Jim Cole, PI
Email: email@example.com Office Phone: (860) 486-4333
I am a professor at the University of Connecticut in the Department of Molecular and Cell Biology and the Department of Chemistry. The main research interest in our lab is the mechanism of the innate immunity response to viral infection. Currently, I teach courses on Biophysical Techniques (MCB 4008/5008 syllabus) and the Foundations of Structural Biochemistry (MCB 5012 syllabus). My CV can be found here. A video of my introduction to the 31st Annual Gibbs Conference on Biological Thermodynamics is here.
Stephen Hesler, Graduate Student
The antiviral effector PKR contains a C-terminal kinase domain. I am interested in how dimerization of the kinase domain promotes both active and inactive conformations. Binding of two PKRs to activating dsRNAs brings the kinase domains into close proximity, thus promoting dimerization and activation. Recently, we demonstrated that the kinase domain can dimerize and not activate. I am using biochemical approaches and analytical ultracentrifugation to probe PKR dimerization and PKR-dsRNA interactions.
Dave Mouser, Graduate Student
I utilize biophysical and biochemical techniques to study protein:protein and protein:RNA interactions that regulate the innate immune system. The RIG-I-like receptors detect cytosolic viral dsRNAs to activate innate immunity. I am currently investigating the mechanism by which RIG-I assembles on dsRNA to form a signaling-competent complexes. I am also interested in the interactions between the 2CARD signaling domain of RIG-I and K63-linked polyubiquitin chains.
Cassie Zerbe, Graduate Student
I am interested in the innate immune response to viral infection, particularly proteins that bind and recognize viral RNA. Currently, I am using biochemical and biophysical approaches to understand the mechanism by which RNAs, including Epstein-Barr Encoded RNA I (EBER1) and Adenovirus virus-associated RNA I (VAI), modulate PKR function. I am also using similar techniques to characterize the assembly of active complexes of MDA5 on dsRNA.