Professor David S. Eisenberg
Mailing address: Dept. Chemistry and Biochemistry Univ. of Calif. Los Angeles 611 Charles Young Dr. East Los Angeles, CA 90095-1569
Romany Abskharon
Amyloid proteins are pathological entities in a variety of neurodegenerative diseases such as Alzheimer’s disease and Parkinson’s disease. My research project focuses on: 1) Determining atomic or near-atomic resolution structures of toxic tau oligomers and amyloid oligomers purified from autopsied brain patients using tau specific antibodies.
Einav Tayeb-Fligelman
My research at the Eisenberg lab is dealing with both functional and pathological amyloid. Amyloid are protein fibrils mainly known for their involvement in neurodegeneration. I am studying the interactions and cross-seeding propensity of Tau and Ab, the two key protein players in Alzheimer’s disease.
Qin Cao
My project seeks to develop liganded tau-fibril-binding magnetic nanoparticles, which could achieve the combined magnetic resonance imaging (MRI) and therapy of Alzheimer’s disease.
David Boyer
I am using cryo-electron microscopy and diffraction techniques, along with X-ray crystallography, to study new and exciting structures of amyloid proteins. My main focus is discovering new structures of tau protein, which is involved in over 26 neurodegenerative diseases.
Jeannette Bowler
My research focuses on functional vs. pathogenic amyloids, determining the structures that these proteins can adopt, and understanding their structure-function relationship.
Sean Jiang
Amyloid diseases are associated with pathological deposits of protein fibrils. Previous work in the field has shown that the structure of fibrils extracted from patient tissues often differ from the fibril structures assembled _in vitro_, underscoring the importance of studying patient-derived samples.