Chapter title |
In Vitro Assessment of Guanylyl Cyclase Activity of Plant Receptor Kinases
|
---|---|
Chapter number | 13 |
Book title |
Plant Receptor Kinases
|
Published in |
Methods in molecular biology, January 2017
|
DOI | 10.1007/978-1-4939-7063-6_13 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7062-9, 978-1-4939-7063-6
|
Authors |
Misjudeen Raji, Chris Gehring, Raji, Misjudeen, Gehring, Chris |
Abstract |
Cyclic nucleotides such as 3',5'-cyclic adenosine monophosphate (cAMP) and 3',5'-cyclic guanosine monophosphate (cGMP) are increasingly recognized as key signaling molecules in plants, and a growing number of plant mononucleotide cyclases, both adenylate cyclases (ACs) and guanylate cyclases (GCs), have been reported. Catalytically active cytosolic GC domains have been shown to be part of many plant receptor kinases and hence directly linked to plant signaling and downstream cellular responses. Here we detail, firstly, methods to identify and express essential functional GC domains of receptor kinases, and secondly, we describe mass spectrometric methods to quantify cGMP generated by recombinant GCs from receptor kinases in vitro. |
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Geographical breakdown
Country | Count | As % |
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Unknown | 4 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
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Professor > Associate Professor | 1 | 25% |
Researcher | 1 | 25% |
Unknown | 2 | 50% |
Readers by discipline | Count | As % |
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Biochemistry, Genetics and Molecular Biology | 1 | 25% |
Agricultural and Biological Sciences | 1 | 25% |
Unknown | 2 | 50% |