Molecular and cellular biology of cholinesterases, Progress in Neurobiology, vol.41, issue.1, pp.31-9190040, 1993. ,
DOI : 10.1016/0301-0082(93)90040-Y
The Cholinesterases: From Genes to Proteins, Annual Review of Pharmacology and Toxicology, vol.34, issue.1, 1994. ,
DOI : 10.1146/annurev.pa.34.040194.001433
Acetylcholinesterase: How is structure related to function?, Chemico-Biological Interactions, vol.175, issue.1-3, 2008. ,
DOI : 10.1016/j.cbi.2008.05.035
Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein, Science, vol.343, issue.6260, p.1678899, 1991. ,
DOI : 10.1038/343771a0
Interaction of fluorescence probes with acetylcholinesterase. Site and specificity of propidium binding, Biochemistry, vol.14, issue.9, 1975. ,
DOI : 10.1021/bi00680a029
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors, Biochemistry, vol.32, issue.45, pp.12074-12084, 1993. ,
DOI : 10.1021/bi00096a018
Substrate and Product Trafficking through the Active Center Gorge of Acetylcholinesterase Analyzed by Crystallography and Equilibrium Binding, Journal of Biological Chemistry, vol.157, issue.158, pp.29256-29267, 2006. ,
DOI : 10.1038/sj.emboj.7601175
URL : https://hal.archives-ouvertes.fr/hal-00134313
Structural insights into substrate traffic and inhibition in acetylcholinesterase, The EMBO Journal, vol.172, issue.12, pp.2746-2756, 2006. ,
DOI : 10.1016/0006-3002(51)90066-2
URL : https://hal.archives-ouvertes.fr/hal-00120647
Role of the peripheral anionic site on acetylcholinesterase: inhibition by substrates and coumarin derivatives, Mol Pharmacol, vol.39, pp.98-104, 1991. ,
Inhibitors Tethered Near the Acetylcholinesterase Active Site Serve as Molecular Rulers of the Peripheral and Acylation Sites, Journal of Biological Chemistry, vol.13, issue.40, pp.38948-38955, 2003. ,
DOI : 10.1016/B978-0-12-185275-7.50007-X
Acetylcholinesterase inhibition by fasciculin: Crystal structure of the complex, Cell, vol.83, issue.3, pp.503-51290128, 1995. ,
DOI : 10.1016/0092-8674(95)90128-0
Allosteric Control of Acetylcholinesterase Catalysis by Fasciculin, Journal of Biological Chemistry, vol.3, issue.35, pp.20391-20399, 1995. ,
DOI : 10.1016/0167-4838(94)90195-3
Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site, The EMBO Journal, vol.22, issue.1, 2003. ,
DOI : 10.1093/emboj/cdg005
Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation, Proceedings of the National Academy of Sciences, vol.175, issue.3, 2004. ,
DOI : 10.1007/3-540-58800-0_16
Acetylcholinesterase Revealed by the Complex Structure with a Bifunctional Inhibitor, Journal of the American Chemical Society, vol.128, issue.14, pp.4526-4527, 2006. ,
DOI : 10.1021/ja058683b
Responses of acetylcholinesterase from Torpedo marmorata to salts and curarizing drugs, Mol Pharmacol, vol.2, pp.369-392, 1966. ,
Two selective inhibitors of cholinesterase, Biochemical Journal, vol.54, issue.4, pp.695-700, 1953. ,
DOI : 10.1042/bj0540695
Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase., Proceedings of the National Academy of Sciences, vol.90, issue.19, p.8415649, 1993. ,
DOI : 10.1073/pnas.90.19.9031
URL : https://hal.archives-ouvertes.fr/hal-00174859
acetylcholinesterase, Acta Crystallographica Section D Biological Crystallography, vol.58, issue.10, pp.1765-1771, 2002. ,
DOI : 10.1107/S0907444902011642
Fasciculins, anticholinesterase toxins from the venom of the green mamba Dendroaspis angusticeps, J Physiol Paris, vol.79, pp.232-240, 1984. ,
Binding of 125I-fasciculin to rat brain acetylcholinesterase. The complex still binds diisopropyl fluorophosphate, J Biol Chem, vol.268, pp.12458-12467, 1993. ,
