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A New Chemical Handle for Protein AMPylation at the Host–Pathogen Interface
Author(s) -
Broncel Malgorzata,
Serwa Remigiusz A.,
Tate Edward W.
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201100743
Subject(s) - adenylylation , host (biology) , posttranslational modification , pathogen , interface (matter) , chemistry , key (lock) , bacterial protein , microbiology and biotechnology , biochemistry , enzyme , biology , molecule , organic chemistry , genetics , biosynthesis , gene , ecology , gibbs isotherm
Tagging protein AMPylation: A new chemical reporter for AMPylation, recently identified as a key post‐translational modification during bacterial infection, is a robust tool for detecting and identifying AMPylated proteins in vitro.