ArticleInternational journal of molecular sciences2023
Serine 31 Phosphorylation-Driven Regulation of AGPase Activity: Potential Implications for Enhanced Starch Yields in Crops.
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 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Identification of transcription factors regulating starch biosynthesis in maize through integrated GWAS and transcriptomic analysis.BMC plant biology · 2026Article
- Modification of starch synthesis in food crops using CRISPR/Cas9 gene editing technology for changing climate.Stress biology · 2026Review
- Transcriptome and targeted metabolome analysis reveals sugar metabolism regulation in maize stalks at different densities.Frontiers in plant science · 2026Article
- Grain under pressure: Harnessing biochemical pathways to beat drought and heat in wheat.The Plant journal : for cell and molecular biology · 2025Review
- Low light reduces saffron corm yield by inhibiting starch synthesis.Frontiers in plant science · 2025Article
- Expression and interaction of AGPase subunits reveal functional enzyme complexes in barley.Frontiers in plant science · 2025Article
- ADP-glucose pyrophosphorylase gene family in soybean and implications in drought stress tolerance.Genes & genomics · 2024Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ADP-Glc pyrophosphorylase (AGPase), which catalyzes the transformation of ATP and glucose-1-phosphate (Glc-1-P) into adenosine diphosphate glucose (ADP-Glc), acts as a rate-limiting enzyme in crop starch biosynthesis. Prior research has hinted at the regulation of AGPase by phosphorylation in maize. However, the identification and functional implications of these sites remain to be elucidated. In this study, we identified the phosphorylation site (serine at the 31st position of the linear amino acid sequence) of the AGPase large subunit (Sh2) using iTRAQ
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Registered trials
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