title: Protein tyrosine nitration in cellular signal transduction pathways.
abstract: How specificity and reversibility in tyrosine nitration are defined biologically in cellular systems is poorly understood. As more investigations identify proteins involved in cell regulatory pathways in which only a small fraction of that protein pool is modified by nitration to affect cell function, the mechanisms of biological specificity and reversal should come into focus. In this review experimental evidence has been summarized to suggest that tyrosine nitration is a highly selective modification and under certain physiological conditions fulfills the criteria of a physiologically relevant signal. It can be specific, reversible, occurs on a physiological time scale, and, depending on a target, can result in either activation or inhibition.
authors.affiliation: Department of Radiation Oncology, Massey Cancer Center, Virginia Commonwealth University, Richmond, VA, USA.
authors.forename: Vasily A
authors.initials: VA
authors.lastname: Yakovlev
authors.forename: Ross B
authors.initials: RB
authors.lastname: Mikkelsen
mesh_terms: D000818:Animals; D006801:Humans; D009566:Nitrates / Q000378:metabolism*; D019001:Nitric Oxide Synthase / Q000378:metabolism; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D026361:Reactive Nitrogen Species / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology*; D014443:Tyrosine / Q000378:metabolism*
chemical_list: D009566:Nitrates; D026361:Reactive Nitrogen Species; D014443:Tyrosine; D019001:Nitric Oxide Synthase