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Phospho-Proteomics

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Cover of 'Phospho-Proteomics'

Table of Contents

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    Book Overview
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    Chapter 1 Thiol-ene-Enabled Detection of Thiophosphorylation as a Labeling Strategy for Phosphoproteins.
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    Chapter 2 Phosphopeptide Detection with Biotin-Labeled Phos-tag.
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    Chapter 3 Phosphopeptide Enrichment by Covalent Chromatography After Solid Phase Derivatization of Protein Digests on Reversed Phase Supports.
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    Chapter 4 Peptide Labeling Using Isobaric Tagging Reagents for Quantitative Phosphoproteomics.
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    Chapter 5 Identification of Direct Kinase Substrates Using Analogue-Sensitive Alleles.
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    Chapter 6 Quantitative Analysis of Tissue Samples by Combining iTRAQ Isobaric Labeling with Selected/Multiple Reaction Monitoring (SRM/MRM).
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    Chapter 7 Enrichment Strategies in Phosphoproteomics.
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    Chapter 8 Phosphopeptide Enrichment by Immobilized Metal Affinity Chromatography.
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    Chapter 9 The Use of Titanium Dioxide for Selective Enrichment of Phosphorylated Peptides.
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    Chapter 10 Sequential Elution from IMAC (SIMAC): An Efficient Method for Enrichment and Separation of Mono- and Multi-phosphorylated Peptides.
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    Chapter 11 Improving the Phosphoproteome Coverage for Limited Sample Amounts Using TiO2-SIMAC-HILIC (TiSH) Phosphopeptide Enrichment and Fractionation.
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    Chapter 12 Offline High pH Reversed-Phase Peptide Fractionation for Deep Phosphoproteome Coverage.
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    Chapter 13 Phosphopeptide Enrichment Using Various Magnetic Nanocomposites: An Overview.
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    Chapter 14 Two Dimensional Gel Electrophoresis-Based Plant Phosphoproteomics.
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    Chapter 15 Variable Digestion Strategies for Phosphoproteomics Analysis.
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    Chapter 16 Online LC-FAIMS-MS/MS for the Analysis of Phosphorylation in Proteins.
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    Chapter 17 Simple and Reproducible Sample Preparation for Single-Shot Phosphoproteomics with High Sensitivity.
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    Chapter 18 Identification of Direct Kinase Substrates via Kinase Assay-Linked Phosphoproteomics.
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    Chapter 19 Phosphoprotein Detection by High-Throughput Flow Cytometry.
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    Chapter 20 Resources for Assignment of Phosphorylation Sites on Peptides and Proteins.
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    Chapter 21 From Phosphosites to Kinases.
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    Chapter 22 Phospho-Proteomics
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    Chapter 23 Systems Analysis for Interpretation of Phosphoproteomics Data.
Attention for Chapter 18: Identification of Direct Kinase Substrates via Kinase Assay-Linked Phosphoproteomics.
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Chapter title
Identification of Direct Kinase Substrates via Kinase Assay-Linked Phosphoproteomics.
Chapter number 18
Book title
Phospho-Proteomics
Published in
Methods in molecular biology, January 2016
DOI 10.1007/978-1-4939-3049-4_18
Pubmed ID
Book ISBNs
978-1-4939-3048-7, 978-1-4939-3049-4
Authors

Liang Xue, Justine V. Arrington, W. Andy Tao

Editors

Louise von Stechow

Abstract

Protein phosphorylation plays an essential role in the regulation of various cellular functions. Dysregulation of phosphorylation is implicated in the pathogenesis of certain cancers, diabetes, cardiovascular diseases, and central nervous system disorders. As a result, protein kinases have become potential drug targets for treating a wide variety of diseases. Identification of kinase substrates is vital not only for dissecting signaling pathways, but also for understanding disease pathologies and identifying novel therapeutic targets. However, identification of bona fide kinase substrates has remained challenging, necessitating the development of new methods and techniques. The kinase assay linked phosphoproteomics (KALIP) approach integrates in vitro kinase assays with global phosphoproteomics experiments to identify the direct substrates of protein kinases. This strategy has demonstrated outstanding sensitivity and a low false-positive rate for kinase substrate screening.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 26 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 1 4%
France 1 4%
Unknown 24 92%

Demographic breakdown

Readers by professional status Count As %
Professor > Associate Professor 4 15%
Student > Ph. D. Student 4 15%
Professor 3 12%
Researcher 3 12%
Student > Master 2 8%
Other 1 4%
Unknown 9 35%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 5 19%
Agricultural and Biological Sciences 4 15%
Chemistry 3 12%
Computer Science 2 8%
Chemical Engineering 1 4%
Other 2 8%
Unknown 9 35%