I. Achour, P. Cavelier, and M. Tichit, Tetrameric and Homodimeric Camelid IgGs Originate from the Same IgH Locus, The Journal of Immunology, vol.181, issue.3, pp.2001-2009, 2008.
DOI : 10.4049/jimmunol.181.3.2001

URL : https://hal.archives-ouvertes.fr/pasteur-00429626

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

D. Cardoso, F. Nato, and P. England, 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

K. Conrath, M. Lauwereys, and M. Galleni, ??-Lactamase Inhibitors Derived from Single-Domain Antibody Fragments Elicited in the Camelidae, Antimicrobial Agents and Chemotherapy, vol.45, issue.10, pp.2807-2812, 2001.
DOI : 10.1128/AAC.45.10.2807-2812.2001

K. Conrath, U. Wernery, S. Muyldermans, and V. Nguyen, Emergence and evolution of functional heavy-chain antibodies in Camelidae, Developmental & Comparative Immunology, vol.27, issue.2, pp.87-103, 2003.
DOI : 10.1016/S0145-305X(02)00071-X

D. Genst, E. Saerens, D. Muyldermans, S. Conrath, and K. , Antibody repertoire development in camelids, Developmental & Comparative Immunology, vol.30, issue.1-2, pp.187-198, 2006.
DOI : 10.1016/j.dci.2005.06.010

D. Genst, E. Silence, K. Decanniere, and K. , 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

S. Dearmond, M. Fajardo, S. Naughton, and L. Eng, Degradation of glial fibrillary acidic protein protein by a calcium dependent proteinase: an electroblot study, Brain Research, vol.262, issue.2, pp.275-282, 1983.
DOI : 10.1016/0006-8993(83)91018-1

A. Desmyter, S. Spinelli, and F. Payan, 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. Transue, and M. Ghahroudi, 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

L. Eng, R. Ghirnikar, and Y. Lee, Glial fibrillary acidic protein: GFAP-thirty-one years, Neurochemical Research, vol.25, issue.9/10, pp.1439-1451, 1969.
DOI : 10.1023/A:1007677003387

L. Frenken, R. Van-der-linden, and P. Hermans, Isolation of antigen specific Llama VHH antibody fragments and their high level secretion by Saccharomyces cerevisiae, Journal of Biotechnology, vol.78, issue.1, pp.11-21, 2000.
DOI : 10.1016/S0168-1656(99)00228-X

B. Friguet, A. Chaffote, L. Djavadi-ohaniance, and M. 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

P. Gabbot and J. Somogyi, The ???single??? section Golgi-impregnation procedure: methodological description, Journal of Neuroscience Methods, vol.11, issue.4, pp.221-230, 1984.
DOI : 10.1016/0165-0270(84)90084-0

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

J. Hanes and A. Pluckthun, In vitro selection and evolution of functional proteins by using ribosome display, Proceedings of the National Academy of Sciences, vol.94, issue.10, pp.4937-4942, 1997.
DOI : 10.1073/pnas.94.10.4937

M. Harmsen and H. De-haard, Properties, production, and applications of camelid single-domain antibody fragments, Applied Microbiology and Biotechnology, vol.77, issue.1, pp.13-22, 2007.
DOI : 10.1007/s00253-007-1142-2

M. Harmsen, C. Van-solt, and H. Fijten, Passive immunization of guinea pigs with llama single-domain antibody fragments against foot-and-mouth disease, Veterinary Microbiology, vol.120, issue.3-4, pp.193-206, 2007.
DOI : 10.1016/j.vetmic.2006.10.029

H. Hoogenboom and G. Winter, By-passing immunisation, Journal of Molecular Biology, vol.227, issue.2, pp.381-388, 1992.
DOI : 10.1016/0022-2836(92)90894-P

P. Lafaye, I. Achour, P. England, C. Duyckaerts, and F. Rougeon, Single-domain antibodies recognize selectively small oligomeric forms of amyloid ??, prevent A??-induced neurotoxicity and inhibit fibril formation, Molecular Immunology, vol.46, issue.4, pp.695-704, 2009.
DOI : 10.1016/j.molimm.2008.09.008

