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PDBsum entry 1ace

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protein links
Hydrolase(carboxylic esterase) PDB id
1ace
Jmol
Contents
Protein chain
527 a.a.
Waters ×71
Superseded by: 2ace
PDB id:
1ace
Name: Hydrolase(carboxylic esterase)
Structure: Acetylcholinesterase
Source: Electric ray (torpedo californica)
Authors: J.L.Sussman,M.Harel,I.Silman
Key ref: J.L.Sussman et al. (1991). Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science, 253, 872-879. PubMed id: 1678899 DOI: 10.1126/science.1678899
Date:
08-Oct-91     Release date:   15-Jan-92    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
No UniProt id for this chain
Struc:  
Struc: 527 a.a.
Key:    Secondary structure  CATH domain

 

 
DOI no: 10.1126/science.1678899 Science 253:872-879 (1991)
PubMed id: 1678899  
 
 
Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein.
J.L.Sussman, M.Harel, F.Frolow, C.Oefner, A.Goldman, L.Toker, I.Silman.
 
  ABSTRACT  
 
The three-dimensional structure of acetylcholinesterase from Torpedo californica electric organ has been determined by x-ray analysis to 2.8 angstrom resolution. The form crystallized is the glycolipid-anchored homodimer that was purified subsequent to solubilization with a bacterial phosphatidylinositol-specific phospholipase C. The enzyme monomer is an alpha/beta protein that contains 537 amino acids. It consists of a 12-stranded mixed beta sheet surrounded by 14 alpha helices and bears a striking resemblance to several hydrolase structures including dienelactone hydrolase, serine carboxypeptidase-II, three neutral lipases, and haloalkane dehalogenase. The active site is unusual because it contains Glu, not Asp, in the Ser-His-acid catalytic triad and because the relation of the triad to the rest of the protein approximates a mirror image of that seen in the serine proteases. Furthermore, the active site lies near the bottom of a deep and narrow gorge that reaches halfway into the protein. Modeling of acetylcholine binding to the enzyme suggests that the quaternary ammonium ion is bound not to a negatively charged "anionic" site, but rather to some of the 14 aromatic residues that line the gorge.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21190057 J.S.Fraser, and C.J.Jackson (2011).
Mining electron density for functionally relevant protein polysterism in crystal structures.
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The preparation, in vitro screening and molecular docking of symmetrical bisquaternary cholinesterase inhibitors containing a but-(2E)-en-1,4-diyl connecting linkage.
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21364766 L.Pezzementi, F.Nachon, and A.Chatonnet (2011).
Evolution of Acetylcholinesterase and Butyrylcholinesterase in the Vertebrates: An Atypical Butyrylcholinesterase from the Medaka Oryzias latipes.
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21155827 L.Weiner, E.Roth, and I.Silman (2011).
Targeted Oxidation of Torpedo californica Acetylcholinesterase by Singlet Oxygen.
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21397501 M.Komloova, K.Musilek, A.Horova, O.Holas, V.Dohnal, F.Gunn-Moore, and K.Kuca (2011).
Preparation, in vitro screening and molecular modelling of symmetrical bis-quinolinium cholinesterase inhibitors--implications for early myasthenia gravis treatment.
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20851778 N.Kitisripanya, P.Saparpakorn, P.Wolschann, and S.Hannongbua (2011).
Binding of huperzine A and galanthamine to acetylcholinesterase, based on ONIOM method.
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21251245 S.H.Lu, J.W.Wu, H.L.Liu, J.H.Zhao, K.T.Liu, C.K.Chuang, H.Y.Lin, W.B.Tsai, and Y.Ho (2011).
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20583856 S.Pecic, M.A.McAnuff, and W.W.Harding (2011).
Nantenine as an acetylcholinesterase inhibitor: SAR, enzyme kinetics and molecular modeling investigations.
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21038057 S.Rieth, K.Hermann, B.Y.Wang, and J.D.Badjić (2011).
Controlling the dynamics of molecular encapsulation and gating.
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21369567 Y.Mo, P.Bao, and J.Gao (2011).
Energy decomposition analysis based on a block-localized wavefunction and multistate density functional theory.
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20336850 C.Li, Q.Xu, J.Li, F.Yao, and X.Jia (2010).
Complex interactions of pillar[5]arene with paraquats and bis(pyridinium) derivatives.
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20964587 D.G.Vlachos, K.H.Schulpis, A.Antsaklis, S.Mesogitis, I.Biliatis, and S.Tsakiris (2010).
Erythrocyte membrane AChE, Na(+), K(+)-ATPase and Mg(2+) ATPase activities in mothers and their premature neonates in relation to the mode of delivery.
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20546069 F.A.Gbore (2010).
Brain and hypophyseal acetylcholinesterase activity of pubertal boars fed dietary fumonisin B1.
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19926290 H.X.Zhou, and J.A.McCammon (2010).
The gates of ion channels and enzymes.
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20034789 L.Guo, A.I.Suarez, M.R.Braden, J.M.Gerdes, and C.M.Thompson (2010).
Inhibition of acetylcholinesterase by chromophore-linked fluorophosphonates.
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20677317 L.Pisani, M.Catto, I.Giangreco, F.Leonetti, O.Nicolotti, A.Stefanachi, S.Cellamare, and A.Carotti (2010).
Design, synthesis, and biological evaluation of coumarin derivatives tethered to an edrophonium-like fragment as highly potent and selective dual binding site acetylcholinesterase inhibitors.
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20382997 M.Weik, and J.P.Colletier (2010).
Temperature-dependent macromolecular X-ray crystallography.
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20190429 N.Toda, T.Kaneko, and H.Kogen (2010).
Development of an efficient therapeutic agent for Alzheimer's disease: design and synthesis of dual inhibitors of acetylcholinesterase and serotonin transporter.
  Chem Pharm Bull (Tokyo), 58, 273-287.  
20004171 P.Masson, and O.Lockridge (2010).
Butyrylcholinesterase for protection from organophosphorus poisons: catalytic complexities and hysteretic behavior.
  Arch Biochem Biophys, 494, 107-120.  
20643924 P.Taylor (2010).
Defining the determinants of nicotine selectivity.
  Proc Natl Acad Sci U S A, 107, 13195-13196.  
20309485 S.K.Mamidyala, and M.G.Finn (2010).
In situ click chemistry: probing the binding landscapes of biological molecules.
  Chem Soc Rev, 39, 1252-1261.  
19757206 T.L.Rosenberry (2010).
Strategies to resolve the catalytic mechanism of acetylcholinesterase.
  J Mol Neurosci, 40, 32-39.  
21052939 Z.Jin, L.Yang, S.J.Liu, J.Wang, S.Li, H.Q.Lin, D.C.Wan, and C.Hu (2010).
Synthesis and biological evaluation of 3,6-diaryl-7H-thiazolo[3,2-b] [1,2,4]triazin-7-one derivatives as acetylcholinesterase inhibitors.
  Arch Pharm Res, 33, 1641-1649.  
  20550720 Z.Ul-Haq, W.Khan, S.Kalsoom, and F.L.Ansari (2010).
In silico modeling of the specific inhibitory potential of thiophene-2,3-dihydro-1,5-benzothiazepine against BChE in the formation of beta-amyloid plaques associated with Alzheimer's disease.
  Theor Biol Med Model, 7, 22.  
19651048 A.A.Gorfe, B.Lu, Z.Yu, and J.A.McCammon (2009).
Enzymatic activity versus structural dynamics: the case of acetylcholinesterase tetramer.
  Biophys J, 97, 897-905.  
19758986 C.A.Ruiz, and R.L.Rotundo (2009).
Limiting role of protein disulfide isomerase in the expression of collagen-tailed acetylcholinesterase forms in muscle.
  J Biol Chem, 284, 31753-31763.  
18729824 D.Barak, A.Ordentlich, D.Stein, Q.S.Yu, N.H.Greig, and A.Shafferman (2009).
Accommodation of physostigmine and its analogues by acetylcholinesterase is dominated by hydrophobic interactions.
  Biochem J, 417, 213-222.  
19019080 D.Liang, J.P.Blouet, F.Borrega, S.Bon, and J.Massoulié (2009).
Respective roles of the catalytic domains and C-terminal tail peptides in the oligomerization and secretory trafficking of human acetylcholinesterase and butyrylcholinesterase.
  FEBS J, 276, 94.  
19533292 D.Toiber, D.S.Greenberg, and H.Soreq (2009).
Pro-apoptotic protein-protein interactions of the extended N-AChE terminus.
  J Neural Transm, 116, 1435-1442.  
19536291 F.Ekström, A.Hörnberg, E.Artursson, L.G.Hammarström, G.Schneider, and Y.P.Pang (2009).
Structure of HI-6*sarin-acetylcholinesterase determined by X-ray crystallography and molecular dynamics simulation: reactivator mechanism and design.
  PLoS One, 4, e5957.
PDB codes: 2whp 2whq 2whr
19016914 F.Nardi, B.Barazzuoli, S.Ciolfi, A.Carapelli, R.Dallai, and F.Frati (2009).
Acetylcholinesterase genes in the basal Hexapod Orchesella villosa.
  Insect Mol Biol, 18, 45-54.  
19276074 J.Lee, X.Wang, B.Di Jeso, and P.Arvan (2009).
The cholinesterase-like domain, essential in thyroglobulin trafficking for thyroid hormone synthesis, is required for protein dimerization.
  J Biol Chem, 284, 12752-12761.  
19924840 J.Liu, Y.Zhang, and C.G.Zhan (2009).
Reaction pathway and free-energy barrier for reactivation of dimethylphosphoryl-inhibited human acetylcholinesterase.
  J Phys Chem B, 113, 16226-16236.  
19345205 J.Zhang, D.Zhu, R.Sheng, H.Wu, Y.Hu, F.Wang, T.Cai, B.Yang, and Q.He (2009).
BZYX, a novel acetylcholinesterase inhibitor, significantly improved chemicals-induced learning and memory impairments on rodents and protected PC12 cells from apoptosis induced by hydrogen peroxide.
  Eur J Pharmacol, 613, 1-9.  
19346618 L.Guo, C.M.Thompson, and B.Twamley (2009).
Diastereomers (R(C),S(P))- and (R(C),R(P))-S-methyl P-(3-azidopropyl)-N-[(1R)-1-phenylethyl]phosphonamidothioate.
  Acta Crystallogr C, 65, o179-o182.  
19452557 M.Amitay, and A.Shurki (2009).
The structure of G117H mutant of butyrylcholinesterase: nerve agents scavenger.
  Proteins, 77, 370-377.  
19292865 M.Pietsch, L.Christian, T.Inhester, S.Petzold, and M.Gütschow (2009).
Kinetics of inhibition of acetylcholinesterase in the presence of acetonitrile.
  FEBS J, 276, 2292-2307.  
19715346 N.H.Barakat, X.Zheng, C.B.Gilley, M.MacDonald, K.Okolotowicz, J.R.Cashman, S.Vyas, J.M.Beck, C.M.Hadad, and J.Zhang (2009).
Chemical synthesis of two series of nerve agent model compounds and their stereoselective interaction with human acetylcholinesterase and human butyrylcholinesterase.
  Chem Res Toxicol, 22, 1669-1679.  
19565307 O.Soukup, J.Proska, J.Binder, J.Z.Karasova, G.Tobin, D.Jun, J.Marek, K.Musílek, J.Fusek, and K.Kuca (2009).
Methylacridinium and its cholinergic properties.
  Neurotox Res, 16, 372-377.  
19433508 P.H.Lee, K.L.Kuo, P.Y.Chu, E.M.Liu, and J.H.Lin (2009).
SLITHER: a web server for generating contiguous conformations of substrate molecules entering into deep active sites of proteins or migrating through channels in membrane transporters.
  Nucleic Acids Res, 37, W559-W564.  
