Evidence map›Paper›PMID 41697321›Full record

ArticleNaunyn-Schmiedeberg's archives of pharmacology2026

An integrated in vitro and in silico approach to assess the potential inhibitory actions of auxins on human placental glutathione S-transferase P1-1.

Pavel Awat Husamadin, Ozlem Dalmizrak, Kerem Teralı, Nazmi Ozer

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Article in Naunyn-Schmiedeberg's archives of pharmacology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Pavel Awat HusamadinDepartment of Biomedical Science, Komar University of Science and Technology, Sulaimaniyah, Iraq.ORCID 0000-0002-4851-9958
Ozlem DalmizrakDepartment of Medical Biochemistry, Faculty of Medicine, Near East University, Nicosia, TRNC, Mersin 10, 99138, Turkey. ozlem.dalmizrak@neu.edu.tr.ORCID 0000-0002-5239-5871
Kerem TeralıDepartment of Medical Biochemistry, Faculty of Medicine, Cyprus Health and Social Sciences University, Kutlu Adalı Boulevard, Morphou, TRNC, Mersin 10, 99750, Turkey.ORCID 0000-0002-9964-6383
Nazmi OzerDepartment of Biochemistry, Faculty of Pharmacy, Girne American University, Kyrenia, TRNC, Mersin 10, 99428, Turkey.ORCID 0000-0002-2630-741X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glutathione S-transferases (GSTs) are multifunctional enzymes involved in the metabolism of a wide variety of xenobiotics and endogenous compounds. Since some GST isozymes are overexpressed in a variety of malignancies and have been shown to play roles in the development of drug resistance, GSTs have become a promising therapeutic target. Although numerous natural and plant-derived compounds have been evaluated as GST inhibitors, the interaction between human GSTP1-1 and auxins-indole-derived plant hormones that are also detectable in human biological systems-has not been previously characterized. The present study aimed to investigate whether selected auxins can modulate the activity of human placental GSTP1-1 (hpGSTP1-1) and to elucidate the mechanistic and structural basis of any interactions. The inhibitory effects of indole-3-acetic acid (IAA), indole-3-propionic acid (IPA), and indole-3-butyric acid (IBA) on hpGSTP1-1 were evaluated using in vitro enzyme kinetic assays. IC

Indexed as

Enzyme InhibitorsGlutathione S-Transferase piIndoleacetic AcidsIndolesPlacentaComputer SimulationFemaleHumansKineticsMolecular Docking SimulationEnzyme InhibitorsGlutathione S-Transferase piGSTP1 protein, humanindoleacetic acidIndoleacetic Acidsindolebutyric acidindolepropionic acidIndolesCompetitive inhibitionHuman placental glutathione S-transferase P1-1Indoleacetic acidIndolebutyric acidIndolepropionic acid

Identifiers

PMID41697321
PMCPMC13269400

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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.