Evidence map›Paper›PMID 26194093›Full record

ArticleScientific reports2015

Protection against β-amyloid-induced synaptic and memory impairments via altering β-amyloid assembly by bis(heptyl)-cognitin.

Lan Chang, Wei Cui, Yong Yang, Shujun Xu, Wenhua Zhou, Hongjun Fu, Shengquan Hu, Shinghung Mak, Juwei Hu, Qin Wang and 9 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed, 1 pooled it
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

17 citing papers in PubMed, 1 synthesis or guideline pooled it, 33 citations in OpenAlex.

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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

19 authors at 6 institutions in 4 countries.

Lan ChangDepartment of Physiology, Ningbo Key Laboratory of Behavioral Neuroscience, Zhejiang Provincial Key Laboratory of Pathophysiology, School of Medicine, Ningbo University. Ningbo 315211, China.
Wei CuiDepartment of Applied Biology and Chemistry Technology, Institute of Modern Chinese Medicine, the Hong Kong Polytechnic University, Hong Kong, China.
Yong YangDepartment of Physiology, Ningbo Key Laboratory of Behavioral Neuroscience, Zhejiang Provincial Key Laboratory of Pathophysiology, School of Medicine, Ningbo University. Ningbo 315211, China.
Shujun XuDepartment of Physiology, Ningbo Key Laboratory of Behavioral Neuroscience, Zhejiang Provincial Key Laboratory of Pathophysiology, School of Medicine, Ningbo University. Ningbo 315211, China.
Wenhua ZhouDepartment of Physiology, Ningbo Key Laboratory of Behavioral Neuroscience, Zhejiang Provincial Key Laboratory of Pathophysiology, School of Medicine, Ningbo University. Ningbo 315211, China.
Hongjun FuDepartment of Applied Biology and Chemistry Technology, Institute of Modern Chinese Medicine, the Hong Kong Polytechnic University, Hong Kong, China.
Shengquan HuDepartment of Applied Biology and Chemistry Technology, Institute of Modern Chinese Medicine, the Hong Kong Polytechnic University, Hong Kong, China.
Shinghung MakDepartment of Applied Biology and Chemistry Technology, Institute of Modern Chinese Medicine, the Hong Kong Polytechnic University, Hong Kong, China.
Juwei HuDepartment of Physiology, Ningbo Key Laboratory of Behavioral Neuroscience, Zhejiang Provincial Key Laboratory of Pathophysiology, School of Medicine, Ningbo University. Ningbo 315211, China.
Qin WangDepartment of Pharmacology, Zhongshan School of Medicine, Sun Yat-Sen University, Guangzhou 510275, China.
Victor Pui-Yan MaDepartment of Chemistry, Hong Kong Baptist University, Hong Kong, China.
Tony Chung-lit ChoiDepartment of Applied Biology and Chemistry Technology, Institute of Modern Chinese Medicine, the Hong Kong Polytechnic University, Hong Kong, China.
Edmond Dik-lung MaDepartment of Chemistry, Hong Kong Baptist University, Hong Kong, China.
Liang TaoDepartment of Pharmacology, Zhongshan School of Medicine, Sun Yat-Sen University, Guangzhou 510275, China.
Yuanping PangMayo Foundation for Medical Education and Research, Rochester 55906-5425, MN, USA.
Michael J RowanTrinity College Institute of Neuroscience, Department of Pharmacology and Therapeutics, Department of Physiology.
Roger AnwylTrinity College Institute of Neuroscience, Department of Pharmacology and Therapeutics, Trinity College, Dublin 2, Ireland.
Yifan HanDepartment of Applied Biology and Chemistry Technology, Institute of Modern Chinese Medicine, the Hong Kong Polytechnic University, Hong Kong, China.
Qinwen WangDepartment of Physiology, Ningbo Key Laboratory of Behavioral Neuroscience, Zhejiang Provincial Key Laboratory of Pathophysiology, School of Medicine, Ningbo University. Ningbo 315211, China.
Ningbo University · CNHong Kong Polytechnic University · HKHong Kong Baptist University · HKSun Yat-sen University · CNTrinity College · CATrinity College Dublin · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-amyloid (Aβ) oligomers have been closely implicated in the pathogenesis of Alzheimer's disease (AD). We found, for the first time, that bis(heptyl)-cognitin, a novel dimeric acetylcholinesterase (AChE) inhibitor derived from tacrine, prevented Aβ oligomers-induced inhibition of long-term potentiation (LTP) at concentrations that did not interfere with normal LTP. Bis(heptyl)-cognitin also prevented Aβ oligomers-induced synaptotoxicity in primary hippocampal neurons. In contrast, tacrine and donepezil, typical AChE inhibitors, could not prevent synaptic impairments in these models, indicating that the modification of Aβ oligomers toxicity by bis(heptyl)-cognitin might be attributed to a mechanism other than AChE inhibition. Studies by using dot blotting, immunoblotting, circular dichroism spectroscopy, and transmission electron microscopy have shown that bis(heptyl)-cognitin altered Aβ assembly via directly inhibiting Aβ oligomers formation and reducing the amount of preformed Aβ oligomers. Molecular docking analysis further suggested that bis(heptyl)-cognitin presumably interacted with the hydrophobic pockets of Aβ, which confers stabilizing powers and assembly alteration effects on Aβ. Most importantly, bis(heptyl)-cognitin significantly reduced cognitive impairments induced by intra-hippocampal infusion of Aβ oligomers in mice. These results clearly demonstrated how dimeric agents prevent Aβ oligomers-induced synaptic and memory impairments, and offered a strong support for the beneficial therapeutic effects of bis(heptyl)-cognitin in the treatment of AD.

Indexed as

alpha7 Nicotinic Acetylcholine ReceptorAmyloid beta-PeptidesAnimalsCells, CulturedCholinesterase InhibitorsElectric StimulationHippocampusHydrophobic and Hydrophilic InteractionsLong-Term PotentiationMaleMemory DisordersMice, Inbred ICRNeuronsNeuroprotective AgentsProtein Structure, SecondaryRats, Sprague-Dawleyalpha7 Nicotinic Acetylcholine ReceptorAmyloid beta-Peptidesbis(heptyl)cognitinCholinesterase InhibitorsNeuroprotective AgentsTacrine

Identifiers

PMID26194093
PMCPMC4508546
OpenAlexW2238244076

What OpenQuestion holds

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Registered trials

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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.