Evidence map›Paper›PMID 34644262›Full record

ArticleAging2021

Nmnat2 attenuates amyloidogenesis and up-regulates ADAM10 in AMPK activity-dependent manner.

Xiang-Shu Cheng, Fang-Xiao Shi, Kun-Peng Zhao, Wang Lin, Xiao-Ying Li, Jun Zhang, Yao-Yao Bu, Rui Zhu, Xiao-Hong Li, Dong-Xiao Duan and 5 more

Open access · hybridAbstract read
In one paragraph

Article in Aging, 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
1.6field-weighted citation impact, top 17% 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, 17 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. The microbiota-gut-brain axis: a potential target in the small-molecule compounds and gene therapeutic strategies for Parkinson's disease.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2025
    Review
  7. Mitochondria in Alzheimer's Disease Pathogenesis.Life (Basel, Switzerland) · 2024
    Review
  8. Article
  9. Review
  10. Review
  11. Article
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

15 authors at 5 institutions in 1 country.

Xiang-Shu ChengDepartment of Neurology, Translational Medicine Center, Huaihe Hospital Affiliated to Henan University, Kaifeng 475000, Henan, China.
Fang-Xiao ShiDepartment of Pathophysiology, Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute for Brain Research, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, Hubei, China.
Kun-Peng ZhaoDepartment of Pathophysiology, Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute for Brain Research, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, Hubei, China.
Wang LinDepartment of Pathophysiology, Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute for Brain Research, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, Hubei, China.
Xiao-Ying LiDepartment of Neurology, Translational Medicine Center, Huaihe Hospital Affiliated to Henan University, Kaifeng 475000, Henan, China.
Jun ZhangDepartment of Neurology, Translational Medicine Center, Huaihe Hospital Affiliated to Henan University, Kaifeng 475000, Henan, China.
Yao-Yao BuDepartment of Neurology, Translational Medicine Center, Huaihe Hospital Affiliated to Henan University, Kaifeng 475000, Henan, China.
Rui ZhuDepartment of Pathophysiology, Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute for Brain Research, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, Hubei, China.
Xiao-Hong LiDepartment of Pathophysiology, Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute for Brain Research, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, Hubei, China.
Dong-Xiao DuanDepartment of Pathophysiology, Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute for Brain Research, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, Hubei, China.
Xin-Ying JiDepartment of Microbiology, Henan International Joint Laboratory for Nuclear Protein Regulation, School of Basic Medical Sciences, Henan University, Kaifeng 475004, Henan, China.
Jian-She WeiBrain Research Laboratory, Henan University, Kaifeng 475004, Henan, China.
Jian-Zhi WangDepartment of Pathophysiology, Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute for Brain Research, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, Hubei, China.
Jin DuDepartment of Neurology, Translational Medicine Center, Huaihe Hospital Affiliated to Henan University, Kaifeng 475000, Henan, China.
Xin-Wen ZhouDepartment of Pathophysiology, Key Laboratory of Neurological Disease of National Education Ministry and Hubei Province, Institute for Brain Research, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, Hubei, China.
Huazhong University of Science and Technology · CNHenan University · CNHenan University Huaihe Hospital and Huaihe Clinical Institute · CNHenan Psychiatric Hospital · CNZhengzhou University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid-β (Aβ) accumulating is considered as a causative factor for formation of senile plaque in Alzheimer's disease (AD), but its mechanism is still elusive. The Nicotinamide mononucleotide adenylyltransferase 2 (Nmnat2), a key redox cofactor for energy metabolism, is reduced in AD. Accumulative evidence has shown that the decrease of α-secretase activity, a disintegrin and metalloprotease domain 10 (ADAM10), is responsible for the increase of Aβ productions in AD patient's brain. Here, we observe that the activity of α-secretase ADAM10 and levels of Nmnat2 are significantly decreased, meanwhile there is a simultaneous elevation of Aβ in Tg2576 mice. Over-expression of Nmnat2 increases the mRNA expression of α-secretase ADAM10 and its activity and inhibits Aβ production in N2a/APPswe cells, which can be abolished by Compound C, an AMPK antagonist, suggesting that AMPK is involved in over-expression of Nmnat2 against Aβ production. The further assays demonstrate that Nmnat2 activates AMPK by up-regulating the ratio of NAD

Indexed as

ADAM10 ProteinAMP-Activated Protein KinasesAmyloidAmyloid Precursor Protein SecretasesMembrane ProteinsNicotinamide-Nucleotide AdenylyltransferaseAnimalsCell LineHumansMiceUp-RegulationADAM10 ProteinAdam10 protein, mouseAMP-Activated Protein KinasesAmyloidAmyloid Precursor Protein SecretasesMembrane ProteinsNicotinamide-Nucleotide AdenylyltransferaseNmnat2 protein, mouseADAM10Alzheimer diseaseAMPKamyloid-βnicotinamide mononucleotide adenylyltransferase 2

Identifiers

PMID34644262
PMCPMC8580354
OpenAlexW3205584821

What OpenQuestion holds

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LicenceCC BY
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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.