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Plant Receptor Kinases

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Cover of 'Plant Receptor Kinases'

Table of Contents

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    Book Overview
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    Chapter 1 Expression of Plant Receptor Kinases in E. coli
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    Chapter 2 Expression of Plant Receptor Kinases in Yeast
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    Chapter 3 Expression of Plant Receptor Kinases in Tobacco BY-2 Cells
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    Chapter 4 Cell-Free Synthesis of Plant Receptor Kinases
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    Chapter 5 Purification of Plant Receptor Kinases from Plant Plasma Membranes
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    Chapter 6 Photoaffinity Labeling of Plant Receptor Kinases
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    Chapter 7 Quantitative Detection of Oxidative Burst upon Activation of Plant Receptor Kinases
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    Chapter 8 Extraction and Curation of Gene Models for Plant Receptor Kinases for Phylogenetic Analysis
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    Chapter 9 In Silico Prediction of Ligand-Binding Sites of Plant Receptor Kinases Using Conservation Mapping
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    Chapter 10 Co-immunoprecipitation of Plant Receptor Kinases
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    Chapter 11 Autophosphorylation Assays Using Plant Receptor Kinases Synthesized in Cell-Free Systems
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    Chapter 12 Investigation of Autophosphorylation Sites of Plant Receptor Kinases and Phosphorylation of Interacting Partners
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    Chapter 13 In Vitro Assessment of Guanylyl Cyclase Activity of Plant Receptor Kinases
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    Chapter 14 BiFC Assay to Detect Calmodulin Binding to Plant Receptor Kinases
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    Chapter 15 Pull-down Assay to Characterize Ca 2+ /Calmodulin Binding to Plant Receptor Kinases
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    Chapter 16 The Use of FRET/FLIM to Study Proteins Interacting with Plant Receptor Kinases
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    Chapter 17 Detection and Analyses of Endocytosis of Plant Receptor Kinases
Attention for Chapter 16: The Use of FRET/FLIM to Study Proteins Interacting with Plant Receptor Kinases
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Chapter title
The Use of FRET/FLIM to Study Proteins Interacting with Plant Receptor Kinases
Chapter number 16
Book title
Plant Receptor Kinases
Published in
Methods in molecular biology, January 2017
DOI 10.1007/978-1-4939-7063-6_16
Pubmed ID
Book ISBNs
978-1-4939-7062-9, 978-1-4939-7063-6
Authors

Stefanie Weidtkamp-Peters, Yvonne Stahl, Weidtkamp-Peters, Stefanie, Stahl, Yvonne

Abstract

The investigation of protein interactions in living plant tissue has become of increasing importance in recent years. A high spatial and temporal resolution for the observation of in vivo protein interaction is needed, e.g., in order to follow changes of plant receptor kinase interactions and complex formation over time. In vivo fluorescence or Förster resonance energy transfer (FRET) measurements allow for detailed analyses of interacting proteins in their natural environment at a subcellular level. Especially FRET-FLIM (fluorescence lifetime imaging microscopy) measurements provide an extremely powerful and reliable tool meeting the demands for investigating in vivo protein interaction quantitatively and with high precision. Here, we will describe in detail how to practically perform in vivo FRET measurements of receptor kinases in plants and discuss potential pitfalls and points of consideration.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 29 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 29 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 10 34%
Researcher 4 14%
Student > Master 3 10%
Professor > Associate Professor 2 7%
Professor 1 3%
Other 2 7%
Unknown 7 24%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 10 34%
Agricultural and Biological Sciences 10 34%
Engineering 1 3%
Unknown 8 28%