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Shaping the Future

Dave Teplow, Ph.D.

Contact Information:

Fax Number:

310-206-1700

Lab Number:

310-206-2030

Work Phone Number:

310-794-2886

Laboratory Address:

635 Charles E. Young Drive South
Los Angeles, CA 90095

Office Address:

NRB 445

Email Address:

dteplow@ucla.edu

Websites:

  

Home Page:

     Mary S. Easton Center

  

Laboratory:

     Teplow Lab

  

Home Page:

     UCLA Access
     DGSOM Website
     Brain Research Institute
     Molecular Biology Institute


Director, Biopolymer Laboratory (A protein/peptide chemistry core facility)

Professor, Neurology

Molecular Biology Institute

Member, Biochemistry, Biophysics & Structural Biology GPB Home Area

Brain Research Institute

Molecular Pharmacology GPB Home Area

Neuroscience GPB Home Area


Detailed Biography:

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.

Publications:

Robin Roychaudhuri, Mingfeng Yang, Atul Deshpande, Gregory M. Cole, Sally Frautschy, Aleksey Lomakin, George B. Benedek, and David B. Teplow   C-terminal turn stability determines assembly differences between Aβ40 and Aβ42, J Mol Biol, in press, 2012; .
Roychaudhuri R, Condron MM, Lazo ND, and Teplow DB   Structural dynamics of the amyloid β-protein monomer folding nucleus. Biochem, in press, (This publication was highlighted on the journal's home page), 2012; .
Ono K, Condron MM, and Teplow DB   Effects of the English (H6R) and Tottori (D7N) familial Alzheimer disease mutations on amyloid β-protein assembly and toxicity, JBC, 285:23186?23197, 2010; .
Urbanc B, Betnel M, Cruz L, Bitan G, Teplow DB   Elucidation of amyloid β-protein oligomerization mechanisms: Discrete molecular dynamics study, JACS, 132:4266?4280, 2010; .
Maji SK, Ogorzalek Loo RR, Spring SM, Vollers SS, Condron MM, Bitan G, Loo JA, and Teplow DB   Amino acid position-specific contributions to amyloid β-protein oligomerization, J Biol Chem, 284:23580?23591, 2009; .
Roychaudhuri R, Yang M, Hoshi MM, Teplow DB   Amyloid β-protein assembly and Alzheimer's disease, J Biol Chem, 284:4749?4753, 2009; .
Ono K, Condron MM, Teplow DB   Structure-neurotoxicity relationships of amyloid β-protein oligomers, PNAS, 106:14745-14750, 2009; .
Ono K, Condron MM, Ho L, Wang J, Zhao W, Pasinetti GM, and Teplow DB   Effects of grape seed-derived polyphenols on amyloid β-protein self-assembly and cytotoxicity, J. Biol Chem, 283: 32176? 32187. (JBC ?Paper of the Week?), 2008; .
Grant MA, Lazo ND, Lomakin A, Condron MM, Arai H, Yamin G, Rigby AC, and Teplow DB   Familial Alzheimer's disease mutations alter the stability of the amyloid β-protein monomer folding nucleus, PNAS, 104: 16522-16527, 2007; .
Maji SK, Amsden JJ, Rothschild KJ, Condron MM, Teplow DB   Conformational dynamics of Aβ assembly probed using intrinsic fluorescence, Biochemistry 44:13365-13376, 2005; .
Lazo ND, Grant MA, Condron MM, Rigby AC, Teplow DB   On the nucleation of amyloid β-protein monomer folding, Prot Sci, 14:1581-1596, 2005; .
Lazo ND, Grant MA, Condron MM, Rigby AC, Teplow DB   On the nucleation of amyloid β protein monomer folding, Prot Sci, 14:1581-1596, 2005; .
Bitan G, Tarus B, Vollers SS, Lashuel HA, Condron MM, Straub JE, Teplow DB   A molecular switch in amyloid assembly: Met35 and amyloid β-protein oligomerization, J Am Chem Soc, 50:15359-15365, 2003; .
Bitan G, Kirkitadze MD, Lomakin A, Vollers SS, Benedek GB, Teplow DB   Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways, Proc Natl Acad Sci USA, 100:330-335, 2003; .
Bitan G, Vollers SS, Teplow DB   Elucidation of primary structure elements controlling early amyloid β-protein oligomerization, J Biol Chem, 278:34882-34889, 2003; .
Bitan G, Lomakin A, Teplow DB   Amyloid β-protein oligomerization. Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins, J Biol Chem, 276: 35176-35184, 2001; .
Kirkitadze MD, Condron MM, Teplow DB   Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis, J Mol Biol 312:1103-1119, 2001; .
Walsh DM, Hartley DM, Fezoui Y, Condron MM, Lomakin A, Kusumoto Y, Benedek GB, Selkoe DJ, Teplow DB   Amyloid β-protein fibrillogenesis: Structure and biological activity of protofibrillar intermediates, J Biol Chem, 274:25945-25952, 1999; .
Walsh DM, Lomakin A, Benedek GB, Condron MM, Teplow DB   Amyloid β-protein fibrillogenesis: Detection of a protofibrillar intermediate, J Biol Chem. 272:22364-22372, 1997; .
Lomakin A, Chung DS, Benedek GB, Kirschner DA, Teplow DB   On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantitation of rate constants, Proc Natl Acad Sci USA 93:1125-1129, 1996; .
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