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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.

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.

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.

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.

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.

Rahimi F, Maiti P, and Bitan G. Photo-Induced Cross-Linking of Unmodified Proteins (PICUP) Applied to Amyloidogenic Peptides. J. Vis. Exp. 2009; .

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.

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.

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.

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.

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.

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.

Bitan G Structural study of metastable amyloidogenic protein oligomers by Photo-Induced Cross-linking of Unmodified Proteins. Methods Enzymol. 2006; 413: 217-236.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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