19827033 S.Y.Chiou, C.F.Huang, M.T.Hwang, and G.Lin (2009).
Comparison of active sites of butyrylcholinesterase and acetylcholinesterase based on inhibition by geometric isomers of benzene-di-N-substituted carbamates.
  J Biochem Mol Toxicol, 23, 303-308.  
19843464 T.Zeev-Ben-Mordehai, E.Mylonas, A.Paz, Y.Peleg, L.Toker, I.Silman, D.I.Svergun, and J.L.Sussman (2009).
The quaternary structure of amalgam, a Drosophila neuronal adhesion protein, explains its dual adhesion properties.
  Biophys J, 97, 2316-2326.  
19714254 Y.P.Pang, F.Ekström, G.A.Polsinelli, Y.Gao, S.Rana, D.H.Hua, B.Andersson, P.O.Andersson, L.Peng, S.K.Singh, R.K.Mishra, K.Y.Zhu, A.M.Fallon, D.W.Ragsdale, and S.Brimijoin (2009).
Selective and irreversible inhibitors of mosquito acetylcholinesterases for controlling malaria and other mosquito-borne diseases.
  PLoS One, 4, e6851.
PDB code: 2wls
19194505 Y.P.Pang, S.K.Singh, Y.Gao, T.L.Lassiter, R.K.Mishra, K.Y.Zhu, and S.Brimijoin (2009).
Selective and irreversible inhibitors of aphid acetylcholinesterases: steps toward human-safe insecticides.
  PLoS ONE, 4, e4349.  
19402731 Y.Pan, J.L.Muzyka, and C.G.Zhan (2009).
Model of human butyrylcholinesterase tetramer by homology modeling and dynamics simulation.
  J Phys Chem B, 113, 6543-6552.  
17948252 A.A.Anderson, D.S.Ushakov, M.A.Ferenczi, R.Mori, P.Martin, and J.L.Saffell (2008).
Morphoregulation by acetylcholinesterase in fibroblasts and astrocytes.
  J Cell Physiol, 215, 82.  
17921202 A.A.Gorfe, C.E.Chang, I.Ivanov, and J.A.McCammon (2008).
Dynamics of the acetylcholinesterase tetramer.
  Biophys J, 94, 1144-1154.  
18279391 A.Frederick, I.Tsigelny, F.Cohenour, C.Spiker, E.Krejci, A.Chatonnet, S.Bourgoin, G.Richards, T.Allen, M.H.Whitlock, and L.Pezzementi (2008).
Acetylcholinesterase from the invertebrate Ciona intestinalis is capable of assembling into asymmetric forms when co-expressed with vertebrate collagenic tail peptide.
  FEBS J, 275, 1309-1322.  
18471807 A.Shafferman, D.Barak, D.Stein, C.Kronman, B.Velan, N.H.Greig, and A.Ordentlich (2008).
Flexibility versus "rigidity" of the functional architecture of AChE active center.
  Chem Biol Interact, 175, 166-172.  
18550038 D.Comoletti, A.Grishaev, A.E.Whitten, P.Taylor, and J.Trewhella (2008).
Characterization of the solution structure of a neuroligin/beta-neurexin complex.
  Chem Biol Interact, 175, 150-155.  
18769671 D.Toiber, A.Berson, D.Greenberg, N.Melamed-Book, S.Diamant, and H.Soreq (2008).
N-acetylcholinesterase-induced apoptosis in Alzheimer's disease.
  PLoS ONE, 3, e3108.  
18798008 F.M.Ho (2008).
Uncovering channels in photosystem II by computer modelling: current progress, future prospects, and lessons from analogous systems.
  Photosynth Res, 98, 503-522.  
18422651 F.Nachon, J.Stojan, and D.Fournier (2008).
Insights into substrate and product traffic in the Drosophila melanogaster acetylcholinesterase active site gorge by enlarging a back channel.
  FEBS J, 275, 2659-2664.  
18855408 H.Wang, J.Wang, C.Timchalk, and Y.Lin (2008).
Magnetic electrochemical immunoassays with quantum dot labels for detection of phosphorylated acetylcholinesterase in plasma.
  Anal Chem, 80, 8477-8484.  
17657601 H.Y.Zhang, H.Yan, and X.C.Tang (2008).
Non-cholinergic effects of huperzine A: beyond inhibition of acetylcholinesterase.
  Cell Mol Neurobiol, 28, 173-183.  
17729287 J.C.Marx, J.Poncin, J.P.Simorre, P.W.Ramteke, and G.Feller (2008).
The noncatalytic triad of alpha-amylases: a novel structural motif involved in conformational stability.
  Proteins, 70, 320-328.  
18538754 J.M.Beck, and C.M.Hadad (2008).
Hydrolysis of nerve agents by model nucleophiles: a computational study.
  Chem Biol Interact, 175, 200-203.  
18701720 J.P.Colletier, D.Bourgeois, B.Sanson, D.Fournier, J.L.Sussman, I.Silman, and M.Weik (2008).
Shoot-and-Trap: use of specific x-ray damage to study structural protein dynamics by temperature-controlled cryo-crystallography.
  Proc Natl Acad Sci U S A, 105, 11742-11747.
PDB codes: 2vja 2vjb 2vjc 2vjd 2vt6 2vt7
18579127 J.Stojan (2008).
Kinetic evaluation of multiple initial rate data by simultaneous analysis with two equations.
  Chem Biol Interact, 175, 242-248.  
18478097 L.Djogbénou, F.Chandre, A.Berthomieu, R.Dabiré, A.Koffi, H.Alout, and M.Weill (2008).
Evidence of introgression of the ace-1(R) mutation and of the ace-1 duplication in West African Anopheles gambiae s. s.
  PLoS ONE, 3, e2172.  
17985237 M.A.Kamal, P.Klein, W.Luo, Y.Li, H.W.Holloway, D.Tweedie, and N.H.Greig (2008).
Kinetics of human serum butyrylcholinesterase inhibition by a novel experimental Alzheimer therapeutic, dihydrobenzodioxepine cymserine.
  Neurochem Res, 33, 745-753.  
18166494 N.A.Jennings, L.Pezzementi, A.L.Lawrence, and S.A.Watts (2008).
Acetylcholinesterase in the sea urchin Lytechinus variegatus: characterization and developmental expression in larvae.
  Comp Biochem Physiol B Biochem Mol Biol, 149, 401-409.  
17803238 O.Carrillo, and M.Orozco (2008).
GRID-MD-A tool for massive simulation of protein channels.
  Proteins, 70, 892-899.  
17879262 P.Tsvetkov, G.Asher, A.Paz, N.Reuven, J.L.Sussman, I.Silman, and Y.Shaul (2008).
Operational definition of intrinsically unstructured protein sequences based on susceptibility to the 20S proteasome.
  Proteins, 70, 1357-1366.  
18563305 S.Y.Chiou, Y.G.Wu, and G.Lin (2008).
Activation mechanisms of butyrylcholinesterase by 2,4,6-trinitrotoluene, 3,3-dimethylbutyl-N-n-butylcarbamate, and 2-trimethylsilyl-ethyl-N-n-butylcarbamate.
  Appl Biochem Biotechnol, 150, 337-344.  
18602908 T.L.Rosenberry, L.K.Sonoda, S.E.Dekat, B.Cusack, and J.L.Johnson (2008).
Monitoring the reaction of carbachol with acetylcholinesterase by thioflavin T fluorescence and acetylthiocholine hydrolysis.
  Chem Biol Interact, 175, 235-241.  
19006330 T.L.Rosenberry, L.K.Sonoda, S.E.Dekat, B.Cusack, and J.L.Johnson (2008).
Analysis of the reaction of carbachol with acetylcholinesterase using thioflavin T as a coupled fluorescence reporter.
  Biochemistry, 47, 13056-13063.  
18194084 T.Parthimos, K.H.Schulpis, P.Angelogianni, C.Tsopanakis, N.Parthimos, and S.Tsakiris (2008).
The in vivo and in vitro effects of L-carnitine supplementation on the erythrocyte membrane acetylcholinesterase, Na(+), K(+)-ATPase and Mg(2+)-ATPase activities in basketball players.
  Clin Chem Lab Med, 46, 137-142.  
17973075 Y.Ma, X.Chen, M.Sun, R.Wan, C.Zhu, Y.Li, and Y.Zhao (2008).
DNA cleavage function of seryl-histidine dipeptide and its application.
  Amino Acids, 35, 251-256.  
18359854 Y.Xu, J.P.Colletier, H.Jiang, I.Silman, J.L.Sussman, and M.Weik (2008).
Induced-fit or preexisting equilibrium dynamics? Lessons from protein crystallography and MD simulations on acetylcholinesterase and implications for structure-based drug design.
  Protein Sci, 17, 601-605.  
18502801 Y.Xu, J.P.Colletier, M.Weik, H.Jiang, J.Moult, I.Silman, and J.L.Sussman (2008).
Flexibility of aromatic residues in the active-site gorge of acetylcholinesterase: X-ray versus molecular dynamics.
  Biophys J, 95, 2500-2511.  
17143857 A.Dörr, and W.D.Lubell (2007).
Synthesis of a new pi-deficient phenylalanine derivative from a common 1,4-diketone intermediate and study of the influence of aromatic density on prolyl amide isomer population.
  Biopolymers, 88, 290-299.  
17324372 A.P.Benfield, N.M.Goodey, L.T.Phillips, and S.F.Martin (2007).
Structural studies examining the substrate specificity profiles of PC-PLC(Bc) protein variants.
  Arch Biochem Biophys, 460, 41-47.
PDB codes: 2ffz 2fgn 2huc
18093522 D.Araç, A.A.Boucard, E.Ozkan, P.Strop, E.Newell, T.C.Südhof, and A.T.Brunger (2007).
Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ interactions.
  Neuron, 56, 992.
PDB codes: 3biw 3bix
17562316 D.Comoletti, A.Grishaev, A.E.Whitten, I.Tsigelny, P.Taylor, and J.Trewhella (2007).
Synaptic arrangement of the neuroligin/beta-neurexin complex revealed by X-ray and neutron scattering.
  Structure, 15, 693-705.  
17175445 H.Alout, A.Berthomieu, A.Hadjivassilis, and M.Weill (2007).
A new amino-acid substitution in acetylcholinesterase 1 confers insecticide resistance to Culex pipiens mosquitoes from Cyprus.
  Insect Biochem Mol Biol, 37, 41-47.  
18093521 I.P.Fabrichny, P.Leone, G.Sulzenbacher, D.Comoletti, M.T.Miller, P.Taylor, Y.Bourne, and P.Marchot (2007).
Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion.
  Neuron, 56, 979-991.
PDB codes: 2vh8 2wqz 3be8
17986339 J.H.Carra, C.A.McHugh, S.Mulligan, L.M.Machiesky, A.S.Soares, and C.B.Millard (2007).
Fragment-based identification of determinants of conformational and spectroscopic change at the ricin active site.
  BMC Struct Biol, 7, 72.
PDB codes: 2p8n 2pjn 2pjo 2r2x 2r3d
18007027 J.P.Colletier, A.Royant, A.Specht, B.Sanson, F.Nachon, P.Masson, G.Zaccai, J.L.Sussman, M.Goeldner, I.Silman, D.Bourgeois, and M.Weik (2007).
Use of a 'caged' analogue to study the traffic of choline within acetylcholinesterase by kinetic crystallography.
  Acta Crystallogr D Biol Crystallogr, 63, 1115-1128.
PDB codes: 2v96 2v97 2v98 2va9
  17350931 L.Mandrich, M.Pezzullo, M.Rossi, and G.Manco (2007).
SSoNDelta and SSoNDeltalong: two thermostable esterases from the same ORF in the archaeon Sulfolobus solfataricus?
  Archaea, 2, 109-115.  
