Evidence map›Paper›PMID 33948899›Full record

ArticleMolecular neurobiology2021

Genipin Attenuates Tau Phosphorylation and Aβ Levels in Cellular Models of Alzheimer's Disease.

Meiting Li, Nan Cai, Liang Gu, Lijun Yao, Decheng Bi, Weishan Fang, Zhijian Lin, Yan Wu, Hong Xu, Hui Li and 2 more

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular neurobiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

11 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Epigenetics in Neurodegenerative Diseases.Sub-cellular biochemistry · 2025
    Review
  3. Interaction between resveratrol and SIRT1: role in neurodegenerative diseases.Naunyn-Schmiedeberg's archives of pharmacology · 2025
    Review
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  6. Article
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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

12 authors at 3 institutions in 1 country.

Meiting Li *Shenzhen Key Laboratory of Marine Bioresources and Ecology, Guangdong Provincial Key Laboratory for Plant Epigenetics, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, 518060, People's Republic of China.
Nan Cai *Shenzhen Key Laboratory of Marine Bioresources and Ecology, Guangdong Provincial Key Laboratory for Plant Epigenetics, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, 518060, People's Republic of China.
Liang GuShenzhen Key Laboratory of Marine Bioresources and Ecology, Guangdong Provincial Key Laboratory for Plant Epigenetics, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, 518060, People's Republic of China.
Lijun YaoShenzhen Key Laboratory of Marine Bioresources and Ecology, Guangdong Provincial Key Laboratory for Plant Epigenetics, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, 518060, People's Republic of China.
Decheng BiShenzhen Key Laboratory of Marine Bioresources and Ecology, Guangdong Provincial Key Laboratory for Plant Epigenetics, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, 518060, People's Republic of China.
Weishan FangSchool of Medicine, Shenzhen University, Shenzhen, 518055, People's Republic of China.
Zhijian LinDepartment of Neurology, Peking University Shenzhen Hospital, Shenzhen, 518036, People's Republic of China.
Yan WuInstrumental Analysis Center, Shenzhen University, Shenzhen, 518055, People's Republic of China.
Hong XuShenzhen Key Laboratory of Marine Bioresources and Ecology, Guangdong Provincial Key Laboratory for Plant Epigenetics, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, 518060, People's Republic of China.
Hui LiShenzhen Key Laboratory of Marine Bioresources and Ecology, Guangdong Provincial Key Laboratory for Plant Epigenetics, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, 518060, People's Republic of China.
Zhangli HuShenzhen Key Laboratory of Marine Bioresources and Ecology, Guangdong Provincial Key Laboratory for Plant Epigenetics, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, 518060, People's Republic of China.
Xu XuShenzhen Key Laboratory of Marine Bioresources and Ecology, Guangdong Provincial Key Laboratory for Plant Epigenetics, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, 518060, People's Republic of China. xuxu@szu.edu.cn.ORCID http://orcid.org/0000-0001-5904-7901
Shenzhen University · CNSun Yat-sen University · CNPeking University Shenzhen Hospital · CN

Funding

National Key Project for Synthetic Biology SQ2018YFA090029National Key R&D Program of China 2018YFD0901106National Natural Science Foundation of China 31970366National Natural Science Foundation of China (CN) 31871734Natural Science Foundation of Guangdong Province 2018A0303130054Natural Science Foundation of Guangdong Province 2018A030313507the Science and Technology Innovation Commission of Shenzhen JCYJ20180305124211995, JCYJ20180305125619343the Science and Technology Innovation Commission of Shenzhen JCYJ20180507182405562the Science and Technology Innovation Commission of Shenzhen JCYJ20190808141415052
6 · The paper itself

Abstract

Alzheimer's disease (AD) is a devastating brain disorder characterized by neurofibrillary tangles and amyloid plaques. Inhibiting Tau protein and amyloid-beta (Aβ) production or removing these molecules is considered potential therapeutic strategies for AD. Genipin is an aglycone and is isolated from the extract of Gardenia jasminoides Ellis fruit. In this study, the effect and molecular mechanisms of genipin on the inhibition of Tau aggregation and Aβ generation were investigated. The results showed that genipin bound to Tau and protected against heparin-induced Tau fibril formation. Moreover, genipin suppressed Tau phosphorylation probably by downregulating the expression of CDK5 and GSK-3β, and activated mTOR-dependent autophagy via the SIRT1/LKB1/AMPK signaling pathway in Tau-overexpressing cells. In addition, genipin decreased Aβ production by inhibiting BACE1 expression through the PERK/eIF2α signaling pathway in N2a/SweAPP cells. These data indicated that genipin could effectively lead to a significant reduction of phosphorylated Tau level and Aβ generation in vitro, suggesting that genipin might be developed into an effective therapeutic complement or a potential nutraceutical for preventing AD.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnimalsCell Line, TumorDose-Response Relationship, DrugHEK293 CellsHumansIridoidsMiceMice, TransgenicPhosphorylationProtein Structure, Tertiarytau ProteinsAmyloid beta-PeptidesgenipinIridoidsMAPT protein, humantau ProteinsAlzheimer’s diseaseAmyloid-betaAutophagyGenipinTau protein

Identifiers

PMID33948899
OpenAlexW3159259126

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.