Gal Bitan, Ph.D.

Mailing Address:
635 Charles E Young Drive South
Los Angeles, CA 90095

Affiliations
Affiliations
Professor In-Residence, Neurology
Member, Biochemistry, Biophysics & Structural Biology GPB Home Area, Brain Research Institute, Molecular Pharmacology GPB Home Area, Neuroscience GPB Home Area
Biography

Gal Bitan completed his graduate studies in organic chemistry at the Hebrew University of Jerusalem, Israel. Dr. Bitan's graduate work on unnatural amino acids and non-conventional peptide cyclization methodologies led him to postdoctoral studies on the structural biology of ligand-receptor systems including integrins and G protein-coupled receptors at Clark University, Worcester, MA and Beth Israel-Deaconess Medical Center/Harvard Medical School, Boston, MA. Dr. Bitan then moved on to tackle the problem of protein misfolding and aggregation, which is involved in over 30 devastating diseases, such as Alzheimer's disease, Parkinson's disease, prion diseases (e.g., Mad Cow disease), amyotrophic lateral sclerosis (Lou Gherig's disease), and type II diabetes. Working at Brigham and Women's Hospital/Harvard Medical School, Boston, MA, Dr. Bitan has made fundamental contributions to the study of early events in the pathologic cascades that cause Alzheimer's disease. In Alzheimer's disease, the amyloid ß-protein (Aß) self-associates to form a variety of oligomeric and polymeric structures with potent neurotoxic activities. In particular, Aß oligomers have been implicated as the probable cause of Alzheimer's disease. Dr. Bitan introduced the use of novel photochemical protein cross-linking techniques for investigation of Aß assembly and discovered one of the earliest oligomers in the assembly cascade, the paranucleus. In 2004, Dr. Bitan joined UCLA where he is currently an Associate Professor of Neurology. His research program is focused on translational science geared at developing novel, mechanism-based diagnostic and therapeutic tools for neurodegenerative diseases, including Alzheimer's disease and other tauopathies, Parkinson's disease, multiple system atrophy, and amyotrophic lateral sclerosis.

Publications
RS Atlasi, R Malik, CI Corrales, L Tzeplaeff, JP Whitelegge, NR Cashman, and G Bitan Investigation of anti-SOD1 antibodies yields new structural insight into SOD1 misfolding and surprising behavior of the antibodies themselves. ACS Chem. Biol. 2018; in press.
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M Nshanian, C Lantz, P Wongkongkathep, T Schrader, F-G Klärner, A Blümke, C Despres, M Ehrmann, C Smet-Nocca, G Bitan, and JA Loo Native Top-Down Mass Spectrometry and Ion Mobility Spectrometry of the Interaction of Tau Protein with a Molecular Tweezer Assembly Modulator. J. Am. Soc. Mass Spectrom. 2018; in press.
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EY Hayden, JL Conovaloff, A Mason, G Bitan, and DB Teplow Preparation of pure populations of amyloid β-protein oligomers of defined size. Methods Mol. Biol. 2018; 1779: 3-12.
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RR Walsh, F Krismer, WR Galpern, GK Wenning, PA Low, G Halliday, WJ Koroshetz, J Holton, NP Quinn, O Rascol, LM Shaw, D Eidelberg, P Bower, JL Cummings, V Abler, J Biedenharn, G Bitan, DJ Brooks, P Brundin, H Fernandez, P Fortier, R Freeman, T Gasser, A Hewitt, GU Höglinger, MJ Huentelman, PH Jensen, A Jeromin, UJ Kang, H Kaufmann, L Kellerman, V Khurana, T Klockgether, WScott Kim, C Langer, P LeWitt, E Masliah, W Meissner, R Melki, S Ostrowitzki, S Piantadosi, W Poewe, D Robertson, C Roemer, D Schenk, M Schlossmacher, JD Schmahmann, K Seppi, L Shih, A Siderowf, GT Stebbins, N Stefanova, S Tsuji, S Sutton and J Zhang Recommendations of the Global Multiple System Atrophy Research Roadmap Meeting. Neurology. 2018; 90: 74-82.
