ArticleJournal of proteome research2012
Proteomic analysis of early-responsive redox-sensitive proteins in Arabidopsis.
Article in Journal of proteome research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed.
- 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
- SnRK1α1-mediated RBOH1 phosphorylation regulates reactive oxygen species to enhance tolerance to low nitrogen in tomato.The Plant cell · 2024Article
- Evidence for dual targeting control of Arabidopsis 6-phosphogluconate dehydrogenase isoforms by N-terminal phosphorylation.Journal of experimental botany · 2024Article
- The Impact of AAPH-Induced Oxidation on the Functional and Structural Properties, and Proteomics of Arachin.Molecules (Basel, Switzerland) · 2023Article
- Hydrogen Peroxide and GAAntioxidants (Basel, Switzerland) · 2023Article
- Redox and Hormonal Changes in the Transcriptome of Grape (Plants (Basel, Switzerland) · 2022Article
- Quantitative redox proteomics revealed molecular mechanisms of salt tolerance in the roots of sugar beet monomeric addition line M14.Botanical studies · 2022Article
- Proteome-wide identification of S-sulfenylated cysteines reveals metabolic response to freezing stress after cold acclimation inFrontiers in plant science · 2022Article
- Topology of the redox network during induction of photosynthesis as revealed by time-resolved proteomics in tobacco.Science advances · 2021Article
- Coordinated regulation of plant immunity by poly(ADP-ribosyl)ation and K63-linked ubiquitination.Molecular plant · 2021Article
- Single Amino Acid Exchange in ACTIN2 Confers Increased Tolerance to Oxidative Stress in ArabidopsisInternational journal of molecular sciences · 2021Article
- Cysteine modifications (oxPTM) and protein sulphenylation-mediated sulfenome expression in plants: evolutionary conserved signaling networks?Plant signaling & behavior · 2021Article
- Plant Proton Pumps and Cytosolic pH-Homeostasis.Frontiers in plant science · 2021Review
- Bringing New Methods to the Seed Proteomics Platform: Challenges and Perspectives.International journal of molecular sciences · 2020Review
- ConCysFind: a pipeline tool to predict conserved amino acids of protein sequences across the plant kingdom.BMC bioinformatics · 2020Article
- Photosynthetic Metabolism and Nitrogen Reshuffling Are Regulated by Reversible Cysteine Thiol Oxidation Following Nitrogen Deprivation in Chlamydomonas.Plants (Basel, Switzerland) · 2020Article
- Glutathionylation primes soluble glyceraldehyde-3-phosphate dehydrogenase for late collapse into insoluble aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Inhibition of TOR inCells · 2019Article
- Proteome-Wide Analysis of Cysteine Reactivity during Effector-Triggered Immunity.Plant physiology · 2019Article
- RBOH-Dependent ROS Synthesis and ROS Scavenging by Plant Specialized Metabolites To Modulate Plant Development and Stress Responses.Chemical research in toxicology · 2019Review
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7 authors.
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Abstract
Regulation of protein function through oxidative modification has emerged as an important molecular mechanism modulating various biological processes. Here, we report a proteomic study of redox-sensitive proteins in Arabidopsis cells subjected to H(2)O(2) treatment. Four gel-based approaches were employed, leading to the identification of four partially overlapping sets of proteins whose thiols underwent oxidative modification in the H(2)O(2)-treated cells. Using a method based on differential labeling of thiols followed by immunoprecipitation and Western blotting, five of the six selected putative redox-sensitive proteins were confirmed to undergo oxidative modification following the oxidant treatment in Arabidopsis leaves. Another method, which is based on differential labeling of thiols coupled with protein electrophoretic mobility shift assay, was adopted to reveal that one of the H(2)O(2)-sensitive proteins, a homologue of cytokine-induced apoptosis inhibitor 1 (AtCIAPIN1), also underwent oxidative modification in Arabidopsis leaves after treatments with salicylic acid or the peptide elicitor flg22, two inducers of defense signaling. The redox-sensitive proteins identified from the proteomic study are involved in various biological processes such as metabolism, the antioxidant system, protein biosynthesis and processing, and cytoskeleton organization. The identification of novel redox-sensitive proteins will be helpful toward understanding of cellular components or pathways previously unknown to be redox-regulated.
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