Teplow, David B., Ph.D.
  • Professor of Neurology (Emeritus), David Geffen School of Medicine at UCLA

  • Director of Biopolymer Laboratory, David Geffen School of Medicine at UCLA

David B. Teplow, Ph.D.


Neuroscience Research Building, Room 445
635 Charles E. Young Drive, South
Los Angeles, CA 90095-7334
Tel: (310) 206-2030
Fax: (310) 206-1700
Email: This email address is being protected from spambots. You need JavaScript enabled to view it.



Alzheimer's Disease, Dementia, Memory Impairment, and Physical Biochemistry and Molecular Biology of Neurodegenerative Diseases.


Research Interests

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, and the Director of the Biopolymer Laboratory 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.



  • A.B., Biochemistry, UC Berkeley, 1974.
  • A.B., Bacteriology and Immunology, UC Berkeley, 1975.
  • Ph.D., Tumor Immunology, U Washington, 1981.
  • Postdoctoral Fellow, Caltech, 1981.
  • Research Biologist, Caltech, 1984.
  • Director, Laboratory of Macromolecular Structure Analysis, Caltech, 1987.
  • Member, Beckman Institute, Caltech, 1990.
  • Assistant Professor of Neurology (Neuroscience), Harvard Medical School, 1991.
  • Director, Biopolymer Laboratory, Brigham and Women's Hospital, 1991.
  • Associate Professor of Neurology, Harvard Medical School, 2001.
  • Associate Professor, Program in Neuroscience, Harvard Medical School, 2002.
  • Associate Professor, Program in Biological and Biomedical Sciences, Harvard Medical School, 2002.
  • Visiting Professor, Department of Neurology, David Geffen School of Medicine at UCLA, 2004.
  • Professor, Department of Neurology, David Geffen School of Medicine at UCLA, 2005 - present.
  • Member, Molecular Biology Institute, UCLA, 2005 - present.
  • Member, Brain Research Institute, UCLA, 2006 - present.
  • Member, Interdepartmental Ph.D. Program in Neuroscience, UCLA, 2006 - present.
  • Member, Chemistry and Biology Interface Training Program, UCLA, 2008 - present.
  • Interim Director, Mary S. Easton Center for Alzheimer's Disease Research, UCLA, 2011 - 2013.
  • Program Director, Alzheimer's Disease, Department of Neurology, David Geffen School of Medicine, UCLA, 2011 - 2013.
  • Visiting Scholar, Department of History and Philosophy of Science, University of Cambridge, Cambridge, United Kingdom, 2013 - 2014.
  • Visiting Fellow, Clare Hall, University of Cambridge, Cambridge, United Kingdom, 2013 - 2014.


Honors and Awards

  • Distinction in General Scholarship, University of California, Berkeley, 1974.
  • NIH Postdoctoral Trainee in Genetics, 1981 - 1984.
  • Travel Award, Fourth International Conference on Alzheimer's Disease and Related Disorders, 1994.
  • First Prize, Best Single Issue Category, Association of American Publishers Professional/Scholarly Publishing Division Annual Award, for the June 2000 Journal of Structural Biology Special Issue on Amyloid, 2001.
  • Turken Lectureship in Alzheimer's Disease, UCLA, 2003.
  • Alzforum Outstanding Contributor Award, 2007.
  • Certificate of Distinction in Education, Department of Neurology, UCLA, 2011.



