My PhD degree obtained at Instituto Superior Técnico in Biotechnology addressed structural-functional relationships of enzymes in non-conventional media. These low water content systems offer several advantages for the biotechnological exploitation of enzymes. Part of the PhD work was done at the lab. of Lipolyse Enzymatique from the Centre National Recherche Scientifique (CNRS) in Marselha, France. My interest on the structure-function of proteins was then shifted to one of the most important issues in Biology: the folding of proteins. Protein folding and stability was since then one of the main focus of my research, using several proteins as models (the enzyme cutinase and multi-copper oxidases among others) and biophysical techniques as experimental tools. Studies on protein folding and stability were strengthened by leaves to the Aalborg University, Denmark, where collaborations with Steffen Petersen and Daniel Otzen were consolidated and fruitful. In 2003, a sabbatical leave to Adriano Aguzzi’s lab, at the Institute of Neuropathology, University Hospital of Zurich, was the opportunity to start working on prions. From this point, protein aggregation, in vitro and in cells, has become my main interest. Several neurodegenerative diseases, including Alzheimer and prion diseases, result from the misfolding of proteins that traffic through the endoplasmic reticulum (ER) to the cell membrane. One of the key features of protein folding in the endoplasmic reticulum is the formation of disulfide bonds, the so-called oxidative protein folding. Studies on oxidative protein folding and protein aggregation were pursuit in 2010 with a sabbatical leave to the lab of David Ron at the New York Univ., now affiliated to the Cambridge Institute for Medical Research, UK. More recently, in collaboration with Edward Avezov from the UK Dementia Research Institute, Cambridge University, we have been focused on the effects of oxidative and thermal stress on protein aggregation. With my recent join to CCMAR I am planning to focus on proteostasis, i.e., the maintenance of protein folding and function in cells, and how stressors, such as ocean warming and acidification, may disturb cell homeostasis and accelerate proteostasis collapse resulting from protein misfolding and aggregation.