering Technology Research Center of Education Ministry of China, Zhujiang Hospital, Southern Medical University, Guangzhou, China.
Zhujiang Hospital · CNSouthern Medical University · CNGuangzhou Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The intracellular aggregation of α-synuclein in neurons/glia is considered to be a key step in the pathogenesis of synucleinopathy [including Parkinson's disease (PD), dementia with Lewy body (DLB), multiple system atrophy (MSA), etc.]. Increasing evidence indicates that the initial pathological α-synuclein aggregates can replicate themselves and propagate in a "seeding" manner to multiple areas of the brain and even to peripheral tissue, which makes it the most important biomarker for the diagnosis of synucleinopathies in recent years. The amplification and propagation capabilities of α-synuclein aggregates are very similar to those of prion-like diseases, which are based on the inherent self-recruitment capabilities of existing misfolded proteins.

Indexed as

aggregatesfibrillationPDPFFsprion-like diseasessynucleinopathyTHTα-synuclein

Identifiers

PMID35692426
PMCPMC9175570
OpenAlexW4281491862

What OpenQuestion holds

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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.