  • NIH Neurological Sciences 1 (NLS1) Study Section.
  • The Review Board of the Medical and Scientific Advisory Council, Ronald and Nancy Reagan Research Institute of the Alzheimer's Association.
  • NIH Medical Biochemistry (MEDB) Study Section.
  • NIH NIA, Special Emphasis Panel, Mayo Clinic Jacksonville.
  • NIH Molecular, Cellular, and Developmental Neurosciences 2 (MDCN2/NDGB) Study Section.
  • The Wellcome Trust Grant Review Panel.
  • NIH NIA, Special Emphasis Panel, Mayo Clinic-Jacksonville (Chairman).
  • NSF, Division of Integrative Biology and Neuroscience, Study Section.
  • NIH NIA, Special Emphasis Panel, Protein Structure & Function in Aging and Late Life Disease.
  • Comitato Telethon Fondazione ONLUS, Rome, Italy, Study Section.
  • Human Frontier Science Program Organization, Strasbourg, France, Study Section.
  • Department of Veterans Affairs, VA Medical Research Service, Study Section.
  • American Federation for Aging Research, National Scientific Advisory Council.
  • NIH NIA, Special Emphasis Panel, Department of Neurology, UC San Francisco.
  • Cottrell College Science Award Program, Research Corporation, External Review Board.
  • United States-Israel Binational Science Foundation, Jerusalem, Israel, Study Section.
  • NIH, Biophysics of Neural Systems (BPNS), Study Section.
  • American Health Assistance Foundation, Alzheimer's Disease Research Grants, Scientific Review Committee.
  • NIH, Molecular, Developmental, and Cellular Neuroscience K(51), Special Emphasis Panel (MDCN-K(51)), Neuroinformatics and Neuroimaging.
  • United States Civilian Research and Development Foundation, Study Section.
  • Centre Européen de Calcul Atomique et Moléculaire, Lausanne, Switzerland, Program Committee.
  • Alzheimer's Disease Research Center, Emory University, Atlanta, GA, Study Section.
  • Spanish Ministry of Science and Innovation, CONSOLIDER-INGENIO 2010 Grant Program, Madrid, Spain, Study Section.
  • Health Research Board, Dublin, Ireland, Study Section.
  • Research on Alzheimer's Disease and Related Disorders, Québec-France-Canada Collaboration, Study Section.
  • NIH Molecular, Developmental, and Cellular Neuroscience.
  • Special Emphasis Panel (2011/05 ZRG1 MDCN-E (03) M).
  • Flanders Interuniversity Institute for Biotechnology, Zwijnaarde, Belgium, Scientific Advisory Board.
  • Program in Proteopathies of the Aging CNS, Gladstone Institute of Neurological Disease, UC San Francisco, Scientific Advisory Board.
  • Channel Islands Alzheimer’s Institute, California State University, Channel Islands, Camarillo, CA, Scientific Advisory Board.
  • Program in Molecular Mechanisms of SOD1-linked ALS, Department of Chemistry and Biochemistry, UCLA, Scientific Advisory Board.
  • Institute for Complex Adaptive Matter, Emergent Universe Project, Protein Aggregation Advisory Committee.
  • Springer Science and Business Media, New Journal Advisory Board.
  • Imperial College Press, London, UK, New Book Advisory Board.
  • Wiley-VCH, Weinheim, Germany, New Book Advisory Board.
  • Journal of Molecular Neuroscience, Founding Editorial Board Member.
  • Amyloid: The Journal of Protein Folding Disorders, Editorial Board Member.
  • The Journal of Biological Chemistry, Editorial Board Member.
  • Yemeni Journal of Science, Editorial Board Member.
  • Current Chemical Biology, Founding Editorial Board Member.
  • Guest Editor, Journal of Structural Biology, Special Issue: "Twist and Sheet: Variations on the theme of amyloid."


Publications (selected peer-reviewed publications)

