Alzheimer's Disease, Dementia, Memory Impairment, and Physical Biochemistry and Molecular Biology of Neurodegenerative Diseases.
Protein structure and function of amyloid proteins, structural biology of neurodegenerative diseases, folding and dynamics, spectroscopy, computational physics, systems biology.
David Teplow received B.A. degrees in Biochemistry (1974) and in Bacteriology and Immunology (1975) at the University of California at Berkeley. He did graduate work in Tumor and Molecular Immunology at the University of Washington, where he received his M.S. (1977) and Ph.D. (1981) degrees. His graduate work, which involved protein chemical studies of cell surface receptors, led him to Caltech in Pasadena, where he worked first as a postdoctoral fellow and then as a junior faculty member to develop highly sensitive methods for protein primary structure analysis and to apply these new methods to the study of proteins in the nervous system. From 1991 through 2004, Dr. Teplow was a faculty member in the Departments of Neurology at Brigham and Women's Hospital and Harvard Medical School, where he established a research program to understand the structural biology of the amyloid beta-protein (Abeta) and its contribution to the pathogenesis of Alzheimer's disease (AD). Dr. Teplow joined the faculty at UCLA in 2005, where he currently is a Professor in Residence in the Department of Neurology, a member of the Molecular Biology Institute and the Brain Research Institute, the Director of the Biopolymer Laboratory at UCLA, and the Interim Director of Mary S. Easton Center for Alzheimer's Disease Research at UCLA. Dr. Teplow is a leader in the areas of the structural biology of amyloid proteins and the biophysics of amyloid assembly. The Teplow laboratory seeks to understand and treat neurodegenerative disorders linked to pathologic protein folding. In AD, Abeta; self-associates to form a variety of oligomeric and polymeric structures with potent neurotoxic activities. Abeta; oligomers have been found in vivo in AD patients and may be the proximate neurotoxins in the disease. To understand how the nascent Abeta; monomer folds and assembles into neurotoxic forms, Dr. Teplow has employed an interdisciplinary strategy comprising in vivo, in vitro, in vacuo, and in silico approaches. The long-term goal is to discover the key factors controlling production of neurotoxic assemblies and then to target these factors in strategies for drug development. Dr. Teplow has published ~140 peer-reviewed articles, including ~100 original articles and ~40 reviews, book chapters, and commentaries. Dr. Teplow was a founding editorial board member of the Journal of Molecular Neuroscience and currently sits on the editorial boards of The Journal of Biological Chemistry, Amyloid: The Journal of Protein Folding Disorders, Current Chemical Biology, and The Yemeni Journal of Science.