title: Protein modification in aging: an update.
abstract: Post-translational modifications of proteins are an important biologic tool for the production of various protein species from a single gene, which may vary in conformation, function, biologic half-life and complex formation with other proteins. The present minireview summarizes a few selected research observations important for the role of post-translational modifications in biologic aging and age-related diseases, including farnesylation, methylglyoxal-derivatization, transglutaminase pathways and the formation of 3-nitrotyrosine and 2-oxo-histidine in vivo.
authors.affiliation: Department of Pharmaceutical Chemistry, The University of Kansas, 2095 Constant Avenue, Lawrence, KS 66047, USA. schoneic@ku.edu
authors.forename: Christian
authors.initials: C
authors.lastname: Schöneich
mesh_terms: D000375:Aging / Q000235:genetics / Q000378:metabolism*; D006639:Histidine / Q000031:analogs & derivatives / Q000378:metabolism; D006801:Humans; D034904:Lamin Type A; D019636:Neurodegenerative Diseases / Q000201:enzymology; D009687:Nuclear Proteins / Q000378:metabolism; D010084:Oxidation-Reduction; D011371:Progeria / Q000209:etiology / Q000378:metabolism; D011498:Protein Precursors / Q000378:metabolism; D011499:Protein Processing, Post-Translational / Q000235:genetics*; D011765:Pyruvaldehyde / Q000378:metabolism; D011503:Transglutaminases / Q000378:metabolism; D014443:Tyrosine / Q000378:metabolism
chemical_list: D034904:Lamin Type A; D009687:Nuclear Proteins; D011498:Protein Precursors; C090764:prelamin A; C083725:2-oxohistidine; D014443:Tyrosine; D006639:Histidine; D011765:Pyruvaldehyde; D011503:Transglutaminases