摘要
Recently, there has been an overwhelming demand for studies on protein post-translational modification （PTM） to understand the increasing complexity from the level of the genome to the proteome. The covalent modifications of proteins with phosphates, lipids, sugars or other residues confer on these proteins additional structural and functional diversity. For instance, protein phosphorylation is involved in a wide range of cellular processes including signal transduction. Protein glycosylation is one of the most abundant PTMs and more than 50% of all human proteins are glycosylated. Glycoproteins are involved in many biological events, such as cell-cell adhesion, communication, immune response and development.
Recently,there has been an overwhelming demand for studies on protein post-translational modification(PTM)to understand the increasing complexity from the level of the genome to the proteome.The covalent modifications of proteins with phosphates,lipids,sugars or other residues confer on these proteins additional structural and functional diversity.For instance,protein phosphorylation is involved in a wide range
作者
Chi Lung Lee
Xuechen Li
Chi Lung Lee;Xuechen Li(Department of Chemistry, Key State Laboratory of Synthetic Chemistry, The University of Hong Kong)
