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Article Synopsis
  • Protein acetylation is a widely studied post-translational modification, and recent research has identified three new forms: lysine malonylation, succinylation, and glutarylation, which mainly affect energy metabolism in diseases caused by Mycobacterium pathogens.
  • Methods involved using high-affinity antibody enrichment and LC-MS/MS analysis to characterize these new lysine modifications and assess their functional impacts in certain proteins.
  • Results showed significant global substrate characterization for these acylations, revealing connections to ribosomal function and various metabolic pathways, highlighting their importance in cellular processes.
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Lysine malonylation is a post-translational modification where a malonyl group, characterized by a negatively charged carboxylate, is covalently attached to the Ɛ-amino side chain of lysine, influencing protein structure and function. Our laboratory identified Mak upregulation in cartilage under aging and obesity, contributing to osteoarthritis (OA). Current antibody-based detection methods face limitations in identifying Mak targets.

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