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Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and reduce chemical noise during analyte detection. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.Secondary fragmentations occur in the interaction cell and can be induced by various factors. Fragmentation induced by collision with inert gases, such as N2, Ar, He, etc., is called...

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Related Experiment Video

Updated: Jun 6, 2026

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Analysis of isobaric quantitative proteomic data using TMT-Integrator and FragPipe computational platform.

Hui-Yin Chang1,2, Yamei Deng1, Ruohong Li1

  • 1Department of Pathology, University of Michigan, Ann Arbor, MI, USA.

Nature Communications
|March 2, 2026
PubMed
Summary
This summary is machine-generated.

TMT-Integrator, a new bioinformatics tool, enhances quantitative proteomics by providing integrated reports from tandem mass tag (TMT) and isobaric tags for relative and absolute quantitation (iTRAQ) experiments. It offers more robust protein and phosphosite quantification compared to existing methods.

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Last Updated: Jun 6, 2026

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

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Published on: November 15, 2017

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Published on: June 8, 2020

Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools
07:01

Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools

Published on: August 19, 2025

Area of Science:

  • Proteomics
  • Bioinformatics
  • Mass Spectrometry

Background:

  • Isobaric mass tags like TMT and iTRAQ are crucial for multiplex quantitative proteomics.
  • Accurate peptide and protein quantification is essential for biological discovery.

Purpose of the Study:

  • To introduce TMT-Integrator, a bioinformatics tool for processing TMT and iTRAQ quantitation results.
  • To provide integrative reports at multiple biological levels (gene, protein, peptide, PTM site).
  • To evaluate the performance of TMT-Integrator within the FragPipe computational platform.

Main Methods:

  • Development and integration of TMT-Integrator into the FragPipe computational platform.
  • Analysis of five diverse TMT datasets, including ccRCC, E. coli spike-in, and human cell lysates.
  • Performance benchmarking against MaxQuant and Proteome Discoverer using OmicsEV.

Main Results:

  • TMT-Integrator, via FragPipe, quantified more proteins in E. coli and ccRCC whole proteome datasets.
  • More phosphorylated sites were quantified in the ccRCC phosphoproteome dataset.
  • FragPipe coupled with TMT-Integrator demonstrated superior and more robust quantification performance.

Conclusions:

  • TMT-Integrator is a versatile tool for comprehensive analysis of TMT and iTRAQ quantitative proteomics data.
  • Integration with FragPipe offers a powerful and robust workflow for quantitative proteomics.
  • This tool advances the analysis of complex proteomic datasets, including phosphoproteomics.