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This volume describes prominent methodologies developed by laboratories that have been leading the field of quantitative proteomics by mass spectrometry. The procedures for performing the experiments are described in an easy-to-understand manner with many technical details that usually are not reported in typical research articles. This second edition of Quantitative Proteomics by Mass Spectrometry provides a broad perspective of the methodologies used for quantifying proteins and post-translational modifications in different types of biomedical specimens. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and thorough, Quantitative Proteomics by Mass Spectrometry, Second Edition is a valuable resource to help researchers understand and learn about the latest tools used in the study of quantitative proteomics by mass spectrometry.
Increased Depth and Breadth of Plasma Protein Quantitation via Two Dimensional Liquid Chromatography/Multiple Reaction Monitoring-Mass Spectrometry with Labeled Peptide Standards.- Quantitative Analysis of the Wirt5-Regulated Lysine Succinylation Proteome in Mammalian Cells.- Determining the Composition and Stability of Protein Complexes Using an Integrated Label-Free and Stable Isotope Labeling Strategy.- Label-Free Quantitation for Clinical Proteomics.- Proteogenomic Methods to Improve Genome Annotation.- Mass Spectrometry-Based Quantitative O-GlcNAcomic Analysis.- Isolating and Quantifying Plasma HDL Proteins by Sequential Density Gradient Ultracentrifugation and Targeted Proteomics.- A Method for Label-Free Differential Top-Down Proteomics.- Multiplexed Immunoaffinity Enrichment of Peptides with Anti-Peptide Antibodies and Quantification by Stable Isotope Dilution Multiple Reaction Monitoring Mass Spectrometry.- High Throughput Quantitative Proteomics Enabled by Mass Defect-Based 12-Plex DiLeu Isobaric Tags.- Isotopic N, N-Dimethyl Leucine (iDiLeu) for Absolute Quantification of Peptides Using a Standard Curve Approach.- Selecting Optimal Peptides for Targeted Proteomic Experiments in Human Plasma Using In Vitro Synthesized Proteins as Analytical Standards.- Using the CPTAC Assay Portal to Identify and Implement Highly Characterized Targeted Proteomics Assays.- Large-Scale and Deep Quantitative Proteome Profiling Using Isobaric Lableing Coupled with Two-Dimensional LC-MS/MS.- Multiple and Selective Reaction Monitoring Using Triple Quadrupole Mass Spectrometer: Pre-Clinical Large Cohort Analysis.- Methods for SWATHT: Data Independent Acquisition on TripleTOF Mass Spectrometers.- Measurement of Phosphorylated Peptides with Absolute Quantification.- Proteomic Analysis of Protein Turnover by Metabolic Whole Rodent Pulse-Chase Isotopic Labeling and Shotgun Mass Spectrometry Analysis.
