Benjamin Wolozin, M.D. Ph.D.

Professor of Pharmacology and Neurology at Boston University School of Medicine

Dr. Wolozin’s research investigates the pathophysiology of neurodegenerative diseases. His research investigates the mechanisms by which genes cause dementia (Alzheimer’s disease and Frontotemporal Dementia) and movement disorders (Parkinson’s disease and Amyotrophic Lateral Sclerosis). The group has recently focused on understanding the role of RNA binding proteins in neurodegenerative diseases, focusing on how the regulated protein aggregation of RNA binding proteins contributes pathological aggregation and neuronal dysfunction.  The laboratory uses a variety of models to study disease, including cell culture (primary neurons, iPSCs and cell lines), C. elegans, transgenic mice and pathological human tissues.  The laboratory also uses these approaches for drug discovery seeking to identify novel compounds for therapy and diagnosis of neurodegenerative diseases. Dr. Wolozin also has experience doing epidemiological research, including studies highlighting the potential value of statins and of angiotensin receptor blockers as therapy for dementia. 


Dr. Wolozin graduated magna cum laude from Wesleyan University in Middletown, CT. He earned his M.D. and Ph.D. degrees from Albert Einstein College of Medicine, and did his postdoctoral fellowships at the National Institute of Mental Health.  He joined Loyola University Medical Center in 1996 moved to Boston University in 2004. Dr. Wolozin has received numerous awards for his research including the Donald B. Lindsley Prize, Society for Neuroscience, the A. E. Bennett Award from the Society for Biological Psychiatry, the Zenith Award from the Alzheimer Association, the Graduate Faculty of the Year Award from Loyola University Medical Center and the Collaborator of the Year from Boston University Evans Center.   He has served on numerous editorial boards, and currently chair of the NIH CMND study section.  Dr. Wolozin has published over 140 papers or book chapters, and been awarded 4 patents.


Funded Research

Project Description Researchers Funding
Inhibition of Tau Pathology in Human Neurons

The work proposed in this application stems from dramatic advances in our understanding of reasons that nerve cells die in Alzheimer’s disease. This work derives from new insights into how our bodies respond to stress. We have discovered a group of proteins, termed RNA-binding proteins (RBPs), that bind directly to tau protein (one of the major proteins that accumulates in the brains of patients with Alzheimer’s disease). Binding of these RBPs causes tau to form small clumps, termed oligomers, which are very harmful.

Regulation of RNA Translation by MAPT in Alzheimer’s Disease

We have recently identified a new type of molecular pathology in AD that develops in concert with neurofibrillary tangles, which are one of the hallmark pathologies of Alzheimer’s disease (AD). Neurofibrillary tangles form from clumping of tau protein, and occur as nerve cells deteriorate. In the Wolozin lab, we have discovered that a class of proteins, termed RNA binding proteins, clump alongside the tau protein and constitute a new type of pathology in the AD.

Regulation of Tau Oligomerization by Interaction with TIA-­‐1, a Component of Stress Granules

Published work from multiple groups indicates that tau phosphorylation causes tau to mis-­‐localize to the soma and dendrites, where TIA-­‐1 is present [20][21][22]. Our preliminary   data   indicates   that   the   TIA-­‐1   binds   the phosphorylated tau. Tau promotes formation of TIA-­‐1 based SGs, and in the process, binding of Tau with TIA-­‐1 stimulates tau misfolding.


Selected Publications

These published papers resulted from Cure Alzheimer’s Fund support.
Tara Vanderweyde, Daniel J. Apicco, Katherine Youmans-Kidder, Peter E.A. Ash, Casey Cook, Edroaldo Lummertz da Rocha, Karen Jansen-West, Alissa A. Frame, Allison Citro, John D. Leszyk, Pavel Ivanov, Jose F. Abisambra, Martin Steffen, Hu Li, Leonard Petrucelli, Benjamin Wolozin, Interaction of tau with the RNA-binding Protein TIA1 Regulates tau Pathophysiology and Toxicity, Cell Reports, May 2016