Zexian Liu , Jun Cao, Qian Ma, Xinjiao Gao, Jian Ren and Yu Xue . (2010) GPS-YNO2: Computational prediction of tyrosine nitration sites in proteins. Molecular BioSystems (In press). |
Early after the discovery of the freely-diffusible signaling molecule and second messenger nitric oxide (NO) and its function in signal transduction within the vasculature and nervous system, it became obvious that NO also take part in cytotoxic cytotoxicity when abundantly produced by iNOS, eNOS or nNOS (Ignarro, L.J. et al ., 1990 ). When NO meets molecular oxygen in hydrophobic environments where these species concentrate, the nitrogen dioxide could be formed, then reactive nitrogen species are derived which leave nitration as the molecular footprints by reactions with proteins. Tyrosine nitration is a kind of covalent post-translational modifications which adds a nitro (-NO2) group onto either one of the two ortho carbons of the aromatic ring of tyrosine resides. Originally, protein tyrosine nitration was considered to take place only in vitro mediated by reactive nitrating agent such as tetranitromethane (