Protein citrullination results from enzymatic deimination of peptidylarginine and plays an important role in health and disease. Despite increasing scientific interest, the identity and function of citrullinated proteins in vivo remain widely unknown. Thorough proteomic studies could contribute to a
Directed evolution of orthogonal ligand specificity in a single scaffold.
Michael J McLachlan et al.
Angewandte Chemie (International ed. in English), 48(42), 7783-7786 (2009-09-12)
We demonstrated that aluminum (Al)-induced oxalate secretion and plasma membrane (PM) H(+)-ATPase activity in tomato (Lycopersicon esculentum 'Hezuo903') roots were poorly correlated. In addition, vanadate, an inhibitor of PM H(+)-ATPase, had no effect on Al-induced oxalate secretion, but significantly inhibited
Analytical sciences : the international journal of the Japan Society for Analytical Chemistry, 26(6), 645-647 (2010-06-15)
Effective recognition and quantitative analysis of the prion protein are important in drug discovery and diagnosis for prion diseases, such as bovine spongiform encephalopathy and Creutzfeldt-Jakob diseases. We have developed a high-throughput method for a specific and sensitive determination of
Journal of the American Chemical Society, 134(41), 17015-17018 (2012-10-04)
Protein arginine deiminases (PADs) catalyze the hydrolysis of peptidyl arginine to form peptidyl citrulline. Abnormally high PAD activity is observed in a host of human diseases, but the exact role of protein citrullination in these diseases and the identities of
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