17994573 M.C.Lin, M.T.Hwang, H.G.Chang, C.S.Lin, and G.Lin (2007).
Benzene-1,2-, 1,3-, and 1,4-di-N-substituted carbamates as conformationally constrained inhibitors of acetylcholinesterase.
  J Biochem Mol Toxicol, 21, 348-353.  
17355286 M.F.Frasco, J.P.Colletier, M.Weik, F.Carvalho, L.Guilhermino, J.Stojan, and D.Fournier (2007).
Mechanisms of cholinesterase inhibition by inorganic mercury.
  FEBS J, 274, 1849-1861.
PDB code: 2j4c
17546082 M.H.Chen, Z.J.Han, X.F.Qiao, and M.J.Qu (2007).
Mutations in acetylcholinesterase genes of Rhopalosiphum padi resistant to organophosphate and carbamate insecticides.
  Genome, 50, 172-179.  
17295372 M.N.Romanelli, P.Gratteri, L.Guandalini, E.Martini, C.Bonaccini, and F.Gualtieri (2007).
Central Nicotinic Receptors: Structure, Function, Ligands, and Therapeutic Potential.
  ChemMedChem, 2, 746-767.  
17913689 P.Taylor, E.Reiner, Z.Kovarik, and Z.Radić (2007).
Application of recombinant DNA methods for production of cholinesterases as organophosphate antidotes and detectors.
  Arh Hig Rada Toksikol, 58, 339-345.  
17467020 R.Kaushik, C.A.Rosenfeld, and L.G.Sultatos (2007).
Concentration-dependent interactions of the organophosphates chlorpyrifos oxon and methyl paraoxon with human recombinant acetylcholinesterase.
  Toxicol Appl Pharmacol, 221, 243-250.  
16955366 S.Darvesh, R.Walsh, and E.Martin (2007).
Homocysteine thiolactone and human cholinesterases.
  Cell Mol Neurobiol, 27, 33-48.  
17106678 S.Kakugawa, S.Fushinobu, T.Wakagi, and H.Shoun (2007).
Characterization of a thermostable carboxylesterase from the hyperthermophilic bacterium Thermotoga maritima.
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PDB codes: 2c4h 2c58 2c5f 2c5g
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Three-dimensional structure determination of proteins related to human health in their functional context at The Israel Structural Proteomics Center (ISPC). This paper was presented at ICCBM10.
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15629944 W.L.Kelly, and C.A.Townsend (2005).
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PDB code: 1vzj
15507109 H.Kurzen, and K.U.Schallreuter (2004).
Novel aspects in cutaneous biology of acetylcholine synthesis and acetylcholine receptors.
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15159570 I.Janda, Y.Devedjiev, D.Cooper, M.Chruszcz, U.Derewenda, A.Gabrys, W.Minor, A.Joachimiak, and Z.S.Derewenda (2004).
Harvesting the high-hanging fruit: the structure of the YdeN gene product from Bacillus subtilis at 1.8 angstroms resolution.
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PDB code: 1uxo
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PDB codes: 1q83 1q84
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A paradigm for single nucleotide polymorphism analysis: the case of the acetylcholinesterase gene.
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14585602 F.G.Scholl, and P.Scheiffele (2003).
Making connections: cholinesterase-domain proteins in the CNS.
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14678739 H.C.Kolb, and K.B.Sharpless (2003).
The growing impact of click chemistry on drug discovery.
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Design of acetylcholinesterases for biosensor applications.
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14627729 J.Kua, Y.Zhang, A.C.Eslami, J.R.Butler, and J.A.McCammon (2003).
Studying the roles of W86, E202, and Y337 in binding of acetylcholine to acetylcholinesterase using a combined molecular dynamics and multiple docking approach.
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14507691 J.M.Bui, R.H.Henchman, and J.A.McCammon (2003).
The dynamics of ligand barrier crossing inside the acetylcholinesterase gorge.
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14604522 J.M.Mancheño, J.Martín-Benito, M.Martínez-Ripoll, J.G.Gavilanes, and J.A.Hermoso (2003).
Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation.
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PDB codes: 1gwy 1o71 1o72
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Cholinergic nicotinic receptors: competitive ligands, allosteric modulators, and their potential applications.
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Inhibition of human cholinesterases by drugs used to treat Alzheimer disease.
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Acetylcholinesterase in motion: visualizing conformational changes in crystal structures by a morphing procedure.
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Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site.
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PDB codes: 1j06 1j07 1ku6 1n5m 1n5r
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Structure of a complex of the potent and specific inhibitor BW284C51 with Torpedo californica acetylcholinesterase.
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PDB code: 1e3q
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11840523 D.Rochu, and P.Masson (2002).
Multiple advantages of capillary zone electrophoresis for exploring protein conformational stability.
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11979423 E.Gavuzzo, and M.Pomponi (2002).
Inhibition of acetylcholinesterase by physostigmine analogs: conformational mobility of cysteine loop due to the steric effect of the alkyl chain.
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Potential active-site residues in polyneuridine aldehyde esterase, a central enzyme of indole alkaloid biosynthesis, by modelling and site-directed mutagenesis.
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12411516 G.Akk (2002).
Contributions of the non-alpha subunit residues (loop D) to agonist binding and channel gating in the muscle nicotinic acetylcholine receptor.
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11807752 H.C.Huang, and J.M.Briggs (2002).
The association between a negatively charged ligand and the electronegative binding pocket of its receptor.
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3D structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 A resolution: kinetic and molecular dynamic correlates.
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PDB code: 1e66
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Thermal denaturation of Bungarus fasciatus acetylcholinesterase: Is aggregation a driving force in protein unfolding?
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Concentration-dependent reversible activation-inhibition of human butyrylcholinesterase by tetraethylammonium ion.
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12022871 M.Alam, D.E.Vance, and R.Lehner (2002).
Structure-function analysis of human triacylglycerol hydrolase by site-directed mutagenesis: identification of the catalytic triad and a glycosylation site.
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Linkage analysis of an acetylcholinesterase gene in the house fly Musca domestica (Diptera: Muscidae).
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11964254 R.H.Henchman, K.Tai, T.Shen, and J.A.McCammon (2002).
Properties of water molecules in the active site gorge of acetylcholinesterase from computer simulation.
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12055623 S.L.Roderick, W.W.Chan, D.S.Agate, L.R.Olsen, M.W.Vetting, K.R.Rajashankar, and D.E.Cohen (2002).
Structure of human phosphatidylcholine transfer protein in complex with its ligand.
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PDB codes: 1ln1 1ln2 1ln3
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The nicotinic receptor ligand binding domain.
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11914484 T.Ursby, M.Weik, E.Fioravanti, M.Delarue, M.Goeldner, and D.Bourgeois (2002).
Cryophotolysis of caged compounds: a technique for trapping intermediate states in protein crystals.
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PDB codes: 1gsi 1gtv
11938352 W.T.Lowther, H.Weissbach, F.Etienne, N.Brot, and B.W.Matthews (2002).
The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB.
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PDB code: 1l1d
12386838 X.Ren, Z.Han, and Y.Wang (2002).
Mechanisms of monocrotophos resistance in cotton bollworm, Helicoverpa armigera (Hübner).
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Extremely stable and versatile carboxylesterase from a hyperthermophilic archaeon.
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11567159 A.A.Vagin, and M.N.Isupov (2001).
Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps.
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Histochemical method for characterization of enzyme crystals: application to crystals of Torpedo californica acetylcholinesterase.
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Kinetics of diffusion-assisted reactions in microheterogeneous systems.
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Progress on the road to new nerve agent treatments.
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A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA.
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PDB codes: 1h8g 1hcx
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Carboxylesterase: specificity and spontaneous reactivation of an endogenous scavenger for organophosphorus compounds.
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Peptide interactions with G-protein coupled receptors.
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11264586 M.Weik, G.Kryger, A.M.Schreurs, B.Bouma, I.Silman, J.L.Sussman, P.Gros, and J.Kroon (2001).
Solvent behaviour in flash-cooled protein crystals at cryogenic temperatures.
  Acta Crystallogr D Biol Crystallogr, 57, 566-573.  
11567086 M.Weik, R.B.Ravelli, I.Silman, J.L.Sussman, P.Gros, and J.Kroon (2001).
Specific protein dynamics near the solvent glass transition assayed by radiation-induced structural changes.
  Protein Sci, 10, 1953-1961.  
11341926 P.Masson, W.Xie, M.T.Froment, and O.Lockridge (2001).
Effects of mutations of active site residues and amino acids interacting with the Omega loop on substrate activation of butyrylcholinesterase.
  Biochim Biophys Acta, 1544, 166-176.  
11257506 R.R.Ramsay, R.D.Gandour, and F.R.van der Leij (2001).
Molecular enzymology of carnitine transfer and transport.
  Biochim Biophys Acta, 1546, 21-43.  
11504610 T.Grutter, and J.P.Changeux (2001).
Nicotinic receptors in wonderland.
  Trends Biochem Sci, 26, 459-463.  
11308872 T.Y.Shen, K.Tai, and J.A.McCammon (2001).
Statistical analysis of the fractal gating motions of the enzyme acetylcholinesterase.
  Phys Rev E Stat Nonlin Soft Matter Phys, 63, 041902.  
11170379 U.Koch, G.Biasiol, M.Brunetti, D.Fattori, M.Pallaoro, and C.Steinkühler (2001).
Role of charged residues in the catalytic mechanism of hepatitis C virus NS3 protease: electrostatic precollision guidance and transition-state stabilization.
  Biochemistry, 40, 631-640.  
11300769 Z.A.Wood, L.B.Poole, and P.A.Karplus (2001).
Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysis.
  Biochemistry, 40, 3900-3911.
PDB code: 1hyu
10769121 A.Gershenson, J.A.Schauerte, L.Giver, and F.H.Arnold (2000).
Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases.
  Biochemistry, 39, 4658-4665.  
10732982 A.Hirashima, E.Kuwano, and M.Eto (2000).
Docking study of enantiomeric fonofos oxon bound to the active site of Torpedo californica acetylcholinesterase.
  Bioorg Med Chem, 8, 653-656.  
10819162 A.Martínez, C.Lanot, C.Perez, A.Castro, P.López-Serrano, and S.Conde (2000).
Lipase-catalysed synthesis of new acetylcholinesterase inhibitors: N-benzylpiperidine aminoacid derivatives.
  Bioorg Med Chem, 8, 731-738.  
11053834 A.Robinson, K.J.Edwards, P.D.Carr, J.D.Barton, G.D.Ewart, and D.L.Ollis (2000).
Structure of the C123S mutant of dienelactone hydrolase (DLH) bound with the PMS moiety of the protease inhibitor phenylmethylsulfonyl fluoride (PMSF).
  Acta Crystallogr D Biol Crystallogr, 56, 1376-1384.
PDB code: 1ggv
10759851 A.S.Hussein, A.M.Smith, M.R.Chacón, and M.E.Selkirk (2000).
Determinants of substrate specificity of a second non-neuronal secreted acetylcholinesterase from the parasitic nematode Nippostrongylus brasiliensis.
  Eur J Biochem, 267, 2276-2282.  
10874122 C.F.Bartels, W.Xie, A.K.Miller-Lindholm, L.M.Schopfer, and O.Lockridge (2000).
Determination of the DNA sequences of acetylcholinesterase and butyrylcholinesterase from cat and demonstration of the existence of both in cat plasma.
  Biochem Pharmacol, 60, 479-487.  
10762042 C.Guillou, A.Mary, D.Z.Renko, E.Gras, and C.Thal (2000).
Potent acetylcholinesterase inhibitors: design, synthesis and structure-activity relationships of alkylene linked bis-galanthamine and galanthamine-galanthaminium salts.
  Bioorg Med Chem Lett, 10, 637-639.  
10757879 C.Legay (2000).
Why so many forms of acetylcholinesterase?
  Microsc Res Tech, 49, 56-72.  
