Ontology highlight
ABSTRACT:
SUBMITTER: Montgomery DC
PROVIDER: S-EPMC6320254 | biostudies-literature | 2016 May
REPOSITORIES: biostudies-literature
Montgomery David C DC Garlick Julie M JM Kulkarni Rhushikesh A RA Kennedy Steven S Allali-Hassani Abdellah A Kuo Yin-Ming YM Andrews Andrew J AJ Wu Hong H Vedadi Masoud M Meier Jordan L JL
Journal of the American Chemical Society 20160517 20
Lysine acetyltransferases (KATs) are key mediators of cell signaling. Methods capable of providing new insights into their regulation thus constitute an important goal. Here we report an optimized platform for profiling KAT-ligand interactions in complex proteomes using inhibitor-functionalized capture resins. This approach greatly expands the scope of KATs, KAT complexes, and CoA-dependent enzymes accessible to chemoproteomic methods. This enhanced profiling platform is then applied in the most ...[more]