ArticleScientific reports2019
First nitrosoproteomic profiling deciphers the cysteine S-nitrosylation involved in multiple metabolic pathways of tea leaves.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Nitric oxide modulates bone anabolism through regulation of osteoblast glycolysis and differentiation.The Journal of clinical investigation · 2021Trial
- Metabolic modulation of TCA cycle bySynthetic and systems biotechnology · 2026Article
- The Role of Protein S-Nitrosylation in Mitochondrial Quality Control in Central Nervous System Diseases.Aging and disease · 2024Review
- Crop Proteomics under Abiotic Stress: From Data to Insights.Plants (Basel, Switzerland) · 2022Review
- Article
- Nitrosative stress in Parkinson's disease.NPJ Parkinson's disease · 2022Review
- Proteomic Analysis ofFrontiers in plant science · 2022Article
- What signals the glyoxalase pathway in plants?Physiology and molecular biology of plants : an international journal of functional plant biology · 2021Review
- Contemporary proteomic strategies for cysteine redoxome profiling.Plant physiology · 2021Review
- Thioredoxin Network in Plant Mitochondria: Cysteine S-Posttranslational Modifications and Stress Conditions.Frontiers in plant science · 2020Review
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cysteine S-nitrosylation is a reversible protein post-translational modification and critically regulates the activity, localization and stability of proteins. Tea (Camellia sinensis (L.) O. Kuntze) is one of the most thoroughly studied evergreen crop due to its broad non-alcoholic beverage and huge economic impact in the world. However, little is known about the S-nitrosylome in this plant. Here, we performed a global analysis of cysteine S-nitrosylation in tea leaves. In total, 228 cysteine S-nitrosylation sites were identified in 191 proteins, representing the first extensive data on the S-nitrosylome in tea plants. These S-nitrosylated proteins were located in various subcellular compartments, especially in the chloroplast and cytoplasm. Furthermore, the analysis of functional enrichment and PPI network revealed that the S-nitrosylated proteins were mainly involved in multiple metabolic pathways, including glycolysis, pyruvate metabolism, Calvin cycle and TCA cycle. Overall, this study not only systematically identified the proteins of S-nitrosylation in cysteines of tea leaves, but also laid the solid foundation for further verifying the roles of S-nitrosylation in cysteines of tea plants.
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