Ontology highlight
ABSTRACT:
SUBMITTER: Yang YY
PROVIDER: S-EPMC3156339 | biostudies-literature | 2011 Sep
REPOSITORIES: biostudies-literature
Yang Yu-Ying YY Grammel Markus M Hang Howard C HC
Bioorganic & medicinal chemistry letters 20110525 17
Proteomic studies have identified a plethora of lysine acetylated proteins in eukaryotes and bacteria. Determining the individual lysine acetyltransferases responsible for each protein acetylation mark is crucial for elucidating the underlying regulatory mechanisms, but has been challenging due to limited biochemical methods. Here, we describe the application of a bioorthogonal chemical proteomics method to profile and identify substrates of individual lysine acetyltransferases. Addition of 4-pe ...[more]