title: Protein synthesis, posttranslational modifications, and aging.
abstract: Posttranslational modifications of proteins are involved in determining their activities, stability, and specificity of interaction. More than 140 major and minor modifications of proteins have been reported. Of these, only a few have been studied in relation to the aging of cells, tissues, and organisms. These include phosphorylation, methylation, ADP-ribosylation, oxidation, glycation, and deamidation. Several of these modifications occur on proteins involved in crucial cellular processes, such as DNA synthesis, protein synthesis, protein degradation, signal transduction, cytoskeletal organization, and the components of extracellular matrix. Some of the modifications are the markers of abnormal and altered proteins for rapid degradation. Others make them less susceptible to degradation by normal proteolytic enzymes, and hence these accumulate during aging.
authors: Department of Chemistry, Aarhus University, Denmark.
authors: S I
authors: SI
authors: Rattan
authors: A
authors: A
authors: Derventzi
authors: B F
authors: BF
authors: Clark
mesh_terms: D000246:Adenosine Diphosphate Ribose / Q000378:metabolism; D000375:Aging; D000577:Amides / Q000737:chemistry; D000818:Animals; D004261:DNA Replication; D017127:Glycation End Products, Advanced; D006801:Humans; D007536:Isomerism; D008745:Methylation; D010084:Oxidation-Reduction; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*; D015398:Signal Transduction
chemical_list: D000577:Amides; D017127:Glycation End Products, Advanced; D011506:Proteins; D000246:Adenosine Diphosphate Ribose