AE Röcker, JA.Müller, E Dietzel, M Harms, F Krüger, C Heid, A Sowisolk, C Frich-Riber, A Kupke, S Lippold, J von Einem, J Beer, B Knöll, S Becker, J Schmidt-Chanasit, M Otto, O Vapalahti, AN Zelikin, G Bitan, T Schrader and J Münch The molecular tweezer CLR01 inhibits Ebola and Zika virus infection. Antiviral Res. 2018; 152: 26-35.
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R Malik, J Di, G Nair, A Attar, K Taylor, E Teng, F-G Klärner, T Schrader, and G Bitan Using Molecular Tweezers to Remodel Abnormal Protein Self-Assembly and Inhibit the Toxicity of Amyloidogenic Proteins. Methods Mol. Biol. 2018; 1777: 369-386.
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F Richter, I Magen, P Lee, S Subramaniam, J Hayes, A Attar, C Zhu, N Franich, N Bove, K De La Rosa, J Kwong, F-G Klärner, T Schrader, M- F Chesselet, and G Bitan A molecular tweezer ameliorates motor deficits in mice overexpressing α-synuclein. Neurotherapeutics. 2017; 14: 1107-1119.
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MU Daloglu, A Ray, Z Gorocs, M Xiong, R Malik, G Bitan, E McLeod, and A Ozcan Computational On-Chip Imaging of Nanoparticles and Bio-molecules using Ultraviolet Light. Sci. Reports. 2017; 7: 44157.
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T Vöpel, K Bravo-Rodriguez, S Mittal, S Vachharajani, D Gnutt, A Sharma, A Steinhoff, F Oluwaseun, G Ellrichmann, N Nshinian, C Heid, JA Loo, F-G Klärner, T Schrader, G Bitan, EE Wanker, S Ebbinghaus, and E Sanchez-Garcia Inhibition of Huntingtin aggregation by the molecular tweezer CLR01. J. Am. Chem. Soc. 2017; 139: 5640–5643.
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N Xu, G Bitan, T Schrader, F-G Klärner, H Osinska, and J Robbins Inhibition of Mutant αB Crystallin-Induced Protein Aggregation by a Molecular Tweezer. J. Am. Heart Assoc. 2017; 6: e006182.
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EY Hayden, JL Conovaloff, A Mason, G Bitan, DB Teplow Preparation of pure populations of covalently stabilized amyloid β-protein oligomers of specific sizes. Anal. Biochem. 2017; 518: 78-85.
H Li, F Rahimi, and G Bitan Modulation of amyloid β-protein (Aβ) assembly by homologous C-terminal fragments as a strategy for inhibiting Aβ toxicity. ACS Chem. Neurosci. 2016; 7(7): 845-856.
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F. Rahimi, H. Li, S. Sinha, and G. Bitan Modulators of Amyloid β-Protein (Aβ) Self-Assembly. in: Developing Therapeutics for Alzheimer's Disease: Progress and Challenges. 2016; 97-191.
T Schrader, G Bitan, and F-G Klärner Molecular Tweezers for Lysine and Arginine – Powerful Inhibitors of Pathologic Protein Aggregation. Chem. Commun. 2016; 52(76): 11318-11334.
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A Lulla, L Barnhill, G Bitan, MI Ivanova, B Nguyen, K O’Donnell, MC. Stahl, C Yamashiro, F-G Klärner, T Schrader, A Sagasti, and JM Bronstein Neurotoxicity of the Parkinson’s Disease-Associated Pesticide Ziram Is Synuclein-Dependent in Zebrafish Embryos. Environ. Health Perspect. 2016; 124: 1766-1775.
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SM Fogerson, AJ van Brummen, DJ Busch, SR Allen, R Roychaudhuri, S Banks, F-G Klärner, T Schrader, G Bitan, and JR Morgan Reducing synuclein accumulation after spinal cord injury improves neuronal survival and axon regeneration. Exp. Neurol. 2016; 278: 105-115.
