Evidence map›Paper›PMID 38803179›Full record

ArticleMedicinal chemistry (Shariqah (United Arab Emirates))2025

Humaera Noor Suha, Md Shamim Hossain, Shofiur Rahman, Abdullah N Alodhayb, Md Mainul Hossain, Sarkar M A Kawsar, Raymond A Poirier, Kabir M Uddin

Abstract read
PubMed Publisher
In one paragraph

Article in Medicinal chemistry (Shariqah (United Arab Emirates)), 2025. 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. Article
  2. Article
  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

8 authors.

Humaera Noor SuhaDepartment of Biochemistry and Microbiology, North South University, Bashundhara, Dhaka- 1229, Bangladesh.
Md Shamim HossainDepartment of Biochemistry and Microbiology, North South University, Bashundhara, Dhaka- 1229, Bangladesh.
Shofiur RahmanBiological and Environmental Sensing Research Unit, King Abdullah Institute for Nanotechnology, King Saud University, Riyadh 11451, Saudi Arabia.ORCID 0000-0003-4219-4758
Abdullah N AlodhaybBiological and Environmental Sensing Research Unit, King Abdullah Institute for Nanotechnology, King Saud University, Riyadh 11451, Saudi Arabia.ORCID 0000-0003-0202-8712
Md Mainul HossainDepartment of Biochemistry and Microbiology, North South University, Bashundhara, Dhaka- 1229, Bangladesh.
Sarkar M A KawsarLab of Carbohydrate and Nucleoside Chemistry, Department of Chemistry, University of Chittagong, Chittagong-4331, Bangladesh.ORCID 0000-0001-7964-9117
Raymond A PoirierDepartment of Chemistry, Memorial University, St. John's, Newfoundland, Canada A1B 3X5.ORCID 0000-0002-8533-7846
Kabir M UddinDepartment of Biochemistry and Microbiology, North South University, Bashundhara, Dhaka- 1229, Bangladesh.ORCID 0000-0002-5518-2345

Funding

King Saud University, Riyadh, Saudi Arabia RICSP-24-1
6 · The paper itself

Abstract

introductionAlzheimer's disease, akin to coronary artery disease of the heart, is a progressive brain disorder driven by nerve cell damage.

methodsThis study utilized computational methods to explore 14 anti-acetylcholinesterase (AChE) derivatives (1 ̶ 14) as potential treatments. By scrutinizing their interactions with 11 essential target proteins (AChE, Aβ, BChE, GSK-3β, MAO B, PDE-9, Prion, PSEN-1, sEH, Tau, and TDP-43) and comparing them with established drugs such as donepezil, galantamine, memantine, and rivastigmine, ligand 14 emerged as notable. During molecular dynamics simulations, the protein boasting the strongest bond with the critical 1QTI protein and exceeding drug-likeness criteria also exhibited remarkable stability within the enzyme's pocket across diverse temperatures (300- 320 K). In addition, we utilized density functional theory (DFT) to compute dipole moments and molecular orbital properties, including assessing the thermodynamic stability of AChE derivatives.

resultThis finding suggests a well-defined, potentially therapeutic interaction further supported by theoretical and future

conclusionLigand 14 thus emerges as a promising candidate in the fight against Alzheimer's disease.

Indexed as

AcetylcholinesteraseAlzheimer DiseaseCholinesterase InhibitorsDrug DiscoveryDensity Functional TheoryHumansLigandsMolecular Dynamics SimulationMolecular StructureStructure-Activity RelationshipThermodynamicsAcetylcholinesteraseCholinesterase InhibitorsLigandsAcetylcholinesterase (AChE)ADMETFMOmolecular dockingmolecular dynamicsPCA.

Identifiers

PMID38803179

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.