11123949 C.Viragh, T.K.Harris, P.M.Reddy, M.A.Massiah, A.S.Mildvan, and I.M.Kovach (2000).
NMR evidence for a short, strong hydrogen bond at the active site of a cholinesterase.
  Biochemistry, 39, 16200-16205.  
11053835 G.Kryger, M.Harel, K.Giles, L.Toker, B.Velan, A.Lazar, C.Kronman, D.Barak, N.Ariel, A.Shafferman, I.Silman, and J.L.Sussman (2000).
Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II.
  Acta Crystallogr D Biol Crystallogr, 56, 1385-1394.
PDB codes: 1b41 1f8u
  10739260 I.Tsigelny, I.N.Shindyalov, P.E.Bourne, T.C.Südhof, and P.Taylor (2000).
Common EF-hand motifs in cholinesterases and neuroligins suggest a role for Ca2+ binding in cell surface associations.
  Protein Sci, 9, 180-185.  
11106384 K.Håkansson, A.H.Wang, and C.G.Miller (2000).
The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad.
  Proc Natl Acad Sci U S A, 97, 14097-14102.
PDB codes: 1fy2 1fye
10801325 L.Wong, Z.Radic, R.J.Brüggemann, N.Hosea, H.A.Berman, and P.Taylor (2000).
Mechanism of oxime reactivation of acetylcholinesterase analyzed by chirality and mutagenesis.
  Biochemistry, 39, 5750-5757.  
  10892800 M.Harel, G.Kryger, T.L.Rosenberry, W.D.Mallender, T.Lewis, R.J.Fletcher, J.M.Guss, I.Silman, and J.L.Sussman (2000).
Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors.
  Protein Sci, 9, 1063-1072.
PDB codes: 1dx4 1qo9 1qon
10639129 M.Weik, R.B.Ravelli, G.Kryger, S.McSweeney, M.L.Raves, M.Harel, P.Gros, I.Silman, J.Kroon, and J.L.Sussman (2000).
Specific chemical and structural damage to proteins produced by synchrotron radiation.
  Proc Natl Acad Sci U S A, 97, 623-628.
PDB codes: 1qid 1qie 1qif 1qig 1qih 1qii 1qij 1qik 1qim 1qio
10718335 M.Wierdl, C.L.Morton, M.K.Danks, and P.M.Potter (2000).
Isolation and characterization of a cDNA encoding a horse liver butyrylcholinesterase: evidence for CPT-11 drug activation.
  Biochem Pharmacol, 59, 773-781.  
10673440 P.C.Bourne, M.N.Isupov, and J.A.Littlechild (2000).
The atomic-resolution structure of a novel bacterial esterase.
  Structure, 8, 143-151.
PDB codes: 1qlw 2wkw
10759065 P.Glynn (2000).
Neural development and neurodegeneration: two faces of neuropathy target esterase.
  Prog Neurobiol, 61, 61-74.  
10836143 P.J.Corringer, N.Le Novère, and J.P.Changeux (2000).
Nicotinic receptors at the amino acid level.
  Annu Rev Pharmacol Toxicol, 40, 431-458.  
10759845 S.Smialowski-Fléter, A.Moulin, C.Villard, and A.Puigserver (2000).
Structure-function relationships in the carboxylic-ester-hydrolase superfamily. Disulfide bridge arrangement in porcine intestinal glycerol-ester hydrolase.
  Eur J Biochem, 267, 2227-2234.  
10679631 S.T.Wlodek, T.Shen, and J.A.McCammon (2000).
Electrostatic steering of substrate to acetylcholinesterase: analysis of field fluctuations.
  Biopolymers, 53, 265-271.  
10869180 W.D.Mallender, T.Szegletes, and T.L.Rosenberry (2000).
Acetylthiocholine binds to asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway.
  Biochemistry, 39, 7753-7763.  
10692319 X.Z.Song, and S.E.Pedersen (2000).
Electrostatic interactions regulate desensitization of the nicotinic acetylcholine receptor.
  Biophys J, 78, 1324-1334.  
10818355 Y.C.Lo, Y.L.Lee, J.F.Shaw, and Y.C.Liaw (2000).
Crystallization and preliminary X-ray crystallographic analysis of thioesterase I from Escherichia coli.
  Acta Crystallogr D Biol Crystallogr, 56, 756-757.  
11131157 Y.Li, Y.Zhao, S.Hatfield, R.Wan, Q.Zhu, X.Li, M.McMills, Y.Ma, J.Li, K.L.Brown, C.He, F.Liu, and X.Chen (2000).
Dipeptide seryl-histidine and related oligopeptides cleave DNA, protein, and a carboxyl ester.
  Bioorg Med Chem, 8, 2675-2680.  
10074358 A.Ordentlich, D.Barak, C.Kronman, H.P.Benschop, L.P.De Jong, N.Ariel, R.Barak, Y.Segall, B.Velan, and A.Shafferman (1999).
Exploring the active center of human acetylcholinesterase with stereomers of an organophosphorus inhibitor with two chiral centers.
  Biochemistry, 38, 3055-3066.  
10047509 A.Watts (1999).
NMR of drugs and ligands bound to membrane receptors.
  Curr Opin Biotechnol, 10, 48-53.  
10491076 A.Weingand-Ziadé, F.Renault, and P.Masson (1999).
Differential effect of pressure and temperature on the catalytic behaviour of wild-type human butyrylcholinesterase and its D70G mutant.
  Eur J Biochem, 264, 327-335.  
10022354 B.A.Thomas, W.B.Church, T.R.Lane, and B.D.Hammock (1999).
Homology model of juvenile hormone esterase from the crop pest, Heliothis virescens.
  Proteins, 34, 184-196.  
10403184 B.M.Veneziani, F.Giallauria, and F.Gentile (1999).
The disulfide bond pattern between fragments obtained by the limited proteolysis of bovine thyroglobulin.
  Biochimie, 81, 517-525.  
10535917 B.Spiller, A.Gershenson, F.H.Arnold, and R.C.Stevens (1999).
A structural view of evolutionary divergence.
  Proc Natl Acad Sci U S A, 96, 12305-12310.
PDB codes: 1c00 1c7i 1c7j 1qe3 1qe8
10353814 C.B.Millard, G.Kryger, A.Ordentlich, H.M.Greenblatt, M.Harel, M.L.Raves, Y.Segall, D.Barak, A.Shafferman, I.Silman, and J.L.Sussman (1999).
Crystal structures of aged phosphonylated acetylcholinesterase: nerve agent reaction products at the atomic level.
  Biochemistry, 38, 7032-7039.
PDB codes: 1cfj 1som 2dfp
10231521 C.Bartolucci, E.Perola, L.Cellai, M.Brufani, and D.Lamba (1999).
"Back door" opening implied by the crystal structure of a carbamoylated acetylcholinesterase.
  Biochemistry, 38, 5714-5719.
PDB code: 1oce
10491113 D.Grisaru, M.Sternfeld, A.Eldor, D.Glick, and H.Soreq (1999).
Structural roles of acetylcholinesterase variants in biology and pathology.
  Eur J Biochem, 264, 672-686.  
9876135 G.Akk, M.Zhou, and A.Auerbach (1999).
A mutational analysis of the acetylcholine receptor channel transmitter binding site.
  Biophys J, 76, 207-218.  
10368299 G.Kryger, I.Silman, and J.L.Sussman (1999).
Structure of acetylcholinesterase complexed with E2020 (Aricept): implications for the design of new anti-Alzheimer drugs.
  Structure, 7, 297-307.
PDB code: 1eve
  10493580 G.Manco, F.Febbraio, E.Adinolfi, and M.Rossi (1999).
Homology modeling and active-site residues probing of the thermophilic Alicyclobacillus acidocaldarius esterase 2.
  Protein Sci, 8, 1789-1796.  
10580988 J.G.Oakeshott, C.Claudianos, R.J.Russell, and G.C.Robin (1999).
Carboxyl/cholinesterases: a case study of the evolution of a successful multigene family.
  Bioessays, 21, 1031-1042.  
10449714 J.P.Gallivan, and D.A.Dougherty (1999).
Cation-pi interactions in structural biology.
  Proc Natl Acad Sci U S A, 96, 9459-9464.  
10547694 K.E.Jaeger, B.W.Dijkstra, and M.T.Reetz (1999).
Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases.
  Annu Rev Microbiol, 53, 315-351.  
10082962 M.Sentjurc, S.Pecar, J.Stojan, P.Marchot, Z.Radić, and Z.Grubic (1999).
Electron paramagnetic resonance reveals altered topography of the active center gorge of acetylcholinesterase after binding of fasciculin to the peripheral site.
  Biochim Biophys Acta, 1430, 349-358.  
10561608 M.T.Garcia-Conesa, P.A.Kroon, J.Ralph, F.A.Mellon, I.J.Colquhoun, L.Saulnier, J.F.Thibault, and G.Williamson (1999).
A cinnamoyl esterase from Aspergillus niger can break plant cell wall cross-links without release of free diferulic acids.
  Eur J Biochem, 266, 644-652.  
  10631970 R.Arnon, I.Silman, and R.Tarrab-Hazdai (1999).
Acetylcholinesterase of Schistosoma mansoni--functional correlates. Contributed in honor of Professor Hans Neurath's 90th birthday.
  Protein Sci, 8, 2553-2561.  
10545346 S.A.Botti, C.E.Felder, S.Lifson, J.L.Sussman, and I.Silman (1999).
A modular treatment of molecular traffic through the active site of cholinesterase
  Biophys J, 77, 2430-2450.  
10570246 S.Longhi, and C.Cambillau (1999).
Structure-activity of cutinase, a small lipolytic enzyme.
  Biochim Biophys Acta, 1441, 185-196.  
9890890 T.Szegletes, W.D.Mallender, P.J.Thomas, and T.L.Rosenberry (1999).
Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect.
  Biochemistry, 38, 122-133.  
9989227 V.Levitsky, W.Xie, M.T.Froment, O.Lockridge, and P.Masson (1999).
Polyol-induced activation by excess substrate of the D70G butyrylcholinesterase mutant.
  Biochim Biophys Acta, 1429, 422-430.  
10037498 V.Talesa, M.Grauso, M.Arpagaus, E.Giovannini, R.Romani, and G.Rosi (1999).
Molecular cloning and expression of a full-length cDNA encoding acetylcholinesterase in optic lobes of the squid Loligo opalescens: a new member of the cholinesterase family resistant to diisopropyl fluorophosphate.
  J Neurochem, 72, 1250-1258.  
10446376 Z.Kovarik, Z.Radić, B.Grgas, M.Skrinjarić-Spoljar, E.Reiner, and V.Simeon-Rudolf (1999).
Amino acid residues involved in the interaction of acetylcholinesterase and butyrylcholinesterase with the carbamates Ro 02-0683 and bambuterol, and with terbutaline.
  Biochim Biophys Acta, 1433, 261-271.  
10576601 Z.Yingge, Z.Delu, B.Chunli, and W.Chen (1999).
Force spectroscopy between acetylcholinesterase molecule and its natural substrate to study the effects of inhibitors and reactivators on enzyme activity.
  Life Sci, 65, PL253-PL260.  
9790671 A.Saxena, C.Viragh, D.S.Frazier, I.M.Kovach, D.M.Maxwell, O.Lockridge, and B.P.Doctor (1998).
The pH dependence of dealkylation in soman-inhibited cholinesterases and their mutants: further evidence for a push-pull mechanism.
  Biochemistry, 37, 15086-15096.  
9695026 C.D.Bhanumathy, and A.S.Balasubramanian (1998).
Selective inactivation of butyrylcholinesterase with metal chelators suggests there is more than one metal binding site.
  Int J Biochem Cell Biol, 30, 695-705.  
