"I am honored to be able to work with the best and the brightest scientists in the industry and have the opportunity to make contributions to the development of novel therapeutics with the potential to treat significant unmet medical needs."
I came to Genentech in 2007 as a Postdoctoral Fellow in the Antibody Engineering department. It was fascinating to have an insider’s view into the drug discovery process and witness groundbreaking basic research being performed at the forefront of the biotechnology industry. Thus when I was offered the opportunity to become a Scientist at Genentech in 2013 I was thrilled. I initially joined the Protein Chemistry department where my group was responsible for purification and characterization of large molecules. In 2015, I joined the Structural Biology department and the focus of my group shifted to purification and characterization of challenging antigens for large molecule therapeutic programs and structure-based drug design for small molecule programs.
The Genentech Postdoctoral Program offers a unique opportunity to carry out cutting-edge basic research in an industry setting. You are surrounded by leading experts in the field and have access to the latest technology and instrumentation. The discoveries made by Postdoctoral Fellows often are the spark for new therapeutic targets or technology developments. As a former Genentech Postdoctoral Fellow I have first-hand experience of how transformative the program can be for developing scientists and am excited to now become a Postdoctoral Fellow mentor.
Cell. 2017 Nov 2;171(4):918-933.e20.
The focus of my lab’s basic research is on engineering and structural characterization of novel antibodies that recognize complex ubiquitin post-translational modifications (PTM). Ubiquitination is a highly conserved PTM where the C-terminus of ubiquitin is linked through an isopeptide bond to a lysine residue of a substrate protein. Ubiquitin contains seven different lysines and a free N-terminus through which additional ubiquitin subunits can be linked to form polyubiquitin chains. Therefore, eight different homotypic polyubiquitin chain linkages can be formed. As a Postdoctoral Fellow, I engineered novel polyubiquitin linkage-specific antibodies that have helped advance the study of the cellular ubiquitination code.
More recently it has been demonstrated that the ubiquitination code is more complex than originally anticipated and the existence of heterotypic polyubiquitin chains containing more than one linkage have been identified. These include both mixed chains, where each ubiquitin subunit has only one lysine involved in a linkage, and branched chains, where ubiquitin subunits have two or more lysines involved in linkages. Since being hired as a Scientist, my lab has expanded the ubiquitin PTM antibody toolbox and established numerous collaborations within the ubiquitin research community. For example, in collaboration with Michael Rape’s lab at UC Berkeley we engineered a bispecific antibody to recognize K11/K48-branched polyubiquitin chains which revealed their novel role in regulation of both cell-cycle and protein quality control.