ArticleBiomolecules2021
Isotopically Dimethyl Labeling-Based Quantitative Proteomic Analysis of Phosphoproteomes of Soybean Cultivars.
Article in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Deciphering the Protein Phosphorylation Dynamics Triggered by Seconds of Force Stimulation.Molecular & cellular proteomics : MCP · 2026Article
- Phylogenetic diversity of light-dependent phosphorylation of Thr78 in Rubisco activase.Journal of experimental botany · 2025Article
- TMT-based quantitative proteomics analysis of defense responses induced by the Bph3 gene following brown planthopper infection in rice.BMC plant biology · 2024Article
- Phosphoproteomics: Advances in Research on Cadmium-Exposed Plants.International journal of molecular sciences · 2024Review
- Interaction of Soybean (Plants (Basel, Switzerland) · 2024Article
- Quantitative Phosphoproteomic Analysis Provides Insights into the Sodium Bicarbonate Responsiveness ofBiomolecules · 2023Article
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Authors and funding
13 authors at 7 institutions in 4 countries.
Funding
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Abstract
Isotopically dimethyl labeling was applied in a quantitative post-translational modification (PTM) proteomic study of phosphoproteomic changes in the drought responses of two contrasting soybean cultivars. A total of 9457 phosphopeptides were identified subsequently, corresponding to 4571 phosphoprotein groups and 3889 leading phosphoproteins, which contained nine kinase families consisting of 279 kinases. These phosphoproteins contained a total of 8087 phosphosites, 6106 of which were newly identified and constituted 54% of the current soybean phosphosite repository. These phosphosites were converted into the highly conserved kinase docking sites by bioinformatics analysis, which predicted six kinase families that matched with those newly found nine kinase families. The overly post-translationally modified proteins (OPP) occupies 2.1% of these leading phosphoproteins. Most of these OPPs are photoreceptors, mRNA-, histone-, and phospholipid-binding proteins, as well as protein kinase/phosphatases. The subgroup population distribution of phosphoproteins over the number of phosphosites of phosphoproteins follows the exponential decay law, Y = 4.13e
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