Dr. Lieberman's research group studies the molecular aspects of protein misfolding in order to understand its impact on human disease and develop research solutions that can lead to new discoveries, therapeutics, and diagnostic tools.

The group's research methods include protein crystallography, as well as biochemical and biophysical characterization, which give them technical expertise into the structure of proteins.  Dr. Lieberman is interested in applying her intimate knowledge of the biophysical nature of proteins in order better understand-and support research related to-protein misfolding and the wide range of diseases it causes. 

One application for this research is the development of a suite of reagents that can be used in a wide variety of research settings. The goal of Dr. Lieberman's team is to help researchers who are dealing with challenging proteins improve the rigor and reproducibility of their experiments by providing them with better reagents–opening the field to new discoveries, as well as potential therapeutics and diagnostic tools. 

Another important ongoing research focus in Dr. Lieberman's lab is the myocilin protein associated with glaucoma. The group's discoveries in this area have far-reaching implications, as they have found similarities between myocilin glaucoma and other protein misfolding disorders, including amyloid diseases. Dr. Lieberman's work with this protein relates back to her passion for developing new reagents: 

"We know that the myocilin protein discovered in the eye is a major played in the prevalent eye disease glaucoma. However, it is a challenging protein to study, so even though this protein was discovered 25 years ago, we still don't understand it. Better reagents could help us make new discoveries related to this protein by producing more stable and consistent results, and in turn could lead to new therapies in the future. I'm passionate about creating new reagents because scientists across the world are dealing with similar difficulties in their own research areas, and new reagents could help them answer important questions."  

Research Goals

  • Characterizing proteins: Using biophysical, structural, and chemical biology to characterize proteins that result in disorders caused by misfolding
  • Improved research outcomes: Developing a suite of new reagents to better control outcomes for scientists working with proteins in many research areas
  • Diagnostic tools: Applying research related to the myocilin protein found in the eye to develop potential tools to help understand and diagnose ophthalmological disorders and diseases
  • Drug development: Utilizing myocilin-related research to develop potential therapeutics to treat glaucoma and other diseases caused by protein misfolding


  • Protein misfolding research: Applying characteristics of protein misfolding disorders to key research areas, including glaucoma  
  • Intramembrane proteolysis: Studying membrane-spanning proteolytic enzymes that are related to those involved in producing amyloid-beta associated with Alzheimer disease
  • Novel small molecule discovery: Researching to discover novel small molecules to inhibit certain mutant protein


  • Pew Scholar in Biomedical Sciences (2010)
  • Blanchard Fellowship (2010)
  • Rosalinde and Arthur Gilbert/American Federation for Aging Research New Investigator Award in Alzheimer Disease (2009)
  • NSF CAREER Award (2008)
  • Glaucoma Research Foundation Shaffer Award for Innovative Glaucoma Research (2008)
  • American Chemical Society Nobel Laureate Signature Award for Graduate Education in Chemistry (2006)