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E Lump, LM Castellano, C Meier, J Seeliger, N Erwin, B Sperlich, CM Stürzel, S Usmani, RM Hammond, J von Einem, G Gerold, F Kreppel, K Bravo-Rodriguez, T Pietschmann, VM Holmes, D Palesch, O Zirafi, D Weissman, A Sowislok, B Wettig, C Heid, F Kirchhoff, T Weil, F-G Klärner, T Schrader, G Bitan, E Sanchez-Garcia, R Winter, J Shorter, and Jan Münch A molecular tweezer antagonizes seminal amyloids and HIV infection. eLife. 2015; (4): e05397.
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X Zheng, D-Y Liu, F-G Klärner, T Schrader, G Bitan, and MT Bowers Amyloid β-protein Assembly: The Effect of Molecular Tweezer CLR01 and CLR03. J. Phys. Chem. B. 2015; 119(14): 4831-4841.
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X Zheng, C Wu, D Liu, H Li, G Bitan, J-E Shea, and MT Bowers Mechanism of C-Terminal Fragments of Amyloid β-Protein as Aβ Inhibitors: Do C-Terminal Interactions Play a Key Role in Their Inhibitory Activity?. J. Phys. Chem. B. 2015; 120(8): 1615-1623.
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DHJ Lopes, A Attar, G Nair, EY Hayden, Z Du, K McDaniel, S Dutt, H Bandmann, K Bravo-Rodriguez, S Mittal, F-G Klärner, C Wang, E Sánchez-García, T Schrader, and G Bitan Molecular tweezers inhibit islet amyloid polypeptide assembly and toxicity by a new mechanism. ACS Chem. Biol. 2015; 10(6): 1555-1569.
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R Roychaudhuri, X Zheng, A Lomakin, P Maiti, MM Condron, GB Benedek, G Bitan, MT Bowers, and DB Teplow Role of species-specific primary structure differences in Aβ42 assembly and neurotoxicity. ACS Chem. Neurosci. 2015; 6: 1941-1955.
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G Herzog, MD Shmueli, L Levy, L Engel, E Gazit, F-G Klärner, T Schrader, G Bitan, and D Segal The Lys-specific molecular tweezer, CLR01, modulates aggregation of mutant p53 DNA binding domain and inhibits its toxicity. Biochemistry. 2015; 54(24): 3729–3738.
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R Malishev, S Nandi, S Kolusheva, Y Levi-Kalisman, F-G Klärner, T Schrader, G Bitan*, and R Jelinek* Toxicity inhibitors protect lipid membranes from disruption by Aβ42. ACS Chem. Neurosci. 2015; 6: 1860-1869.
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A Attar and G Bitan Disrupting self-assembly and toxicity of amyloidogenic protein oligomers by "molecular tweezers"- from the test tube to animal models. Curr Pharm Des. 2014; 20: 2469-2483.
F Rahimi and G Bitan Methods for studying and structure–function relationships of non-fibrillar protein assemblies in Alzheimer's disease and related disorders. Advances in Alzheimer Research. 2014; 2: 291-374.
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S Acharya, BM Safaie, P Wongkongkathep, MI Ivanova, A Attar, F-G Klärner, T Schrader, JA Loo, G Bitan, and LJ Lapidus Molecular Basis for Preventing α-Synuclein Aggregation by a Molecular Tweezer. J. Biol. Chem. 2014; 289(15): 10727-10737.
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N Ferreira, A Pereira-Henriques, A Attar, F-G Klärner, T Schrader, G Bitan, L Gales, MJ Saraiva, and MR Almeida Molecular Tweezers Targeting Transthyretin Amyloidosis. Neurotherapeutics. 2014; 11: 450-461.
