Titlebook: Kinase Signaling Networks; Aik-Choon Tan,Paul H. Huang Book 2017 Springer Science+Business Media, LLC, part of Springer Nature 2017 Protei

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Expression of Recombinant Phosphoproteins for Signal Transduction Studiesf recombinant phosphoproteins by directly incorporating phosphoserine as a nonstandard amino acid. This protocol utilizes an optimized phosphoserine orthogonal translation system and an engineered strain of . containing no genomic amber codons. This approach has been used to generate a variety of ph

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Allosteric Modulation of Src Family Kinases with ATP-Competitive Inhibitorsf SFK SH2 and SH3 domains with their intramolecular ligands leads to reduced kinase activity by stabilizing an inactive ATP-binding site conformation. Disruption of these intramolecular interactions stabilizes a more active ATP-binding site conformation and restores SFK activity. Interestingly, this

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Proteomic Profiling of Protein Kinase Inhibitor Targets by Mass Spectrometryrapeutics. Our rapid small-molecule target profiling protocol combines affinity enrichment and SILAC for proteomic identification of small molecule-protein interactions. Selective interactions are easily discernable from nonspecific protein binding by quantitative ratios. Using kinase inhibitors as

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Utilizing the Luminex Magnetic Bead-Based Suspension Array for Rapid Multiplexed Phosphoprotein Quanphorylation, the addition of phosphate groups, most often occurs on serine, threonine, or tyrosine residues due to the action of protein kinases. This structural change causes the protein to become activated (or deactivated) and enables it in turn to initiate the phosphorylation of other proteins in

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Label-Free Phosphoproteomic Approach for Kinase Signaling Analysismed by means of either labeling or label-free mass spectrometry (MS) methods. Because of their simplicity and universality, label-free methodology is gaining acceptance and popularity in molecular biology research. Analytical workflows for label-free quantification of phosphorylation, however, need

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Cell-Specific Labeling for Analyzing Bidirectional Signaling by Mass Spectrometryue insight in contact-initiated receptor tyrosine kinase signaling, transfer of proteomic material between heterotypic cells, and interactions between normal and oncogenic cells. Here we describe current methods for cell-specific labeling of heterotypic cells with isotopic labeled amino acids (e.g.,