Evidence map›Paper›PMID 32848600›Full record

ReviewFrontiers in molecular neuroscience2020

Targeting Amyloidogenic Processing of APP in Alzheimer's Disease.

Jing Zhao, Xinyue Liu, Weiming Xia, Yingkai Zhang, Chunyu Wang

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in molecular neuroscience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
9.0field-weighted citation impact, top 1% 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

76 citing papers in PubMed, 152 citations in OpenAlex.

  1. Review
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  15. Signs of Alzheimer's Disease: Tied to Aging.International journal of molecular sciences · 2025
    Review
  16. Article
  17. Review
  18. Polyoxometalates bind multiple targets involved in Alzheimer's disease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
    Article
  19. Review
  20. Review

16 more citing papers are in PubMed but not listed here.

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 at 3 institutions in 1 country.

Jing ZhaoCenter for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, United States.
Xinyue LiuCenter for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, United States.
Weiming XiaGeriatric Research Education Clinical Center, Edith Nourse Rogers Memorial Veterans Hospital, Bedford, MA, United States.
Yingkai ZhangDepartment of Chemistry, New York University, New York, NY, United States.
Chunyu WangCenter for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, United States.
Rensselaer Polytechnic Institute · USEdith Nourse Rogers Memorial Veterans Hospital · USNew York University · US

Funding

Predoctoral Training Program for Alzheimer’s Disease at the Interface of Data Science, Engineering and BiologyT32AG078123 · NIA · RENSSELAER POLYTECHNIC INSTITUTE · PI Chunyu Wang · 2023 to 2026
$974k
Structural Basis of Substrate Docking in Intramembrane ProteolysisR21NS109926 · NINDS · RENSSELAER POLYTECHNIC INSTITUTE · PI WANG, CHUNYU · 2019 to 2019
$469k
Single molecule kinetic studies of gamma-secretase/substrate interaction and the effects of AD-causing mutationsR21AG067436 · NIA · RENSSELAER POLYTECHNIC INSTITUTE · PI FORTH, SCOTT THOMAS, WANG, CHUNYU · 2021 to 2022
$426k
NIA NIH HHS R21 AG067436NIA NIH HHS T32 AG078123NINDS NIH HHS R21 NS109926
6 · The paper itself

Abstract

Alzheimer's disease (AD) is the most common type of senile dementia, characterized by neurofibrillary tangle and amyloid plaque in brain pathology. Major efforts in AD drug were devoted to the interference with the production and accumulation of amyloid-β peptide (Aβ), which plays a causal role in the pathogenesis of AD. Aβ is generated from amyloid precursor protein (APP), by consecutive cleavage by β-secretase and γ-secretase. Therefore, β-secretase and γ-secretase inhibition have been the focus for AD drug discovery efforts for amyloid reduction. Here, we review β-secretase inhibitors and γ-secretase inhibitors/modulators, and their efficacies in clinical trials. In addition, we discussed the novel concept of specifically targeting the γ-secretase substrate APP. Targeting amyloidogenic processing of APP is still a fundamentally sound strategy to develop disease-modifying AD therapies and recent advance in γ-secretase/APP complex structure provides new opportunities in designing selective inhibitors/modulators for AD.

Indexed as

Alzheimer’s diseaseamyloid-βclinical trialβ-secretase inhibitorγ-secretase inhibitorsγ-secretase modulator

Identifiers

PMID32848600
PMCPMC7418514
OpenAlexW3047278342

What Socratic 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 Socratic graph.