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A Attar, W-TC Chan, F-G Klärner, T Schrader, and G Bitan Safety and pharmacological characterization of the molecular tweezer CLR01 - a broad-spectrum inhibitor of amyloid proteins' toxicity. BMC Pharm. Tox. 2014; 15(23): doi:10.1186/2050-6511-15-23.
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A Attar, T Liu, W-T C Chan, J Hayes, M Nejad, K Lei, and G Bitan A Shortened Barnes Maze Protocol Reveals Memory Deficits at 4-Months of Age in the Triple-Transgenic Mouse Model of Alzheimer's Disease. PLoS ONE. 2013; 8(11): e80355.
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A Attar, D Meral, B Urbanc, and G Bitan Assembly of Amyloid β-Protein Variants Containing Familial Alzheimer’s Disease-Linked Amino Acid Substitutions. In: Bio-nanoimaging - Protein Misfolding & Aggregation. 2013; 429-442.
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C Ripoli, R Piacentini, E Riccardi, L Leone, DDL Puma, G Bitan, and C Grassi Effects of different amyloid β-protein analogues on synaptic function. Neurobiol. Aging. 2013; 34: 1032-1044.
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A Attar, F Rahimi, and G Bitan Modulators of amyloid protein aggregation and toxicity: EGCG and CLR01. Translational Neuroscience. 2013; 4(4): 385-409.
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CR Connors, DJ Rosenman, DHJ Lopes, S Mittal, G Bitan, M Sorci, G Belfort, A Garcia, and C Wang Tranilast Binds to Aβ Monomers and Promotes Aβ Fibrillation. Biochemistry. 2013; 52: 3995-4002.
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S Sinha, DHJ Lopes, and G Bitan A Key Role for Lysine Residues in Amyloid β-Protein Folding, Assembly, and Toxicity. ACS Chem. Neurosci. 2012; 3(6): 473-481.
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S Prabhudesai*, S Sinha*, A Attar, A Kotagiri, AG Fitzmaurice, R Lakshmanan, MI Ivanova, JA Loo, F-G Klärner, T Schrader, M Stahl, G Bitan#, and JM Bronstein# A Novel “Molecular Tweezer” Inhibitor of α-Synuclein Neurotoxicity in Vitro and in Vivo . Neurotherapeutics. 2012; 9(2): 464-476.
H Li, R Zemel, DHJ Lopes, BH Monien, and G Bitan A Two-Step Strategy for Structure–Activity Relationship Studies of N-Methylated Aβ42 C-Terminal Fragments as Aβ42 Toxicity Inhibitors. ChemMedChem. 2012; 7: 515-522.
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DHJ Lopes, S Sinha, C Rosensweig, and G Bitan Application of Photochemical Cross-linking to the Study of Oligomerization of Amyloidogenic Proteins. Methods Mol. Biol. 2012; 489: 11-22.
MM Gessel*, C Wu*, H Li*, G Bitan, J-E Shea, and MT Bowers Aβ(39−42) Modulates Aβ Oligomerization but Not Fibril Formation. Biochemistry. 2012; 51(1): 108-118.
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G Bitan Can We Accelerate the Path towards Therapy for Amyloid-Related Disease?. J. Gerontol. Geriatr. Res. 2012; 1(2): doi: 10.4172/jggr.1000e106.
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S Sinha, Z Du, P Maiti, F-G Klärner, T Schrader, C Wang, and G Bitan Comparison of Three Amyloid Assembly Inhibitors: The Sugar scyllo-Inositol, the Polyphenol Epigallocatechin Gallate, and the Molecular Tweezer CLR01. ACS Chem. Neurosci. 2012; 3(6): 451-458.
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PA Novick*, DH Lopes*, KM Branson, A Estera-Chopo, IA Graef, G Bitan, and VS Pande Design of β-Amyloid Aggregation Inhibitors from a Predicted Structural Motif. J. Med. Chem. 2012; 55: 3002-3010.
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T Liu and G Bitan Modulating Self-Assembly of Amyloidogenic Proteins as a Therapeutic Approach for Neurodegenerative Diseases: Strategies and Mechanisms. ChemMedChem. 2012; 7: 359-374.
