Angewandte Chemie International Edition
10.1002/anie.202004105
RESEARCH ARTICLE
phosphopantetheinylation that are known to date. In combination
with advanced chemical proteomic technologies, our work here
provides an all-in-one snapshot of these known 4'-
phosphopantetheinylated proteins with the resolution of exact
modification sites and suggests potential candidates such as
DHRS2. Methodologically, sample preparations need further
optimization (e.g. auxiliary proteases for peptide digestion, new
cell lines and longer LC gradients) to increase the probability of
identifying new 4'-phosphopantetheinylation sites. Biologically,
our work opens new opportunities to study the functional role of
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We thank the Computing Platform of the Center for Life Science
for supporting the LC-MS/MS data analysis. This work was
supported by Ministry of Science and Technology of China
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