Site of fasciculin interaction with acetylcholinesterase, J Biol Chem, vol.269, pp.11233-11239, 1994. ,
Fasciculin 2 binds to the peripheral site on acetylcholinesterase and inhibits substrate hydrolysis by slowing a step involving proton transfer during enzyme acylation, J Biol Chem, vol.270, p.7649979, 1995. ,
Crystal structure of an acetylcholinesterase???fasciculin complex: interaction of a three-fingered toxin from snake venom with its target, Structure, vol.3, issue.12, pp.1355-136610, 1995. ,
DOI : 10.1016/S0969-2126(01)00273-8
An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase., Proceedings of the National Academy of Sciences, vol.90, issue.11, p.8506359, 1993. ,
DOI : 10.1073/pnas.90.11.5128
Open "back door" in a molecular dynamics simulation of acetylcholinesterase, Science, vol.263, issue.5151, p.8122110, 1994. ,
DOI : 10.1126/science.8122110
Long Route or Shortcut? A Molecular Dynamics Study of Traffic of Thiocholine within the Active-Site Gorge of Acetylcholinesterase, Biophysical Journal, vol.99, issue.12, pp.4003-4011, 2010. ,
DOI : 10.1016/j.bpj.2010.10.047
Insights into substrate and product traffic in the Drosophila???melanogaster acetylcholinesterase active site gorge by enlarging a back channel, FEBS Journal, vol.7, issue.120, pp.2659-2664, 2008. ,
DOI : 10.1016/0006-2952(61)90145-9
Backdoor opening mechanism in acetylcholinesterase based on X-ray crystallography and molecular dynamics simulations, Protein Science, vol.83, issue.7, pp.1114-1118, 2011. ,
DOI : 10.1016/0092-8674(95)90128-0
Acetylcholinesterases from Elapidae snake venoms: biochemical, immunological and enzymatic characterization, Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol.1339, issue.2, pp.253-26710, 1997. ,
DOI : 10.1016/S0167-4838(97)00009-5
Efficient amplification and direct sequencing of mouse variable regions from any immunoglobulin gene family, FEBS Letters, vol.176, issue.3, pp.386-394, 1999. ,
DOI : 10.1084/jem.176.3.761
A general method allowing the design of oligonucleotide primers to amplify the variable regions from immunoglobulin cDNA, Journal of Immunological Methods, vol.279, issue.1-2, pp.251-26610, 2003. ,
DOI : 10.1016/S0022-1759(03)00242-4
IMGT/V-QUEST: the highly customized and integrated system for IG and TR standardized V-J and V-D-J sequence analysis, Nucleic Acids Research, vol.22, issue.1, 2008. ,
DOI : 10.1038/sj.leu.2404969
URL : https://hal.archives-ouvertes.fr/hal-00322389
IMGT/V-QUEST: IMGT Standardized Analysis of the Immunoglobulin (IG) and T Cell Receptor (TR) Nucleotide Sequences, Cold Spring Harbor Protocols, vol.2011, issue.6, pp.695-715, 2011. ,
DOI : 10.1101/pdb.prot5633
URL : https://hal.archives-ouvertes.fr/hal-00616475
: an automated package for molecular replacement, Acta Crystallographica Section A Foundations of Crystallography, vol.50, issue.2, pp.157-16310, 1994. ,
DOI : 10.1107/S0108767393007597
Automated protein model building combined with iterative structure refinement, Nature Structural Biology, vol.6, issue.5, pp.458-463, 1999. ,
DOI : 10.1038/8263
: model-building tools for molecular graphics, Acta Crystallographica Section D Biological Crystallography, vol.60, issue.12, pp.2126-2132, 2004. ,
DOI : 10.1107/S0907444904019158
Refinement of Macromolecular Structures by the Maximum-Likelihood Method, Acta Crystallographica Section D Biological Crystallography, vol.53, issue.3, pp.240-255, 1997. ,
DOI : 10.1107/S0907444996012255
Conformations of immunoglobulin hypervariable regions, Nature, vol.342, issue.6252, 1989. ,
DOI : 10.1038/342877a0
Accessing the Kabat antibody sequence database by computer, Proteins: Structure, Function, and Genetics, vol.25, issue.1, pp.130-133, 1996. ,
