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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 15: Multiple and Selective Reaction Monitoring Using Triple Quadrupole Mass Spectrometer: Preclinical Large Cohort Analysis.
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Chapter title
Multiple and Selective Reaction Monitoring Using Triple Quadrupole Mass Spectrometer: Preclinical Large Cohort Analysis.
Chapter number 15
Book title
Quantitative Proteomics by Mass Spectrometry
Published in
Methods in molecular biology, January 2016
DOI 10.1007/978-1-4939-3524-6_15
Pubmed ID
Book ISBNs
978-1-4939-3522-2, 978-1-4939-3524-6
Authors

Qin Fu, Zhaohui Chen, Shenyan Zhang, Sarah J. Parker, Zongming Fu, Adrienne Tin, Xiaoqian Liu, Jennifer E. Van Eyk

Editors

Salvatore Sechi

Abstract

Multiple reaction monitoring (MRM), sometimes referred to as selective reaction monitoring (SRM), is a mass spectrometry method that can target selective peptides for the detection and quantitation of a protein. Compared to traditional ELISA, MRM assays have a number of advantages including ease in multiplexing several proteins in the same assay and independence from the necessity for high-quality, expensive, and at times unreliable antibodies. Furthermore, MRM assays can be developed to quantify multiple proteoforms of a single protein allowing the quantification of allelic expression of a particular sequence polymorphism, protein isoform, as well as determining site occupancy of posttranslational modification(s). In this chapter, we describe our workflow for target peptide selection, assay optimization, and acquisition multiplexing. Our workflow is presented using the example of constrained MRM assays developed for the serum protein ApoL1 in its various proteoforms to highlight the specific technical considerations necessary for the difficult task of quantifying peptide targets based on highly specific amino acid sequences by MRM.

Mendeley readers

The data shown below were compiled from readership statistics for 38 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 38 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 10 26%
Researcher 6 16%
Student > Master 6 16%
Professor > Associate Professor 5 13%
Other 3 8%
Other 5 13%
Unknown 3 8%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 12 32%
Agricultural and Biological Sciences 8 21%
Chemistry 6 16%
Computer Science 1 3%
Business, Management and Accounting 1 3%
Other 5 13%
Unknown 5 13%