Evidence map›Paper›PMID 28069007›Full record

ArticleBMC complementary and alternative medicine2017

The Benzopyrone Biochanin-A as a reversible, competitive, and selective monoamine oxidase B inhibitor.

Najla O Zarmouh, Suresh K Eyunni, Karam F A Soliman

Open access · goldAbstract read
In one paragraph

Article in BMC complementary and alternative medicine, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

14 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. 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

3 authors at 1 institution in 1 country.

Najla O ZarmouhCollege of Pharmacy and Pharmaceutical Sciences, Florida A&M University, Tallahassee, FL, 32307, USA.
Suresh K EyunniCollege of Pharmacy and Pharmaceutical Sciences, Florida A&M University, Tallahassee, FL, 32307, USA.
Karam F A SolimanCollege of Pharmacy and Pharmaceutical Sciences, Florida A&M University, Tallahassee, FL, 32307, USA. karam.soliman@famu.edu.
Florida Agricultural and Mechanical University · US

Funding

Research Project-3: Effectiveness of an eHealth intervention for uptake of cervical cancer screening in Hispanic womenU54MD007582 · NIMHD · FLORIDA AGRICULTURAL AND MECHANICAL UNIV · PI Seth Y Ablordeppey · 2019 to 2026
$28.1M
Recruitment and HiringG12MD007582 · NIMHD · FLORIDA AGRICULTURAL AND MECHANICAL UNIV · PI SOLIMAN, KARAM F.A. · 2012 to 2017
$16.0M
Targeted Nanocarrier Combination Based Therapy for Lung CancerP20MD006738 · NIMHD · FLORIDA AGRICULTURAL AND MECHANICAL UNIV · PI RAHMAN, SALEH MD. MAHMUDUR · 2012 to 2016
$5.6M
NIMHD NIH HHS G12 MD007582NIMHD NIH HHS P20 MD006738NIMHD NIH HHS U54 MD007582
6 · The paper itself

Abstract

backgroundMonoamine oxidase-B (MAO-B) inhibitors are widely used in the treatment of Parkinson's disease. They increase vital monoamine neurotransmitters in the brain. However, there is a need for safer natural reversible MAO inhibitors with MAO-B selectivity. Our previous studies showed that Psoralea corylifolia seeds (PCS) extract contains compounds that inhibit monoamine oxidase-B.

methodsIn this study, six of PCS constituents sharing a benzopyrone structure were investigated. The compounds Biochanin-A (BIO-A), isopsoralen, 6-prenylnaringenin, neobavaisoflavone, psoralen, and psoralidin, were tested for their ability to inhibit recombinant human MAO-A and B (hMAO-A and hMAO-B) isozymes. The ability of these compounds to inhibit MAO-A and MAO-B were compared to that of PCS ethanolic extract (PCSEE) using spectrophotometric assays and confirmed by luminescence assays. The highly potent and selective MAO-B inhibitor, BIO-A, was further investigated for both isozymes reversibility and enzyme kinetics. Molecular docking studies were used to predict the bioactive conformation and molecular interactions of BIO-A with both isozymes.

resultsThe data obtained indicate that benzopyrones inhibited hMAO-A and hMAO-B with different degrees as confirmed with the luminescence assay. BIO-A inhibited hMAO-B with high potency and selectivity in the present study (IC

conclusionsThe data obtained indicate that BIO-A is a potent, reversible and selective MAO-B inhibitor and may be recommended for further investigation in its possible use in the therapeutic management of Parkinson's and Alzheimer's diseases.

Indexed as

BenzoquinonesBinding, CompetitiveGenisteinHumansKineticsMolecular Docking SimulationMolecular StructureMonoamine OxidaseMonoamine Oxidase InhibitorsPlant ExtractsPsoraleaBenzoquinonesbiochanin AGenisteinMonoamine OxidaseMonoamine Oxidase InhibitorsPlant ExtractsquinoneBenzopyroneBiochanin-ACoumarinsDocking studiesFlavonoidsHuman monoamine oxidase-AHuman monoamine oxidase-BPsoralea corylifolia ethanolic extractReversible competitive inhibition

Identifiers

PMID28069007
PMCPMC5223566
OpenAlexW2567913970

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.