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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 11: The Peptide Microarray ChloroPhos1.0: A Screening Tool for the Identification of Arabidopsis thaliana Chloroplast Protein Kinase Substrates
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Chapter title
The Peptide Microarray ChloroPhos1.0: A Screening Tool for the Identification of Arabidopsis thaliana Chloroplast Protein Kinase Substrates
Chapter number 11
Book title
Plant Phosphoproteomics
Published in
Methods in molecular biology, January 2015
DOI 10.1007/978-1-4939-2648-0_11
Pubmed ID
Book ISBNs
978-1-4939-2647-3, 978-1-4939-2648-0
Authors

Anna Schönberg, Sacha Baginsky, Schönberg, Anna, Baginsky, Sacha

Abstract

We designed the peptide microarray ChloroPhos1.0 to screen for substrates of chloroplast protein kinases. The peptides represented on the microarray were selected from phosphoproteomics data, and the identified chloroplast phosphopeptides were spotted as 15-mers on a glass slide with the phosphorylation site centered. Altogether, 905 distinct peptides from chloroplast proteins are present on the array. Here we describe how the array can be used to identify the target protein spectrum of chloroplast kinases. We present the method and discuss limitations and challenges associated with the determination of phosphorylation activity on peptide substrates in vitro.

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The data shown below were compiled from readership statistics for 3 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Germany 1 33%
Unknown 2 67%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 1 33%
Student > Bachelor 1 33%
Researcher 1 33%
Readers by discipline Count As %
Computer Science 1 33%
Agricultural and Biological Sciences 1 33%
Medicine and Dentistry 1 33%