Protein malonylation, a reversible post-translational modification of lysine residues, is associated with various biological functions, such as cellular regulation and pathogenesis. In proteomics, to improve our understanding of the mechanisms of malonylation at the molecular level, the identification of malonylation sites via an efficient methodology is essential. However, experimental identification of malonylated substrates via mass spectrometry is time-consuming, labor-intensive, and expensive.

Reference
Pubmed: Chung CR, Chang YP, Hsu YL, Chen S, Wu LC, Horng JT, Lee TY. Incorporating hybrid models into lysine malonylation sites prediction on mammalian and plant proteins. Sci Rep. 2020 Jun 29;10(1):10541. doi: 10.1038/s41598-020-67384-w.

    Protein malonylation, a reversible post-translational modification of lysine residues, is associated with various biological functions, such as cellular regulation and pathogenesis. In proteomics, to improve our understanding of the mechanisms of malonylation at the molecular level, the identification of malonylation sites via an efficient methodology is essential. However, experimental identification of malonylated substrates via mass spectrometry is time-consuming, labor-intensive, and expensive.

Reference
Pubmed: Chung CR, Chang YP, Hsu YL, Chen S, Wu LC, Horng JT, Lee TY. Incorporating hybrid models into lysine malonylation sites prediction on mammalian and plant proteins. Sci Rep. 2020 Jun 29;10(1):10541. doi: 10.1038/s41598-020-67384-w.