  • Hori Y, Hashimoto T, Wakutani Y, Urakami K, Nakashima K, Condron MM, Tsubuki S, Saido TC, Teplow DB , and Iwatsubo T. (2007) The Tottori (D7N) and English (H6R) familial Alzheimer's disease mutations accelerate Aβ fibril formation without increasing protofibril formation. J Biol Chem, 282:4916-4923. PMID: 17170111
  • Yun S, Urbanc B, Cruz L, Bitan G, Teplow DB , Stanley HE (2007) Role of electrostatic interactions in amyloid β-protein (A beta) oligomer formation: a discrete molecular dynamics study. Biophys J, 92:4064-4077. PMID: 17307823 ; PMCID: PMC1868995
  • Grant MA, Lazo ND, Lomakin A, Condron MM, Arai H, Yamin G, Rigby AC, and Teplow DB (2007) Familial Alzheimer's disease mutations alter the stability of the amyloid β-protein monomer folding nucleus. PNAS, 104: 16522-16527. PMID: 17940047 ; PMCID: PMC2034231
  • Ren Y, Strobel GA, Graff JC, Jutila M, Park SG, Gosh S, Teplow D , Condron M, Pang E, Hess WM, and Moore E (2008) Colutellin A, an immunosuppressive peptide from Colletotrichum dematium. Microbiology, 154: 1973-1979. PMID: 18599825
  • Krone MG, Baumketner A, Bernstein SL, Wyttenbach T, Lazo ND, Teplow DB , Bowers MT, Shea J-E (2008) Effects of familial Alzheimer's disease mutations on the folding nucleation of the amyloid β-protein. J Mol Biol, 381: 221-228. PMID: 18597778 ; PMCID: PMC2597412
  • Wang J, Ho L, Zhao W, Ono K, Rosensweig C, Chen L, Humala N, Teplow DB , Pasinetti GM (2008) Grape-derived polyphenolics prevent Abeta oligomerization and attenuate cognitive deterioration in a mouse model of Alzheimer's disease. J Neurosci, 28: 6388-6392. PMID: 18562609 ; PMCID: PMC2806059
  • Fluhrer R, Fukumori A, Martin L, Grammer G, Haug-Kröperr M, Klier B, Winkler E, Kremmer E, Condron MM, Teplow DB , Steiner H, and Haass C (2008) Intramembrane proteolysis of GxGD-type aspartyl proteases is slowed by a familial Alzheimer disease-like mutation. J Biol Chem, 283: 30121-30128. PMID: 18768471 ; PMCID: PMC2573083
  • Yang M and Teplow DB (2008) Amyloid β-protein monomer folding: free energy landscapes reveal alloform specific differences. J Mol Biol, 384: 450-464. PMID: 18835397 ; PMCID: PMC2673916
  • Ono K, Condron MM, Ho L, Wang J, Zhao W, Pasinetti GM, and Teplow DB (2008) Effects of grape seed-derived polyphenols on amyloid β-protein self-assembly and cytotoxicity. J. Biol Chem, 283: 32176-32187. (This paper was selected as a JBC "Paper of the Week," an honor accorded to papers in the top 1% of all published, based on significance and overall importance.) PMID: 18815129 ; PMCID: PMC2583320
  • Lam AR, Teplow DB , Stanley HE, and Urbanc B (2008) Effects of the Arctic (Glu22->Gly) mutation on amyloid β-protein folding: Discrete molecular dynamics study. JACS, 130:17413-17422. PMID: 19053400
  • Zhao W, Wang J, Ho, L, Ono K, Teplow DB , Pasinetti GM (2009) Identification of antihypertensive drugs which inhibit amyloid-β protein oligomerization. J Alzheimer's Dis, 16:49-57. PMID: 19158421
  • Ho L, Chen LH, Wang J, Zhao W, Talcott ST, Ono K, Teplow DB , Humala N, Cheng A, Percival SS, Ferruzzi M, Janle E, Weaver C, Dickstein DL, Pasinetti GM (2009) Heterogeneity in red wine polyphenolic contents differentially influences Alzheimer's disease-type neuropathology and cognitive deterioration. J Alzheimer's Dis, 16:59-72. PMID: 19158422 ; PMCID: PMC2857553
  • Zaghi J, Goldenson B, Inayathullah M, Lossinsky AS, Masoumi A, Avagyan H, Mahanian M, Bernas M, Weinand M, Rosenthal MJ, Espinosa-JeVrey A, De Vellis JS, Teplow DB , Fiala M (2009) Alzheimer disease macrophages shuttle amyloid-beta from neurons to vessels, contributing to amyloid angiopathy. Acta Neuropathol, 117:111-124. PMID: 19139910
