Evidence map›Paper›PMID 27364962›Full record

ArticleNeurochemical research2016

Epigallocatechin Gallate (EGCG) Inhibits Alpha-Synuclein Aggregation: A Potential Agent for Parkinson's Disease.

Yan Xu, Yanyan Zhang, Zhenzhen Quan, Winnie Wong, Jianping Guo, Rongkai Zhang, Qinghu Yang, Rongji Dai, Patrick L McGeer, Hong Qing

Abstract read
PubMed Publisher
In one paragraph

Article in Neurochemical research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed, 1 pooled it
4.9field-weighted citation impact, top 5% 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

64 citing papers in PubMed, 1 synthesis or guideline pooled it, 126 citations in OpenAlex.

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  15. Imidazo[2,1-ACS chemical neuroscience · 2024
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4 more citing papers are in PubMed but not listed here.

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

10 authors at 2 institutions in 2 countries.

Yan XuResearch Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China.
Yanyan ZhangResearch Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China.
Zhenzhen QuanResearch Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China.
Winnie WongKinsmen Laboratory of Neurological Research, University of British Columbia, Vancouver, BC, Canada.
Jianping GuoKinsmen Laboratory of Neurological Research, University of British Columbia, Vancouver, BC, Canada.
Rongkai ZhangResearch Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China.
Qinghu YangResearch Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China.
Rongji DaiResearch Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China.
Patrick L McGeerKinsmen Laboratory of Neurological Research, University of British Columbia, Vancouver, BC, Canada.
Hong QingResearch Center for Biopharmaceutical and Bioengineering, Beijing Institute of Technology, School of Life Science, 5 South Zhongguancun Street, Haidian District, Beijing, 100081, China. hqing@bit.edu.cn.
Beijing Institute of Technology · CNUniversity of British Columbia · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein aggregation is a prominent feature of many neurodegenerative disorders including Parkinson's disease (PD). Aggregation of alpha-synuclein (SNCA) may underlie the pathology of PD. They are the main components of Lewy bodies and dystrophic neurites that are the intraneuronal inclusions characteristic of the disease. We have demonstrated that the polyphenol (-)-epi-gallocatechine gallate (EGCG) inhibited SNCA aggregation, which made it a candidate for therapeutic intervention in PD. Three methods were used: SNCA fibril formation inhibition by EGCG in incubates; inhibition of the SNCA fluorophore A-Syn-HiLyte488 binding to plated SNCA in microwells; and inhibition of the A-Syn-HiLyte488 probe binding to aggregated SNCA in postmortem PD tissue. Recombinant human SNCA was incubated under conditions that result in fibril formation. The aggregation was blocked by 100 nM EGCG in a concentration-dependent manner, as shown by an absence of thioflavin T binding. In the microplate assay system, the ED

Indexed as

alpha-SynucleinCatechinCells, CulturedHumansLewy BodiesParkinson Diseasealpha-SynucleinCatechinepigallocatechin gallateSNCA protein, humanEGCGParkinson’s diseaseSNCA aggregationα-synucleinopathy

Identifiers

PMID27364962
OpenAlexW2475133359

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.