Effect of S-nitrosylation on enzymes involved in glycogen and glucose metabolism of CNS
Several neuropathology are characterized by excessive production of nitric oxide (NO) where one of the major consequence is S-nitrosylation of protein a non-protein thiols. CNS glycogen is biosynthesized in astrocyte, where it is metabolized to lactate and it is delivered to neurons. The goal of this project consists in study the effect of S-nitrosylation on structure-function of enzymes involved in metabolism of glycogen and glucose of CNS as hexokinase, triosephosphate isomerase, aldolase, glycogen synthase and glycogen phosphorylase.
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- Jorge Romero M, and Curtino Juan A. C-chain-bound glycogenin is released from proteoglycogen by isoamylase and is able to autoglucosylate. (2003) Biochemical and Biophysical Research Communications 2003 305 (4): 811-814.
- Romero Jorge M., Mary E. Reed, Montich Guillermo, and Curtino Juan A. Inactivation and Thermal Stabilization of Glycogenin by Linked Glycogen. (2001) Biochemical and Biophysical Research Communications 2001 289 (1): 69-74.
- Degree in Biological Chemistry, UNC, 1995.
- PhD in Chemistry, UNC, 2003.
- Postdoctoral: Dep. Cell Biology and Physiology, University of New Mexico, Albuquerque, NM, USA, 2005-2007
- Research Career of CONICET member at CIQUIBIC-CONICET-Extra. Qca. Biological-FCQ-UNC
- Assistant professor at the College of Chemical Sciences-National University of Córdoba-Argentina