DOI : 10.1002/(SICI)1097-0134(199605)25:1<130::AID-PROT11>3.3.CO;2-Y
MolProbity: all-atom contacts and structure validation for proteins and nucleic acids, Nucleic Acids Research, vol.35, issue.Web Server, pp.375-383, 2007. ,
DOI : 10.1093/nar/gkm216
Evaluation of comparative protein modeling by MODELLER, Proteins: Structure, Function, and Genetics, vol.270, issue.3, pp.318-326, 1995. ,
DOI : 10.1002/prot.340230306
The HHpred interactive server for protein homology detection and structure prediction, Nucleic Acids Research, vol.33, issue.Web Server, 2005. ,
DOI : 10.1093/nar/gki408
HADDOCK:?? A Protein???Protein Docking Approach Based on Biochemical or Biophysical Information, Journal of the American Chemical Society, vol.125, issue.7, pp.1731-1737, 2003. ,
DOI : 10.1021/ja026939x
Electrostatics of nanosystems: Application to microtubules and the ribosome, Proceedings of the National Academy of Sciences, vol.377, issue.6547, 2001. ,
DOI : 10.1038/377309a0
The Intrinsic Contributions of Tyrosine, Serine, Glycine and Arginine to the Affinity and Specificity of Antibodies, Journal of Molecular Biology, vol.377, issue.5, 2008. ,
DOI : 10.1016/j.jmb.2008.01.093
A novel molecular analysis of genes encoding catalytic antibodies, Molecular Immunology, vol.50, issue.3, pp.160-168, 2012. ,
DOI : 10.1016/j.molimm.2012.01.004
URL : https://hal.archives-ouvertes.fr/hal-00737752
Conformational Flexibility of the Acetylcholinesterase Tetramer Suggested by X-ray Crystallography, Journal of Biological Chemistry, vol.2, issue.43, pp.30370-30376, 1999. ,
DOI : 10.1002/pro.5560020309
Modulation of circulatory residence of recombinant acetylcholinesterase through biochemical or genetic manipulation of sialylation levels, Biochemical Journal, vol.336, issue.3, pp.647-658, 1998. ,
DOI : 10.1042/bj3360647
Complete amino acid sequence of human serum cholinesterase, J Biol Chem, vol.262, pp.549-557, 1987. ,
Human butyrylcholinesterase produced in insect cells: huprine-based affinity purification and crystal structure, FEBS Journal, vol.66, issue.158, pp.2905-2916, 2012. ,
DOI : 10.1107/S0907444910007493
URL : https://hal.archives-ouvertes.fr/hal-00996490
Comparison of protein-protein interactions in serine protease-inhibitor and antibody-antigen complexes: Implications for the protein docking problem, Protein Science, vol.3, issue.3, pp.603-613, 1999. ,
DOI : 10.1080/07391102.1991.10507882
The atomic structure of protein-protein recognition sites 1 1Edited by A. R. Fersht, Journal of Molecular Biology, vol.285, issue.5, pp.2177-2198, 1999. ,
DOI : 10.1006/jmbi.1998.2439
Structure, function and properties of antibody binding sites, Journal of Molecular Biology, vol.217, issue.1, pp.133-1510022, 1991. ,
DOI : 10.1016/0022-2836(91)90617-F
Structure of acetylcholinesterase complexed with E2020 (Aricept??): implications for the design of new anti-Alzheimer drugs, Structure, vol.7, issue.3, pp.297-307, 1995. ,
DOI : 10.1016/S0969-2126(99)80040-9
External and internal electrostatic potentials of cholinesterase models, Journal of Molecular Graphics and Modelling, vol.15, issue.5, pp.318-32710, 1997. ,
DOI : 10.1016/S1093-3263(98)00005-9
Electrotactins: a class of adhesion proteins with conserved electrostatic and structural motifs, Protein Engineering Design and Selection, vol.11, issue.6, pp.415-420, 1998. ,
DOI : 10.1093/protein/11.6.415
Development of acetylcholinesterase inhibitors in the therapy of Alzheimer's disease, Neurology, vol.51, issue.Issue 1, Supplement 1, pp.30-67, 1998. ,
DOI : 10.1212/WNL.51.1_Suppl_1.S30