9922164 D.J.Quirk, C.Park, J.E.Thompson, and R.T.Raines (1998).
His...Asp catalytic dyad of ribonuclease A: conformational stability of the wild-type, D121N, D121A, and H119A enzymes.
  Biochemistry, 37, 17958-17964.  
9739094 E.Schlagenhauf, R.Etges, and P.Metcalf (1998).
The crystal structure of the Leishmania major surface proteinase leishmanolysin (gp63).
  Structure, 6, 1035-1046.
PDB code: 1lml
9427736 F.J.Medrano, J.Alonso, J.L.García, A.Romero, W.Bode, and F.X.Gomis-Rüth (1998).
Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family.
  EMBO J, 17, 1-9.
PDB code: 1azw
9671522 F.Nachon, L.Ehret-Sabatier, D.Loew, C.Colas, A.van Dorsselaer, and M.Goeldner (1998).
Trp82 and Tyr332 are involved in two quaternary ammonium binding domains of human butyrylcholinesterase as revealed by photoaffinity labeling with [3H]DDF.
  Biochemistry, 37, 10507-10513.  
9597732 F.Villatte, V.Marcel, S.Estrada-Mondaca, and D.Fournier (1998).
Engineering sensitive acetylcholinesterase for detection of organophosphate and carbamate insecticides.
  Biosens Bioelectron, 13, 157-164.  
9744565 G.Amitai, D.Moorad, R.Adani, and B.P.Doctor (1998).
Inhibition of acetylcholinesterase and butyrylcholinesterase by chlorpyrifos-oxon.
  Biochem Pharmacol, 56, 293-299.  
9873615 G.Lin, G.H.Chen, and H.C.Ho (1998).
Conformationally restricted carbamate inhibitors of horse serum butyrylcholinesterase.
  Bioorg Med Chem Lett, 8, 2747-2750.  
9774723 G.Lin, Y.C.Tsai, H.C.Liu, W.C.Liao, and C.H.Chang (1998).
Enantiomeric inhibitors of cholesterol esterase and acetylcholinesterase.
  Biochim Biophys Acta, 1388, 161-174.  
9770445 H.S.Choi, S.B.Suh, S.J.Cho, and K.S.Kim (1998).
Ionophores and receptors using cation-pi interactions: collarenes.
  Proc Natl Acad Sci U S A, 95, 12094-12099.  
9530014 H.X.Zhou, J.M.Briggs, S.Tara, and J.A.McCammon (1998).
Correlation between rate of enzyme-substrate diffusional encounter and average Boltzmann factor around active site.
  Biopolymers, 45, 355-360.  
9689071 H.X.Zhou, S.T.Wlodek, and J.A.McCammon (1998).
Conformation gating as a mechanism for enzyme specificity.
  Proc Natl Acad Sci U S A, 95, 9280-9283.  
9689034 J.Lindstrom (1998).
Mutations causing muscle weakness.
  Proc Natl Acad Sci U S A, 95, 9070-9071.  
9856454 J.P.Changeux, and S.J.Edelstein (1998).
Allosteric receptors after 30 years.
  Neuron, 21, 959-980.  
9720251 J.Pleiss, M.Fischer, and R.D.Schmid (1998).
Anatomy of lipase binding sites: the scissile fatty acid binding site.
  Chem Phys Lipids, 93, 67-80.  
  9792097 K.Johansson, M.El-Ahmad, S.Ramaswamy, L.Hjelmqvist, H.Jörnvall, and H.Eklund (1998).
Structure of betaine aldehyde dehydrogenase at 2.1 A resolution.
  Protein Sci, 7, 2106-2117.
PDB codes: 1a4s 1bpw
9748587 K.Sepcić, V.Marcel, A.Klaebe, T.Turk, D.Suput, and D.Fournier (1998).
Inhibition of acetylcholinesterase by an alkylpyridinium polymer from the marine sponge, Reniera sarai.
  Biochim Biophys Acta, 1387, 217-225.  
9751636 L.M.Kauvar, and H.O.Villar (1998).
Deciphering cryptic similarities in protein binding sites.
  Curr Opin Biotechnol, 9, 390-394.  
9636030 L.W.Schultz, D.J.Quirk, and R.T.Raines (1998).
His...Asp catalytic dyad of ribonuclease A: structure and function of the wild-type, D121N, and D121A enzymes.
  Biochemistry, 37, 8886-8898.
PDB codes: 3rsd 4rsd
10089494 M.Hendlich (1998).
Databases for protein-ligand complexes.
  Acta Crystallogr D Biol Crystallogr, 54, 1178-1182.  
9707574 P.S.Kim, S.A.Hossain, Y.N.Park, I.Lee, S.E.Yoo, and P.Arvan (1998).
A single amino acid change in the acetylcholinesterase-like domain of thyroglobulin causes congenital goiter with hypothyroidism in the cog/cog mouse: a model of human endoplasmic reticulum storage diseases.
  Proc Natl Acad Sci U S A, 95, 9909-9913.  
10089512 R.B.Ravelli, M.L.Raves, Z.Ren, D.Bourgeois, M.Roth, J.Kroon, I.Silman, and J.L.Sussman (1998).
Static Laue diffraction studies on acetylcholinesterase.
  Acta Crystallogr D Biol Crystallogr, 54, 1359-1366.
PDB codes: 1ax9 2ack
10021768 R.H.ffrench-Constant, B.Pittendrigh, A.Vaughan, and N.Anthony (1998).
Why are there so few resistance-associated mutations in insecticide target genes?
  Philos Trans R Soc Lond B Biol Sci, 353, 1685-1693.  
  9420267 R.P.Valle, and B.Falgout (1998).
Mutagenesis of the NS3 protease of dengue virus type 2.
  J Virol, 72, 624-632.  
9627407 S.Estrada-Mondaca, A.Lougarre, and D.Fournier (1998).
Drosophila acetylcholinesterase: effect of post-translational [correction of post-traductional] modifications on the production in the baculovirus system and substrate metabolization.
  Arch Insect Biochem Physiol, 38, 84-90.  
9838872 S.Tara, A.H.Elcock, P.D.Kirchhoff, J.M.Briggs, Z.Radic, P.Taylor, and J.A.McCammon (1998).
Rapid binding of a cationic active site inhibitor to wild type and mutant mouse acetylcholinesterase: Brownian dynamics simulation including diffusion in the active site gorge.
  Biopolymers, 46, 465-474.  
9521743 T.Szegletes, W.D.Mallender, and T.L.Rosenberry (1998).
Nonequilibrium analysis alters the mechanistic interpretation of inhibition of acetylcholinesterase by peripheral site ligands.
  Biochemistry, 37, 4206-4216.  
  9827998 W.M.Liu, and K.C.Chou (1998).
Singular points of protein beta-sheets.
  Protein Sci, 7, 2324-2330.  
9770444 W.Zhong, J.P.Gallivan, Y.Zhang, L.Li, H.A.Lester, and D.A.Dougherty (1998).
From ab initio quantum mechanics to molecular neurobiology: a cation-pi binding site in the nicotinic receptor.
  Proc Natl Acad Sci U S A, 95, 12088-12093.  
9399841 X.Cousin, T.Hotelier, K.Giles, J.P.Toutant, and A.Chatonnet (1998).
aCHEdb: the database system for ESTHER, the alpha/beta fold family of proteins and the Cholinesterase gene server.
  Nucleic Acids Res, 26, 226-228.  
9448738 Y.Ashani, H.Leader, N.Rothschild, and C.Dosoretz (1998).
Combined effect of organophosphorus hydrolase and oxime on the reactivation rate of diethylphosphoryl-acetylcholinesterase conjugates.
  Biochem Pharmacol, 55, 159-168.  
  9385633 A.C.Wallace, N.Borkakoti, and J.M.Thornton (1997).
TESS: a geometric hashing algorithm for deriving 3D coordinate templates for searching structural databases. Application to enzyme active sites.
  Protein Sci, 6, 2308-2323.  
9188741 A.V.Efimov (1997).
Structural trees for protein superfamilies.
  Proteins, 28, 241-260.  
9261870 C.Albaret, S.Lacoutière, W.P.Ashman, D.Froment, and P.L.Fortier (1997).
Molecular mechanic study of nerve agent O-ethyl S-[2-(diisopropylamino)ethyl]methylphosphonothioate (VX) bound to the active site of Torpedo californica acetylcholinesterase.
  Proteins, 28, 543-555.  
9204869 C.Viragh, R.Akhmetshin, I.M.Kovach, and C.Broomfield (1997).
Unique push-pull mechanism of dealkylation in soman-inhibited cholinesterases.
  Biochemistry, 36, 8243-8252.  
17029877 D.Porschke (1997).
Macrodipoles. Unusual electric properties of biological macromolecules.
  Biophys Chem, 66, 241-257.  
9062997 D.Sutherland, J.S.McClellan, D.Milner, W.Soong, N.Axon, M.Sanders, A.Hester, Y.H.Kao, T.Poczatek, S.Routt, and L.Pezzementi (1997).
Two cholinesterase activities and genes are present in amphioxus.
  J Exp Zool, 277, 213-229.  
9342220 E.Baudouin, M.Charpenteau, D.Roby, Y.Marco, R.Ranjeva, and B.Ranty (1997).
Functional expression of a tobacco gene related to the serine hydrolase family -- esterase activity towards short-chain dinitrophenyl acylesters.
  Eur J Biochem, 248, 700-706.  
  9029508 G.Klebe, and H.J.Böhm (1997).
Energetic and entropic factors determining binding affinity in protein-ligand complexes.
  J Recept Signal Transduct Res, 17, 459-473.  
9403137 H.R.Arias (1997).
Topology of ligand binding sites on the nicotinic acetylcholine receptor.
  Brain Res Brain Res Rev, 25, 133-191.  
9223291 I.Rousso, E.Khachatryan, Y.Gat, I.Brodsky, M.Ottolenghi, M.Sheves, and A.Lewis (1997).
Microsecond atomic force sensing of protein conformational dynamics: implications for the primary light-induced events in bacteriorhodopsin.
  Proc Natl Acad Sci U S A, 94, 7937-7941.  
9095190 J.A.Grobler, and J.H.Hurley (1997).
Similarity between C2 domain jaws and immunoglobulin CDRs.
  Nat Struct Biol, 4, 261-262.  
9047296 J.Basran, M.Mewies, F.S.Mathews, and N.S.Scrutton (1997).
Selective modification of alkylammonium ion specificity in trimethylamine dehydrogenase by the rational engineering of cation-pi bonding.
  Biochemistry, 36, 1989-1998.  
  9171386 K.B.Merck, H.de Cock, H.M.Verheij, and J.Tommassen (1997).
Topology of the outer membrane phospholipase A of Salmonella typhimurium.
  J Bacteriol, 179, 3443-3450.  
9048550 K.H.Han, K.J.Hwang, S.M.Kim, S.K.Kim, W.R.Gray, B.M.Olivera, J.Rivier, and K.J.Shon (1997).
NMR structure determination of a novel conotoxin, [Pro 7,13] alpha A-conotoxin PIVA.
  Biochemistry, 36, 1669-1677.
PDB code: 1p1p
9032073 K.K.Kim, H.K.Song, D.H.Shin, K.Y.Hwang, and S.W.Suh (1997).
The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor.
  Structure, 5, 173-185.
PDB code: 1oil
8989325 M.L.Raves, M.Harel, Y.P.Pang, I.Silman, A.P.Kozikowski, and J.L.Sussman (1997).
Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A.
  Nat Struct Biol, 4, 57-63.
PDB codes: 1vot 2ace
9291997 M.Recanatini, A.Cavalli, and C.Hansch (1997).
A comparative QSAR analysis of acetylcholinesterase inhibitors currently studied for the treatment of Alzheimer's disease.
  Chem Biol Interact, 105, 199-228.  
