Molecular and cellular biology of cholinesterases

A new and rapid colorimetric determination of acetylcholinesterase activity

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A "DIRECT-COLORING" THIOCHOLINE METHOD FOR CHOLINESTERASES

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Atomic Structure of Acetylcholinesterase from Torpedo californica : A Prototypic Acetylcholine-Binding Protein

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The α / β hydrolase fold

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Progress in Clinical and Biological Research

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CELL-SURFACE ANCHORING OF PROTEINS VIA GLYCOSYL-PHOSPHATIDYLINOSITOL STRUCTURES

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The Molecular Basis of Muscular Dystrophy in the mdx Mouse: a Point Mutation

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Structure of human pancreatic lipase

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A serine protease triad forms the catalytic centre of a triacylglycerol lipase

Brady, L., Brzozowski, A. M., Derewenda, Z. S., Dodson, E. J., Dodson, G. G., Tolley, S. P., Turkenburg, J. P., Christiansen, L., Huge‐Jensen, B., Nørskov, L., et al. (1990) · Nature · doi:10.1038/343767a0 · Cited by 1,219

A Histochemical Method for Localizing Cholinesterase Activity.

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Acetylcholinesterase: Enzyme structure, reaction dynamics, and virtual transition states

Quinn, D. M. (1987) · Chemical Reviews · doi:10.1021/cr00081a005 · Cited by 1,072

The biology of cholinesterases

Silver, A. (1974) · Medical Entomology and Zoology · Cited by 890

The Molecular Forms of Cholinesterase and Acetylcholinesterase in Vertebrates

Massoulié, J., & Bon, S. (1982) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.05.030182.000421 · Cited by 818

Neurotransmitter regulation of neuronal outgrowth, plasticity and survival

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Enzyme immunoassays of eicosanoids using acetylcholine esterase as label: an alternative to radioimmunoassay

Pradelles, P., Grassi, J. J., & Maclouf, J. (1985) · Analytical Chemistry · doi:10.1021/ac00284a003 · Cited by 706

A rapid, simple radiometric assay for cholinesterase, suitable for multiple determinations

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THE ACTION OF CERTAIN ESTERS AND ETHERS OF CHOLINE, AND THEIR RELATION TO MUSCARINE

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Dissecting the catalytic triad of a serine protease

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Acetylcholine Binding by a Synthetic Receptor: Implications for Biological Recognition

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The J1 glycoprotein—a novel nervous system cell adhesion molecule of the L2/HNK-1 family

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The molecular evolution of genes and proteins: a tale of two serines

Brenner, S. (1988) · Nature · doi:10.1038/334528a0 · Cited by 551

Comparison of butyrylcholinesterase and acetylcholinesterase

Chatonnet, A., & Lockridge, O. (1989) · Biochemical Journal · doi:10.1042/bj2600625 · Cited by 550

Mosaic distribution of opiate receptors, parafascicular projections and acetylcholinesterase in rat striatum

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Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum

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The glycosyl-phosphatidylinositol anchor of membrane proteins

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Multiple forms of acetylcholinesterase and their distribution in endplate and non‐endplate regions of rat diaphragm muscle

Hall, Z. W. (1973) · Journal of Neurobiology · doi:10.1002/neu.480040404 · Cited by 508

Differential inhibition of neurone–neurone, neurone–astrocyte and astrocyte–astrocyte adhesion by L1, L2 and N-CAM antibodies

Keilhauer, G., Faissner, A., & Schachner, M. (1985) · Nature · doi:10.1038/316728a0 · Cited by 494

Identification of agrin, a synaptic organizing protein from Torpedo electric organ.

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Prenyl proteins in eukaryotic cells: a new type of membrane anchor

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Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence

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Polarized sorting of viral glycoproteins to the axon and dendrites of hippocampal neurons in culture

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Isolation of full-length putative rat lysophospholipase cDNA using improved methods for mRNA isolation and cDNA cloning

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Cholinesterase is associated with the basal lamina at the neuromuscular junction

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An immunohistochemical study of enkephalins and other neuropeptides in the striatum of the cat with evidence that the opiate peptides are arranged to form mosaic patterns in register with the striosomal compartments visible by acetylcholinesterase staining

Graybiel, A. M., Ragsdale, C. W., Yoneoka, E. S., & Elde, R. P. (1981) · Neuroscience · doi:10.1016/0306-4522(81)90131-7 · Cited by 396

Cytotactin, an extracellular matrix protein of neural and non-neural tissues that mediates glia-neuron interaction.

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Complete amino acid sequence of human serum cholinesterase.

Lockridge, O., Bartels, C. F., Vaughan, T. A., Wong, C. K., Norton, S., & Johnson, L. L. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75818-9 · Cited by 376

Enzyme inhibitors as substrates

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Primary structure of human thyroglobulin deduced from the sequence of its 8448-base complementary DNA

Malthièry, Y., & Lissitzky, S. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb11466.x · Cited by 329

Responses of Acetylcholinesterase from Torpedo marmorata to Salts and Curarizing Drugs

Changeux, J. (1966) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)14802-5 · Cited by 327

Two selective inhibitors of cholinesterase

Austin, L., & Berry, W. K. (1953) · Biochemical Journal · doi:10.1042/bj0540695 · Cited by 320

Human transferrin: cDNA characterization and chromosomal localization.

