Evidence map›Paper›PMID 27419051›Full record

ArticleFEBS open bio2016

Identification of approved drugs that inhibit the binding of amyloid β oligomers to ephrin type-B receptor 2.

Koichiro Suzuki, Takahiro Aimi, Tomoaki Ishihara, Tohru Mizushima

Open access · goldAbstract read
In one paragraph

Article in FEBS open bio, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

9 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Drug repurposing for neurodegenerative diseases using Zebrafish behavioral profiles.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2024
    Article
  3. Review
  4. Article
  5. Pharmacological Activity of Cepharanthine.Molecules (Basel, Switzerland) · 2023
    Review
  6. Article
  7. Cepharanthine: An update of its mode of action, pharmacological properties and medical applications.Phytomedicine : international journal of phytotherapy and phytopharmacology · 2019
    Review
  8. The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade.Journal of Alzheimer's disease : JAD · 2018
    Review
  9. Perspectives on Treatment of Alzheimer's Disease: A Closer Look into EphB2 Depletion.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    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

4 authors at 2 institutions in 1 country.

Koichiro SuzukiDivision of Drug Discovery and Development Faculty of Pharmacy Keio University Minato-ku Tokyo Japan; Research Fellow of Japan Society for the Promotion of Science Chiyoda-ku Tokyo Japan.
Takahiro AimiDivision of Drug Discovery and Development Faculty of Pharmacy Keio University Minato-ku Tokyo Japan.
Tomoaki IshiharaDivision of Drug Discovery and Development Faculty of Pharmacy Keio University Minato-ku Tokyo Japan.
Tohru MizushimaLTT Bio-Pharma Co., Ltd Minato-ku Tokyo Japan.
Keio University · JPLTT Bio-Pharma (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ephrin type-B receptor 2 (EphB2) is a member of the receptor tyrosine kinase family and plays an important role in learning and memory functions. In patients with Alzheimer's disease (AD) and in mouse models of AD, a reduction in the hippocampal EphB2 level is observed. It was recently reported that normalization of the EphB2 level in the dentate gyrus rescues memory function in a mouse model of AD, suggesting that drugs that restore EphB2 levels may be beneficial in the treatment of AD. Amyloid β (Aβ) oligomers, which are believed to be key molecules involved in the pathogenesis of AD, induce EphB2 degradation through their direct binding to EphB2. Thus, compounds that inhibit the binding of Aβ oligomers to EphB2 may be beneficial. Here, we screened for such compounds from drugs already approved for clinical use in humans. Utilizing a cell-free screening assay, we determined that dihydroergotamine mesilate, bromocriptine mesilate, cepharanthine, and levonorgestrel inhibited the binding of Aβ oligomers to EphB2 but not to cellular prion protein, another endogenous receptor for Aβ oligomers. Additionally, these four compounds did not affect the binding between EphB2 and ephrinB2, an endogenous ligand for EphB2, suggesting that the compounds selectively inhibited the binding of Aβ oligomers to EphB2. This is the first identification of compounds that selectively inhibit the binding of Aβ oligomers to EphB2. These results suggest that these four compounds may be safe and effective drugs for treatment of AD.

Indexed as

Alzheimer's diseaseamyloid β oligomerephrin type‐B receptor 2

Identifiers

PMID27419051
PMCPMC4856424
OpenAlexW2302962481

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.