ArticleInternational journal of molecular sciences2023
Iron Availability Influences Protein Carbonylation in
Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Nano-iron modulates salt stress responses in Lycium barbarum via enhanced nutrient uptake, antioxidant defense, and phenolic metabolism.BMC plant biology · 2026Article
- Maize Crops Under Rising Temperatures: Bacterial Influence on Biochemical and Lipidomic Changes Induced by Heat.Plants (Basel, Switzerland) · 2025Article
- Assessing the efficacy of different nano-iron sources for alleviating alkaline soil challenges in goji berry trees (Lycium barbarum L.).BMC plant biology · 2024Article
- Research Progress on the Mechanism of the Impact of Myofibrillar Protein Oxidation on the Flavor of Meat Products.Foods (Basel, Switzerland) · 2024Review
- Post-Translational Modifications to Cysteine Residues in Plant Proteins and Their Impact on the Regulation of Metabolism and Signal Transduction.International journal of molecular sciences · 2024Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Protein carbonylation is an irreversible form of post-translational modification triggered by reactive oxygen species in animal and plant cells. It occurs either through the metal-catalyzed oxidation of Lys, Arg, Pro, and Thr side chains or the addition of α, β-unsaturated aldehydes and ketones to the side chains of Cys, Lys, and His. Recent genetic studies concerning plants pointed to an implication of protein carbonylation in gene regulation through phytohormones. However, for protein carbonylation to stand out as a signal transduction mechanism, such as phosphorylation and ubiquitination, it must be controlled in time and space by a still unknown trigger. In this study, we tested the hypothesis that the profile and extent of protein carbonylation are influenced by iron homeostasis in vivo. For this, we compared the profile and the contents of the carbonylated proteins in the
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Registered trials
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