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JM Ringman, AT Fithian, K Gylys, JL Cummings, G Coppola, D Elashoff, D Pratico, J Moskovitz, and G Bitan Plasma Methionine Sulfoxide in Persons with Familial Alzheimer’s Disease Mutations. Dement. Geriatr. Cogn. Disord. 2012; 33(4): 219-225.
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C Rosensweig, K Ono, K Murakami, D Lowenstein, G Bitan, and DB Teplow Preparation of stable amyloid β-protein oligomers of defined assembly order. Methods Mol. Biol. 2012; 489: 23-31.
A Attar, C Ripoli, E Riccardi, P Maiti, DD Li Puma, T Liu, J Hayes, MR Jones, K Lichti-Kaiser, F Yang, GD Gale, C-h Tseng, M Tan, C-W Xie, JL Straudinger, F-G Klärner, T Schrader, SA Frautschy, C Grassi and G Bitan Protection of primary neurons and mouse brain from Alzheimer’s pathology by molecular tweezers. Brain. 2012; 135(Pt 12): 3735-3748.
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F Rahimi and G Bitan The structure and function of fibrillar and oligomeric assemblies of amyloidogenic proteins. In: Pre-fibrillar amyloidogenic protein assemblies—common cytotoxins underlying degenerative diseases. 2012; 1-36.
I Solomonov, E Korkotian, B Born, Y Feldman, A Bitler, F Rahimi, H Li, G Bitan, and I Sagi Zn2+-Aβ40 complexes form metastable quasi-spherical oligomers that are cytotoxic to cultured hippocampal neurons. J. Biol. Chem. 2012; 287(24): 20555-20564.
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H Li, Z Du, DHJ Lopes, EA Fradinger, C Wang, and G Bitan C-terminal tetrapeptides inhibit Aβ42-induced neurotoxicity primarily through specific interaction at the N-terminus of Aβ42. J. Med. Chem. 2011; 54: 8451-8460.
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J Moskovitz, P Maiti, DHJ Lopes, DB Oien, A Attar, T Liu, S Mittal, J Hayes, and G Bitan Induction of Methionine-Sulfoxide Reductases Protects Neurons from Amyloid β-Protein Insults in Vitro and in Vivo. Biochemistry. 2011; 50(49): 10687–10697.
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S Sinha, DHJ Lopes, Z Du, ES Pang, A Shanmugam, A Lomakin, P Talbiersky, A Tennstaedt, K McDaniel, R Bakshi, P-Y Kuo, M Ehrmann, GB Benedek, JA Loo, F-G Klärner, T Schrader, C Wang, and G Bitan Lysine-specific molecular tweezers are broad-spectrum inhibitor of aggregation and toxicity of amyloid proteins. J. Am. Chem. Soc. 2011; 133(42): 16958–16969.
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K Hochdörffer, J März-Berberic, L Nagel-Steger, M Epple, W Meyer-Zaika, AHC Horn, H Sticht, S Sinha, G Bitan, and T Schrader Rational Design of β-Sheet Ligands Against Aβ42-Induced Toxicity. J. Am. Chem. Soc. 2011; 133: 4348-4358.
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B Urbanc, M Betnel, L Cruz, H Li, EA Fradinger, BH Monien, and G Bitan Structural Basis for Aβ1–42 Toxicity Inhibition by Aβ C-Terminal Fragments: Discrete Molecular Dynamics Study. J. Mol. Biol. 2011; 410(2): 316-328.
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Li H, Monien BH, Fradinger EA, Urbanc B, and Bitan G Biophysical Characterization of Aβ42 C-Terminal Fragments: Inhibitors of Aβ42 Neurotoxicity. Biochemistry. 2010; 49: 159-1267.
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Maiti P, Lomakin A, Benedek GB, and Bitan G Despite its role in assembly, methionine 35 is not necessary for amyloid β-protein toxicity. J. Neurochem. 2010; 113: 1252-1262.
