Biography
Dr. Magdalena Ivanova’s background is in the structural biology, biophysics and biochemistry of protein aggregation and amyloid fibril formation. She joined the University of Michigan Department of Neurology as an Assistant Research Professor in 2013. She is also a member of Program of Biophysics. She completed her PhD in the Institute of Molecular Biophysics at the Florida State University, where she studied the structure of filamentous bacteriophage using x-ray fiber diffraction. After completing her PhD, Dr. Ivanova was a postdoctoral fellow with Prof. David Eisenberg at the UCLA Molecular Biology Institute. She was a research associate at UCLA until she was recruited as a faculty at the University of Michigan. At UCLA, Dr. Ivanova participated in the development of x-ray micro-diffraction, which revealed the first high-resolution structures of amyloid fibrils. The structures of amyloid fibrils brought insights into how they are formed and possible strategies to intervene their formation.
Description of research
The Ivanova Lab (www.umich.edu/~mivanova) applies biochemical and biophysical methods to study protein misfolding, aggregation and amyloid fibril formation. The main focus of the Lab research revolves around the structure of alpha-synuclein, ubiquilin2, and RAN peptides. The abnormal folding of these proteins is implicated in Parkinson’s disease (PD), Amyotrophic Lateral Sclerosis (ALS), and Frontotemporal dementia (FTD). The ultimate goal is to understand the link between the abnormal protein conversion and cellular death. To study the driving forces that cause protein misfolding, Lab researchers develop and validate in vitro systems and examine chemical and physical parameters impacting the formation, isolation and characterization of protein aggregates. Because structurally different aggregates often result from protein misfolding, a range of molecular and cellular systems may be utilized to study how protein aggregation affects cellular homeostasis. The Ivanova Lab employs advanced biophysical (electron microscopy and x-ray diffraction), biochemical (fluorescent based assays and kinetic) and cellular (brain tissue and immortal cells) systems.
Areas of Interest
- Apply biochemical and biophysical methods to study the abnormal amyloid structures.
- Understand the link between protein misfolding and cell phenotypes.
- Develop strategies that interfere, or prevent, the formation of abnormal toxic structures
Clinical Interests
The applications of the Ivanova Lab research address a wide spectrum of protein misfolding disorders like Alzheimer’s disease, Parkinson’s disease, Dementia with Lewy bodies, Amyotrophic lateral sclerosis, and frontotemporal dementia.
