Posttranslational modifications of lysine and evolving role in heart pathologies-Recent developments
作者： Miroslava Stastna , Jennifer E. Van Eyk
关键词: Cell signaling 、 Proteome 、 Cell type 、 Cell 、 Amino acid residue 、 Neddylation 、 SUMO protein 、 Lysine 、 Computational biology 、 Biology 、 Biochemistry 、 Molecular biology
摘要: The alteration in proteome composition induced by environmental changes and various pathologies is accompanied the modifications of proteins specific cotranslational PTMs. type site stoichiometry PTMs can affect protein functions, alter cell signaling, have acute chronic effects. particular interest drawn to those amino acid residues that undergo several different We hypothesize these selected are biologically rare act within as molecular switches. There are, at least, 12 lysine currently known, them been shown be competitive they influence ability a modified PTM. In this review, we discuss occur on lysine, specifically neddylation sumoylation, proteomic approaches applied for identification quantification Of emerging roles heart disease what inferred from work other types organs.
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