MS3 eliminates ratio distortion in isobaric labeling-based multiplexed quantitative proteomics

Quantitative mass spectrometry-based proteomics is highly versatile, but not easily multiplexed. Isobaric labeling strategies allow mass spectrometry-based multiplexed proteome quantification; however, ratio distortion due to protein quantification interference is a common effect. We present a multi...

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Detalles Bibliográficos
Autores principales: Ting, Lily, Rad, Ramin, Gygi, Steven P., Haas, Wilhelm
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2011
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3205343/
https://www.ncbi.nlm.nih.gov/pubmed/21963607
http://dx.doi.org/10.1038/nmeth.1714
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author Ting, Lily
Rad, Ramin
Gygi, Steven P.
Haas, Wilhelm
author_facet Ting, Lily
Rad, Ramin
Gygi, Steven P.
Haas, Wilhelm
author_sort Ting, Lily
collection PubMed
description Quantitative mass spectrometry-based proteomics is highly versatile, but not easily multiplexed. Isobaric labeling strategies allow mass spectrometry-based multiplexed proteome quantification; however, ratio distortion due to protein quantification interference is a common effect. We present a multi-proteome model (mixture of human and yeast proteins) in a 6-plex isobaric labeling system to fully document the interference effect, and we report that a multistage MS3-based approach almost completely eliminates interference.
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spelling pubmed-32053432012-05-01 MS3 eliminates ratio distortion in isobaric labeling-based multiplexed quantitative proteomics Ting, Lily Rad, Ramin Gygi, Steven P. Haas, Wilhelm Nat Methods Article Quantitative mass spectrometry-based proteomics is highly versatile, but not easily multiplexed. Isobaric labeling strategies allow mass spectrometry-based multiplexed proteome quantification; however, ratio distortion due to protein quantification interference is a common effect. We present a multi-proteome model (mixture of human and yeast proteins) in a 6-plex isobaric labeling system to fully document the interference effect, and we report that a multistage MS3-based approach almost completely eliminates interference. 2011-10-02 /pmc/articles/PMC3205343/ /pubmed/21963607 http://dx.doi.org/10.1038/nmeth.1714 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Ting, Lily
Rad, Ramin
Gygi, Steven P.
Haas, Wilhelm
MS3 eliminates ratio distortion in isobaric labeling-based multiplexed quantitative proteomics
title MS3 eliminates ratio distortion in isobaric labeling-based multiplexed quantitative proteomics
title_full MS3 eliminates ratio distortion in isobaric labeling-based multiplexed quantitative proteomics
title_fullStr MS3 eliminates ratio distortion in isobaric labeling-based multiplexed quantitative proteomics
title_full_unstemmed MS3 eliminates ratio distortion in isobaric labeling-based multiplexed quantitative proteomics
title_short MS3 eliminates ratio distortion in isobaric labeling-based multiplexed quantitative proteomics
title_sort ms3 eliminates ratio distortion in isobaric labeling-based multiplexed quantitative proteomics
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3205343/
https://www.ncbi.nlm.nih.gov/pubmed/21963607
http://dx.doi.org/10.1038/nmeth.1714
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AT gygistevenp ms3eliminatesratiodistortioninisobariclabelingbasedmultiplexedquantitativeproteomics
AT haaswilhelm ms3eliminatesratiodistortioninisobariclabelingbasedmultiplexedquantitativeproteomics

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