Gal Bitan, Ph.D.
Titles
Professor In-Residence, Neurology
Member, Biochemistry, Biophysics & Structural Biology GPB Home Area
Brain Research Institute
Molecular Pharmacology GPB Home Area
Neuroscience GPB Home Area
Contact Information
Mailing Address:
635 Charles E Young Drive SouthLos Angeles, CA 90095
UNITED STATES
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
AE Röcker, JA.Müller, E Dietzel, M Harms, F Krüger, C Heid, A Sowisolk, C Frich-Riber, A Kupke3, S Lippold4, 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;
in press.
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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;
in press.
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):
37293738.
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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 structurefunction 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 Alzheimers 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 StructureActivity 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 Alzheimers 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 Alzheimers 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 assembliescommon 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):
1068710697.
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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):
1695816969.
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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 Aβ142 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 Aggregationanalytical 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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