article Open AccessTop 1% cited
Nanoceria exhibit redox state-dependent catalase mimetic activity
Chemical Communications · 2010 · Vol. 46(16) · pp. 2736–2736
Talib Pirmohamed✉Janet M. DowdingSanjay SinghBrian WassermanEric HeckertAjay Karakoti(Materials Processing (United States))Jessica E. S. King(University of Central Florida)Sudipta Seal(Materials Processing (United States))William T. Self
Abstract
In this study we have found that cerium oxide nanoparticles exhibit catalase mimetic activity. Surprisingly, the catalase mimetic activity correlates with a reduced level of cerium in the +3 state, in contrast to the relationship between surface charge and superoxide scavenging properties.
Advanced Nanomaterials in CatalysisCarbon and Quantum Dots ApplicationsElectrochemical sensors and biosensorsCatalaseCeriumCerium oxideChemistryRedoxOxidation stateSuperoxideSuperoxide dismutaseInorganic chemistryPhotochemistry
MeSH terms
CatalaseCeriumOxidation-ReductionFree Radical ScavengersBiomimeticsNanoparticles
Citations
1,173
FWCI
15.18
field-weighted impact
References
17
Percentile
99%
vs. same field & year
Citations per year
Cited by
In vivo study of oxidative effect of aspirin nanoparticles in rat blood samples utilizing electrochemical analysis by cyclic voltammetry
Journal of Entomology and Zoology Studies · 2025 · 0 citations
Pharmacological potential of cerium oxide nanoparticles
Nanoscale · 2011 · 1,104 citations
Nanomaterials with enzyme-like characteristics (nanozymes): next-generation artificial enzymes
Chemical Society Reviews · 2013 · 4,206 citations
References
Mitochondrial free radical generation, oxidative stress, and aging
Free Radical Biology and Medicine · 2000 · 2,948 citations
Superoxide dismutase mimetic properties exhibited by vacancy engineered ceria nanoparticles
Chemical Communications · 2007 · 1,252 citations
Neurodegenerative diseases and oxidative stress
Biomedicine & Pharmacotherapy · 2003 · 1,020 citations
Citation Network
How this paper connects to the literature. Drag to explore, click any node to open that paper.
