Bruce A. Yankner, M.D., Ph.D.

Bruce A. Yankner, M.D., Ph.D.Bruce A. Yankner, M.D., Ph.D. is Professor of Genetics and Neurology at Harvard Medical School, Director of the Harvard Neurodegeneration Training Program, and Co-Director of the Paul F. Glenn Laboratories for Biological Mechanisms of Aging. Dr. Yankner graduated from Princeton University, received his M.D. and Ph.D. from Stanford University, and did a residency at Massachusetts General Hospital. His work has contributed to understanding pathogenic mechanisms in Alzheimer’s disease, Down’s syndrome and Parkinson’s disease, beginning with the initial observation that amyloid beta protein is a toxic molecule, and later with investigations into the roles of presenilin proteins, notch and wnt in neuronal signaling and pathology. Work from his laboratory has defined the transcriptome of the aging human brain, its evolution from mouse to man, and a role for DNA damage in brain aging.  His laboratory has recently identified a stress response network controlled by the REST transcription factor that is required for survival of aging neurons and becomes compromised early in the course of Alzheimer’s disease. He has received the Major Award for Medical Research from the Metropolitan Life Foundation, the Derek Denny-Brown Neurological Scholar Award from the American Neurological Association, the Irving S. Cooper Award from the Mayo Clinic, the Ellison Medical Foundation Senior Scholar Award, the Nathan W. Shock award from NIA and the NIH Director’s Pioneer Award.

Direct Contact

Telephone: 617-432-6800
Email:
Lab Website: http://genetics.med.harvard.edu/yankner/

Selected Publications

Zhang Z, Nadeau P, Song W, Donoviel D, Yuan M, Bernstein A and Yankner BA (2000). Presenilins are required for γ-secretase cleavage of b-APP and transmembrane cleavage of Notch-1. Nature Cell Biol. 2:463-465.

Lu T, Pan Y, Kao S-Y, Li C, Kohane I, Chan J and Yankner BA (2004). Gene regulation and DNA damage in the ageing human brain. Nature 429:833-891.

Hass M and Yankner BA (2005). A γ-secretase-independent mechanism of signal transduction by the amyloid precursor protein. J. Biol. Chem. 280: 36895-36904.