Poirier, Michelle A., Ph.D.

Assistant Professor
Director, Structural Neurobiology Laboratory

Main Office Address

CMSC 8-121
The Johns Hopkins Hospital
600 North Wolfe St.
Baltimore, MD 21287-5371

Phone: 410-502-4232
Fax: 410-614-0013

E-mail: mpoirie1@jhmi.edu

Laboratory Technician/Assistant

Zhipeng Hou
Phone 410-614-0012
E-mail: zhou1@jhmi.edu

Education

Professional Interests

Dr. Poirier and her research group use biophysical and biochemical techniques as well as cell and transgenic mouse models to investigate the role of protein aggregation in Huntington’s disease and, more recently, Parkinson’s disease.  Their efforts are aimed at isolating and identifying the toxic species in these diseases and how abnormal protein structure may be contributing to cell toxicity.  A better understanding of the pathogenic pathways of these neurodegenerative disorders could lead to rational therapies that may have implications for other related protein aggregation diseases.

Selected Publications

Ross, C.A. and Poirier, M.A.  What is the role of protein aggregation in  neurodegeneration?  Nature Reviews Molecular and Cell Biology  (2005) 6:891-898.

Poirier, M.A. , Jiang, H., and Ross, C.A.  A structure-based analysis of huntingin mutant polyglutamine aggregation and toxicity: evidence for a compact beta-sheet structure.  Human Molecular Genetics (2005) 14: 765-774.

Ross, C.A. and Poirier, M.A.  Protein aggregation and neurodegenerative disease.  Nature Medicine (2004) 10 Suppl: S10-17.

Ross, C.A., Poirier, M.A., Wanker, E.E., and Amzel, M.  Polyglutamine fibrillogenesis: the pathway unfolds.  Proceedings of the National Academy of Sciences, U.S.A. (2003) 100: 1-3.

Poirier, M.A., Li, H., Macosko, J., Cai, S., Amzel, M.and Ross, C.A.  Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrillization. The Journal of Biological Chemistry  (2002) 277: 41032-41037.