Evidence map›Paper›PMID 30382490›Full record

ArticleEuropean journal of drug metabolism and pharmacokinetics2019

Effects of Phenothiazines on Aldehyde Oxidase Activity Towards Aldehydes and N-Heterocycles: an In Vitro and In Silico Study.

Farnaz Deris-Abdolahpour, Lida Abdolalipouran-Sadegh, Siavoush Dastmalchi, Maryam Hamzeh-Mivehroud, Omid Zarei, Gholamreza Dehgan, Mohammad-Reza Rashidi

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In one paragraph

Article in European journal of drug metabolism and pharmacokinetics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.5field-weighted citation impact, top 41% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 1 country.

Farnaz Deris-AbdolahpourDepartment of Zoology, Faculty of Natural Science, University of Tabriz, Tabriz, Iran.
Lida Abdolalipouran-SadeghDepartment of Zoology, Faculty of Natural Science, University of Tabriz, Tabriz, Iran.
Siavoush DastmalchiBiotechnology Research Center, Tabriz University of Medical Sciences, Tabriz, Iran.
Maryam Hamzeh-MivehroudBiotechnology Research Center, Tabriz University of Medical Sciences, Tabriz, Iran.
Omid ZareiNeurosciences Research Center, Kurdistan University of Medical Sciences, Sanandaj, Iran.
Gholamreza DehganDepartment of Zoology, Faculty of Natural Science, University of Tabriz, Tabriz, Iran.
Mohammad-Reza RashidiSchool of Pharmacy, Tabriz University of Medical Sciences, Tabriz, Iran. rashidi@tbzmed.ac.ir.
University of Tabriz · IRTabriz University of Medical Sciences · IRBiotechnology Research Center · IRKurdistan University of Medical Sciences · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAldehyde oxidase (AOX) is an important molybdenum-containing enzyme with high similarity with xanthine oxidase (XO). AOX involved in the metabolism of a large array of aldehydes and N-heterocyclic compounds and its activity is highly substrate-dependent.

objectivesThe aim of this work was to study the effect of five important phenothiazine drugs on AOX activity using benzaldehyde and phenanthridine as aldehyde and N-heterocyclic substrates, respectively.

methodsThe effect of trifluperazine, chlorpromazine, perphenazine, thioridazine and promethazine on rat liver AOX was measured spectrophotometrically. To predict the mode of interactions between the studied compounds and AOX, a combination of homology modeling and a molecular docking study was performed.

resultsAll phenothiazines could inhibit AOX activity measured either by phenanthridine or benzaldehyde with almost no effect on XO activity. In the case of benzaldehyde oxidation, the lowest and highest half-maximal inhibitory concentration (IC

conclusionThe five studied phenothiazine drugs showed dual inhibitory effects on AOX activity towards aldehydes and N-heterocycles as two major classes of enzyme substrates. Most of the interactions between the phenothiazine-related drugs and AOX in the binding pocket showed a hydrophobic nature.

Indexed as

Computer SimulationAldehyde OxidaseAldehydesAmino Acid SequenceAnimalsBinding SitesEnzyme ActivationEnzyme InhibitorsHeterocyclic CompoundsMaleMolecular Docking SimulationPhenothiazinesProtein Structure, SecondaryRatsRats, WistarAldehyde OxidaseAldehydesEnzyme InhibitorsHeterocyclic CompoundsPhenothiazines

Identifiers

PMID30382490
OpenAlexW2899495951

What OpenQuestion holds

Textmetadata
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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.