Biosciences at UCLA
Cores and Resources Serving UCLA
David B Teplow, Ph.D.

Email Address:
dteplow@ucla.edu Laboratory Address:
635 Charles E. Young Drive South
Los Angeles, CA 90095

Office Address:
NRB 445


Fax Number:
310-206-1700
Lab Number:
310-206-2030
Work Phone Number:
310-794-2886

Web Address:
http://www.eastonad.ucla.edu/David_Teplow.asp
Web Address:
http://teplowlab.neurology.ucla.edu/
Web Address:
http://www.uclaaccess.ucla.edu/Faculty.aspx?rv_FacultyId=10019
Web Address:
http://dgsom.healthsciences.ucla.edu/research/institution/personnel?personnel%5fid=75099
Web Address:
http://faculty.bri.ucla.edu/institution/personnel?personnel_id=75099
Web Address:
http://www.mbi.ucla.edu/

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Department / Division Affiliations
Director, Biopolymer Laboratory (A protein/peptide chemistry core facility)
Professor, Neurology, Molecular Biology Institute
Professor in Residence, Neuroscience IDP
Member, ACCESS Program: MBI IDP, Access Biochemistry, Biophysics, Structural Biology Home Area, Access Molecular Pharmacology: Therapeutics, Diagnostics, and Biology of Disease Home Area, Access Neuroscience Home Area, Brain Research Institute, Pharmacology Home Area
Bio:

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; .