William Van Nostrand, Ph.D.

Headshot photo

Professor, Stony Brook University, Department of Neurosurgery

Dr. Van Nostrand is interested in understanding the role of amyloid ß-protein precursor (AßPP) and its derived fragment Aß in the cerebrovascular in the pathogenesis of Alzheimer’s disease and related disorders. His research focuses on identifying factors that regulate the assembly of Aß peptides in brain, with an emphasis of understanding their pathogenic interactions with cells in cerebral blood vessels that lead to cellular degeneration, loss of vessel wall integrity, and hemorrhagic stroke. His studies in this area are multi-leveled involving basic protein-protein interactions between Aß peptides and distinct chaperone proteins, in vitro cell culture models, and several in vivo transgenic mouse models recently developed in the laboratory. In addition, he has a strong interest in physiologic functions of AßPP in regulating hemostatic mechanisms. To this end he utilizes several in vivo mouse gene knockout and transgenic models to elucidate the role of AßPP in vascular processes involved in coagulation, stroke, and traumatic brain injury.

Dr. Van Nostrand earned his undergraduate degree in biochemistry from the State University of New York, Stony Brook, NY, and his Ph.D. from the University of California, Irvine, CA.

Funded Research

Project Description Researchers Funding
Modulation of Abeta Assembly and Cytotoxicity by a Fragment of Myelin Basic Protein

We have identified myelin basic protein (MBP) as a novel factor in brain that can bind Abeta and potently inhibit its assembly into fibrils. In light of this novel finding the overall hypothesis of this proposal is that defined fragments of MBP can regulate Abeta assembly and modulate its cytotoxic properties. This will provide the basis for developing novel and potent Abeta assembly inhibitors.


Selected Publications

These published papers resulted from Cure Alzheimer’s Fund support.
Hoos MD, Ahmed M, Smith SO, Van Nostrand WE, Myelin basic protein binds to and inhibits the fibrillar assembly of Aß42 in vitro, Biochemistry, 48, June 9, 2009, 4720-4727