title: Tyrosine modifications in aging.
abstract: CONCLUSIONS
  The understanding of physiological and pathological processes involving protein oxidation, particularly under conditions of aging and oxidative stress, can be aided by proteomic identification of proteins that accumulate oxidative post-translational modifications only if these detected modifications are connected to functional consequences. The modification of tyrosine (Tyr) residues can elicit significant changes in protein structure and function, which, in some cases, may contribute to biological aging and age-related pathologies, such as atherosclerosis, neurodegeneration, and cataracts.
  
  
  BACKGROUND
  Studies characterizing proteins in which Tyr has been modified to 3-nitrotyrosine, 3,4-dihydroxyphenylalanine, 3,3'-dityrosine and other cross-links, or 3-chlorotyrosine are reviewed, with an emphasis on structural and functional consequences.
  
  
  RESULTS
  Distinguishing between inconsequential modifications and functionally significant ones requires careful biochemical and biophysical analysis of target proteins, as well as innovative methods for isolating the effects of the multiple modifications that often occur under oxidizing conditions.
  
  
  CONCLUSIONS
  The labor-intensive task of isolating and characterizing individual modified proteins must continue, especially given the expanding list of known modifications. Emerging approaches, such as genetic and metabolic incorporation of unnatural amino acids, hold promise for additional focused studies of this kind.
authors.affiliation: Department of Pharmaceutical Chemistry, The University of Kansas, Lawrence, KS 66047, USA.
authors.forename: Maria B
authors.initials: MB
authors.lastname: Feeney
authors.forename: Christian
authors.initials: C
authors.lastname: Schöneich
mesh_terms: D000375:Aging; D050197:Atherosclerosis / Q000378:metabolism / Q000503:physiopathology; D002386:Cataract / Q000378:metabolism / Q000503:physiopathology; D006801:Humans; D009410:Nerve Degeneration / Q000378:metabolism / Q000503:physiopathology; D018384:Oxidative Stress; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship; D014443:Tyrosine / Q000737:chemistry / Q000378:metabolism*
chemical_list: D011506:Proteins; D014443:Tyrosine