9020776 O.Lockridge, R.M.Blong, P.Masson, M.T.Froment, C.B.Millard, and C.A.Broomfield (1997).
A single amino acid substitution, Gly117His, confers phosphotriesterase (organophosphorus acid anhydride hydrolase) activity on human butyrylcholinesterase.
  Biochemistry, 36, 786-795.  
9310385 P.A.Kroon, C.B.Faulds, C.Brézillon, and G.Williamson (1997).
Methyl phenylalkanoates as substrates to probe the active sites of esterases.
  Eur J Biochem, 248, 245-251.  
9047329 P.Masson, P.Legrand, C.F.Bartels, M.T.Froment, L.M.Schopfer, and O.Lockridge (1997).
Role of aspartate 70 and tryptophan 82 in binding of succinyldithiocholine to human butyrylcholinesterase.
  Biochemistry, 36, 2266-2277.  
9207114 R.D.Newcomb, P.M.Campbell, D.L.Ollis, E.Cheah, R.J.Russell, and J.G.Oakeshott (1997).
A single amino acid substitution converts a carboxylesterase to an organophosphorus hydrolase and confers insecticide resistance on a blowfly.
  Proc Natl Acad Sci U S A, 94, 7464-7468.  
  9041628 S.Longhi, M.Mannesse, H.M.Verheij, G.H.De Haas, M.Egmond, E.Knoops-Mouthuy, and C.Cambillau (1997).
Crystal structure of cutinase covalently inhibited by a triglyceride analogue.
  Protein Sci, 6, 275-286.
PDB code: 1oxm
9016525 X.Cousin, T.Hotelier, K.Giles, P.Lievin, J.P.Toutant, and A.Chatonnet (1997).
The alpha/beta fold family of proteins database and the cholinesterase gene server ESTHER.
  Nucleic Acids Res, 25, 143-146.  
9331420 X.Wang, C.S.Wang, J.Tang, F.Dyda, and X.C.Zhang (1997).
The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism.
  Structure, 5, 1209-1218.
PDB codes: 1akn 1aql
  8951687 A.A.al-Jafari (1996).
The nature of the inhibition of camel retina acetylcholinesterase (EC 3.1.1.7) activity by tetrahydroaminoacridine.
  J Ocul Pharmacol Ther, 12, 503-514.  
  8762132 A.C.Wallace, R.A.Laskowski, and J.M.Thornton (1996).
Derivation of 3D coordinate templates for searching structural databases: application to Ser-His-Asp catalytic triads in the serine proteinases and lipases.
  Protein Sci, 5, 1001-1013.  
  8961166 A.Galli, E.Ranaudo, L.Giannini, and C.Costagli (1996).
Reversible inhibition of cholinesterases by opioids: possible pharmacological consequences.
  J Pharm Pharmacol, 48, 1164-1168.  
8555209 A.Nicolas, M.Egmond, C.T.Verrips, J.de Vlieg, S.Longhi, C.Cambillau, and C.Martinez (1996).
Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state.
  Biochemistry, 35, 398-410.
PDB codes: 1ffa 1ffb 1ffc 1ffd 1ffe
8879546 C.H.Faerman, S.N.Savvides, C.Strickland, M.A.Breidenbach, J.A.Ponasik, B.Ganem, D.Ripoll, R.L.Krauth-Siegel, and P.A.Karplus (1996).
Charge is the major discriminating factor for glutathione reductase versus trypanothione reductase inhibitors.
  Bioorg Med Chem, 4, 1247-1253.  
  8703090 C.Robin, R.J.Russell, K.M.Medveczky, and J.G.Oakeshott (1996).
Duplication and divergence of the genes of the alpha-esterase cluster of Drosophila melanogaster.
  J Mol Evol, 43, 241-252.  
8780506 C.T.Craescu, N.Rouvière, A.Popescu, E.Cerpolini, M.C.Lebeau, E.E.Baulieu, and J.Mispelter (1996).
Three-dimensional structure of the immunophilin-like domain of FKBP59 in solution.
  Biochemistry, 35, 11045-11052.
PDB codes: 1rot 1rou
  8880909 D.I.Kreimer, I.Shin, V.L.Shnyrov, E.Villar, I.Silman, and L.Weiner (1996).
Two partially unfolded states of Torpedo californica acetylcholinesterase.
  Protein Sci, 5, 1852-1864.  
8785319 D.Porschke, C.Créminon, X.Cousin, C.Bon, J.Sussman, and I.Silman (1996).
Electrooptical measurements demonstrate a large permanent dipole moment associated with acetylcholinesterase.
  Biophys J, 70, 1603-1608.  
8744302 G.Akk, and A.Auerbach (1996).
Inorganic, monovalent cations compete with agonists for the transmitter binding site of nicotinic acetylcholine receptors.
  Biophys J, 70, 2652-2658.  
8664265 G.Xiao, S.Liu, X.Ji, W.W.Johnson, J.Chen, J.F.Parsons, W.J.Stevens, G.L.Gilliland, and R.N.Armstrong (1996).
First-sphere and second-sphere electrostatic effects in the active site of a class mu gluthathione transferase.
  Biochemistry, 35, 4753-4765.
PDB codes: 6gst 6gsu 6gsv 6gsw 6gsx 6gsy
  8890157 I.Darboux, Y.Barthalay, M.Piovant, and R.Hipeau-Jacquotte (1996).
The structure-function relationships in Drosophila neurotactin show that cholinesterasic domains may have adhesive properties.
  EMBO J, 15, 4835-4843.  
  8771195 I.Shin, I.Silman, and L.M.Weiner (1996).
Interaction of partially unfolded forms of Torpedo acetylcholinesterase with liposomes.
  Protein Sci, 5, 42-51.  
8924629 J.Antosiewicz, S.T.Wlodek, and J.A.McCammon (1996).
Acetylcholinesterase: role of the enzyme's charge distribution in steering charged ligands toward the active site.
  Biopolymers, 39, 85-94.  
9630920 J.C.Moore, and F.H.Arnold (1996).
Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents.
  Nat Biotechnol, 14, 458-467.  
8718877 L.Peng, I.Silman, J.Sussman, and M.Goeldner (1996).
Biochemical evaluation of photolabile precursors of choline and of carbamylcholine for potential time-resolved crystallographic studies on cholinesterases.
  Biochemistry, 35, 10854-10861.  
8718893 N.A.Hosea, Z.Radić, I.Tsigelny, H.A.Berman, D.M.Quinn, and P.Taylor (1996).
Aspartate 74 as a primary determinant in acetylcholinesterase governing specificity to cationic organophosphonates.
  Biochemistry, 35, 10995-11004.  
  8845756 P.Marchot, R.B.Ravelli, M.L.Raves, Y.Bourne, D.C.Vellom, J.Kanter, S.Camp, J.L.Sussman, and P.Taylor (1996).
Soluble monomeric acetylcholinesterase from mouse: expression, purification, and crystallization in complex with fasciculin.
  Protein Sci, 5, 672-679.  
8631355 P.Masson, M.T.Froment, C.F.Bartels, and O.Lockridge (1996).
Asp7O in the peripheral anionic site of human butyrylcholinesterase.
  Eur J Biochem, 235, 36-48.  
8799740 R.D.Newcomb, P.D.East, R.J.Russell, and J.G.Oakeshott (1996).
Isolation of alpha cluster esterase genes associated with organophosphate resistance in Lucilia cuprina.
  Insect Mol Biol, 5, 211-216.  
  8554068 S.L.Primo-Parmo, C.F.Bartels, B.Wiersema, A.F.van der Spek, J.W.Innis, and B.N.La Du (1996).
Characterization of 12 silent alleles of the human butyrylcholinesterase (BCHE) gene.
  Am J Hum Genet, 58, 52-64.  
8547248 T.L.Rosenberry, C.R.Rabl, and E.Neumann (1996).
Binding of the neurotoxin fasciculin 2 to the acetylcholinesterase peripheral site drastically reduces the association and dissociation rate constants for N-methylacridinium binding to the active site.
  Biochemistry, 35, 685-690.  
8805565 U.G.Wagner, M.Hasslacher, H.Griengl, H.Schwab, and C.Kratky (1996).
Mechanism of cyanogenesis: the crystal structure of hydroxynitrile lyase from Hevea brasiliensis.
  Structure, 4, 811-822.
PDB code: 1yas
9082459 U.Holzgrabe (1996).
[Can drugs be designed on a computer?]
  Pharm Unserer Zeit, 25, 322-325.  
8594562 X.Cousin, T.Hotelier, P.Liévin, J.P.Toutant, and A.Chatonnet (1996).
A cholinesterase genes server (ESTHER): a database of cholinesterase-related sequences for multiple alignments, phylogenetic relationships, mutations and structural data retrieval.
  Nucleic Acids Res, 24, 132-136.  
  8877268 Y.Fraenkel, D.E.Shalev, J.M.Gershoni, and G.Navon (1996).
Nuclear magnetic resonance (NMR) analysis of ligand receptor interactions: the cholinergic system--a model.
  Crit Rev Biochem Mol Biol, 31, 273-301.  
8894101 Y.Kawakami, A.Inoue, T.Kawai, M.Wakita, H.Sugimoto, and A.J.Hopfinger (1996).
The rationale for E2020 as a potent acetylcholinesterase inhibitor.
  Bioorg Med Chem, 4, 1429-1446.  
7584632 A.A.Aljafari (1995).
Kinetics for the inhibition of acetylcholinesterase from human erythrocyte by cisplatin.
  Int J Biochem Cell Biol, 27, 965-970.  
  8580856 A.R.Raine, C.C.Yang, L.C.Packman, S.A.White, F.S.Mathews, and N.S.Scrutton (1995).
Protein recognition of ammonium cations using side-chain aromatics: a structural variation for secondary ammonium ligands.
  Protein Sci, 4, 2625-2628.  
  8770646 B.Espinoza, M.Parizade, E.Ortega, R.Tarrab-Hazdai, D.Zilberg, and R.Arnon (1995).
Monoclonal antibodies against acetylcholinesterase of Schistosoma mansoni: production and characterization.
  Hybridoma, 14, 577-586.  
7611670 B.M.Conti-Fine, A.Maelicke, S.Reinhardt-Maelicke, V.Chiappinelli, and K.E.McLane (1995).
Binding sites for neurotoxins and cholinergic ligands in peripheral and neuronal nicotinic receptors. Studies with synthetic receptor sequences.
  Ann N Y Acad Sci, 757, 133-152.  
7556160 C.C.Yang, L.C.Packman, and N.S.Scrutton (1995).
The primary structure of Hyphomicrobium X dimethylamine dehydrogenase. Relationship to trimethylamine dehydrogenase and implications for substrate recognition.
  Eur J Biochem, 232, 264-271.  
7744040 C.Cervenanský, A.Engström, and E.Karlsson (1995).
Role of arginine residues for the activity of fasciculin.
  Eur J Biochem, 229, 270-275.  
7766682 D.Aslanian, P.Gróf, F.Renault, and P.Masson (1995).
Raman spectroscopic study of conjugates of butyrylcholinesterase with organophosphates.
  Biochim Biophys Acta, 1249, 37-44.  
7788294 D.Ghosh, Z.Wawrzak, V.Z.Pletnev, N.Li, R.Kaiser, W.Pangborn, H.Jörnvall, M.Erman, and W.L.Duax (1995).
Structure of uncomplexed and linoleate-bound Candida cylindracea cholesterol esterase.
  Structure, 3, 279-288.
PDB code: 1cle
  8528091 F.N.Musayev, Y.L.Lee, J.F.Shaw, and Y.C.Liaw (1995).
Crystallization and preliminary X-ray crystallographic analysis of arylesterase from Vibrio mimicus.
  Protein Sci, 4, 1931-1933.  
  7769716 G.A.Cox, M.Wakulchik, L.M.Sassmannshausen, W.Gibson, and E.C.Villarreal (1995).
Human cytomegalovirus proteinase: candidate glutamic acid identified as third member of putative active-site triad.
