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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 6: Mass Spectrometry-Based Quantitative O-GlcNAcomic Analysis.
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Chapter title
Mass Spectrometry-Based Quantitative O-GlcNAcomic Analysis.
Chapter number 6
Book title
Quantitative Proteomics by Mass Spectrometry
Published in
Methods in molecular biology, January 2016
DOI 10.1007/978-1-4939-3524-6_6
Pubmed ID
Book ISBNs
978-1-4939-3522-2, 978-1-4939-3524-6
Authors

Junfeng Ma, Gerald W. Hart Ph.D., Gerald W. Hart

Editors

Salvatore Sechi

Abstract

The dynamic co- and post-translational modification (PTM) of proteins, O-linked β-D-N-acetylglucosamine modification (O-GlcNAcylation) of serine/threonine residues is critical in many cellular processes, contributing to multiple physiological and pathological events. The term "O-GlcNAcome" refers to not only the complete set of proteins that undergo O-GlcNAcylation but also the O-GlcNAc status at individual residues, as well as the dynamics of O-GlcNAcylation in response to various stimuli. O-GlcNAcomic analyses have been a challenge for many years. In this chapter, we describe a recently developed approach for the identification and quantification of O-GlcNAc proteins/peptides from complex samples.

Mendeley readers

The data shown below were compiled from readership statistics for 3 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 3 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 2 67%
Other 1 33%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 1 33%
Chemistry 1 33%
Neuroscience 1 33%