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Plant Phosphoproteomics

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Cover of 'Plant Phosphoproteomics'

Table of Contents

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    Book Overview
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    Chapter 1 The Plant Kinome
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    Chapter 2 Phosphatases in plants.
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    Chapter 3 Phosphoproteomics in cereals.
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    Chapter 4 Screening of Kinase Substrates Using Kinase Knockout Mutants
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    Chapter 5 Phosphopeptide Profiling of Receptor Kinase Mutants
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    Chapter 6 Combining Metabolic (15)N Labeling with Improved Tandem MOAC for Enhanced Probing of the Phosphoproteome.
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    Chapter 7 Kinase activity and specificity assay using synthetic peptides.
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    Chapter 8 Absolute quantitation of protein posttranslational modification isoform.
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    Chapter 9 Phosphorylation Stoichiometry Determination in Plant Photosynthetic Membranes
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    Chapter 10 Phosphopeptide immuno-affinity enrichment to enhance detection of tyrosine phosphorylation in plants.
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    Chapter 11 The Peptide Microarray ChloroPhos1.0: A Screening Tool for the Identification of Arabidopsis thaliana Chloroplast Protein Kinase Substrates
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    Chapter 12 Plant Protein Kinase Substrates Identification Using Protein Microarrays
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    Chapter 13 Targeted Analysis of Protein Phosphorylation by 2D Electrophoresis.
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    Chapter 14 Computational phosphorylation network reconstruction: methods and resources.
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    Chapter 15 Computational Identification of Protein Kinases and Kinase-Specific Substrates in Plants
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    Chapter 16 Databases for plant phosphoproteomics.
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    Chapter 17 Phosphorylation Site Prediction in Plants
Attention for Chapter 5: Phosphopeptide Profiling of Receptor Kinase Mutants
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Chapter title
Phosphopeptide Profiling of Receptor Kinase Mutants
Chapter number 5
Book title
Plant Phosphoproteomics
Published in
Methods in molecular biology, January 2015
DOI 10.1007/978-1-4939-2648-0_5
Pubmed ID
Book ISBNs
978-1-4939-2647-3, 978-1-4939-2648-0
Authors

Xu Na Wu, Waltraud X. Schulze, Wu, Xu Na, Schulze, Waltraud X.

Abstract

The family of transmembrane receptor kinase is the largest protein kinase family in Arabidopsis. However many of these kinases have yet uncharacterized functions and little is known about direct substrates of these kinases. Here, we present a large-scale phosphoproteomics method involving label-free quantitation-based comparative phosphopeptide profiling of knockout mutants in receptor-like kinases. This approach, among other physiological and cell biological experiments, is one step in understanding the functional roles of plant kinases in the context of their signaling networks.

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The data shown below were compiled from readership statistics for 4 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 4 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 2 50%
Unspecified 1 25%
Researcher 1 25%
Readers by discipline Count As %
Unspecified 1 25%
Biochemistry, Genetics and Molecular Biology 1 25%
Computer Science 1 25%
Agricultural and Biological Sciences 1 25%