  J Virol, 69, 4524-4528.  
8591035 G.Rudenko, E.Bonten, A.d'Azzo, and W.G.Hol (1995).
Three-dimensional structure of the human 'protective protein': structure of the precursor form suggests a complex activation mechanism.
  Structure, 3, 1249-1259.
PDB code: 1ivy
  7613468 H.K.van den Born, Z.Radić, P.Marchot, P.Taylor, and I.Tsigelny (1995).
Theoretical analysis of the structure of the peptide fasciculin and its docking to acetylcholinesterase.
  Protein Sci, 4, 703-715.  
7787844 J.A.Argentine, and A.A.James (1995).
Characterization of a salivary gland-specific esterase in the vector mosquito, Aedes aegypti.
  Insect Biochem Mol Biol, 25, 621-630.  
8519985 J.Chen, Y.Zhang, G.Akk, S.Sine, and A.Auerbach (1995).
Activation kinetics of recombinant mouse nicotinic acetylcholine receptors: mutations of alpha-subunit tyrosine 190 affect both binding and gating.
  Biophys J, 69, 849-859.  
7736595 K.Ichtchenko, Y.Hata, T.Nguyen, B.Ullrich, M.Missler, C.Moomaw, and T.C.Südhof (1995).
Neuroligin 1: a splice site-specific ligand for beta-neurexins.
  Cell, 81, 435-443.  
7607235 K.M.Loomes (1995).
Structural organisation of human bile-salt-activated lipase probed by limited proteolysis and expression of a recombinant truncated variant.
  Eur J Biochem, 230, 607-613.  
8580913 K.Y.Zhu, and J.M.Clark (1995).
Cloning and sequencing of a cDNA encoding acetylcholinesterase in Colorado potato beetle, Leptinotarsa decemlineata (Say).
  Insect Biochem Mol Biol, 25, 1129-1138.  
7649165 M.H.Remy, Y.Frobert, and J.Grassi (1995).
Characterization of monoclonal antibodies that strongly inhibit Electrophorus electricus acetylcholinesterase.
  Eur J Biochem, 231, 651-658.  
8747462 M.Harel, G.J.Kleywegt, R.B.Ravelli, I.Silman, and J.L.Sussman (1995).
Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target.
  Structure, 3, 1355-1366.
PDB code: 1fss
7494866 M.Schwarz, D.Glick, Y.Loewenstein, and H.Soreq (1995).
Engineering of human cholinesterases explains and predicts diverse consequences of administration of various drugs and poisons.
  Pharmacol Ther, 67, 283-322.  
7898167 N.H.Greig, X.F.Pei, T.T.Soncrant, D.K.Ingram, and A.Brossi (1995).
Phenserine and ring C hetero-analogues: drug candidates for the treatment of Alzheimer's disease.
  Med Res Rev, 15, 3.  
8597093 P.Taylor, Z.Radic, N.A.Hosea, S.Camp, P.Marchot, and H.A.Berman (1995).
Structural bases for the specificity of cholinesterase catalysis and inhibition.
  Toxicol Lett, 82, 453-458.  
7608746 R.J.Zauhar (1995).
SMART: a solvent-accessible triangulated surface generator for molecular graphics and boundary element applications.
  J Comput Aided Mol Des, 9, 149-159.  
7895271 S.A.Jones, C.Holmes, T.C.Budd, and S.A.Greenfield (1995).
The effect of acetylcholinesterase on outgrowth of dopaminergic neurons in organotypic slice culture of rat mid-brain.
  Cell Tissue Res, 279, 323-330.  
8521480 Y.Bourne, P.Taylor, and P.Marchot (1995).
Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex.
  Cell, 83, 503-512.
PDB code: 1mah
7566364 Y.Cho, T.S.Ko, S.H.Cha, and D.E.Sok (1995).
Properties of acetylcholinesterase reconstituted in liposomes of a different charge.
  Neurochem Res, 20, 681-687.  
7773790 Y.Wei, J.L.Schottel, U.Derewenda, L.Swenson, S.Patkar, and Z.S.Derewenda (1995).
A novel variant of the catalytic triad in the Streptomyces scabies esterase.
  Nat Struct Biol, 2, 218-223.
PDB codes: 1esc 1esd 1ese
7599168 Z.Grubic, A.Stalc, M.Sentjurc, S.Pecar, M.K.Gentry, and B.P.Doctor (1995).
Different effects of two peripheral anionic site-binding ligands on acetylcholinesterase active-site gorge topography revealed by electron paramagnetic resonance.
  Biochim Biophys Acta, 1249, 155-160.  
7944340 A.Friboulet, L.Izadyar, B.Avalle, A.Roseto, and D.Thomas (1994).
Abzyme generation using an anti-idiotypic antibody as the "internal image" of an enzyme active site.
  Appl Biochem Biotechnol, 47, 229.  
8016090 A.Mutero, M.Pralavorio, J.M.Bride, and D.Fournier (1994).
Resistance-associated point mutations in insecticide-insensitive acetylcholinesterase.
  Proc Natl Acad Sci U S A, 91, 5922-5926.  
  7849595 A.Saxena, N.Qian, I.M.Kovach, A.P.Kozikowski, Y.P.Pang, D.C.Vellom, Z.Radić, D.Quinn, P.Taylor, and B.P.Doctor (1994).
Identification of amino acid residues involved in the binding of Huperzine A to cholinesterases.
  Protein Sci, 3, 1770-1778.  
  8062821 A.Shafferman, A.Ordentlich, D.Barak, C.Kronman, R.Ber, T.Bino, N.Ariel, R.Osman, and B.Velan (1994).
Electrostatic attraction by surface charge does not contribute to the catalytic efficiency of acetylcholinesterase.
  EMBO J, 13, 3448-3455.  
8069632 B.Golinelli-Pimpaneau, B.Gigant, T.Bizebard, J.Navaza, P.Saludjian, R.Zemel, D.S.Tawfik, Z.Eshhar, B.S.Green, and M.Knossow (1994).
Crystal structure of a catalytic antibody Fab with esterase-like activity.
  Structure, 2, 175-183.
PDB code: 2gfb
  8026215 B.M.Conti-Tronconi, K.E.McLane, M.A.Raftery, S.A.Grando, and M.P.Protti (1994).
The nicotinic acetylcholine receptor: structure and autoimmune pathology.
  Crit Rev Biochem Mol Biol, 29, 69.  
7991597 D.I.Kreimer, R.Szosenfogel, D.Goldfarb, I.Silman, and L.Weiner (1994).
Two-state transition between molten globule and unfolded states of acetylcholinesterase as monitored by electron paramagnetic resonance spectroscopy.
  Proc Natl Acad Sci U S A, 91, 12145-12149.  
8001575 D.R.Gjellesvik, J.B.Lorens, and R.Male (1994).
Pancreatic carboxylester lipase from Atlantic salmon (Salmo salar). cDNA sequence and computer-assisted modelling of tertiary structure.
  Eur J Biochem, 226, 603-612.  
8161688 E.Perozo, L.Santacruz-Toloza, E.Stefani, F.Bezanilla, and D.M.Papazian (1994).
S4 mutations alter gating currents of Shaker K channels.
  Biophys J, 66, 345-354.  
7664081 H.J.Hecht, H.Sobek, T.Haag, O.Pfeifer, and K.H.van Pée (1994).
The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an alpha/beta hydrolase fold.
  Nat Struct Biol, 1, 532-537.
PDB code: 1bro
7972273 H.Kubinyi (1994).
[The key to the castle. II. Hansch analysis, 3d-QSAR and de novo design]
  Pharm Unserer Zeit, 23, 281-290.  
8168535 H.Le Moual, N.Dion, B.P.Roques, P.Crine, and G.Boileau (1994).
Asp650 is crucial for catalytic activity of neutral endopeptidase 24-11.
  Eur J Biochem, 221, 475-480.  
8087556 J.Uppenberg, M.T.Hansen, S.Patkar, and T.A.Jones (1994).
The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica.
  Structure, 2, 293-308.
PDB codes: 1tca 1tcb 1tcc
7946464 K.E.Jaeger, S.Ransac, B.W.Dijkstra, C.Colson, M.van Heuvel, and O.Misset (1994).
Bacterial lipases.
  FEMS Microbiol Rev, 15, 29-63.  
7881908 K.M.Fox, and P.A.Karplus (1994).
Old yellow enzyme at 2 A resolution: overall structure, ligand binding, and comparison with related flavoproteins.
  Structure, 2, 1089-1105.
PDB codes: 1oya 1oyb 1oyc
7937759 L.Brocchieri, and S.Karlin (1994).
Geometry of interplanar residue contacts in protein structures.
  Proc Natl Acad Sci U S A, 91, 9297-9301.  
7853361 M.S.Dehlawi, A.T.Eldefrawi, M.E.Eldefrawi, N.A.Anis, and J.J.Valdes (1994).
Choline derivatives and sodium fluoride protect acetylcholinesterase against irreversible inhibition and aging by DFP and paraoxon.
  J Biochem Toxicol, 9, 261-268.  
7925428 O.Jbilo, Y.L'Hermite, V.Talesa, J.P.Toutant, and A.Chatonnet (1994).
Acetylcholinesterase and butyrylcholinesterase expression in adult rabbit tissues and during development.
  Eur J Biochem, 225, 115-124.  
  8142901 P.Grochulski, Y.Li, J.D.Schrag, and M.Cygler (1994).
Two conformational states of Candida rugosa lipase.
  Protein Sci, 3, 82-91.
PDB code: 1trh
  8003956 P.H.Axelsen, M.Harel, I.Silman, and J.L.Sussman (1994).
Structure and dynamics of the active site gorge of acetylcholinesterase: synergistic use of molecular dynamics simulation and X-ray crystallography.
  Protein Sci, 3, 188-197.  
7712290 P.M.Colman (1994).
Structure-based drug design.
  Curr Opin Struct Biol, 4, 868-874.  
  8300539 R.G.Brok, E.Brinkman, R.van Boxtel, A.C.Bekkers, H.M.Verheij, and J.Tommassen (1994).
Molecular characterization of enterobacterial pldA genes encoding outer membrane phospholipase A.
  J Bacteriol, 176, 861-870.  
7765546 R.J.Kazlauskas (1994).
Elucidating structure-mechanism relationships in lipases: prospects for predicting and engineering catalytic properties.
  Trends Biotechnol, 12, 464-472.  
  7914789 U.H.Mortensen, and K.Breddam (1994).
A conserved glutamic acid bridge in serine carboxypeptidases, belonging to the alpha/beta hydrolase fold, acts as a pH-dependent protein-stabilizing element.
  Protein Sci, 3, 838-842.  
7969748 Y.Cho, S.H.Cha, and D.E.Sok (1994).
Differential inhibition of soluble and membrane-bound acetylcholinesterase forms from mouse brain by choline esters with an acyl moiety of an intermediate size.
  Neurochem Res, 19, 799-803.  
7738603 Y.P.Pang, and A.P.Kozikowski (1994).
Prediction of the binding sites of huperzine A in acetylcholinesterase by docking studies.
  J Comput Aided Mol Des, 8, 669-681.  
7738604 Y.P.Pang, and A.P.Kozikowski (1994).
Prediction of the binding site of 1-benzyl-4-[(5,6-dimethoxy-1-indanon-2-yl)methyl]piperidine in acetylcholinesterase by docking studies with the SYSDOC program.
  J Comput Aided Mol Des, 8, 683-693.
PDB codes: 3ace 4ace
8041797 Z.Shi, C.J.Buntel, and J.H.Griffin (1994).
Isolation and characterization of the gene encoding 2,3-oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae.
  Proc Natl Acad Sci U S A, 91, 7370-7374.  