  • Murray M, Krone MG, Bernstein SL, Baumketner A, Condron, M, Lazo ND, Teplow DB , Wyttenbach T, Shea J-E, Bowers MT (2009) Amyloid β-protein: Experiment and theory on the 21-30 fragment. J Phys Chem B, 113: 6041-6046. PMID: 19341254 ; PMCID: PMC2693341
  • Bernstein SL, Dupuis NF, Lazo ND, Wyttenbach T, Condron MM, Bitan G, Teplow DB , Shea J-E, Ruotolo BT, Robinson CV & Bowers MT (2009) Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. Nature Chem, 1: 326-331. PMID: 20703363 ; PMCID: PMC2918915
  • Murray M, Bernstein S, Nyugen V, Condron MM, Teplow D , Bowers M (2009) Amyloid β-protein: Aβ40 inhibits Aβ42 oligomerization. JACS, 131:6316-6317. PMID: 19385598 ; PMCID: PMC2697393
  • Ono K, Condron MM, Teplow DB (2009) Structure-neurotoxicity relationships of amyloid β-protein oligomers. PNAS, 106:14745-14750. PMID: 19706468 ; PMCID: PMC2736424
  • Maji SK, Ogorzalek Loo RR, Spring SM, Vollers SS, Condron MM, Bitan G, Loo JA, and Teplow DB (2009) Amino acid position-specific contributions to amyloid β-protein oligomerization. J Biol Chem, 284:23580-23591. PMID: 19567875 ; PMCID: PMC2749133
  • Noguchi A, Matsumura S, Dezawa M, Tada M, Yanazawa M, Ito A, Akioka M, Kikuchi S, Sato M, Ideno S, Noda M, Fukunari A, Muramatsu S, Itokazu Y, Sato K, Takahashi H, Teplow DB , Nabeshima Y, Kakita A, Imahori K, and Hoshi M (2009) Isolation and characterization of patient-derived, toxic, high-mass amyloid β-protein (Aβ) assembly from Alzheimer disease brains. J Biol Chem, 284:32895-32905. PMID: 19759000 ; PMCID: PMC2781705
  • Yamin G, Ruchala P, Teplow DB (2009) A peptide hairpin inhibitor of amyloid β-protein oligomerization and fibrillogenesis. Biochem, 48:11329-11331. PMID: 19877710
  • Walsh DM, Thulin E, Minogue AM, Gustavsson N, Pang E, Teplow DB , Linse S (2009) Aβ facile method for expression and purification of the Alzheimer's disease-associated amyloid β-peptide. FEBS J, 276:1266-1281. PMID: 19175671 ; PMCID: PMC2702495
  • Ikeda T, Ono K, Elashoff D, Condron MM, Noguchi-Shinohara M, Yoshita M, Teplow DB , and Yamada M (2010) Cerebrospinal fluid of Alzheimer patients promotes amyloid β-protein oligomerization. J Alzheimer's Dis, 21:81-86. PMID: 20413863
  • Urbanc B, Betnel M, Cruz L, Bitan G, Teplow DB (2010) Elucidation of amyloid β-protein oligomerization mechanisms: Discrete molecular dynamics study. JACS, 132:4266-4280. PMID: 20218566
  • Wang J, Santa-Maria I, Ho L, Ksiezak-Reding H, Ono K, Teplow DB , Pasinetti GM (2010) Grape-derived polyphenols attenuate tau neuropathology in a mouse model of Alzheimer's disease. J Alzheimer's Dis, 22:653-661. PMID: 20858961
  • Ono K, Condron MM, and Teplow DB (2010) Effects of the English (H6R) and Tottori (D7N) familial Alzheimer disease mutations on amyloid β-protein assembly and toxicity. JBC, 285:23186-23197. PMID: 20452980 ; PMCID: PMC2906312
  • Matsumura S, Shinoda K, Yamada M, Yokojima S, Inoue M, Ohnishi T, Shimada T, Kikuchi K, Masui D, Hashimoto S, Sato M, Ito A, Akioka M, Takagi S, Nakamura Y, Nemoto K, Hasegawa Y, Takamoto H, Inoue H, Nakamura S, Nabeshima Y, Teplow DB , Kinjo M, and Hoshi M (2011) Two distinct amyloid β-protein (Aβ) assembly pathways leading to oligomers and fibrils identified by combined fluorescence correlation spectroscopy, morphology and toxicity analyses. JBC, 286:11555-11562. PMID: 21292768 ; PMCID: PMC3064209
  • Inayathullah M and Teplow DB (2011) Structural dynamics of the ΔE22 (Osaka) familial Alzheimer's disease-linked amyloid β-protein. Amyloid: J. Prot. Fold. Dis., in press. PMID: 21668291


