In most neurodegenerative disorders, disease is caused by a single protein misfolding into a beta-sheet rich conformation that is capable of self-templating and spreading throughout the brain. This mechanism was first described in 1982 by Dr. Stanley Prusiner for the prion protein (PrP). In prion diseases, such as scrapie, chronic wasting disease, or Creutzfeldt-Jakob disease, cellular PrP (PrPC) misfolds into the scrapie conformation (PrPSc) to cause progressive degeneration. More recently, this phenomenon has been seen with a handful of additional proteins, including α-synuclein, beta-amyloid, SOD-1, tau, and TDP-43.
Research in the Woerman Lab is focused on investigating the formation of α-synuclein prions in multiple system atrophy and Parkinson’s disease, as well as tau prion formation in Alzheimer’s disease, chronic traumatic encephalopathy, progressive supranuclear palsy, and other frontotemporal dementias. In particular, we are interested in understanding the factors driving the conformation differences in α-synuclein and tau prion strains, and developing diagnostic and therapeutic tools reflective of these strain differences.
Learn more at https://www.woermanlab.com/
BA Ohio Wesleyan University, 2008
PhD George Washington University, 2013
Postdoctoral Fellow University of California, San Francisco, 2013-2016