A. Ghahroudi, M. Desmyter, A. Wyns, L. Hamers, R. Muyldermans et al., Selection and identification of single domain antibody fragments from camel heavy-chain antibodies, FEBS Letters, vol.15, issue.3, pp.521-526, 1997.
DOI : 10.1016/S0014-5793(97)01062-4

F. Bard, C. Cannon, R. Barbour, R. L. Burke, D. Games et al., Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease, Nature Medicine, vol.6, issue.8, pp.916-919, 2000.
DOI : 10.1038/78682

H. Barelli, A. Lebeau, J. Vizzavona, P. Delaere, N. Chevallier et al., Characterization of new polyclonal antibodies specific for 40 and 42 amino acid-long amyloid beta peptides: their use to examine the cell biology of presenilins and the immunohistochemistry of sporadic Alzheimer's disease and cerebral amyloid angiopathy cases, Mol. Med, vol.3, pp.695-707, 1997.

G. Bitan, M. D. Kirkitadze, A. Lomakin, S. S. Vollers, G. B. Benedek et al., Amyloid ??-protein (A??) assembly: A??40 and A??42 oligomerize through distinct pathways, Proceedings of the National Academy of Sciences, vol.100, issue.1, pp.330-335, 2003.
DOI : 10.1073/pnas.222681699

H. Braak and E. Braak, Neuropathological stageing of Alzheimer-related changes, Acta Neuropathologica, vol.80, issue.4, pp.239-259, 1991.
DOI : 10.1007/BF00308809

D. F. Cardoso, F. Nato, P. England, M. L. Ferreira, T. J. Vaughan et al., Neutralizing Human Anti Crotoxin scFv Isolated from a Nonimmunized Phage Library, Scandinavian Journal of Immunology, vol.22, issue.4, pp.337-344, 2000.
DOI : 10.1111/j.1432-1033.1995.tb20355.x

J. P. Cleary, D. M. Walsh, J. J. Hofmeister, G. M. Shankar, M. A. Kuskowski et al., Natural oligomers of the amyloid-?? protein specifically disrupt cognitive function, Nature Neuroscience, vol.62, issue.1, pp.79-84, 2005.
DOI : 10.1073/pnas.94.4.1550

D. Genst, E. Silence, K. Decanniere, K. Conrath, K. Loris et al., Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies, Proceedings of the National Academy of Sciences, vol.103, issue.12, pp.4586-4591, 2006.
DOI : 10.1073/pnas.0505379103

A. Delacourte, N. Sergeant, D. Champain, A. Wattez, C. Maurage et al., Nonoverlapping but synergetic tau and APP pathologies in sporadic Alzheimer's disease, Neurology, vol.59, issue.3, pp.398-407, 2002.
DOI : 10.1212/WNL.59.3.398

A. Desmyter, S. Spinelli, F. Payan, M. Lauwereys, L. Wyns et al., Three Camelid VHH Domains in Complex with Porcine Pancreatic alpha -Amylase. INHIBITION AND VERSATILITY OF BINDING TOPOLOGY, Journal of Biological Chemistry, vol.277, issue.26, pp.23645-23650, 2002.
DOI : 10.1074/jbc.M202327200

A. Desmyter, T. R. Transue, M. A. Ghahroudi, M. H. Thi, F. Poortmans et al., Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme, Nature Structural Biology, vol.50, issue.9, pp.803-811, 1996.
DOI : 10.1107/S0021889891004399

R. C. Dodel, H. Hampel, and Y. L. Du, Immunotherapy for Alzheimer's disease, The Lancet Neurology, vol.2, issue.4, pp.215-220, 2003.
DOI : 10.1016/S1474-4422(03)00349-1

B. Friguet, A. F. Chaffote, L. Djavadi-ohaniance, and M. E. Goldberg, Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay, Journal of Immunological Methods, vol.77, issue.2, pp.305-319, 1985.
DOI : 10.1016/0022-1759(85)90044-4

G. G. Glenner, Amyloid Deposits and Amyloidosis, New England Journal of Medicine, vol.302, issue.23, pp.1283-1292, 1980.
DOI : 10.1056/NEJM198006053022305

