ArticleAntioxidants (Basel, Switzerland)2022
The Activity of the Durum Wheat (
Article in Antioxidants (Basel, Switzerland), 2022. 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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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Isolation and characterization of Avena sativa catalase 1 gene (AsCAT1) with potential role in plant response to abiotic stress conditions.Protoplasma · 2026Article
- Genome-Wide Identification and Expression Analysis of Catalase Gene Families inPlants (Basel, Switzerland) · 2023Article
- Genome-Wide Investigation and Expression Analysis of the Catalase Gene Family in Oat Plants (Plants (Basel, Switzerland) · 2023Article
- Identification of a putative kinase interacting domain in the durum wheat catalase 1 (TdCAT1) protein.Heliyon · 2023Article
- Catalase Gene Family in Durum Wheat: Genome-Wide Analysis and Expression Profiling in Response to Multiple Abiotic Stress Conditions.Plants (Basel, Switzerland) · 2023Article
- Genome-Wide Identification and Expression Profiling of Pathogenesis-Related Protein 1 (Plants (Basel, Switzerland) · 2023Article
- Identification and Expression Profiling of Two Saudi Arabia Catalase Genes from Wheat and Barley in Response to Abiotic and Hormonal Stresses.Antioxidants (Basel, Switzerland) · 2022Article
- The Putative Auto-Inhibitory Domain of Durum Wheat Catalase (TdCAT1) Positively Regulates Bacteria Cells in Response to Different Stress Conditions.Antioxidants (Basel, Switzerland) · 2022Article
- Isolation and Characterization of a Novel Pathogenesis-Related Protein-1 Gene (Plants (Basel, Switzerland) · 2022Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plant catalases (CAT) are involved in the cellular scavenging of the reactive oxygen species during developmental processes and in response to abiotic and biotic stresses. However, little is known about the regulation of the CAT activity to ensure efficient antioxidant function. Using bioinformatic analyses, we showed that durum wheat catalase 1 (TdCAT1) harbors highly conserved cation-binding and calmodulin binding (CaMBD) domains which are localized at different positions of the protein. As a result, the catalytic activity of TdCAT1 is enhanced in vitro by the divalent cations Mn
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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 Socratic graph.