Diana Mitrea, Phd Email & Phone Number

Boston, Ma, Us

Boston, Massachusetts, United States

Lead the publication & scientific education strategy, including peer-review publications, conference presentations & posters and community engagement. Collaborate with the executive, R&D and corporate development teams to develop and refine the scientific narrative for interactions with investors, partners, collaborators and regulators.

Boston, Massachusetts, United States

Led biochemical and in vitro assay reconstitution assay development and their applications in programs across neurodegeneration, cardiopulmonary, virology and oncology therapeutic areas. Conceptualized and led the execution of several initiatives, including an oncology project (concept to HTS) and application of advanced image analysis to gain mechanism of action insights. Managed a team of up to 10 scientists.

Established the biochemistry lab in the new Boston office; enabled on-site protein production and biochemistry/biophysics. Led in vitro assay development and early discovery efforts, with applications across neurology and oncology therapeutic areas.

My work at St. Jude Children’s Research Hospital focuses on two primary directions: (1) the structure-function relationship and molecular mechanisms for controlling it in the multifunctional nucleolar phospho-protein nucleophosmin (NPM1), and (2) structural, biophysical and functional characterization of membraneless organelles under physiological and pathological conditions. I have experience in the biophysical and structural characterization of folded and intrinsically disordered proteins, as well as protein-protein and protein-RNA coacervates. As part of our recent studies, I discovered that the nucleolar protein NPM1 forms liquid-like coacervates via three different mechanisms: with itself, with nucleolar proteins and ribosomal RNA, providing the first insights into the structural makeshift of the liquid-like matrix of the nucleolus. Furthermore, based on previous findings that the ALS-associated, toxic di-peptide repeats accumulate within nucleoli, I discovered that they insinuate within NPM1-mediated coacervates, subsequently leading to their dissolution, thus providing a potential molecular mechanism for their cellular toxicity.

It has long been understood that protein function is dictated by its three dimensional structure. In recent years, however, an increasing importance has been attributed to structural disorder and structural dynamics in modulating function, especially for proteins involved in molecular signalling. For example, the intrinsically disordered cell cycle regulator p27 inhibits cell cycle progression by folding upon binding to cyclin-dependent kinase/cyclin complexes, while the redox-responsive chaperone Hsp33 is active in an unfolded state. My research focuses on understanding the molecular mechanisms utilized in biological systems that allow protein function to be regulated through local or global unfolding of an otherwise robustly folded polypeptide chain, a general mechanism we like to call "regulated unfolding".

Doctor Of Philosophy (Ph.D.), Biochemistry And Molecular Biology

Activities and Societies: Founding member of ISA (International Student Association)

Bs, Biochemical Engineering

Activities and Societies: Active member in BEST (Board of European Students of Technology)