Director, Biopolymer Laboratory (A protein/peptide chemistry core facility)
Molecular Biology Institute
Member, Biochemistry, Biophysics & Structural Biology GPB Home Area
Brain Research Institute
Molecular Pharmacology GPB Home Area
Neuroscience GPB Home Area
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
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.
Zheng X, Liu D, Roychaudhuri R, Teplow DB, Bowers MT Amyloid β-Protein Assembly: Differential Effects of the Protective A2T Mutation and Recessive A2V Familial Alzheimer's Disease Mutation ACS Chem Neurosci, 2015; .
Takayuki Ohnishi, Masako Yanazawa1, Tomoya Sasahara, Yasuki Kitamura, Hidekazu Hiroaki, Yugo Fukazawa, Isao Kii, Takashi Nishiyama, Akiyoshi Kakita, Hiroyuki Takeda, Akihide Takeuchi, Yoshie Arai, Akane Ito, Hitomi Komura, Hajime Hirao, Kaori Satomura, Masafumi Inoue, Shin-ichi Muramatsu, Ko Matsui, Mari Tadag, Michio Sato, Eri Saijo, Yoshiki Shigemitsu, Satoko Sakai, Yoshitaka Umetsu, Natsuko Godd, Naomi Takino, Hitoshi Takahashi, Masatoshi Hagiwara, Tatsuya Sawasaki, Genji Iwasaki, Yu Nakamura, Yo-ichi Nabeshima, David B. Teplow, and Minako Hoshi Na,K-ATPaseα3 Is a Death Target of Alzheimer Patient Amyloid-β Assembly PNAS, 2015; .
Thanh D. Do, Nichole E. LaPointe, Smriti Sangwan, David B. Teplow, Stuart C. Feinstein, Michael R. Sawaya, David S. Eisenberg, and Michael T. Bowers Factors that drive peptide assembly from native to amyloid assembly:Experimental and theoretical analysis of [Leu-5]-enkephalin mutants J Phys Chem B, 2014; 188:7247-7256: .
Robin Roychaudhuri, Aleksey Lomakin, Summer Bernstein, Xueyun Zheng, Margaret M. Condron, George B. Benedek, Michael Bowers, and David B. Teplow Gly25-Ser26 amyloid β-protein structural isomorphs produce distinct Aβ42 conformational dynamics and assembly characteristics J Mol Biol, 2014; 426:24222441: .
Do, Thanh; Economou, Nicholas; LaPointe, Nichole; Kincannon, William; Bleiholder, Christian; Feinstein, Stuart; Teplow, David; Buratto, Steven; Bowers, Michael Factors That Drive Peptide Assembly and Fibril Formation: Experimental and Theoretical Analysis of Sup35 NNQQNY Mutants J Phys Chem B, 2013; 117:8436-46: .
Zhengjian Lv, Robin Roychaudhuri, Margaret M. Condron, David B. Teplow, Yuri L. Lyubchenko Mechanism of amyloid β-protein dimerization determined using single-molecule AFM force spectroscopy Sci Rep, 2013; 3: doi:10.1038/srep02880.: .
Zhengjian Lv, Margaret M. Condron, David B. Teplow, and Yuri L. Lyubchenko Nanoprobing of the effect of Cu2+ cations on misfolding, interaction and aggregation of amyloid β peptide J Neuroimmune Pharmacol, 2013; 8:262-273: .
Jun Wang, Mario G. Ferruzzi, Lap Ho, Jack Blount, Elsa M. Janle, Bing Gong, Yong Pan, G. A. Nagana Gowda, Daniel Raftery, Isabel Arrieta-Cruz, Vaishali Sharma, Bruce Cooper, Jessica Lobo, James E. Simon, Chungfen Zhang, Alice Cheng, Xianjuan Qian, Kenjiro Ono, David B. Teplow, Constantine Pavlides, Richard A. Dixon, and Giulio M. Pasinetti Brain-Targeted Proanthocyanidin Metabolites for Alzheimer's Disease Treatment J Neuroscience, 2012; (32): 5144-5150.
Hayden EY and Teplow DB Continuous-flow reactor for production of stable amyloid protein oligomers Biochemistry, 2012; 51:6342-6349: .
L. Cruz, J. Srinivasa Rao, D. B. Teplow and B. Urbanc. Dynamics of metastable β-hairpin structures in the folding nucleus of amyloid β-protein J Phys Chem B , 2012; 116:6311-6325: .
Gessel MM, Bernstein S, Kemper M, Teplow DB, Bowers MT Familial Alzheimers disease mutations differentially alter amyloid β-protein oligomerization ACS Chem Neurosci, 2012; 3:909-918.: .
Ono K, Li L, Takamura Y, Yoshiike Y, Zhu L, Han F, Mao X, Ikeda T, Takasaki JI, Nishijo H, Takashima A, Teplow DB, Zagorski MG, Yamada M. Phenolic compounds prevent amyloid β-protein oligomerization and synaptic dysfunction by site specific binding. J Biol Chem, 2012; 287:14631-14643.: .
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; .