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. Lefranc, V. Giudicelli, and C. Ginestoux, IMGT, the international ImMunoGeneTics database, Nucleic Acids Research, vol.27, issue.1, pp.209-212, 1999.
DOI : 10.1093/nar/27.1.209

S. Mao, C. Gao, and C. Lo, Phage-display library selection of high-affinity human single-chain antibodies to tumor-associated carbohydrate antigens sialyl Lewisx and Lewisx, Proceedings of the National Academy of Sciences, vol.96, issue.12, pp.6953-6958, 1999.
DOI : 10.1073/pnas.96.12.6953

B. Mouratou, F. Schaeffer, and I. Guilvout, Remodeling a DNA-binding protein as a specific in vivo inhibitor of bacterial secretin PulD, Proceedings of the National Academy of Sciences, vol.104, issue.46, pp.17983-17988, 2007.
DOI : 10.1073/pnas.0702963104

URL : https://hal.archives-ouvertes.fr/hal-00412884

S. Muyldermans, Single domain camel antibodies: current status, Reviews in Molecular Biotechnology, vol.74, issue.4, pp.277-302, 2001.
DOI : 10.1016/S1389-0352(01)00021-6

S. Muyldermans, T. Atarhouch, J. Saldanha, J. 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

URL : http://peds.oxfordjournals.org/cgi/content/short/7/9/1129

S. Muyldermans and M. Lauwereys, Unique single-domain antigen binding fragments derived from naturally occurring camel heavy-chain antibodies, Journal of Molecular Recognition, vol.16, issue.2, pp.131-140, 1999.
DOI : 10.1002/(SICI)1099-1352(199903/04)12:2<131::AID-JMR454>3.0.CO;2-M

V. Nguyen, C. Su, S. Muyldermans, and W. Van-der-loo, Heavy-chain antibodies in Camelidae; a case of evolutionary innovation, Immunogenetics, vol.54, pp.39-47, 2002.

A. Olichon, D. Schweizer, S. Muyldermans, and A. De-marco, Heating as a rapid purification method for recovering correctlyfolded thermotolerant VH and VHH domains, BMC Biotechnology, vol.7, issue.1, p.7, 2007.
DOI : 10.1186/1472-6750-7-7

D. Saerens, J. Kinne, and E. Bosmans, Single Domain Antibodies Derived from Dromedary Lymph Node and Peripheral Blood Lymphocytes Sensing Conformational Variants of Prostate-specific Antigen, Journal of Biological Chemistry, vol.279, issue.50, pp.51965-51972, 2004.
DOI : 10.1074/jbc.M409292200

W. Schlaepfer and V. Zimmerman, Calcium-mediated breakdown of glial filaments and neurofilaments in rat optic nerve and spinal cord, Neurochemical Research, vol.73, issue.3, pp.243-255, 1981.
DOI : 10.1007/BF00964040

B. Stijlemans, K. Conrath, and V. Cortez-retamozo, Efficient Targeting of Conserved Cryptic Epitopes of Infectious Agents by Single Domain Antibodies: AFRICAN TRYPANOSOMES AS PARADIGM, Journal of Biological Chemistry, vol.279, issue.2, pp.1256-1261, 2004.
DOI : 10.1074/jbc.M307341200

J. Tanha, G. Dubuc, T. Hirama, S. Narang, and C. Mackenzie, Selection by phage display of llama conventional VH fragments with heavy chain antibody VHH properties, Journal of Immunological Methods, vol.263, issue.1-2, pp.97-109, 2002.
DOI : 10.1016/S0022-1759(02)00027-3

R. Van-der-linden, L. Frenken, and B. De-geus, Comparison of physical chemical properties of llama VHH antibody fragments and mouse monoclonal antibodies, Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol.1431, issue.1, pp.37-46, 1999.
DOI : 10.1016/S0167-4838(99)00030-8

C. Zahnd, P. Amstutz, and A. Pluckthun, Ribosome display: selecting and evolving proteins in vitro that specifically bind to a target, Nature Methods, vol.254, issue.3, pp.269-279, 2007.
DOI : 10.1038/nmeth1003