Experience

Dewpoint Therapeutics

• United States
• Biotechnology Research
• 100 - 200 Employee

• Associate Director

  • Mar 2022 - Present

• Group Leader - Biochemistry

  • Apr 2020 - Mar 2022

  Boston, Massachusetts, United States

• Research Investigator

  • Aug 2019 - Apr 2020



St. Jude Children's Research Hospital

• United States
• Hospitals and Health Care
• 700 & Above Employee

• Staff Scientist

  • Jul 2015 - Aug 2019

  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… Show more 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.

• Postdoctoral Research Associate

  • Sep 2010 - Jul 2015

  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… Show more 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".



SUNY Upstate Medical University

• United States
• Hospitals and Health Care
• 700 & Above Employee

• Postoctoral Research Associate

  • Dec 2009 - Aug 2010

• Graduate Research Assistant

  • Aug 2004 - Nov 2009


Babes-Bolyai University
• Romania
• Higher Education
• 700 & Above Employee
• Undergraduate Student

  • 1999 - 2004
• Undergraduate Student Researcher

  • Jun 2003 - Aug 2003