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The toxic effects of alizarin red S on catalase at the molecular level
48/48 checkable references clean · checked 2026-07-22
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
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The 48 checked references that resolve
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Importance of catalase in the disposal of hydrogen peroxide within human erythrocytes
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A simple method to measure effective catalase activities: Optimization, validation, and application in green coffee
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Purification, characterization and identification of a novel bifunctional catalase-phenol oxidase from Scytalidium thermophilum
resolves10.1002/elan.200704016
Voltammetric Behavior of the Alizarin Red S Interaction with DNA and Damage to DNA
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Characterization of Alizarin Red S binding sites and structural changes on human serum albumin: A biophysical study
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The use of alizarin red S and alizarin complexone for immersion marking Japanese flounder Paralichthys olivaceus (T.)
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Alizarin red S–TiO
<sub>2</sub>
-catalyzed cascade C(sp
<sup>3</sup>
)–H to C(sp
<sup>2</sup>
)–H bond formation/cyclization reactions toward tetrahydroquinoline derivatives under visible light irradiation
resolves10.1016/j.molstruc.2006.12.033
Probing the binding of flavonoids to catalase by molecular spectroscopy
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Catalase inhibition an anti cancer property of flavonoids: A kinetic and structural evaluation
resolves10.1016/j.jinorgbio.2019.110699
The role of catalases in the prevention/promotion of oxidative stress
resolves10.1016/j.envint.2011.12.003
Recent progress and perspectives on the toxicity of carbon nanotubes at organism, organ, cell, and biomacromolecule levels
resolves10.1016/j.proeng.2014.09.032
Hydroxyapatite and Alizarin Sulfonate ARS Modeling Interactions for Textile Dyes Removal from Wastewaters
resolves10.1016/j.electacta.2011.01.098
Electrochemical site marker competitive method for probing the binding site and binding mode between bovine serum albumin and alizarin red S
resolves10.1099/mic.0.28542-0
The catalase and superoxide dismutase genes are transcriptionally up-regulated upon oxidative stress in the strictly anaerobic archaeon Methanosarcina barkeri
resolves10.1016/j.plantsci.2011.06.003
Catalase is a key enzyme in seed recovery from ageing during priming
resolves10.1016/S0140-6736(00)03238-4
Hereditary catalase deficiencies and increased risk of diabetes
resolves10.1016/j.neulet.2010.08.063
Hydrogen peroxide induces apoptosis through the mitochondrial pathway in rat Schwann cells
resolves10.1073/pnas.86.7.2516
Endotoxin pretreatment increases endogenous myocardial catalase activity and decreases ischemia-reperfusion injury of isolated rat hearts.
resolves10.1021/jf048340h
Mushroom Tyrosinase: Catalase Activity, Inhibition, and Suicide Inactivation
resolves10.1016/j.saa.2013.06.093
Potential toxicity of sarafloxacin to catalase: Spectroscopic, ITC and molecular docking descriptions
resolves10.1016/j.jlumin.2014.10.049
Investigation on the toxic interaction of superparamagnetic iron oxide nanoparticles with catalase
resolves10.1006/abio.2000.4880
Estimation of Protein Secondary Structure from Circular Dichroism Spectra: Comparison of CONTIN, SELCON, and CDSSTR Methods with an Expanded Reference Set
resolves10.1016/j.envres.2019.05.008
PFOA and PFOS interact with superoxide dismutase and induce cytotoxicity in mouse primary hepatocytes: A combined cellular and molecular methods
resolves10.1016/j.jhazmat.2015.11.060
Molecular mechanism of catalase activity change under sodium dodecyl sulfate-induced oxidative stress in the mouse primary hepatocytes†
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Insights into potentially toxic effects of 4-aminoantipyrine on the antioxidant enzyme copper–zinc superoxide dismutase
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The interaction mechanism between anionic or cationic surfactant with HSA by using spectroscopy, calorimetry and molecular docking methods
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Spectroscopy, calorimetry and molecular simulation studies on the interaction of catalase with copper ion
resolves10.1039/C7RA03805D
Characterizing the binding interaction between ultrafine carbon black (UFCB) and catalase: electron microscopy and spectroscopic analysis
resolves10.1016/S0039-9140(00)00667-6
Electrochemical studies of rutin interacting with hemoglobin and determination of hemoglobin
resolves10.1039/C6RA03122F
Investigation of the effects of nanoAg on the enzyme lysozyme at the molecular level
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Probing the binding interaction between cadmium(
<scp>ii</scp>
) chloride and lysozyme
resolves10.1016/S0003-2670(00)01041-2
Study of the interaction of nucleic acids with acridine red and CTMAB by a resonance light scattering technique and determination of nucleic acids at nanogram levels
resolves10.1007/s11481-007-9074-2
Stem Cell Transplantation: A Promising Therapy for Parkinson’s Disease
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Fluorescence Quenching to Study Protein-ligand Binding: Common Errors
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Investigation on the interaction between lysozyme and cefepime hydrochloride by synchronous fluorescence and fluorescence quenching spectroscopy
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Effect of urea on serum albumin complex with antithyroid drugs: fluorescence study
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Interaction rule and mechanism of perfluoroalkyl sulfonates containing different carbon chains with human serum albumin
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Synchronous fluorescence determination of DNA based on the interaction between methylene blue and DNA
resolves10.1016/j.ejmech.2007.11.006
Study on the binding interaction between carnitine optical isomer and bovine serum albumin
resolves10.1021/ja036166s
On the Value of <i>c</i>: Can Low Affinity Systems Be Studied by Isothermal Titration Calorimetry?
resolves10.1039/C8NJ00124C
Comprehensive insights into the interaction mechanism between perfluorodecanoic acid and human serum albumin
resolves10.1021/bi00517a022
Investigation of the nature of enzyme-coenzyme interactions in binary and ternary complexes of liver alcohol dehydrogenase with coenzymes, coenzyme analogs, and substrate analogs by ultraviolet absorption and phosphorescence spectroscopy
resolves10.1006/jmbi.1999.3458
Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism 1 1Edited by R. Huber
resolves10.1073/pnas.78.8.4767
Structure and heme environment of beef liver catalase at 2.5 A resolution.
The 2 references without a DOI — listed, not checked
no DOI — not checkedP. O.Seglen , in Methods in Cell Biology , ed. D. M. Prescott , Academic Press , 1976 , vol. 13 , pp. 29–83
no DOI — not checkedJ.Rodes , J.-P.Benhamou , A.Blei , J.Reichen and M.Rizzetto , The textbook of hepatology: from basic science to clinical practice , Wiley-Blackwell , 2008
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