UCLA Neuroscience Program Ph.D. Admissions Neuroscience Faculty UCLA and Beyond  



Gal Bitan
Neurodegenerative Diseases

Work Email Address:  gbitan@mednet.ucla.edu

Mailing Address:
635 Charles E Young Drive South


Phone Numbers:
310-206 2082


Selected Publications:

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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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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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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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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Rahimi F, Maiti P, and Bitan G. Photo-Induced Cross-Linking of Unmodified Proteins (PICUP) Applied to Amyloidogenic Peptides. J. Vis. Exp. 2009; .
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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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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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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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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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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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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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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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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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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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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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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 Abeta42 and its Pro19 alloform. J. Am. Chem. Soc. 2005; 127(7): 2075-2084.
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Lazo ND, Maji SK, Fradinger EA, Bitan G, and Teplow DB The Amyloid β-protein. . 2005; In: Sipe J, Ed. Amyloid Proteins: the β-sheet Conformation and Disease: 385-492.
Vollers SS, Teplow DB, and Bitan G Determination of peptide oligomerization state using rapid photochemical cross-linking. Methods Mol. Biol. 2005; 299: 11-18.
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.
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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Bitan G, Scheibler L, Teng H, Rosenblatt M, and Chorev M Design and evaluation of benzophenone-containing conformationally constrained ligands as tools for photoaffinity scanning of the integrin αVβ3-ligand bimolecular interaction. J. Pept. Res. 2000; 55(3): 181-194.
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Bitan G, Scheibler L, Mierke DF, Rosenblatt M, and Chorev M Ligand--Integrin αVβ3 Interaction Determined by Photoaffinity Crosslinking: A Challenge to the Prevailing Model. Biochemistry. 2000; 39: 11014-11023.
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Bitan G, Scheibler L, Greenberg Z, Teng H, Rosenblatt M, and Chorev M Mapping the Integrin αVβ3--Ligand Interface by Photoaffinity Cross-linking. Biochemistry. 1999; 38: 3414-3420.
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Bitan G, Muller D, Kasher R, Gluhov EV, and Gilon C Building Units for N-Backbone Cyclic Peptides. Part 4. Synthesis of Protected Nα-ω-functionalized alkylamino acids by reductive alkylation of natural amino acids. J. Chem. Soc. Perkin Trans. 1. 1997; 1501-1510.
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Muller D, Zeltser I, Bitan G, and Gilon C Building Units for N-Backbone Cyclic Peptides. Part 3. Synthesis of Protected Nα-ω-carboxyalkylene and Nα-ω-aminoalkylene Amino Acids. J. Org. Chem. 1997; 62: 411-416.
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Bitan G, Sukhotinsky I, Mashriki Y, Hanani M, Selinger Z, and Gilon C Synthesis and biological activity of novel backbone-bicyclic substance-P analogs containing lactam and disulfide bridges. J. Pept. Res. 1997; 49(5): 421-426.
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Bitan G, Zeltser I, Byk G, Halle D, Mashriki Y, Gluhov EV, Sukhotinsky I, Hanani M, Selinger Z, and Gilon C Backbone cyclization of the C-terminal part of substance P. Part 1: The important role of the sulphur in position 11. J. Pept. Sci. 1996; 2(4): 261-269.
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Byk G, Halle D, Zeltser I, Bitan G, Selinger Z, and Gilon C Synthesis and biological activity of NK-1 selective, N-backbone cyclic analogs of the C-terminal hexapeptide of substance P. J. Med. Chem. 1996; 39(16): 3174-3178.
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Bitan G and Gilon C Building Units for N-Backbone Cyclic Peptides. Part 2. Synthesis of Protected Nα-ω-thioalkylene Amino Acids and Their Incorporation into Dipeptide Units. Tetrahedron. 1995; 51: 10513-10522.
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Bitan G, Behrens S, Matha B, Mashriki Y, Hanani H, Kessler H, and Gilon C New Backbone-Cyclic Substance P Analogs. Lett. Pept. Sci. 1995; 2: 121-124.
Research Interest:

The Bitan laboratory focuses on structure-based design of new therapeutic agents for neurodegenerative diseases, particularly Alzheimer's disease. The laboratory synthesizes novel molecules and explores their potential for diagnostic and therapeutic uses. These synthetic efforts are guided by structural knowledge that is obtained though multifaceted experimental and theoretical studies involving several laboratories in Massachusetts and California.