Prof. Andrea Mozzarelli

Andrea Mozzarelli has been Full Professor of Biochemistry in the Department of Pharmacy, University of Parma, Parma, Italy, since 2000. He has served as Coordinator of the Ph.D program in Biochemistry and Molecular Biology, University of Parma, since 2011. Prof. Mozzarelli was also a Fogarty Fellow at the NIH, Laboratory of Chemical Physics, 1984-1985.

He is a Member of the Editorial Board of Biochimica et Biophysica Acta: Protein and  Proteomics, Current Medicinal Chemistry, and Frontiers in Molecular Biosciences. He has also been Guest Editor for special issues of Biochimica et Biophysica Acta: Protein and  Proteomics on “Hemoglobin-Based Oxygen Carriers,” “Protein structure and function in the crystalline state: from x-ray crystallography to spectroscopy,” and “Cofactor-dependent enzymes: evolution, molecular mechanisms and bioapplications."

The scientific activity of Prof. Mozzarelli's group is aimed at:

  1. the characterisation of the stability, catalytic mechanism and regulation of cofactor-dependent enzymes
  2. in silico and in vitro identification of enzyme effectors
  3. the elucidation of structure-dynamics-function relationships of hemoglobins exploiting biochemical and biophysical methods, including absorption microspectrophotometry in solution, in silica gels and in the crystalline state
  4. the development of haemoglobin-based oxygen carriers as blood substitutes
  5. the application of proteomic approaches for the analysis of food products and biological fluids.

He has published more than 150 papers in peered review journals, H-index  35.

In the INTEGRATE-ETN, Prof. Mozzarelli is the main supervisor for ESR2. The research project of ESR2 focuses on expressing and characterising the enzymes SAT and OASS; screening optimized OASS inhibitors and SAT ligands; crystallising SAT and OASS in the absence and presence of inhibitors, and SAT-OASS complex; identifying the regulatory mechanism controlling SAT-OASS activities; and understanding the gene control for the expression of SRAP enzymes under different bacteria environmental conditions, via analysis of mRNA pattern and protein pattern in bacteria extracts.(WP3). 

Integrate-etn.eu

This project has received funding from the European Union’s Horizon 2020 research and innovation programme under the Marie Sklodowska Curie grant agreement No  642620
European Union