Eduardo Pinho Melo
My PhD was in the area of Biotechnology and I have addressed structural-functional relationships of enzymes in non-conventional media. Part of the PhD work was done at the lab. of Lipolyse Enzymatique from the Centre National Recherche Scientifique (CNRS) in France, under the supervision of Robert Verger. My interest on structure-function of proteins was then guided to one of the most important issues in Biology: the folding of proteins. Protein folding and stability was since then the main focus of my research using several proteins and several biophysical techniques. Collaborations with Steffen Petersen and Daniel Otzen from Denmark were very important in this topic. In 2003, a sabbatical leave to the lab. of Adriano Aguzzi, at the University Hospital of Zurich, was the opportunity to initiate work on prion diseases. Several neurodegenerative diseases, including prion diseases, result from misfolding of proteins that traffic through the endoplasmic reticulum to the cell membrane and one of the key features during this traffic is disulfide bond formation, the so-called oxidative protein folding. Studies on oxidative protein folding and its relation to neurodegenerative diseases were initiated in 2010 with a sabbatical leave to the lab of David Ron at the New York Univ., Skirball Institute of Biomolecular Medicine, and were pursued actively in collaboration with David Ron, now affiliated to the Cambridge Institute for Medical Research, University of Cambridge, UK.