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Kinase Inhibitors

Overview of attention for book
Cover of 'Kinase Inhibitors'

Table of Contents

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    Book Overview
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    Chapter 1 Targeting Cancer with Small-Molecular-Weight Kinase Inhibitors.
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    Chapter 2 Small-Molecule Protein and Lipid Kinase Inhibitors in Inflammation and Specific Models for Their Evaluation
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    Chapter 3 Measuring the Activity of Leucine-Rich Repeat Kinase 2: A Kinase Involved in Parkinson’s Disease
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    Chapter 4 Measuring PI3K Lipid Kinase Activity
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    Chapter 5 A Fluorescence Polarization Assay for the Discovery of Inhibitors of the Polo-Box Domain of Polo-Like Kinase 1
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    Chapter 6 Assessment of Hepatotoxicity Potential of Drug Candidate Molecules Including Kinase Inhibitors by Hepatocyte Imaging Assay Technology and Bile Flux Imaging Assay Technology
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    Chapter 7 Kinase Inhibitors
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    Chapter 8 Chemoproteomic characterization of protein kinase inhibitors using immobilized ATP.
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    Chapter 9 Proteome-Wide Identification of Staurosporine-Binding Kinases Using Capture Compound Mass Spectrometry
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    Chapter 10 Affinity Purification of Proteins Binding to Kinase Inhibitors Immobilized on Self-Assembling Monolayers
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    Chapter 11 Kinase Inhibitor Profiling Using Chemoproteomics
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    Chapter 12 Covalent cross-linking of kinases with their corresponding peptide substrates.
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    Chapter 13 Receptor Tyrosine Kinase Inhibitor Profiling Using Bead-Based Multiplex Sandwich Immunoassays
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    Chapter 14 Monitoring Phosphoproteomic Response to Targeted Kinase Inhibitors Using Reverse-Phase Protein Microarrays
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    Chapter 15 Measuring Phosphorylation-Specific Changes in Response to Kinase Inhibitors in Mammalian Cells Using Quantitative Proteomics
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    Chapter 16 Investigation of Acquired Resistance to EGFR-Targeted Therapies in Lung Cancer Using cDNA Microarrays
Attention for Chapter 12: Covalent cross-linking of kinases with their corresponding peptide substrates.
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Chapter title
Covalent cross-linking of kinases with their corresponding peptide substrates.
Chapter number 12
Book title
Kinase Inhibitors
Published in
Methods in molecular biology, January 2012
DOI 10.1007/978-1-61779-337-0_12
Pubmed ID
21960223
Book ISBNs
978-1-61779-336-3, 978-1-61779-337-0
Authors

Alexander V. Statsuk, Kevan M. Shokat, Statsuk, Alexander V., Shokat, Kevan M.

Abstract

Protein phosphorylation represents the most dominant and evolutionary conserved posttranslational modification for information transfer in cells and organisms. The human genome encodes >500 protein kinases, and thousands of phosphorylation sites are present in mammalian proteome. To develop a global view of phosphorylation network, there is a need to map the connectivity between kinases and phosphoproteome. We developed a chemical kinase-substrate cross-linker 1 that converts transient kinase-substrate interactions into a covalently linked kinase-substrate complex in vitro and in the presence of cell lysates. The method can be applied to identify unknown upstream kinases responsible for phosphorylation events in cell lysates.

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X Demographics

The data shown below were collected from the profile of 1 X user who shared this research output. Click here to find out more about how the information was compiled.
 Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 15 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 15 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 6 40%
Researcher 3 20%
Professor > Associate Professor 2 13%
Student > Master 2 13%
Lecturer > Senior Lecturer 1 7%
Other 0 0%
Unknown 1 7%
Readers by discipline Count As %
Agricultural and Biological Sciences 8 53%
Biochemistry, Genetics and Molecular Biology 2 13%
Computer Science 1 7%
Medicine and Dentistry 1 7%
Neuroscience 1 7%
Other 1 7%
Unknown 1 7%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 05 December 2011.
All research outputs
#15,239,825
of 22,659,164 outputs
Outputs from Methods in molecular biology
#5,279
of 13,019 outputs
Outputs of similar age
#163,118
of 244,041 outputs
Outputs of similar age from Methods in molecular biology
#263
of 473 outputs
Altmetric has tracked 22,659,164 research outputs across all sources so far. This one is in the 22nd percentile – i.e., 22% of other outputs scored the same or lower than it.
So far Altmetric has tracked 13,019 research outputs from this source. They receive a mean Attention Score of 3.3. This one is in the 45th percentile – i.e., 45% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 244,041 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 21st percentile – i.e., 21% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 473 others from the same source and published within six weeks on either side of this one. This one is in the 34th percentile – i.e., 34% of its contemporaries scored the same or lower than it.

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