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Urbanc B, Bentel M, Cruz L, Bitan G, and Teplow DB Elucidation of Amyloid β-Protein Oligomerization Mechanisms: Discrete Molecular Dynamics Study. J. Am. Chem. Soc. 2010; 132: 4266-4280.
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Li H, Monien BH, Lomakin A, Zemel R, Fradinger EA, Tan M, Spring SM, Urbanc B, Xie C-W, Benedek GB, and Bitan G Mechanistic Investigation of the Inhibition of Aβ42 Assembly and Neurotoxicity by Aβ42 C-Terminal Fragments. Biochemistry. 2010; 49(30): 6358-6364.
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Rahimi F and Bitan G Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease. J. Vis. Exp. 2010; (39): doi: 10.3791/1955.
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P Maiti, R Piacentini, C Ripoli, C Grassi, and G Bitan Surprising toxicity and assembly behavior of amyloid β-protein oxidized to sulfone. Biochem. J. 2010; 443(2): 323-332.
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Maji SK, Orgozalek Loo RR, Inayatullah M, 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. 2009; 284: 23580-23591.
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Bernstein SL, Dupuis NF, Lazo ND, Wyttenbach T, Condron MM, Bitan G , Teplow DB, Shea J-E, Ruotolo BT, Robinson CV, and Bowers MT. Amyloid β-protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. Nat. Chem. 2009; 1(4): 326-331.
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Li H, Rahimi F, Sinha S, Maiti P, Murakami K, and Bitan G. Amyloids and Protein Aggregation—analytical methods. Encyclopedia Anal. Chem. 2009; Published online, DOI: 10.1002/9780470027318.a9038.
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Rahimi F, Maiti P, and Bitan G. Photo-Induced Cross-Linking of Unmodified Proteins (PICUP) Applied to Amyloidogenic Peptides. J. Vis. Exp. 2009; (23): doi: 10.3791/1071.
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Rahimi F, Murakami K, Summers JL, Chen C-HB, and Bitan G. RNA Aptamers Generated against Oligomeric Aβ40 Recognize Common Amyloid Aptatopes with Low Specificity but High Sensitivity. PLoS ONE. 2009; 4(11): doi:10.1371/journal.pone.0007694.
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Wu* C, Murray* MM, Bernstein* SL, Condron MM, Bitan G, Bowers MT, and Shea J-E. The Structure of Aβ42 C-Terminal Fragments Probed by a Combined Experimental and Theoretical Study. J. Mol. Biol. 2009; 387(2): 492-501.
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Fradinger EA*, Monien BH*, Urbanc B, Lomakin A, Tan M, Li H, Spring SM, Condron MM, Cruz L, Xie, C-W, Benedek GB, and Bitan G C-terminal peptides co-assemble into Aβ42 oligomers and protect neurons against Aβ42-induced neurotoxicity. Proc. Natl. Acad. Sci. USA. 2008; 105(37): 14175-14180.
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Shanmugam A, Monien BH, and Bitan G Development in Diagnostic and Therapeutic Strategies for Alzheimer's Disease. in Research Progress in Alzheimer's Disease and Dementia. 2008; 3: 193-250.
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Rahimi F, Shanmugam A, and Bitan G Structure-Function Relationships of Pre-Fibrillar Protein Assemblies in Alzheimer's Disease and Related Disorders. Curr. Alz. Res. 2008; 5(3): 319-341.
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Condron MM, Monien BH, and Bitan G Synthesis and Purification of Highly Hydrophobic Peptides Derived from the C-Terminus of Amyloid β-Protein. Open Biotechnol. J. 2008; 2(1): 87-93.
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Seabrook TJ, Thomas K, Jiang L, Bloom J, Spooner E, Maier M, Bitan G, and Lemere CA Dendrimeric Aβ1-15 is an effective immunogen in wildtype and APP-tg mice. Neurobiol. Aging. 2007; 28(6): 813-823.
