Evidence map›Paper›PMID 27115710›Full record

ReviewExpert opinion on therapeutic targets2016

Asparagine endopeptidase is an innovative therapeutic target for neurodegenerative diseases.

Zhentao Zhang, Manling Xie, Keqiang Ye

Open access · greenAbstract readReview
In one paragraph

Review in Expert opinion on therapeutic targets, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

35 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
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  14. Legumain Functions as a Transient TrkB Sheddase.International journal of molecular sciences · 2023
    Article
  15. Article
  16. Review
  17. The Mammalian Cysteine Protease Legumain in Health and Disease.International journal of molecular sciences · 2022
    Review
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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

3 authors at 2 institutions in 2 countries.

Zhentao Zhanga Department of Neurology , Renmin Hospital of Wuhan University , Wuhan , China.
Manling Xieb Department of Pathology and Laboratory Medicine , Emory University School of Medicine , Atlanta , GA , USA.
Keqiang Yeb Department of Pathology and Laboratory Medicine , Emory University School of Medicine , Atlanta , GA , USA.
Emory University · USWuhan University · CN

Funding

Molecular Regulation of AEP during AgeingRF1AG051538 · NIA · EMORY UNIVERSITY · PI YE, KEQIANG · 2016 to 2016
$3.4M
Nuclear GTPase PIKE Regulation and FunctionsR01NS045627 · NINDS · EMORY UNIVERSITY · PI YE, KEQIANG · 2004 to 2013
$3.1M
NIA NIH HHS RF1 AG051538NINDS NIH HHS R01 NS045627
6 · The paper itself

Abstract

introductionAsparagine endopeptidase (AEP) is a pH-dependent endolysosomal cysteine protease that cleaves its substrates after asparagine residues. Our most recent study identifies that it possesses the delta-secretase activity, and that it is implicated in numerous neurological diseases such as Alzheimer's disease (AD) and stroke. Accumulating evidence supports that the inhibition of AEP exhibits beneficial effects for treating these devastating diseases. AREAS COVERED: Based on recent evidence, it is clear that AEP cleaves its substrate, such as amyloid precursor protein (APP), tau and SET, and plays a critical role in neuronal cell death in various neurodegenerative diseases and stroke. In this article, the basic biology of AEP, its knockout phenotypes in mouse models, its substrates in neurodegenerative diseases, and its small peptidyl inhibitors and prodrugs are discussed. In addition, we discuss the potential of AEP as a novel therapeutic target for neurodegenerative diseases. EXPERT OPINION: AEP plays a unique role in numerous biological processes, depending on both pH and context. Most striking is our most recent finding; that AEP is activated in an age-dependent manner and simultaneously cleaves both APP and tau, thereby unifying both major pathological events in AD. Thus, AEP acts as an innovative trigger for neurodegenerative diseases. Inhibition of AEP will provide a disease-modifying treatment for neurodegenerative diseases including AD.

Indexed as

Age FactorsAlzheimer DiseaseAnimalsAsparaginyl EndopeptidaseCysteine EndopeptidasesCysteine Proteinase InhibitorsDisease Models, AnimalHumansHydrogen-Ion ConcentrationMiceMolecular Targeted TherapyNeurodegenerative DiseasesStrokeAsparaginyl EndopeptidaseCysteine EndopeptidasesCysteine Proteinase InhibitorsAsparagine endopeptidasecysteine proteaselegumainneurodegenerative diseases

Identifiers

PMID27115710
PMCPMC5315368
OpenAlexW2342980355

What OpenQuestion holds

Textmetadata
LicenceTDM
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.