  • Dreyer WJ, Roman J, Teplow DB . (1984) New instrumentation facilitates the study of genes coding for molecules involved in cell surface recognition. In: Lauder JM, Nelson P, eds. Advances in Experimental Medicine and Biology: Gene Expression and Cell-Cell Interactions in the Developing Nervous System v181. Plenum Press, New York, pp. 175-184. PMID: 6442535
  • Aebersold R, Teplow DB , Hood LE, Kent SBH. (1986) Electroblotting from immobiline isoelectric focusing gels for direct protein sequence determination. In: Peeters H, ed. Protides of the Biological Fluids v34. Pergamon Press, Ltd., pp. 715-718.
  • Aebersold R, Teplow DB , Hood LE, Kent SBH. (1987) A novel approach to isolation of proteins for microsequence analysis: Electroblotting onto activated glass. In: L'Italien JJ, ed. Proteins: Structure and Function. Plenum Press, New York, pp. 105-109.
  • Hood L, Kent S, Smith L, Aebersold R, Teplow D , Kaiser R, Clark-Lewis I, Hines W, Sanders J. (1987) The development of a facility to analyze and synthesize proteins and genes. In: Walsh K, ed. Methods in Protein Sequence Analysis. Humana Press, Clifton, NJ, pp. 21-41.
  • Cook RM, Hudson D, Tsou D, Teplow DB , Wong H, Zou A-Q, Wickstrom E. (1989) FMOC-mediated solid-phase assembly of HIV TAT protein. In: Jung G, Bayer E, eds. Peptides 1988: Proceedings of the XX European Peptide Symposium. Universitat of Tubingen, Tubingen, FRG, pp. 187-189.
  • Stahl N, Baldwin M, Teplow D , Hood L, Beavis R, Chait B, Gibson B, Burlingame A, Prusiner SB. (1992) Cataloguing post-translational modifications of the scrapie prion protein by mass spectrometry. In: Prion Diseases of Humans and Animals; Prusiner SB, Collinge J, Powell J, Anderton B, eds., Ellis Horwood, Chichester, U.K., Publishers, pp. 361-379.
  • Selkoe DJ, Haass C, Schlossmacher M, Hung A, Citron M, Teplow D . (1995) Normal production of the amyloid β-protein and the pathogenesis of Alzheimer's disease. In: Hanin, I, Yoshida, M, Fisher, A, eds., Advances in Behavioral Biology, Alzheimer's and Parkinson's Diseases: Recent Advances, Plenum Press, New York, Vol. 44, pp. 95-97.
  • Teplow DB , Lomakin A, Benedek GB, Kirschner DA, Walsh DM. (1997) Effects of β-protein mutations on amyloid fibril nucleation and elongation. In: Alzheimer's Disease: Biology, Diagnosis and Therapeutics, Iqbal K, Winblad B, Nishimura T, Takeda M, Wisniewski HM. (eds.), John Wiley & Sons Ltd, Chichester, U.K., pp. 311-319.
  • Teplow DB . (1998) The Biophysics of Amyloid β-protein Fibrillogenesis. In: Molecular Biology of Alzheimer's Disease-Genes and Mechanisms Involved in Amyloid Generation, Haass, C. (ed.), Harwood Acad. Publ., Amsterdam, 163-189.
  • Lomakin A, Benedek GB, Teplow DB . (1999) Monitoring protein assembly using quasielastic light scattering spectroscopy. In: Amyloid, Prions, and Other Protein Aggregates. Methods in Enzymology, v309, Wetzel, R. (ed.), Academic Press, San Diego, 429-459. PMID: 10507039
