ArticleElectronic physician2016
Effects of Fenton Reaction on Human Serum Albumin: An In Vitro Study.
Article in Electronic physician, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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.
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.
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Who cites it
9 citing papers in PubMed, 24 citations in OpenAlex.
- 4-Dimethylamino-1,8-Naphthalimide as a Fluorescence Signal Amplification for Site Selective and in Situ Probing of the Hydroxyl Radical.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Antioxidant Properties of Albumin and Diseases Related to Obstetrics and Gynecology.Antioxidants (Basel, Switzerland) · 2025Review
- Metal-Based Regenerative Strategies for Peripheral Nerve Injuries: From Biodegradable Ion Source to Stable Conductive Implants.Biomaterials research · 2025Review
- Serum Albumin Levels: A Biomarker to Be Repurposed in Different Disease Settings in Clinical Practice.Journal of clinical medicine · 2023Review
- Article
- Investigation of Antioxidant Markers in Diabetic Patients.Archives of Razi Institute · 2021Article
- [Chronic leg ulcers in older patients].Zeitschrift fur Gerontologie und Geriatrie · 2019Article
- Oxidative Damage Control during Decay of Wood by Brown Rot Fungus Using Oxygen Radicals.Applied and environmental microbiology · 2018Article
- Oxidative Alteration of Trp-214 and Lys-199 in Human Serum Albumin Increases Binding Affinity with Phenylbutazone: A Combined Experimental and Computational Investigation.International journal of molecular sciences · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
introductionHuman serum albumin (HSA) is a critical protein in human blood plasma, which can be highly damaged by oxidative stress. The aim of this study was to analyze modifications of this protein after oxidation using a Fenton system.
methodsIn this 2015 experiment, different ratios of Fenton reagent (Fe2+/H
resultsAn SDS-PAGE profile showed no cross link and aggregation. However, protein band intensity has decreased to 50% in the highest ratio of H
conclusionTo sum, the structure of HSA has been changed following treatment with Hydroxyl Radical as the main product of Fenton reaction. These data confirm the antioxidant activity of HSA.
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Registered trials
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.