7508983 A.Devillers-Thiéry, J.L.Galzi, J.L.Eiselé, S.Bertrand, D.Bertrand, and J.P.Changeux (1993).
Functional architecture of the nicotinic acetylcholine receptor: a prototype of ligand-gated ion channels.
  J Membr Biol, 136, 97.  
8369624 A.Karlin (1993).
Structure of nicotinic acetylcholine receptors.
  Curr Opin Neurobiol, 3, 299-309.  
8434007 A.L.Swain, M.Jaskólski, D.Housset, J.K.Rao, and A.Wlodawer (1993).
Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy.
  Proc Natl Acad Sci U S A, 90, 1474-1478.
PDB code: 3eca
8375401 A.Schrattenholz, J.Godovac-Zimmermann, H.J.Schäfer, E.X.Albuquerque, and A.Maelicke (1993).
Photoaffinity labeling of Torpedo acetylcholine receptor by physostigmine.
  Eur J Biochem, 216, 671-677.  
  8251933 A.W.Chan, E.G.Hutchinson, D.Harris, and J.M.Thornton (1993).
Identification, classification, and analysis of beta-bulges in proteins.
  Protein Sci, 2, 1574-1590.  
8327511 C.Czajkowski, C.Kaufmann, and A.Karlin (1993).
Negatively charged amino acid residues in the nicotinic receptor delta subunit that contribute to the binding of acetylcholine.
  Proc Natl Acad Sci U S A, 90, 6285-6289.  
  8488842 C.F.Bartels, T.Zelinski, and O.Lockridge (1993).
Mutation at codon 322 in the human acetylcholinesterase (ACHE) gene accounts for YT blood group polymorphism.
  Am J Hum Genet, 52, 928-936.  
8417155 C.Legay, S.Bon, P.Vernier, F.Coussen, and J.Massoulié (1993).
Cloning and expression of a rat acetylcholinesterase subunit: generation of multiple molecular forms and complementarity with a Torpedo collagenic subunit.
  J Neurochem, 60, 337-346.  
8473905 D.J.McCormick, J.A.Liebenow, G.E.Griesmann, and V.A.Lennon (1993).
Nine residues influence the binding of alpha-bungarotoxin in alpha-subunit region 185-200 of human muscle acetylcholine receptor.
  J Neurochem, 60, 1906-1914.  
8506359 D.R.Ripoll, C.H.Faerman, P.H.Axelsen, I.Silman, and J.L.Sussman (1993).
An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase.
  Proc Natl Acad Sci U S A, 90, 5128-5132.  
7680497 J.Deuchars, and A.M.Thomson (1993).
Synapses and receptors: a molecular perspective in honour of Professor E. A. Barnard.
  Trends Neurosci, 16, 43-46.  
8119594 J.G.Oakeshott, E.A.van Papenrecht, T.M.Boyce, M.J.Healy, and R.J.Russell (1993).
Evolutionary genetics of Drosophila esterases.
  Genetica, 90, 239-268.  
8369448 J.Gao, L.W.Chou, and A.Auerbach (1993).
The nature of cation-pi binding: interactions between tetramethylammonium ion and benzene in aqueous solution.
  Biophys J, 65, 43-47.  
8375665 J.Karotam, A.C.Delves, and J.G.Oakeshott (1993).
Conservation and change in structural and 5' flanking sequences of esterase 6 in sibling Drosophila species.
  Genetica, 88, 11-28.  
8321908 J.Massoulié, L.Pezzementi, S.Bon, E.Krejci, and F.M.Vallette (1993).
Molecular and cellular biology of cholinesterases.
  Prog Neurobiol, 41, 31-91.  
8457664 K.A.McGroddy, A.A.Carter, M.M.Tubbert, and R.E.Oswald (1993).
Analysis of cyclic and acyclic nicotinic cholinergic agonists using radioligand binding, single channel recording, and nuclear magnetic resonance spectroscopy.
  Biophys J, 64, 325-338.  
8441756 K.K.Kim, K.Y.Hwang, K.D.Choi, J.H.Kang, O.J.Yoo, and S.W.Suh (1993).
Crystallization and preliminary X-ray crystallographic analysis of arylesterase from Pseudomonas fluorescens.
  Proteins, 15, 213-215.  
8415624 L.Izadyar, A.Friboulet, M.H.Remy, A.Roseto, and D.Thomas (1993).
Monoclonal anti-idiotypic antibodies as functional internal images of enzyme active sites: production of a catalytic antibody with a cholinesterase activity.
  Proc Natl Acad Sci U S A, 90, 8876-8880.  
7504082 L.Wasserman, B.P.Doctor, M.K.Gentry, and P.Taylor (1993).
Epitope mapping of form-specific and nonspecific antibodies to acetylcholinesterase.
  J Neurochem, 61, 2124-2132.  
8302294 L.Y.Zang, and H.P.Misra (1993).
Acetylcholinesterase inhibition by 1-methyl-4-phenylpyridinium ion, a bioactivated metabolite of MPTP.
  Mol Cell Biochem, 126, 93.  
8274134 M.A.Myers, M.J.Healy, and J.G.Oakeshott (1993).
Effects of the residue adjacent to the reactive serine on the substrate interactions of Drosophila esterase 6.
  Biochem Genet, 31, 259-278.  
7504273 M.Balass, Y.Heldman, S.Cabilly, D.Givol, E.Katchalski-Katzir, and S.Fuchs (1993).
Identification of a hexapeptide that mimics a conformation-dependent binding site of acetylcholine receptor by use of a phage-epitope library.
  Proc Natl Acad Sci U S A, 90, 10638-10642.  
  8453375 M.Cygler, J.D.Schrag, J.L.Sussman, M.Harel, I.Silman, M.K.Gentry, and B.P.Doctor (1993).
Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins.
  Protein Sci, 2, 366-382.  
8095116 M.F.Hibert, S.Trumpp-Kallmeyer, J.Hoflack, and A.Bruinvels (1993).
This is not a G protein-coupled receptor.
  Trends Pharmacol Sci, 14, 7.  
8458061 M.Fischer, A.Ittah, I.Liefer, and M.Gorecki (1993).
Expression and reconstitution of biologically active human acetylcholinesterase from Escherichia coli.
  Cell Mol Neurobiol, 13, 25-38.  
8415649 M.Harel, I.Schalk, L.Ehret-Sabatier, F.Bouet, M.Goeldner, C.Hirth, P.H.Axelsen, I.Silman, and J.L.Sussman (1993).
Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase.
  Proc Natl Acad Sci U S A, 90, 9031-9035.
PDB codes: 1acj 1ack 1acl
15335777 M.S.Sansom (1993).
Acetylcholine receptors: peering down a pore.
  Curr Biol, 3, 240-241.  
7679054 N.Unwin (1993).
Neurotransmitter action: opening of ligand-gated ion channels.
  Cell, 72, 31-41.  
8103422 P.G.Layer, T.Weikert, and R.Alber (1993).
Cholinesterases regulate neurite growth of chick nerve cells in vitro by means of a non-enzymatic mechanism.
  Cell Tissue Res, 273, 219-226.  
8224790 R.N.Alon, and D.L.Gutnick (1993).
Esterase from the oil-degrading Acinetobacter lwoffii RAG-1: sequence analysis and over-expression in Escherichia coli.
  FEMS Microbiol Lett, 112, 275-280.  
8427627 R.V.Rao, and A.S.Balasubramanian (1993).
The peptidase activity of human serum butyrylcholinesterase: studies using monoclonal antibodies and characterization of the peptidase.
  J Protein Chem, 12, 103-110.  
7763978 S.J.Remington (1993).
Serine carboxypeptidases: a new and versatile family of enzymes.
  Curr Opin Biotechnol, 4, 462-468.  
8136015 S.K.Burgess, and S.L.Oxendine (1993).
Thermal inactivation of butyrylcholinesterase and acetylcholinesterase.
  J Protein Chem, 12, 651-658.  
8415719 S.M.Sine (1993).
Molecular dissection of subunit interfaces in the acetylcholine receptor: identification of residues that determine curare selectivity.
  Proc Natl Acad Sci U S A, 90, 9436-9440.  
8389298 U.Görne-Tschelnokow, D.Naumann, C.Weise, and F.Hucho (1993).
Secondary structure and temperature behaviour of acetylcholinesterase. Studies by Fourier-transform infrared spectroscopy.
  Eur J Biochem, 213, 1235-1242.  
8438232 Z.S.Derewenda, and A.M.Sharp (1993).
News from the interface: the molecular structures of triacylglyceride lipases.
  Trends Biochem Sci, 18, 20-25.  
  1396557 A.Shafferman, B.Velan, A.Ordentlich, C.Kronman, H.Grosfeld, M.Leitner, Y.Flashner, S.Cohen, D.Barak, and N.Ariel (1992).
Substrate inhibition of acetylcholinesterase: residues affecting signal transduction from the surface to the catalytic center.
  EMBO J, 11, 3561-3568.  
  1415224 C.P.Nogueira, C.F.Bartels, M.C.McGuire, S.Adkins, T.Lubrano, H.M.Rubinstein, H.Lightstone, A.F.Van der Spek, O.Lockridge, and B.N.La Du (1992).
Identification of two different point mutations associated with the fluoride-resistant phenotype for human butyrylcholinesterase.
  Am J Hum Genet, 51, 821-828.  
1380164 D.Barchan, S.Kachalsky, D.Neumann, Z.Vogel, M.Ovadia, E.Kochva, and S.Fuchs (1992).
How the mongoose can fight the snake: the binding site of the mongoose acetylcholine receptor.
  Proc Natl Acad Sci U S A, 89, 7717-7721.  
  1304887 E.Meyer (1992).
Internal water molecules and H-bonding in biological macromolecules: a review of structural features with functional implications.
  Protein Sci, 1, 1543-1562.  
1412713 H.Soreq, A.Gnatt, Y.Loewenstein, and L.F.Neville (1992).
Excavations into the active-site gorge of cholinesterases.
  Trends Biochem Sci, 17, 353-358.  
1384213 J.P.Changeux, A.Devillers-Thiéry, J.L.Galzi, and D.Bertrand (1992).
New mutants to explore nicotinic receptor functions.
  Trends Pharmacol Sci, 13, 299-301.  
1293635 J.P.Changeux, J.L.Galzi, A.Devillers-Thiéry, and D.Bertrand (1992).
The functional architecture of the acetylcholine nicotinic receptor explored by affinity labelling and site-directed mutagenesis.
  Q Rev Biophys, 25, 395-432.  
1735432 L.Ehret-Sabatier, I.Schalk, M.Goeldner, and C.Hirth (1992).
Photoaffinity labelling of cholinesterases. Discrimination between active and peripheral sites.
  Eur J Biochem, 203, 475-481.  
  1373381 L.F.Neville, A.Gnatt, Y.Loewenstein, S.Seidman, G.Ehrlich, and H.Soreq (1992).
Intramolecular relationships in cholinesterases revealed by oocyte expression of site-directed and natural variants of human BCHE.
  EMBO J, 11, 1641-1649.  
1550673 L.Heginbotham, and R.MacKinnon (1992).
The aromatic binding site for tetraethylammonium ion on potassium channels.
  Neuron, 8, 483-491.  
1397329 L.Polgár (1992).
Structural relationship between lipases and peptidases of the prolyl oligopeptidase family.
  FEBS Lett, 311, 281-284.  
1438284 M.Harel, J.L.Sussman, E.Krejci, S.Bon, P.Chanal, J.Massoulié, and I.Silman (1992).
Conversion of acetylcholinesterase to butyrylcholinesterase: modeling and mutagenesis.
  Proc Natl Acad Sci U S A, 89, 10827-10831.  
1529103 P.T.Francis, M.N.Pangalos, and D.M.Bowen (1992).
Animal and drug modelling for Alzheimer synaptic pathology.
  Prog Neurobiol, 39, 517-545.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.