ArticleFrontiers in plant science2013
Redox-dependent functional switching of plant proteins accompanying with their structural changes.
Article in Frontiers in plant science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 47 citations in OpenAlex.
- A redox-regulated RCC1-like protein controls catalase activity in Arabidopsis.Nature communications · 2026Article
- Redox-mediated regulation of ABSCISIC ACID-INSENSITIVE 5 affects seed germination and seedling development in Arabidopsis.Journal of experimental botany · 2026Article
- Natural Negative Feedback Loops Confer Indica-Japonica Differentiation for Grain Size Homeostasis in Rice.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Plant-BeneficialScientifica · 2026Article
- More questions than answers: insights into potential cysteine-rich receptor-like kinases redox signalling in Arabidopsis.The Plant journal : for cell and molecular biology · 2025Review
- Moonlighting Proteins: Unveiling Their Multifunctionality in Metabolic Regulation and Drug Discovery.Current drug metabolism · 2025Review
- Genetic diversity of durum wheat (Triticum turgidum ssp. durum) to mitigate abiotic stress: Drought, heat, and their combination.PloS one · 2024Article
- Universal Stress Proteins: From Gene to Function.International journal of molecular sciences · 2023Review
- Coping with the cold: unveiling cryoprotectants, molecular signaling pathways, and strategies for cold stress resilience.Frontiers in plant science · 2023Review
- Adenosine monophosphate deaminase modulates BIN2 activity through hydrogen peroxide-induced oligomerization.The Plant cell · 2022Article
- Redox-dependent structural switch and CBF activation confer freezing tolerance in plants.Nature plants · 2021Article
- Comparison of Light Condition-Dependent Differences in the Accumulation and Subcellular Localization of Glutathione inInternational journal of molecular sciences · 2021Article
- Redox-Dependent Structural Modification of Nucleoredoxin Triggers Defense Responses againstInternational journal of molecular sciences · 2020Article
- The immune-related, TGA1 redox-switch: to be or not to be?The New phytologist · 2020Article
- The Physiological Functions of Universal Stress Proteins and Their Molecular Mechanism to Protect Plants From Environmental Stresses.Frontiers in plant science · 2019Article
- Proteomics of Heat-Stress and Ethylene-Mediated Thermotolerance Mechanisms in Tomato Pollen Grains.Frontiers in plant science · 2018Article
- Resistance to citrus canker induced by a variant of Xanthomonas citri ssp. citri is associated with a hypersensitive cell death response involving autophagy-associated vacuolar processes.Molecular plant pathology · 2017Article
- RNA Chaperone Function of a Universal Stress Protein in Arabidopsis Confers Enhanced Cold Stress Tolerance in Plants.International journal of molecular sciences · 2017Article
- Cadmium Stress Leads to Rapid Increase in RNA Oxidative Modifications in Soybean Seedlings.Frontiers in plant science · 2017Article
- Functional analysis of thioredoxin from the desert lichen-forming fungus, Endocarpon pusillum Hedwig, reveals its role in stress tolerance.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Reactive oxygen species (ROS) can be generated during the course of normal aerobic metabolism or when an organism is exposed to a variety of stress conditions. It can cause a widespread damage to intracellular macromolecules and play a causal role in many degenerative diseases. Like other aerobic organisms plants are also equipped with a wide range of antioxidant redox proteins, such as superoxide dismutase, catalase, glutaredoxin, thioredoxin (Trx), Trx reductase, protein disulfide reductase, and other kinds of peroxidases that are usually significant in preventing harmful effects of ROS. To defend plant cells in response to stimuli, a part of redox proteins have shown to play multiple functions through the post-translational modification with a redox-dependent manner. For the alternative switching of their cellular functions, the redox proteins change their protein structures from low molecular weight to high molecular weight (HMW) protein complexes depending on the external stress. The HMW proteins are reported to act as molecular chaperone, which enable the plants to enhance their stress tolerance. In addition, some transcription factors and co-activators have function responding to environmental stresses by redox-dependent structural changes. This review describes the molecular mechanism and physiological significance of the redox proteins, transcription factors and co-activators to protect the plants from environmental stresses through the redox-dependent structural and functional switching of the plant redox proteins.
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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.