Evidence map›Paper›PMID 36934384›Full record

ArticleMolecular diversity2024

Monoamine oxidase inhibition properties of 2,1-benzisoxazole derivatives.

Anton Shetnev, Alexandr Kotov, Anna Kunichkina, Irina Proskurina, Sergey Baykov, Mikhail Korsakov, Anél Petzer, Jacobus P Petzer

Open access · hybridAbstract read
In one paragraph

Article in Molecular diversity, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.2field-weighted citation impact, top 25% 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

2 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. 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 at 3 institutions in 2 countries.

Anton ShetnevPharmaceutical Technology Transfer Center, Yaroslavl State Pedagogical University Named After K.D. Ushinsky, 108 Respublikanskaya St., Yaroslavl, 150000, Russian Federation.
Alexandr KotovPharmaceutical Technology Transfer Center, Yaroslavl State Pedagogical University Named After K.D. Ushinsky, 108 Respublikanskaya St., Yaroslavl, 150000, Russian Federation.
Anna KunichkinaDepartment of Organic Chemistry, Kosygin Russian State University, 115035, Moscow, Russia.
Irina ProskurinaPharmaceutical Technology Transfer Center, Yaroslavl State Pedagogical University Named After K.D. Ushinsky, 108 Respublikanskaya St., Yaroslavl, 150000, Russian Federation.
Sergey BaykovInstitute of ChemistryDepartment of Organic Chemistry, Kosygin Russian State University, 115035, Moscow, Russia, Saint Petersburg State University, 7/9 Universitetskaya Nab., Saint Petersburg, 199034, Russian Federation.
Mikhail KorsakovPharmaceutical Technology Transfer Center, Yaroslavl State Pedagogical University Named After K.D. Ushinsky, 108 Respublikanskaya St., Yaroslavl, 150000, Russian Federation.
Anél PetzerPharmaceutical Chemistry and Centre of Excellence for Pharmaceutical Sciences, North-West University, Potchefstroom, 2520, South Africa.
Jacobus P PetzerPharmaceutical Chemistry and Centre of Excellence for Pharmaceutical Sciences, North-West University, Potchefstroom, 2520, South Africa. jacques.petzer@nwu.ac.za.ORCID http://orcid.org/0000-0002-7114-8120
Yaroslavl State Pedagogical University · RUNorth-West University · ZASt Petersburg University · RU

Funding

National Research Foundation 132168National Research Foundation 137997Russian Science Foundation 22-13-20085
6 · The paper itself

Abstract

Monoamine oxidase (MAO) are flavoenzymes that metabolize neurotransmitter, dietary and xenobiotic amines to their corresponding aldehydes with the production of hydrogen peroxide. Two isoforms, MAO-A and MAO-B, are expressed in humans and mammals, and display different substrate and inhibitor specificities as well as different physiological roles. MAO inhibitors are of much therapeutic value and are used for the treatment of neuropsychiatric and neurodegenerative disorders such as depression, anxiety disorders, and Parkinson's disease. To discover MAO inhibitors with good potencies and interesting isoform specificities, the present study synthesized a series of 2,1-benzisoxazole (anthranil) derivatives and evaluated them as in vitro inhibitors of human MAO. The compounds were in most instances specific inhibitors of MAO-B with the most potent MAO-B inhibition observed for 7a (IC

Indexed as

IsoxazolesMonoamine OxidaseMonoamine Oxidase InhibitorsHumansMolecular Docking SimulationStructure-Activity RelationshipIsoxazolesMonoamine OxidaseMonoamine Oxidase Inhibitors2,1-benzisoxazoleInhibitionMAOMonoamine oxidaseSpecificity

Identifiers

PMID36934384
PMCPMC11269473
OpenAlexW4327857158

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.