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Chapter title |
Investigation of Autophosphorylation Sites of Plant Receptor Kinases and Phosphorylation of Interacting Partners
|
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Chapter number | 12 |
Book title |
Plant Receptor Kinases
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Published in |
Methods in molecular biology, January 2017
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DOI | 10.1007/978-1-4939-7063-6_12 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7062-9, 978-1-4939-7063-6
|
Authors |
Matthew R. Meyer, Shweta Shah, A. Gururaj Rao, Meyer, Matthew R., Shah, Shweta, Gururaj Rao, A. |
Abstract |
The optimal kinase activity of plant receptor-like kinases (RLKs) is often regulated by autophosphorylation of specific sites. Many of these phosphorylated residues then serve as recruiting sites for downstream interacting proteins. Therefore, identification of the phosphosites can be an important first step in delineating the signaling network. This chapter describes a protocol for identification of phosphorylated residues by mass spectrometry as well as a protocol to determine if an interacting partner can be phosphorylated in vitro. |
Mendeley readers
The data shown below were compiled from readership statistics for 1 Mendeley reader of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
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Unknown | 1 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
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Researcher | 1 | 100% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 1 | 100% |