Brian Eckenroth, PhD
Faculty Scientist
Structural Biology of DNA Replication and Repair
Doublie Lab, Larner College of Medicine
89 Beaumont Ave, Given E312, E314
Burlington, VT 05405
United States
- Dept of Microbiology and Molecular Genetics
- Larner College of Medicine
- UVM Center of X-Ray Crystallography
BIO
- Ph.D. in biochemistry with Dr. Robert Hondal at the University of Vermont investigating the molecular mechanism of the mammalian selenoprotein thioredoxin reductase.
- Postdoctoral work with Dr. Stephen Everse and Dr. Anne Mason - Solved the crystal structure of human transferrin in complex with its cellular receptor TFR1.
- Joined the Doublié research group in 2009 as research staff, receiving further training in crystal structure determination from Dr. Sylvie Doublié and Dr. Mark Rould.
- Trained on the mechanical details of x-ray diffraction equipment maintenance with Dr. Rould.
Area(s) of expertise
The focus of my research in the Doublié group is the structural investigation of proteins that play a critical role in maintaining genomic stability. The broad theme is understanding the molecular mechanisms of the enzymes that encounter the thousands of sites of DNA damage that occur within each cell on a daily basis. Aberrant function of these enzymes or mutations in them can contribute to mechanisms of cancer development. I am honored to be recipient of a National Cancer Institute R50 award (R50 CA233185) to support structural studies of DNA polymerase theta which functions in error prone DNA replication or repair in response to DNA breaks, and cancer-based variants of the DNA glycosylases NEIL1-3 as well as DNA polymerase beta that function in the base excision repair pathway.
My broader interest in structural biology is not only for the answers that the structures can provide, but that their investigation generates a platform for researchers to ask better and more specific questions. My combination of academic and industrial experiences, in concert with biochemical, structural and facility management training allow to me serve as the day-to-day resource for students and postdoctoral fellows engaged in structural biology investigating diverse molecular targets.
Bio
- Ph.D. in biochemistry with Dr. Robert Hondal at the University of Vermont investigating the molecular mechanism of the mammalian selenoprotein thioredoxin reductase.
- Postdoctoral work with Dr. Stephen Everse and Dr. Anne Mason - Solved the crystal structure of human transferrin in complex with its cellular receptor TFR1.
- Joined the Doublié research group in 2009 as research staff, receiving further training in crystal structure determination from Dr. Sylvie Doublié and Dr. Mark Rould.
- Trained on the mechanical details of x-ray diffraction equipment maintenance with Dr. Rould.
Areas of Expertise
The focus of my research in the Doublié group is the structural investigation of proteins that play a critical role in maintaining genomic stability. The broad theme is understanding the molecular mechanisms of the enzymes that encounter the thousands of sites of DNA damage that occur within each cell on a daily basis. Aberrant function of these enzymes or mutations in them can contribute to mechanisms of cancer development. I am honored to be recipient of a National Cancer Institute R50 award (R50 CA233185) to support structural studies of DNA polymerase theta which functions in error prone DNA replication or repair in response to DNA breaks, and cancer-based variants of the DNA glycosylases NEIL1-3 as well as DNA polymerase beta that function in the base excision repair pathway.
My broader interest in structural biology is not only for the answers that the structures can provide, but that their investigation generates a platform for researchers to ask better and more specific questions. My combination of academic and industrial experiences, in concert with biochemical, structural and facility management training allow to me serve as the day-to-day resource for students and postdoctoral fellows engaged in structural biology investigating diverse molecular targets.