ReviewAntioxidants & redox signaling2008
Evolution of catalases from bacteria to humans.
Review in Antioxidants & redox signaling, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 158 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.
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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
158 citing papers in PubMed, 462 citations in OpenAlex.
- An Effector TaCRVP From Tuta Absoluta Oral Secretion Impairs HAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Non-target influence of natural insecticide neem oil on bacterial growth and metabolism.International microbiology : the official journal of the Spanish Society for Microbiology · 2026Article
- Heterologous expression of a heme-dependent catalase from Avicennia marina confers multi-stress tolerance in Escherichia coli for biotechnological applications.Scientific reports · 2026Article
- Extracellular Redox Balance as a Determinant of Immune Regulation and Tissue Inflammation.Antioxidants (Basel, Switzerland) · 2026Review
- Enhanced oxidative stress resilience inExperimental biology and medicine (Maywood, N.J.) · 2026Article
- A redox-dependent switch governing sensory axon degeneration and regeneration.Scientific reports · 2025Article
- Ultrasound-responsive engineered bacteria mediated specific controlled expression of catalase and efficient radiotherapy.Materials today. Bio · 2025Article
- Dual-pathway tumor radiosensitization strategy based on engineered bacteria capable of targeted delivery of AuNPs and specific hypoxia alleviation.Journal of nanobiotechnology · 2025Article
- Oxidative and Molecular-Structural Alterations of Spermatozoa in Swine and Ram Exposed to the Triazole Ipconazole.Toxics · 2025Article
- Article
- Exploring Tetraselmis chui microbiomes-functional metagenomics for novel catalases and superoxide dismutases.Applied microbiology and biotechnology · 2025Article
- "mSphere · 2024Article
- Hemoglobin in Submicron Particles (HbMPs) Is Stabilized Against Oxidation.Antioxidants (Basel, Switzerland) · 2024Article
- LSU family members and NBR1 are novel factors that contribute to homeostasis of catalases and peroxisomes in Arabidopsis thaliana.Scientific reports · 2024Article
- The significance of the apelinergic system in doxorubicin-induced cardiotoxicity.Heart failure reviews · 2024Review
- Antioxidant Systems of Plant Pathogenic Fungi: Functions in Oxidative Stress Response and Their Regulatory Mechanisms.The plant pathology journal · 2024Review
- Methionine oxidation of carbohydrate-active enzymes during white-rot wood decay.Applied and environmental microbiology · 2024Article
- Article
- Co-Delivery of Bioengineered Exosomes and Oxygen for Treating Critical Limb Ischemia in Diabetic Mice.ACS nano · 2023Article
- Genome-Wide Identification and Expression Analysis of Catalase Gene Families inPlants (Basel, Switzerland) · 2023Article
98 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Excessive hydrogen peroxide is harmful for almost all cell components, so its rapid and efficient removal is of essential importance for aerobically living organisms. Conversely, hydrogen peroxide acts as a second messenger in signal-transduction pathways. H(2)O(2) is degraded by peroxidases and catalases, the latter being able both to reduce H(2)O(2) to water and to oxidize it to molecular oxygen. Nature has evolved three protein families that are able to catalyze this dismutation at reasonable rates. Two of the protein families are heme enzymes: typical catalases and catalase-peroxidases. Typical catalases comprise the most abundant group found in Eubacteria, Archaeabacteria, Protista, Fungi, Plantae, and Animalia, whereas catalase-peroxidases are not found in plants and animals and exhibit both catalatic and peroxidatic activities. The third group is a minor bacterial protein family with a dimanganese active site called manganese catalases. Although catalyzing the same reaction (2 H(2)O(2)--> 2 H(2)O+ O(2)), the three groups differ significantly in their overall and active-site architecture and the mechanism of reaction. Here, we present an overview of the distribution, phylogeny, structure, and function of these enzymes. Additionally, we report about their physiologic role, response to oxidative stress, and about diseases related to catalase deficiency in humans.
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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.