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Quantitative Proteomics by Mass Spectrometry

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Cover of 'Quantitative Proteomics by Mass Spectrometry'

Table of Contents

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    Book Overview
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    Chapter 1 Increased Depth and Breadth of Plasma Protein Quantitation via Two-Dimensional Liquid Chromatography/Multiple Reaction Monitoring-Mass Spectrometry with Labeled Peptide Standards.
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    Chapter 2 Quantitative Analysis of the Sirt5-Regulated Lysine Succinylation Proteome in Mammalian Cells.
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    Chapter 3 Determining the Composition and Stability of Protein Complexes Using an Integrated Label-Free and Stable Isotope Labeling Strategy.
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    Chapter 4 Label-Free Quantitation for Clinical Proteomics.
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    Chapter 5 Proteogenomic Methods to Improve Genome Annotation
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    Chapter 6 Mass Spectrometry-Based Quantitative O-GlcNAcomic Analysis.
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    Chapter 7 Isolating and Quantifying Plasma HDL Proteins by Sequential Density Gradient Ultracentrifugation and Targeted Proteomics.
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    Chapter 8 A Method for Label-Free, Differential Top-Down Proteomics. - PubMed - NCBI
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    Chapter 9 Multiplexed Immunoaffinity Enrichment of Peptides with Anti-peptide Antibodies and Quantification by Stable Isotope Dilution Multiple Reaction Monitoring Mass Spectrometry.
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    Chapter 10 High-Throughput Quantitative Proteomics Enabled by Mass Defect-Based 12-Plex DiLeu Isobaric Tags
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    Chapter 11 Isotopic N,N-Dimethyl Leucine (iDiLeu) for Absolute Quantification of Peptides Using a Standard Curve Approach.
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    Chapter 12 Selecting Optimal Peptides for Targeted Proteomic Experiments in Human Plasma Using In Vitro Synthesized Proteins as Analytical Standards.
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    Chapter 13 Using the CPTAC Assay Portal to Identify and Implement Highly Characterized Targeted Proteomics Assays
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    Chapter 14 Large-Scale and Deep Quantitative Proteome Profiling Using Isobaric Labeling Coupled with Two-Dimensional LC-MS/MS
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    Chapter 15 Multiple and Selective Reaction Monitoring Using Triple Quadrupole Mass Spectrometer: Preclinical Large Cohort Analysis.
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    Chapter 16 Methods for SWATH™: Data Independent Acquisition on TripleTOF Mass Spectrometers. - PubMed - NCBI
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    Chapter 17 Measurement of Phosphorylated Peptides with Absolute Quantification.
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    Chapter 18 Proteomic Analysis of Protein Turnover by Metabolic Whole Rodent Pulse-Chase Isotopic Labeling and Shotgun Mass Spectrometry Analysis
Attention for Chapter 1: Increased Depth and Breadth of Plasma Protein Quantitation via Two-Dimensional Liquid Chromatography/Multiple Reaction Monitoring-Mass Spectrometry with Labeled Peptide Standards.
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Chapter title
Increased Depth and Breadth of Plasma Protein Quantitation via Two-Dimensional Liquid Chromatography/Multiple Reaction Monitoring-Mass Spectrometry with Labeled Peptide Standards.
Chapter number 1
Book title
Quantitative Proteomics by Mass Spectrometry
Published in
Methods in molecular biology, January 2016
DOI 10.1007/978-1-4939-3524-6_1
Pubmed ID
Book ISBNs
978-1-4939-3522-2, 978-1-4939-3524-6
Authors

Andrew J. Percy Ph.D., Juncong Yang, Andrew G. Chambers, Christoph H. Borchers Ph.D., Andrew J. Percy, Christoph H. Borchers

Editors

Salvatore Sechi

Abstract

Absolute quantitative strategies are emerging as a powerful and preferable means of deriving concentrations in biological samples for systems biology applications. Method development is driven by the need to establish new-and validate current-protein biomarkers of high-to-low abundance for clinical utility. In this chapter, we describe a methodology involving two-dimensional (2D) reversed-phase liquid chromatography (RPLC), operated under alkaline and acidic pH conditions, combined with multiple reaction monitoring (MRM)-mass spectrometry (MS) (also called selected reaction monitoring (SRM)-MS) and a complex mixture of stable isotope-labeled standard (SIS) peptides, to quantify a broad and diverse panel of 253 proteins in human blood plasma. The quantitation range spans 8 orders of magnitude-from 15 mg/mL (for vitamin D-binding protein) to 450 pg/mL (for protein S100-B)-and includes 31 low-abundance proteins (defined as being <10 ng/mL) of potential disease relevance. The method is designed to assess candidates at the discovery and/or verification phases of the biomarker pipeline and can be adapted to examine smaller or alternate panels of proteins for higher sample throughput. Also detailed here is the application of our recently developed software tool-Qualis-SIS-for protein quantitation (via regression analysis of standard curves) and quality assessment of the resulting data. Overall, this chapter provides the blueprint for the replication of this quantitative proteomic method by proteomic scientists of all skill levels.

Mendeley readers

The data shown below were compiled from readership statistics for 6 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 6 100%

Demographic breakdown

Readers by professional status Count As %
Other 1 17%
Student > Bachelor 1 17%
Professor 1 17%
Researcher 1 17%
Professor > Associate Professor 1 17%
Other 1 17%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 2 33%
Agricultural and Biological Sciences 1 17%
Chemistry 1 17%
Neuroscience 1 17%
Unknown 1 17%