  • Bitan G, Kirkitadze MD, Lashuel HA, Vollers SS, Teplow DB. (2004) Primary-quaternary structure relationships controlling early Aβ oligomerization. In: Chorev M and Sawyer TK, eds., Peptide Revolution: Genomics, Proteomics & Therapeutics, American Peptide Society, Cardiff, CA, pp. 765-767.
  • Fradinger EA, Maji S, Lazo ND, Teplow DB. (2005) Studying amyloid β-protein assembly. In: Xia W, Xu H, eds. Amyloid Precursor Protein, A Practical Approach. CRC Press, Boca Raton, FL, 83-110.
  • Vollers SS, Teplow DB , Bitan G. (2005) Determination of peptide oligomerization state using rapid photochemical cross-linking. In: Sigurdsson EM, ed. Amyloidogenic Proteins-Methods in Molecular Biology. Humana Press, Totawa, NJ, 11-18. PMID: 15980592
  • Bitan G, Teplow DB. (2005) Preparation of aggregate-free, low molecular weight Aβ for assembly and toxicity assays. In: Sigurdsson EM, ed. Amyloidogenic Proteins-Methods in Molecular Biology. Humana Press, Totawa, NJ, 3-9. PMID: 15980591
  • Lomakin A, Teplow DB , Benedek GB. (2005) Quasielastic light scattering for protein assembly studies. In: Sigurdsson EM, ed. Amyloidogenic Proteins-Methods in Molecular Biology. Humana Press, Totawa, NJ, 153-174. PMID: 15980600
  • Lazo ND, Maji, SK, Fradinger EA, Bitan G, and Teplow DB. (2005) The amyloid β-protein. In Sipe J (Ed.), Amyloid Proteins: The beta sheet conformation and disease, vol. 2, Wiley-VCH Verlag GmbH, Weinheim, Germany, 385-491.
  • Spring SM, Bernstein SL, Lazo ND, Urbanc B, Stanley HE, Bowers MT, Teplow DB and Bitan G. (2006) Towards Inhibition of Amyloid β-protein Oligomerization. In: Blondelle SE, ed. Understanding Biology Using Peptides, American Peptide Society. pp. 515-516.
  • Lam A, Urbanc B, Borreguero JM, Lazo ND, Teplow DB , Stanley HE. (2006) Discrete molecular dynamics study of Alzheimer amyloid β-protein (Aβ) folding. In: Arabnia, H. R. & Valafar, H., eds., Proceedings of the 2006 International Conference on Bioinformatics & Computational Biology, BIOCOMP'06, Las Vegas, Nevada, USA, June 26-29, 2006, CSREA Press, Irvine, CA. pp. 322-328.
  • Teplow DB. (2006) Preparation of amyloid β-protein for structural and functional studies. In: Amyloid, Prions, and Other Protein Aggregates. Methods in Enzymology, v413, Kheterpal, I. and Wetzel, R. (eds.), Academic Press, San Diego, 20-33. PMID: 17046389
  • Rosensweig C, Ono K, Murakami K, Lowenstein DK, Bitan G, and Teplow DB. (2010) Preparation of stable amyloid β-protein oligomers of defined assembly order. In: Sigurdsson EM, ed. Amyloidogenic Proteins-Methods in Molecular Biology. Humana Press, Totawa, NJ. In Press.
  • Lomakin A, and Teplow DB. (2010) Quasielastic light scattering study of amyloid β-protein fibrillogenesis. In: Sigurdsson EM, ed. Amyloidogenic Proteins-Methods in Molecular Biology. Humana Press, Totawa, NJ. In Press.
  • Teplow DB. (2012) Molecular biology of neurodegenerative diseases. Pregress in Molecular Biology and Translational Science, vol 107, Academic Press.

