Evidence map›Paper›PMID 38913089›Full record

ArticleJournal of fluorescence2025

Unveiling the Detrimental Effect of Glipizide on Structure and Function of Catalase: Spectroscopic, Thermodynamics and Simulation Studies.

Mohd Shahnawaz Khan, Nojood Al-Twaijry, Fai N Alotaibi, Amal M Alenad, Majed S Alokail, Mohammed Arshad, Abdul Aziz Al Kheraif, Mohamed Elrobh, Gouse M Shaik

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Article in Journal of fluorescence, 2025. 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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0cells of the map it votes in
0citing papers in PubMed
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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

9 authors.

Mohd Shahnawaz KhanDepartment of Biochemistry, College of Science, King Saud University, 11451, Riyadh, Saudi Arabia. moskhan@ksu.edu.sa.
Nojood Al-TwaijryDepartment of Biochemistry, College of Science, King Saud University, 11451, Riyadh, Saudi Arabia.
Fai N AlotaibiDepartment of Biochemistry, College of Science, King Saud University, 11451, Riyadh, Saudi Arabia.
Amal M AlenadDepartment of Biochemistry, College of Science, King Saud University, 11451, Riyadh, Saudi Arabia.
Majed S AlokailDepartment of Biochemistry, College of Science, King Saud University, 11451, Riyadh, Saudi Arabia.
Mohammed ArshadCollege of Applied Medical Science, King Saud University, Riyadh, Saudi Arabia.
Abdul Aziz Al KheraifCollege of Applied Medical Science, King Saud University, Riyadh, Saudi Arabia.
Mohamed ElrobhDepartment of Biochemistry, College of Science, King Saud University, 11451, Riyadh, Saudi Arabia.
Gouse M ShaikDepartment of Biochemistry, College of Science, King Saud University, 11451, Riyadh, Saudi Arabia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Free radicals, products of oxidative processes, induce cellular damage linked to diseases like Parkinson's and diabetes due to increased reactive oxygen species (ROS) levels. Catalase, crucial for scavenging ROS, emerges as a therapeutic agent against ailments including atherosclerosis and tumor progression. Its primary function involves breaking down hydrogen peroxide into water and oxygen. Research on catalase-drug interactions reveals structural changes under specific conditions, affecting its activity and cellular antioxidant balance, highlighting its pivotal role in defending against oxidative stress-related diseases. Hence, targeting catalase is considered an effective strategy for controlling ROS-induced cellular damage. This study investigates the interaction between bovine liver catalase and glipizide using spectroscopic and computational methods. It also explores glipizide's effect on catalase activity. More than 20% inhibition of catalase enzymatic activity was recorded in the presence of 50 µM glipizide. To investigate the inhibition of catalase activity by glipizide, we performed a series of binding studies. Glipizide was found to form a complex with catalase with moderate affinity and binding constant in the range of 3.822 to 5.063 × 10

Indexed as

CatalaseGlipizideThermodynamicsAnimalsCattleMolecular Dynamics SimulationSpectrometry, FluorescenceCatalaseGlipizideCatalase: glipizideCatalase inhibitionInteractionMolecular dockingSpectroscopy

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Registered trials

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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.