A Ca2+-dependent protein kinase phosphorylates phosphoenolpyruvate carboxylase in maize
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(92)80291-N/fullpdf
Reference15 articles.
1. Posttranslational Regulation of Phosphoenolpyruvate Carboxylase in C4 and Crassulacean Acid Metabolism Plants
2. Regulatory seryl-phosphorylation of C4 phosphoenolpyruvate carboxylase by a soluble protein kinase from maize leaves
3. Reversible light activation of the phosphoenol pyruvate carboxylase protein-serine kinase in maize leaves
4. The phosphorylation of Sorghum leaf phosphoenolpyruyate carboxylase is a Ca++-calmodulin dependent process
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1. In Vivo Phosphorylation: Development of Specific Antibodies to Detect the Phosphorylated PEPC Isoform for the C4 Photosynthesis in Zea mays;Methods in Molecular Biology;2019-09-21
2. Large-scale analysis of phosphorylated proteins in maize leaf;Planta;2010-10-30
3. Regulatory phosphorylation of phosphoenolpyruvate carboxylase in the leaves of Kalanchoë pinnata, K. daigremontiana and Ananas comosus;Biologia plantarum;2008-06-01
4. Modulation of phosphoenolpyruvate carboxylase in vivo by Ca2+ in Amaranthus hypochondriacus, a NAD-ME type C4 plant: Possible involvement of Ca2+ in up-regulation of PEPC-protein kinase in vivo;Journal of Plant Physiology;2005-10
5. Thioredoxin-Mediated Reductive Activation of a Protein Kinase for the Regulatory Phosphorylation of C4-form Phosphoenolpyruvate Carboxylase from Maize;Plant and Cell Physiology;2001-12-15
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