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Natural isotope correction improves analysis of protein modification dynamics
Stable isotope labelling in combination with high-resolution mass spectrometry approaches are increasingly used to analyze both metabolite and protein modification dynamics. To enable correct estimation of the resulting dynamics, it is critical to correct the measured values for naturally occurring...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8626371/ https://www.ncbi.nlm.nih.gov/pubmed/34705077 http://dx.doi.org/10.1007/s00216-021-03732-7 |
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author | Dietze, Jörn van Pijkeren, Alienke Egger, Anna-Sophia Ziegler, Mathias Kwiatkowski, Marcel Heiland, Ines |
author_facet | Dietze, Jörn van Pijkeren, Alienke Egger, Anna-Sophia Ziegler, Mathias Kwiatkowski, Marcel Heiland, Ines |
author_sort | Dietze, Jörn |
collection | PubMed |
description | Stable isotope labelling in combination with high-resolution mass spectrometry approaches are increasingly used to analyze both metabolite and protein modification dynamics. To enable correct estimation of the resulting dynamics, it is critical to correct the measured values for naturally occurring stable isotopes, a process commonly called isotopologue correction or deconvolution. While the importance of isotopologue correction is well recognized in metabolomics, it has received far less attention in proteomics approaches. Although several tools exist that enable isotopologue correction of mass spectrometry data, the majority is tailored for the analysis of low molecular weight metabolites. We here present PICor which has been developed for isotopologue correction of complex isotope labelling experiments in proteomics or metabolomics and demonstrate the importance of appropriate correction for accurate determination of protein modifications dynamics, using histone acetylation as an example. |
format | Online Article Text |
id | pubmed-8626371 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-86263712021-12-01 Natural isotope correction improves analysis of protein modification dynamics Dietze, Jörn van Pijkeren, Alienke Egger, Anna-Sophia Ziegler, Mathias Kwiatkowski, Marcel Heiland, Ines Anal Bioanal Chem Communication Stable isotope labelling in combination with high-resolution mass spectrometry approaches are increasingly used to analyze both metabolite and protein modification dynamics. To enable correct estimation of the resulting dynamics, it is critical to correct the measured values for naturally occurring stable isotopes, a process commonly called isotopologue correction or deconvolution. While the importance of isotopologue correction is well recognized in metabolomics, it has received far less attention in proteomics approaches. Although several tools exist that enable isotopologue correction of mass spectrometry data, the majority is tailored for the analysis of low molecular weight metabolites. We here present PICor which has been developed for isotopologue correction of complex isotope labelling experiments in proteomics or metabolomics and demonstrate the importance of appropriate correction for accurate determination of protein modifications dynamics, using histone acetylation as an example. Springer Berlin Heidelberg 2021-10-27 2021 /pmc/articles/PMC8626371/ /pubmed/34705077 http://dx.doi.org/10.1007/s00216-021-03732-7 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Communication Dietze, Jörn van Pijkeren, Alienke Egger, Anna-Sophia Ziegler, Mathias Kwiatkowski, Marcel Heiland, Ines Natural isotope correction improves analysis of protein modification dynamics |
title | Natural isotope correction improves analysis of protein modification dynamics |
title_full | Natural isotope correction improves analysis of protein modification dynamics |
title_fullStr | Natural isotope correction improves analysis of protein modification dynamics |
title_full_unstemmed | Natural isotope correction improves analysis of protein modification dynamics |
title_short | Natural isotope correction improves analysis of protein modification dynamics |
title_sort | natural isotope correction improves analysis of protein modification dynamics |
topic | Communication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8626371/ https://www.ncbi.nlm.nih.gov/pubmed/34705077 http://dx.doi.org/10.1007/s00216-021-03732-7 |
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