Multifunctional Reagents for Quantitative Proteome-Wide Analysis of Protein Modification in Human Cells and Dynamic Profiling of Protein Lipidation During Vertebrate Development**

Novel multifunctional reagents were applied in combination with a lipid probe for affinity enrichment of myristoylated proteins and direct detection of lipid-modified tryptic peptides by mass spectrometry. This method enables high-confidence identification of the myristoylated proteome on an unprece...

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Autores principales: Broncel, Malgorzata, Serwa, Remigiusz A, Ciepla, Paulina, Krause, Eberhard, Dallman, Margaret J, Magee, Anthony I, Tate, Edward W
Formato: Online Artículo Texto
Lenguaje:English
Publicado: WILEY-VCH Verlag 2015
Materias:
Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4471546/
https://www.ncbi.nlm.nih.gov/pubmed/25807930
http://dx.doi.org/10.1002/anie.201500342
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author Broncel, Malgorzata
Serwa, Remigiusz A
Ciepla, Paulina
Krause, Eberhard
Dallman, Margaret J
Magee, Anthony I
Tate, Edward W
author_facet Broncel, Malgorzata
Serwa, Remigiusz A
Ciepla, Paulina
Krause, Eberhard
Dallman, Margaret J
Magee, Anthony I
Tate, Edward W
author_sort Broncel, Malgorzata
collection PubMed
description Novel multifunctional reagents were applied in combination with a lipid probe for affinity enrichment of myristoylated proteins and direct detection of lipid-modified tryptic peptides by mass spectrometry. This method enables high-confidence identification of the myristoylated proteome on an unprecedented scale in cell culture, and allowed the first quantitative analysis of dynamic changes in protein lipidation during vertebrate embryonic development.
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spelling pubmed-44715462015-06-23 Multifunctional Reagents for Quantitative Proteome-Wide Analysis of Protein Modification in Human Cells and Dynamic Profiling of Protein Lipidation During Vertebrate Development** Broncel, Malgorzata Serwa, Remigiusz A Ciepla, Paulina Krause, Eberhard Dallman, Margaret J Magee, Anthony I Tate, Edward W Angew Chem Int Ed Engl Communications Novel multifunctional reagents were applied in combination with a lipid probe for affinity enrichment of myristoylated proteins and direct detection of lipid-modified tryptic peptides by mass spectrometry. This method enables high-confidence identification of the myristoylated proteome on an unprecedented scale in cell culture, and allowed the first quantitative analysis of dynamic changes in protein lipidation during vertebrate embryonic development. WILEY-VCH Verlag 2015-05-11 2015-03-25 /pmc/articles/PMC4471546/ /pubmed/25807930 http://dx.doi.org/10.1002/anie.201500342 Text en © 2015 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. http://creativecommons.org/licenses/by/3.0/ This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Communications
Broncel, Malgorzata
Serwa, Remigiusz A
Ciepla, Paulina
Krause, Eberhard
Dallman, Margaret J
Magee, Anthony I
Tate, Edward W
Multifunctional Reagents for Quantitative Proteome-Wide Analysis of Protein Modification in Human Cells and Dynamic Profiling of Protein Lipidation During Vertebrate Development**
title Multifunctional Reagents for Quantitative Proteome-Wide Analysis of Protein Modification in Human Cells and Dynamic Profiling of Protein Lipidation During Vertebrate Development**
title_full Multifunctional Reagents for Quantitative Proteome-Wide Analysis of Protein Modification in Human Cells and Dynamic Profiling of Protein Lipidation During Vertebrate Development**
title_fullStr Multifunctional Reagents for Quantitative Proteome-Wide Analysis of Protein Modification in Human Cells and Dynamic Profiling of Protein Lipidation During Vertebrate Development**
title_full_unstemmed Multifunctional Reagents for Quantitative Proteome-Wide Analysis of Protein Modification in Human Cells and Dynamic Profiling of Protein Lipidation During Vertebrate Development**
title_short Multifunctional Reagents for Quantitative Proteome-Wide Analysis of Protein Modification in Human Cells and Dynamic Profiling of Protein Lipidation During Vertebrate Development**
title_sort multifunctional reagents for quantitative proteome-wide analysis of protein modification in human cells and dynamic profiling of protein lipidation during vertebrate development**
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4471546/
https://www.ncbi.nlm.nih.gov/pubmed/25807930
http://dx.doi.org/10.1002/anie.201500342
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