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Quantitative Proteomics by Mass Spectrometry

Overview of attention for book
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 8: A Method for Label-Free, Differential Top-Down Proteomics. - PubMed - NCBI
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Chapter title
A Method for Label-Free, Differential Top-Down Proteomics. - PubMed - NCBI
Chapter number 8
Book title
Quantitative Proteomics by Mass Spectrometry
Published in
Methods in molecular biology, January 2016
DOI 10.1007/978-1-4939-3524-6_8
Pubmed ID
Book ISBNs
978-1-4939-3522-2, 978-1-4939-3524-6
Authors

Ntai, Ioanna, Toby, Timothy K, LeDuc, Richard D, Kelleher, Neil L, Ioanna Ntai, Timothy K. Toby, Richard D. LeDuc, Neil L. Kelleher

Editors

Salvatore Sechi

Abstract

Biomarker discovery in the translational research has heavily relied on labeled and label-free quantitative bottom-up proteomics. Here, we describe a new approach to biomarker studies that utilizes high-throughput top-down proteomics and is the first to offer whole protein characterization and relative quantitation within the same experiment. Using yeast as a model, we report procedures for a label-free approach to quantify the relative abundance of intact proteins ranging from 0 to 30 kDa in two different states. In this chapter, we describe the integrated methodology for the large-scale profiling and quantitation of the intact proteome by liquid chromatography-mass spectrometry (LC-MS) without the need for metabolic or chemical labeling. This recent advance for quantitative top-down proteomics is best implemented with a robust and highly controlled sample preparation workflow before data acquisition on a high-resolution mass spectrometer, and the application of a hierarchical linear statistical model to account for the multiple levels of variance contained in quantitative proteomic comparisons of samples for basic and clinical research.

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The data shown below were collected from the profiles of 2 X users who shared this research output. Click here to find out more about how the information was compiled.
Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 28 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 28 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 6 21%
Student > Bachelor 5 18%
Student > Master 5 18%
Researcher 4 14%
Professor 2 7%
Other 4 14%
Unknown 2 7%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 10 36%
Chemistry 4 14%
Chemical Engineering 2 7%
Engineering 2 7%
Agricultural and Biological Sciences 2 7%
Other 7 25%
Unknown 1 4%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 13 February 2016.
All research outputs
#17,785,991
of 22,846,662 outputs
Outputs from Methods in molecular biology
#7,242
of 13,127 outputs
Outputs of similar age
#267,675
of 393,581 outputs
Outputs of similar age from Methods in molecular biology
#752
of 1,470 outputs
Altmetric has tracked 22,846,662 research outputs across all sources so far. This one is in the 19th percentile – i.e., 19% of other outputs scored the same or lower than it.
So far Altmetric has tracked 13,127 research outputs from this source. They receive a mean Attention Score of 3.4. This one is in the 39th percentile – i.e., 39% of its peers scored the same or lower than it.
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We're also able to compare this research output to 1,470 others from the same source and published within six weeks on either side of this one. This one is in the 42nd percentile – i.e., 42% of its contemporaries scored the same or lower than it.