G. K. Gouras, J. Tsai, J. Naslund, B. Vincent, M. Edgar et al., Intraneuronal A??42 Accumulation in Human Brain, The American Journal of Pathology, vol.156, issue.1, pp.15-20, 2000.
DOI : 10.1016/S0002-9440(10)64700-1

C. Haass and D. J. Selkoe, Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid ??-peptide, Nature Reviews Molecular Cell Biology, vol.26, issue.2, 2007.
DOI : 10.1038/nrm2101

G. Habicht, C. Haupt, R. P. Friedrich, P. Hortchansky, C. Sachse et al., Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing A protofibrils, Proc. Natl. Acad. Sci. U.S.A. 104, pp.19232-19237, 2007.
DOI : 10.1073/pnas.0703793104

C. Hamers-casterman, T. Atarhouch, S. Muyldermans, G. Robinson, C. Hamers et al., Naturally occurring antibodies devoid of light chains, Nature, vol.363, issue.6428, pp.446-448, 1993.
DOI : 10.1038/363446a0

D. M. Hartley, D. M. Walsh, C. P. Ye, T. Diehl, S. Vasquez et al., Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons, J. Neurosci, vol.19, pp.8876-8884, 1999.

K. Johnson-wood, M. Lee, R. Motter, K. Hu, G. Gordon et al., Amyloid precursor protein processing and Abeta 42 deposition in a transgenic mouse model of Alzheimer disease, Proc. Natl. Acad. Sci. U.S.A. 94, pp.1550-1555, 1997.

R. Kayed, E. Head, J. L. Thompson, T. M. Mcintire, S. C. Milton et al., Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis, Science, vol.300, issue.5618, pp.486-489, 2003.
DOI : 10.1126/science.1079469

Y. M. Kuo, M. R. Emmerling, C. Vigo-pelfrey, T. C. Kasunic, J. B. Kirkpatrick et al., Water-soluble Abeta (N-40, N-42) oligomers in normal and Alzheimer disease brains, J. Biol. Chem, vol.271, pp.4077-4081, 1996.

P. N. Lacor, M. C. Buniel, L. Chang, S. J. Fernandez, Y. Gong et al., Synaptic Targeting by Alzheimer's-Related Amyloid ?? Oligomers, Journal of Neuroscience, vol.24, issue.45, pp.10191-10200, 2004.
DOI : 10.1523/JNEUROSCI.3432-04.2004

P. Lafaye, F. Nato, J. Mazié, and N. Doyen, Similar binding properties for a neutralizing anti-tetanus toxoid human monoclonal antibody and its bacterially expressed Fab, Research in Immunology, vol.146, issue.6, pp.373-382, 1995.
DOI : 10.1016/0923-2494(96)81041-8

M. P. Lambert, P. T. Velasco, L. Chang, K. L. Viola, S. Fernandez et al., Monoclonal antibodies that target pathological assemblies of A??, Journal of Neurochemistry, vol.579, issue.Suppl 2, pp.23-35, 2007.
DOI : 10.1111/j.1471-4159.2006.04157.x

C. Lapresle, Enzyme immunoassay using monoclonal antibodies to study conformational changes of human serum albumin, Analytical Biochemistry, vol.174, issue.1, pp.308-312, 1988.
DOI : 10.1016/0003-2697(88)90550-7

E. B. Lee, L. Z. Leng, B. Zhang, L. Kwong, J. Q. Trojanowski et al., Targeting Amyloid-beta Peptide (Abeta) Oligomers by Passive Immunization with a Conformation-selective Monoclonal Antibody Improves Learning and Memory in Abeta Precursor Protein (APP) Transgenic Mice, Journal of Biological Chemistry, vol.281, issue.7, pp.4292-4299, 2006.
DOI : 10.1074/jbc.M511018200

J. Legleiter, D. L. Czilli, B. Gitter, R. B. Demattos, D. M. Holtzman et al., Effect of Different Anti-A?? Antibodies on A?? Fibrillogenesis as Assessed by Atomic Force Microscopy, Journal of Molecular Biology, vol.335, issue.4, pp.997-1006, 2004.
DOI : 10.1016/j.jmb.2003.11.019

