Evidence map›Paper›PMID 31491967›Full record

ArticleMolecules (Basel, Switzerland)2019

Computational Study of Natural Compounds for the Clearance of Amyloid-Βeta: A Potential Therapeutic Management Strategy for Alzheimer's Disease.

Syed Sayeed Ahmad, Haroon Khan, Syed Mohd Danish Rizvi, Siddique Akber Ansari, Riaz Ullah, Luca Rastrelli, Hafiz Majid Mahmood, Mohd Haris Siddiqui

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed, 1 pooled it
2.0field-weighted citation impact, top 13% 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

12 citing papers in PubMed, 1 synthesis or guideline pooled it, 19 citations in OpenAlex.

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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

8 authors at 5 institutions in 4 countries.

Syed Sayeed AhmadDepartment of Bioengineering, Faculty of Engineering, Integral University, Lucknow 226026, India.
Haroon KhanDepartment of Pharmacy, Abdul Wali Khan University Mardan 23200, Pakistan. hkdr2006@gmail.com.ORCID 0000-0002-1736-4404
Syed Mohd Danish RizviDepartment of Pharmaceutics, College of Pharmacy, University of Hail, PO Box 2440, Ha'il - 81451, Saudi Arabia.
Siddique Akber AnsariDepartment of Pharmaceutical Chemistry, College of Pharmacy, King Saud University, P.O. Box: 2457, Riyadh 11451, Saudi Arabia.ORCID 0000-0003-3966-2282
Riaz UllahMedicinal, Aromatic and Poisonous Plants Research Center (MAPRC), College of Pharmacy, King Saud University, PO Box 2457, Riyadh 11451, Saudi Arabia.ORCID 0000-0002-2860-467X
Luca RastrelliDipartimento di Farmacia, University of Salerno, 84084 Fisciano, Italy.
Hafiz Majid MahmoodDepartment of Pharmacology, College of Pharmacy, King Saud University PO Box 2457, Riyadh 11451, Saudi Arabia.ORCID 0000-0001-9215-0505
Mohd Haris SiddiquiDepartment of Bioengineering, Faculty of Engineering, Integral University, Lucknow 226026, India. haroonkhan@awkum.edu.pk.
King Saud University · SAIntegral University · INAbdul Wali Khan University Mardan · PKUniversity of Ha'il · SAUniversity of Salerno · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease (AD) is a widespread dynamic neurodegenerative malady. Its etiology is still not clear. One of the foremost pathological features is the extracellular deposits of Amyloid-beta (Aβ) peptides in senile plaques. The interaction of Aβ and the receptor for advanced glycation end products at the blood-brain barrier is also observed in AD, which not only causes the neurovascular anxiety and articulation of proinflammatory cytokines, but also directs reduction of cerebral bloodstream by upgrading the emission of endothelin-1 to induce vasoconstriction. In this process, RAGE is deemed responsible for the influx of Aβ into the brain through BBB. In the current study, we predicted the interaction potential of the natural compounds vincamine, ajmalicine and emetine with the Aβ peptide concerned in the treatment of AD against the standard control, curcumin, to validate the Aβ peptide-compounds results. Protein-protein interaction studies have also been carried out to see their potential to inhibit the binding process of Aβ and RAGE. Moreover, the current study verifies that ligands are more capable inhibitors of a selected target compared to positive control with reference to ΔG values. The inhibition of Aβ and its interaction with RAGE may be valuable in proposing the next round of lead compounds for effective Alzheimer's disease treatment.

Indexed as

Models, MolecularAlzheimer DiseaseAmino AcidsAmyloid beta-PeptidesAmyloidogenic ProteinsBinding SitesBiological ProductsHumansHydrogen BondingLigandsMolecular ConformationMolecular Docking SimulationMolecular Dynamics SimulationProtein BindingStructure-Activity RelationshipAmino AcidsAmyloid beta-PeptidesAmyloidogenic ProteinsBiological ProductsLigandsAlzheimer’s diseasebinding energydockingnatural compoundsZ-dock

Identifiers

PMID31491967
PMCPMC6767296
OpenAlexW2971811525

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.