Evidence map›Paper›PMID 36359916›Full record

ArticleCells2022

Arginine Reduces Glycation in γ

Rui Zhu, Ying Lei, Fangxiao Shi, Qing Tian, Xinwen Zhou

Abstract read
In one paragraph

Article in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Amino acid metabolism in health and disease.Signal transduction and targeted therapy · 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

5 authors.

Rui ZhuKey Laboratory of Neurological Disease of Education Ministry, Department of Pathophysiology, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China.ORCID 0000-0001-9387-9672
Ying LeiKey Laboratory of Neurological Disease of Education Ministry, Department of Pathophysiology, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China.
Fangxiao ShiKey Laboratory of Neurological Disease of Education Ministry, Department of Pathophysiology, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China.
Qing TianKey Laboratory of Neurological Disease of Education Ministry, Department of Pathophysiology, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China.
Xinwen ZhouKey Laboratory of Neurological Disease of Education Ministry, Department of Pathophysiology, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The metabolism disorders are a common convergence of Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM). The characteristics of AD are senile plaques and neurofibrillary tangles (NFTs) composed by deposits of amyloid-β (Aβ) and phosphorylated tau, respectively. Advanced glycation end-products (AGEs) are a stable modification of proteins by non-enzymatic reactions, which could result in the protein dysfunction. AGEs are associated with some disease developments, such as diabetes mellitus and AD, but the effects of the glycated γ

methodsWe studied the effect of glycated γ

resultsThe glycation level of γ

conclusionsArginine treatment decreases glycated γ

Indexed as

Alzheimer DiseaseDiabetes Mellitus, Type 2AMP-Activated Protein KinasesAnimalsArginineMicePlaque, AmyloidAMP-Activated Protein KinasesArginineadvanced glycation end−productsAlzheimer’s diseaseAMPKglycationL−arginine

Identifiers

PMID36359916
PMCPMC9655994

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.