We investigate the biological chemistry and molecular mechanisms of nitric oxide signaling. Nitric oxide is a free radical that mediates blood flow and many other physiological responses within every major organ system.
Currently mass spectrometry-based proteomic data in conjunction with structure-function analysis explore the biochemical and biophysical specificity of two nitric oxide-mediated post translational modifications cysteine S-nitrosation and tyrosine nitration. Studies also explore the consequences of these modifications on protein function.
In addition, we are evaluating the usefulness of tracking specific nitric oxide-modified and oxidized proteins in human diseases (e.g., respiratory distress syndromes of neonates and adults, vascular disorders and neurodegenerative disorders). Our goal is to determine if they can be used as predictors of disease development, disease outcome or as surrogate markers for determining the efficacy of therapeutic interventions.
Finally, we are exploring the use of protein tyrosine nitration to heighten immune responses and to augment the function of proteins in the coagulation cascade.