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Yun S, Urbanc B, Cruz L, Bitan G, Teplow DB, and Stanely HS Role of Electrostatic Interactions in Amyloid β-Protein (Aβ) Oligomer Formation: A Discrete Molecular Dynamics Study. Biophys. J. 2007; 94: 4064-4077.
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Baumketner A, Bernstein SL, Wyttenbach T, Bitan G, Teplow DB, Bowers MT, and Shea J-E Amyloid β-protein monomer structure: A computational and experimental study. Prot. Sci. 2006; 15: 420-428.
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Monien BH, Apostolova LG, and Bitan G Early diagnostics and therapeutics for Alzheimer's disease - how early can we get there?. Expert Rev. Neurother. 2006; 6(9): 1293-1306.
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Teplow DB, Lazo ND, Bitan G, Bernstein S, Wyttenbach T, Bowers MT, Baumketner A, Shea J-E, Urbanc B, Cruz L, Borreguero J, and Stanley HE Elucidating Amyloid β-Protein Folding and Assembly: A Multidisciplinary Approach. Acc. Chem. Res. 2006; 39(9): 635-345.
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Bitan G Structural study of metastable amyloidogenic protein oligomers by Photo-Induced Cross-linking of Unmodified Proteins. Methods Enzymol. 2006; 413: 217-236.
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Bernstein SL, Wyttenbach T, Baumketner A, Shea J-E, Bitan G, Teplow DB, and Bowers MT Amyloid β-protein: monomer structure and early aggregation states of Aβ42 and its Pro19 alloform. J. Am. Chem. Soc. 2005; 127(7): 2075-2084.
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Vollers SS, Teplow DB, and Bitan G Determination of peptide oligomerization state using rapid photochemical cross-linking. Methods Mol. Biol. 2005; 299: 11-18.
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Fradinger EA and Bitan G En route to early diagnosis of Alzheimer's disease--are we there yet?. Trends Biotech. 2005; 23(11): 531-533.
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Bitan G, Fradinger EA, Spring SM, and Teplow DB Neurotoxic protein oligomers-what you see is not always what you get. Amyloid. 2005; 12: 88-95.
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Bitan G and Teplow DB Preparation of aggregate-free, low molecular weight amyloid-β for assembly and toxicity assays. Methods Mol. Biol. 2005; 299: 3-9.
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Lazo ND, Maji SK, Fradinger EA, Bitan G, and Teplow DB The Amyloid β-protein. In: Sipe J, Ed. Amyloid Proteins: the β-sheet Conformation and Disease. 2005; 385-492.
Urbanc B, Cruz L, Yun S, Buldyrev SV, Bitan G, Teplow DB, and Stanley HE In silico study of amyloid β-protein folding and oligomerization. Proc. Natl. Acad. Sci. USA. 2004; 101(50): 17345-17350.
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Bitan G and Teplow DB Rapid photochemical cross-linking--a new tool for studies of metastable, amyloidogenic protein assemblies. Acc. Chem. Res. 2004; 37(6): 357-364.
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Bitan G, Tarus B, Vollers SS, Lashuel HA, Condron MM, Straub JE, and Teplow DB A molecular switch in amyloid assembly: Met35 and amyloid β-protein oligomerization. J. Am. Chem. Soc. 2003; 125(50): 15359-15365.
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Bitan G, Kirkitadze MD, Lomakin A, Vollers SS, Benedek GB, and Teplow DB Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways. Proc. Natl. Acad. Sci. USA. 2003; 100(1): 330-335.
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Bitan G, Vollers SS, and Teplow DB Elucidation of primary structure elements controlling early amyloid β-protein oligomerization. J. Biol. Chem. 2003; 278(37): 34882-34889.
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Kirkitadze MD, Bitan G, and Teplow DB Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies. J. Neurosci. Res. 2002; 69(5): 567-577.
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Bitan G, Lomakin A, and Teplow DB Amyloid β-protein oligomerization: prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins. J. Biol. Chem. 2001; 276(37): 35176-35184.
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