Evidence map›Paper›PMID 39408835›Full record

ArticleInternational journal of molecular sciences2024

Determination of Potential Lead Compound from

Kumju Youn, Mira Jun

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. 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

2 authors.

Kumju YounDepartment of Food Science and Nutrition, Dong-A University, Busan 49315, Republic of Korea.ORCID 0000-0002-3124-2665
Mira JunDepartment of Food Science and Nutrition, Dong-A University, Busan 49315, Republic of Korea.

Funding

The National Research Foundation of Korea (NRF) RS-2023-00253188
6 · The paper itself

Abstract

Amyloid β protein (Aβ) deposition has been implicated as the molecular driver of Alzheimer's disease (AD) progression. The modulation of the formation of abnormal aggregates and their post-translational modification is strongly suggested as the most effective approach to anti-AD. Beta-site APP-cleaving enzyme 1 (BACE1) acts upstream in amyloidogenic processing to generate Aβ, which rapidly aggregates alone or in combination with acetylcholinesterase (AChE) to form fibrils. Accumulated Aβ promotes BACE1 activation via glycogen synthase kinase-3β (GSK-3β) and is post-translationally modified by glutaminyl cyclase (QC), resulting in increased neurotoxicity. A novel multi-target inhibitor as a potential AD agent was identified using an in silico approach and experimental validation.

Indexed as

AcetylcholinesteraseAlzheimer DiseaseAmyloid Precursor Protein SecretasesAspartic Acid EndopeptidasesBiphenyl CompoundsGlycogen Synthase Kinase 3 betaLignansMagnoliaMolecular Docking SimulationMolecular Dynamics SimulationAllyl CompoundsAminoacyltransferasesAmyloid beta-PeptidesAnimalsHumansPhenolsAcetylcholinesteraseAllyl CompoundsAminoacyltransferasesAmyloid beta-PeptidesAmyloid Precursor Protein SecretasesAspartic Acid EndopeptidasesBACE1 protein, humanBiphenyl Compoundsglutaminyl-peptide cyclotransferaseGlycogen Synthase Kinase 3 betahonokiolLignansPhenolsPlant ExtractsAChEAlzheimer’s diseaseAβBACE1GSK-3βhonokiolQC

Identifiers

PMID39408835
PMCPMC11477134

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.