Evidence map›Paper›PMID 31911834›Full record

ReviewTranslational neurodegeneration2020

δ-secretase in neurodegenerative diseases: mechanisms, regulators and therapeutic opportunities.

Zhentao Zhang, Ye Tian, Keqiang Ye

Open access · goldAbstract readReview
In one paragraph

Review in Translational neurodegeneration, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.4field-weighted citation impact, top 6% 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

26 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Asparagine endopeptidase (AEP) inhibitor formulation via zein-based nanoparticle improves the therapeutic efficacy toward Alzheimer's disease.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Roles of C/EBPβ/AEP in Neurodegenerative Diseases.Current topics in medicinal chemistry · 2025
    Review
  10. Review
  11. Legumain in cardiovascular diseases.Experimental biology and medicine (Maywood, N.J.) · 2024
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. The Mammalian Cysteine Protease Legumain in Health and Disease.International journal of molecular sciences · 2022
    Review
  17. Article
  18. Review
  19. Review
  20. 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

3 authors at 3 institutions in 2 countries.

Zhentao Zhang1Department of Neurology, Renmin Hospital of Wuhan University, Wuhan, 430060 People's Republic of China.
Ye Tian1Department of Neurology, Renmin Hospital of Wuhan University, Wuhan, 430060 People's Republic of China.
Keqiang Ye2Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, GA 30322 USA.
Emory University · USRenmin Hospital of Wuhan University · CNWuhan University · CN

Funding

Molecular Regulation of AEP during AgeingRF1AG051538 · NIA · EMORY UNIVERSITY · PI YE, KEQIANG · 2016 to 2016
$3.4M
The Molecular Mechanism and Therapeutics in Axon RegenerationR01NS105982 · NINDS · EMORY UNIVERSITY · PI ENGLISH, ARTHUR W., KANG, SEONG SU · 2018 to 2022
$1.7M
NIA NIH HHS RF1 AG051538NINDS NIH HHS R01 NS105982
6 · The paper itself

Abstract

Mammalian asparagine endopeptidase (AEP) is a cysteine protease that cleaves its protein substrates on the C-terminal side of asparagine residues. Converging lines of evidence indicate that AEP may be involved in the pathogenesis of several neurological diseases, including Alzheimer's disease, Parkinson's disease, and frontotemporal dementia. AEP is activated in the aging brain, cleaves amyloid precursor protein (APP) and promotes the production of amyloid-β (Aβ). We renamed AEP to δ-secretase to emphasize its role in APP fragmentation and Aβ production. AEP also cleaves other substrates, such as tau, α-synuclein, SET, and TAR DNA-binding protein 43, generating neurotoxic fragments and disturbing their physiological functions. The activity of δ-secretase is tightly regulated at both the transcriptional and posttranslational levels. Here, we review the recent advances in the role of δ-secretase in neurodegenerative diseases, with a focus on its biochemical properties and the transcriptional and posttranslational regulation of its activity, and discuss the clinical implications of δ-secretase as a diagnostic biomarker and therapeutic target for neurodegenerative diseases.

Indexed as

Amyloid beta-PeptidesAmyloid Precursor Protein SecretasesAnimalsAsparaginyl EndopeptidaseCysteine EndopeptidasesHumansNeurodegenerative DiseasesAmyloid beta-PeptidesAmyloid Precursor Protein SecretasesAsparaginyl EndopeptidaseCysteine EndopeptidasesAEPAlzheimer’s diseaseC/EBPβParkinson’s diseaseTDP-43TrkB

Identifiers

PMID31911834
PMCPMC6943888
OpenAlexW3009785240

What OpenQuestion holds

Textmetadata
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.