Nunilo Cremades Casasin
Centre: BIFI
Institution: University of Zaragoza, Zaragoza (Spain)
Position: Researcher from the University of Zaragoza
E-mail: ncc@unizar.es
Phone: 876 555415
Profile: Ver
Personal statement
Since I began my research career I have focused on the field of protein biophysics, from the study of the conformational landscape of proteins and characterization of ligand binding, to the assembly of proteins into amyloid aggregates and biomolecular condensates formed by phase separation processes. I completed my doctoral thesis at the University of Zaragoza, with research stays at Johns Hopkins University (USA) and the University of Virginia (USA). Later, I joined Professor Christopher Dobson’s group at the University of Cambridge, in the United Kingdom; with an international Human Frontier Science Program scholarship. In 2014, I formed my own research group, first at the University of Cambridge with a Dorothy Hodgkin scholarship from the Royal Society of London, and then at the University of Zaragoza, at BIFI, with a Ramón y Cajal contract. I am currently a Professor at that university, and serve as the academic secretary of the BIFI Management Team.
Researcher profile
Currently, I am an R4 researcher and principal investigator of the research group focused on the study of protein assembly processes in amyloid aggregates and biomolecular condensates associated with neurodegenerative diseases such as Alzheimer’s and Parkinson’s. The accumulation of amyloid aggregates of certain proteins in the brain is the histopathological hallmark of these diseases, although the molecular origins and mechanisms of amyloid protein aggregation, as well as its associated toxicity, are unknown. In recent years, it has been proposed that aberrant liquid-liquid and liquid-solid phase separation processes of proteins may be involved in the initial events of these diseases. Our group aims to help resolve these fundamental questions by combining a wide range of biophysical techniques, including single particle fluorescence, with cell biology experiments. In turn, we are developing methodology that allows early diagnosis and the design of more effective treatments for these types of diseases.
Why my research is important
The phenomenon of protein amyloid misfolding and aggregation has emerged in recent years as a topic of fundamental relevance in a wide range of scientific disciplines, such as physics, chemistry, biology and medicine. This explosion of interest has arisen following the recognition that approximately 50 human diseases and disorders are associated with the process of protein amyloid aggregation, some of which are among the most common and debilitating medical conditions in the modern world, including Alzheimer’s disease, Parkinson’s disease and type II diabetes. In turn, a new mode of cellular compartmentalization through the formation of liquid biomolecular condensates by a protein assembly process has recently been identified and it has been proposed that the anomalous formation or maturation of this type of condensates could be related to multiple human diseases, including certain neurodegenerative diseases. Understanding these processes at the molecular level is essential for the development of diagnostic methods, as well as for the design of new and better specific treatments.
Know more about me and my research here
– https://www.bifi.es/biophysics/#4
– https://sites.google.com/view/neuromol
– https://www.linkedin.com/in/nunilo-cremades-casasin-009346275