Invited Comments/Commentaries


  • Teplow DB . (1990) Amphipathy in protein purification prose. Cell 62(1):13-14.
  • Haass C, Hung AY, Schlossmacher MG, Oltersdorf T, Teplow DB , Selkoe DJ. (1993) Normal cellular processing of the β-amyloid precursor protein results in the secretion of the amyloid " peptide and related molecules. Ann NY Acad Sci 695:109-116. PMID: 8239267
  • Haass C, Hung AY, Citron M, Teplow DB , Selkoe DJ. (1995) β-Amyloid protein processing and Alzheimer's disease. Arzneim-Forsch/Drug Res 45:398-402.
  • Selkoe DJ, Yamazaki T, Citron M, Podlisny MB, Koo EH, Teplow DB , Haass C. (1996) The role of APP processing and trafficking pathways in the formation of amyloid β-protein. Ann NY Acad Sci. 777:57-64. PMID: 8624127
  • Teplow DB . (1998) Structural and kinetic features of amyloid β-protein fibrillogenesis. Amyloid-Int J Exp Clin Invest 5:121-142. PMID: 9686307
  • Teplow DB . (1999) Truncating the amyloid cascade hypothesis: The role of COOH-terminal Aβ peptides in Alzheimer's disease. Neurobiol Aging, 20:71-73. PMID: 10466896
  • Teplow DB . (2000) Cogitations on a proteocentric lexicon. Neurobiol Aging, 21:563-564. PMID: 10924771
  • Kirschner DA, Teplow DB , Damas AM. (2000) Twist and sheet: Variations on the theme of amyloid. J Struct Biol, 130:87. (Recipient of Association of American Publishers award for "Best Single Issue of 2000" (see HONORS AND SPECIAL AWARDS above).) PMID: 10940216
  • Teplow DB . (2001) Early diagnosis of Alzheimer's disease (Book Review). Amyloid: J Protein Folding Disord, 8: 293-294.
  • Kirkitadze MD, Bitan G, Teplow DB . (2002) Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies. J Neurosci Res, 69: 567-577. PMID: 12210822
  • Teplow DB . (2002) Neurobiology of Alzheimer's disease (Book Review). Amyloid: J Protein Folding Disord, 9: 216-217.
  • Bitan G, Teplow DB . (2004) Rapid photochemical cross-linking-A new tool for studies of metastable, amyloidogenic protein assemblies. Acc Chem Res, 37:357-364. PMID: 15196045
  • Klein WL, Stine Jr WB, Teplow DB . (2004) Small assemblies of unmodified amyloid β-protein are the proximate neurotoxin in Alzheimer's disease. Neurobiol Aging, 25:569-580. PMID: 15172732
  • Lomakin A, Teplow DB . (2006) Quasielastic light scattering study of amyloid β-protein fibril formation. Prot Pept Lett, 13: 247-254. PMID: 16515452
  • Urbanc B, Cruz L, Teplow DB , Stanley HE (2006) Computer simulations of Alzheimer's amyloid β-protein folding and assembly. Curr Alzheimer's Res, 3:493-504. PMID: 17168648
  • Teplow DB , Lazo ND, Bitan G, Bernstein S, Wyttenbach T, Bowers MT, Baumketner A, Shea J-E, Urbanc B, Cruz L, Borreguero J, Stanley HE (2006) Elucidating amyloid β-protein folding and assembly: A multidisciplinary approach. Acc Chem Res, 39:635-645. PMID: 16981680
  • Yamin G, Ono K, Inayathullah M, Teplow DB. (2008) Amyloid β-protein assembly as a therapeutic target of Alzheimer's disease. Curr Pharm Des, 14:3231-3246. PMID: 19075703
  • Roychaudhuri R, Yang M, Hoshi MM, Teplow DB . (2009) Amyloid β-protein assembly and Alzheimer's disease. J Biol Chem, 284:4749-4753.


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