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Lysine residues are the basic, positively charged amino acids located at various positions within proteins. Their ε-amino group is highly reactive and serves as both a structural and functional anchor for numerous critical post-translational modifications, including acetylation, methylation, ubiquitination, and SUMOylation. These modifications regulate protein activity, stability, localization, and interactions, playing vital roles in gene regulation, cell signaling, and metabolic processes. Altered lysine modification status has been implicated in various diseases, highlighting the biological importance of targeted lysine residue study—but "protein lysine residues" itself does not correspond to a singular therapeutic target, receptor, or molecule.
Inhibition or modulation of enzymes that modify lysine residues (e.g., acetylation, methylation, ubiquitination, SUMOylation)
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