Evidence map›Paper›PMID 35682848›Full record

ArticleInternational journal of molecular sciences2022

Ibuprofen Favors Binding of Amyloid-β Peptide to Its Depot, Serum Albumin.

Ekaterina A Litus, Alexey S Kazakov, Evgenia I Deryusheva, Ekaterina L Nemashkalova, Marina P Shevelyova, Andrey V Machulin, Aliya A Nazipova, Maria E Permyakova, Vladimir N Uversky, Sergei E Permyakov

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

8 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Novel ibuprofen prodrug: A possible promising agent for the management of complications of Alzheimer's disease.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2024
    Article
  7. Article
  8. 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

10 authors at 3 institutions in 2 countries.

Ekaterina A LitusInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.ORCID 0000-0002-7459-6295
Alexey S KazakovInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.
Evgenia I DeryushevaInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.
Ekaterina L NemashkalovaInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.
Marina P ShevelyovaInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.
Andrey V MachulinSkryabin Institute of Biochemistry and Physiology of Microorganisms, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.ORCID 0000-0002-4859-7219
Aliya A NazipovaInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.
Maria E PermyakovaInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.
Vladimir N UverskyDepartment of Molecular Medicine, Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA.ORCID 0000-0002-4037-5857
Sergei E PermyakovInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.ORCID 0000-0003-4086-3137
Institute for Biological Instrumentation · RUG. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms · RUUniversity of South Florida · US

Funding

Russian Science Foundation 20-74-10072
6 · The paper itself

Abstract

The deposition of amyloid-β peptide (Aβ) in the brain is a critical event in the progression of Alzheimer's disease (AD). This Aβ deposition could be prevented by directed enhancement of Aβ binding to its natural depot, human serum albumin (HSA). Previously, we revealed that specific endogenous ligands of HSA improve its affinity to monomeric Aβ. We show here that an exogenous HSA ligand, ibuprofen (IBU), exerts the analogous effect. Plasmon resonance spectroscopy data evidence that a therapeutic IBU level increases HSA affinity to monomeric Aβ

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnimalsIbuprofenLigandsMiceMolecular Docking SimulationPeptide FragmentsSerum AlbuminSerum Albumin, HumanAmyloid beta-PeptidesIbuprofenLigandsPeptide FragmentsSerum AlbuminSerum Albumin, HumanAlzheimer’s diseaseamyloid-β peptideAβ fibrillationelectron microscopyhuman serum albuminibuprofenmolecular dockingsurface plasmon resonance

Identifiers

PMID35682848
PMCPMC9181795
OpenAlexW4281628485

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.