RNA-protein interactions in bacterial antibiotic resistance and the mammalian anti-viral response; mammalian sweet taste receptor and sweet protein structure, function and interaction.
Christine Dunham, Ph.D.
Ribosome function and structure; mechanism of viral mRNA frameshifts; structure and function of RNA-binding proteins involved in mRNA processing and transport
Dr. Dynan, a Georgia Research Alliance Eminent Scholar, will focus his research on repairing double-strand breaks that occur in DNA from ionizing radiation. Such studies hold promise in cancer treatment because selective inhibition of DNA repair in tumor cells provides a strategy to increase the effectiveness of radiation therapy, while limiting normal tissue damage. Dynan’s research also has applications for gene correction for sickle cell disease.
The principal goal of our research is to scrutinize high-resolution structural details and to understand the molecular mechanisms of large assemblies, including ribonucleoprotein complexes and membrane proteins using integrated approaches of cryo-EM, x-ray crystallography and fluorescence light microscopy.
Ichiro Matsumura, Ph.D.
Faculty Research Page
My objective is to understand the adaptive evolution of protein structure and function. I recapitulate the evolutionary process in the laboratory, and identify the correlations between specific changes in tertiary structure and improvements in fitness. These experiments often yield proteins with enhanced industrial or pharmaceutical utility.
The lab will use structural biology to focus on nuclear receptor mediated transcription, on complexes between specific lipid transporters and their cognate nuclear receptor recipients and will utilize structure and ancestral gene resurrection to understand the evolution of novel function within proteins.
The primary purpose of the research in my laboratory is to understand the molecular basis of the control of cell proliferation and of mechanisms by which this control is circumvented in neoplastic cell growth. This knowledge will be applied to help identify new targets for small molecule drug therapy for cancer and other diseases in which aberrant cell proliferation is involved.
We use a quantitative mass spectrometry approach to define protein aggregation and post-translational modification events observed in neurodegenerative disease.
Keith D. Wilkinson, Ph.D.
Professor and Associate Chair
Our laboratory concentrates on the regulation of protein amount and location in the cell. We are studying the ubiquitin-dependent proteolysis system that is responsible for regulated degradation of intracellular proteins as well as the role of ubiquitin and ubiquitin-like proteins as a targeting signal.
Eric Dammer, Ph.D.
Faculty with Secondary Appointments in the Department of Biochemistry
Lou Ann Brown (Pediatrics)
Judith Fridovich-Keil (Human Genetics)
Dean Jones (Pulmonology)
David Lambeth (Pathology)
Allan Platt (Family & Preventive Medicine)
Stephen Warren (Human Genetics)