H. Levine, Thioflavine T interaction with synthetic Alzheimer's disease ??-amyloid peptides: Detection of amyloid aggregation in solution, Protein Science, vol.8, issue.3, pp.404-410, 1993.
DOI : 10.1002/pro.5560020312

A. Mochizuki, A. Tamaoka, A. Shimonata, Y. Komatsuzaki, and S. Shoji, A??42-positive non-pyramidal neurons around amyloid plaques in Alzheimer's disease, The Lancet, vol.355, issue.9197, pp.42-43, 2000.
DOI : 10.1016/S0140-6736(99)04937-5

T. R. Mosmann, Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays, Journal of Immunological Methods, vol.65, issue.1-2, pp.55-63, 1983.
DOI : 10.1016/0022-1759(83)90303-4

S. Muyldermans, T. Atarhouch, J. Saldanha, J. A. Barbosa, and R. Hamers, domain from naturally occurring camel heavy chain immunoglobulins lacking light chains, "Protein Engineering, Design and Selection", vol.7, issue.9, pp.1129-1135, 1994.
DOI : 10.1093/protein/7.9.1129

S. Muyldermans, C. Cambillau, and L. Wyns, Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains, Trends in Biochemical Sciences, vol.26, issue.4, pp.230-235, 2001.
DOI : 10.1016/S0968-0004(01)01790-X

B. Solomon, Anti-Aggregating Antibodies, a New Approach Towards Treatment of Conformational Diseases, Current Medicinal Chemistry, vol.9, issue.19, pp.1737-1749, 2002.
DOI : 10.2174/0929867023369141

R. H. Takahashi, T. A. Milner, F. Li, E. E. Nam, M. A. Edgar et al., Intraneuronal Alzheimer A??42 Accumulates in Multivesicular Bodies and Is Associated with Synaptic Pathology, The American Journal of Pathology, vol.161, issue.5, pp.1869-1878, 2002.
DOI : 10.1016/S0002-9440(10)64463-X

M. Townsend, G. M. Shankar, T. Mehta, D. M. Walsh, and D. J. Selkoe, Effects of secreted oligomers of amyloid ??-protein on hippocampal synaptic plasticity: a potent role for trimers, The Journal of Physiology, vol.64, issue.2, pp.477-492, 2006.
DOI : 10.1113/jphysiol.2005.103754

D. M. Walsh and D. J. Selkoe, Oligomers on the Brain: the Emerging Role of Soluble Protein Aggregates in Neurodegeneration., Protein & Peptide Letters, vol.11, issue.3, pp.213-228, 2004.
DOI : 10.2174/0929866043407174

J. Wegiel, I. Kuchna, K. Nowicki, J. Frackowiak, B. Mazur-kolecka et al., Intraneuronal Abeta immunoreactivity is not a predictor of brain amyloidosis-beta or neurofibrillary degeneration, Acta Neuropathol, 2007.

P. Westermark, Aspects on human amyloid forms and their fibril polypeptides, FEBS Journal, vol.145, issue.23, pp.5942-5949, 2005.
DOI : 10.1111/j.1742-4658.2005.05024.x

O. Wirths, G. Multhaup, C. Czech, N. Feldmann, V. Blanchard et al., Intraneuronal APP/A?? Trafficking and Plaque Formation in ??-Amyloid Precursor Protein and Presenilin-1 Transgenic Mice, Brain Pathology, vol.273, issue.3, pp.275-286, 2002.
DOI : 10.1111/j.1750-3639.2002.tb00442.x

Y. Yamaguchi, S. Sugihara, A. Ogawa, T. Saido, and Y. Ihara, Diffuse plaques associated with astroglial amyloid ?? protein, possibly showing a disappearing stage of senile plaques, Acta Neuropathologica, vol.95, issue.3, pp.217-222, 1998.
DOI : 10.1007/s004010050790

Y. Yan and C. L. Wang, A??42 is More Rigid than A??40 at the C Terminus: Implications for A?? Aggregation and Toxicity, Journal of Molecular Biology, vol.364, issue.5, pp.853-862, 2006.
DOI : 10.1016/j.jmb.2006.09.046