Multifunctional Reagents for Quantitative Proteome-Wide Analysis of Protein Modification in Human Cells and Dynamic Profiling of Protein Lipidation During Vertebrate Development
Author(s)
Type
Journal Article
Abstract
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.
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.
Date Issued
2015-05-11
Date Acceptance
2015-02-14
Citation
Angewandte Chemie-International Edition, 2015, 54 (20), pp.5948-5951
ISSN
1521-3773
Publisher
Wiley-VCH Verlag
Start Page
5948
End Page
5951
Journal / Book Title
Angewandte Chemie-International Edition
Volume
54
Issue
20
Copyright Statement
© 2015 The Authors. Published by Wiley-VCH Verlag GmbH & Co.
KGaA. 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
KGaA. 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
License URL
Subjects
Science & Technology
Physical Sciences
Chemistry, Multidisciplinary
Chemistry
capture reagents
lipidation
mass spectrometry
post-translational modification
proteomics
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IDENTIFICATION
Publication Status
Published