Evidence map›Paper›PMID 37307834›Full record

ReviewAging and disease2024

Amyloid Precursor Protein: A Regulatory Hub in Alzheimer's Disease.

Jiang Chen, Jun-Sheng Chen, Song Li, Fengning Zhang, Jie Deng, Ling-Hui Zeng, Jun Tan

Open access · goldAbstract readReview
In one paragraph

Review in Aging and disease, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

30 citing papers in PubMed, 27 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

7 authors at 3 institutions in 1 country.

Jiang ChenKey Laboratory of Endemic and Ethnic Diseases, Laboratory of Molecular Biology, Ministry of Education, Guizhou Medical University, Guiyang, Guizhou, China.
Jun-Sheng ChenKey Laboratory of Endemic and Ethnic Diseases, Laboratory of Molecular Biology, Ministry of Education, Guizhou Medical University, Guiyang, Guizhou, China.
Song LiThe First Affiliated Hospital of Dalian Medical University, Dalian, Liaoning, China.
Fengning ZhangKey Laboratory of Endemic and Ethnic Diseases, Laboratory of Molecular Biology, Ministry of Education, Guizhou Medical University, Guiyang, Guizhou, China.
Jie DengKey Laboratory of Endemic and Ethnic Diseases, Laboratory of Molecular Biology, Ministry of Education, Guizhou Medical University, Guiyang, Guizhou, China.
Ling-Hui ZengKey Laboratory of Novel Targets and Drug Study for Neural Repair of Zhejiang Province, School of Medicine, Zhejiang University City College, Hangzhou, Zhejiang, China.
Jun TanKey Laboratory of Endemic and Ethnic Diseases, Laboratory of Molecular Biology, Ministry of Education, Guizhou Medical University, Guiyang, Guizhou, China.
Guiyang Medical University · CNDalian Medical University · CNZhejiang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Decades of research have demonstrated an incontrovertible role of amyloid-β (Aβ) in the etiology of Alzheimer's disease (AD). However, the overemphasis on the pathological impacts of Aβ may obscure the role of its metabolic precursor, amyloid precursor protein (APP), as a significant hub in the occurrence and progression of AD. The complicated enzymatic processing, ubiquitous receptor-like properties, and abundant expression of APP in the brain, as well as its close links with systemic metabolism, mitochondrial function and neuroinflammation, imply that APP plays multifaceted roles in AD. In this review, we briefly describe the evolutionarily conserved biological characteristics of APP, including its structure, functions and enzymatic processing. We also discuss the possible involvement of APP and its enzymatic metabolites in AD, both detrimental and beneficial. Finally, we describe pharmacological agents or genetic approaches with the capability to reduce APP expression or inhibit its cellular internalization, which can ameliorate multiple aspects of AD pathologies and halt disease progression. These approaches provide a basis for further drug development to combat this terrible disease.

Indexed as

Alzheimer DiseaseAmyloid beta-Protein PrecursorAmyloid beta-PeptidesBrainHumansMitochondriaAmyloid beta-PeptidesAmyloid beta-Protein Precursor

Identifiers

PMID37307834
PMCPMC10796103
OpenAlexW4380423047

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.