Yang, F., Lum, J. B., McGill, J. R., Moore, C. M., Naylor, S. L., van Bragt, P. H., Baldwin, W. D., & Bowman, B. H. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.9.2752 · Cited by 314

Changes in acetylcholinesterase and butyrylcholinesterase in Alzheimer’s disease resemble embryonic development—A study of molecular forms

Arendt, T., Brückner, M. K., Lange, M., & Bigl, V. (1992) · Neurochemistry International · doi:10.1016/0197-0186(92)90189-x · Cited by 314

Amino acid residues controlling acetylcholinesterase and butyrylcholinesterase specificity

Vellom, D. C., Radić, Z., Li, Y., Pickering, N. A., Camp, S., & Taylor, P. (1993) · Biochemistry · doi:10.1021/bi00052a003 · Cited by 314

Structure and expression of a rat agrin

Rupp, F., Payan, D. G., Magill, C., Cowan, D. M., & Scheller, R. H. (1991) · Neuron · doi:10.1016/0896-6273(91)90177-2 · Cited by 306

Conversion of acetylcholinesterase to butyrylcholinesterase: modeling and mutagenesis.

Harel, M., Sussman, J. L., Krejci, É., Bon, S., Chanal, P., Massoulié, J., & Silman, I. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.22.10827 · Cited by 291

Decay accelerating factor of complement is anchored to cells by a C-terminal glycolipid

Medof, M. E., Walter, E. I., Roberts, W. L., Haas, R., & Rosenberry, T. L. (1986) · Biochemistry · doi:10.1021/bi00370a003 · Cited by 285

Structural characterization of the glycoinositol phospholipid membrane anchor of human erythrocyte acetylcholinesterase by fast atom bombardment mass spectrometry.

Roberts, W. L., Santikarn, S., Reinhold, V. N., & Rosenberry, T. L. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37350-2 · Cited by 281

Primary structure of bovine thyroglobulin deduced from the sequence of its 8,431-base complementary DNA

Mercken, L., Simons, M.-J., Swillens, S., Massaer, M., & Vassart, G. (1985) · Nature · doi:10.1038/316647a0 · Cited by 273

Glycosyl‐phosphatidylinositol: a versatile anchor for cell surface proteins 1

Low, M. G. (1989) · The FASEB Journal · doi:10.1096/fasebj.3.5.2522071 · Cited by 267

The Ace locus of Drosophila melanogaster: structural gene for acetylcholinesterase with an unusual 5′ leader.

Hall, L. M. C., & Spierer, P. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04591.x · Cited by 265

Segment‐related, mosaic neurogenetic pattern in the forebrain and mesencephalon of early chick embryos: I. Topography of ache‐positive neuroblasts up to stage HH18

Puelles, L., Amat, J., & Martinez-de-la-Torre, M. (1987) · The Journal of Comparative Neurology · doi:10.1002/cne.902660210 · Cited by 264

Cholinesterase in embryonic development.

Drews, U. (1975) · PubMed · Cited by 263

Myogenic differentiation in permanent clonal mouse myoblast cell lines: Regulation by macromolecular growth factors in the culture medium

Linkhart, T. A., Clegg, C. H., & Hauschka, S. D. (1981) · Developmental Biology · doi:10.1016/0012-1606(81)90311-0 · Cited by 256

The agrin gene codes for a family of basal lamina proteins that differ in function and distribution

Rüegg, M. A., Tsim, K. W. K., Horton, S. E., Kröger, S., Escher, G., Gensch, E. M., & McMahan, U. J. (1992) · Neuron · doi:10.1016/0896-6273(92)90090-z · Cited by 254

Enzymatic Detachment of Endplate Acetylcholinesterase from Muscle

Hall, Z. W., & Kelly, R. B. (1971) · Nature New Biology · doi:10.1038/newbio232062a0 · Cited by 249

Acetylcholinesterase

Rosenberry, T. L. (1975) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122884.ch3 · Cited by 249

THE MOTOR END‐PLATE SPECIFIC FORM OF ACETYLCHOLINESTERASE: APPEARANCE DURING EMBRYOGENESIS AND RE‐INNERVATION OF RAT MUSCLE

Vigny, M., Koenig, J., & Rieger, F. (1976) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1976.tb02614.x · Cited by 243

A new myasthenic syndrome with end‐plate acetylcholinesterase deficiency, small nerve terminals, and reduced acetylcholine release

Engel, A. G., Lambert, E. H., & Gómez, M. R. (1977) · Annals of Neurology · doi:10.1002/ana.410010403 · Cited by 238

Polarized sorting of glypiated proteins in hippocampal neurons

Dotti, C. G., Parton, R. G., & Simons, K. (1991) · Nature · doi:10.1038/349158a0 · Cited by 231

Biosynthesis of Trypanosoma brucei variant surface glycoproteins. N-glycosylation and addition of a phosphatidylinositol membrane anchor.

Ferguson, M. A. J., Duszenko, M., Lamont, G., Overath, P., & Cross, G. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42479-3 · Cited by 227

Substrate inhibition of acetylcholinesterase: residues affecting signal transduction from the surface to the catalytic center.

Avigdor Shafferman, C., Velan, B., Ordentlich, A., Kronman, C., Grosfeld, H., Leitner, M., Flashner, Y., Cohen, S., Barak, D., & Ariel, N. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05439.x · Cited by 222

Acetylcholinesterase. Two types of modifications confer resistance to insecticide.

Fournier, D. D., Bride, J. M., Hoffmann, F., & Karch, F. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49708-1 · Cited by 221

Insect acetylcholinesterase: Catalytic properties, tissue distribution and molecular forms

Toutant, J.-P. (1989) · Progress in Neurobiology · doi:10.1016/0301-0082(89)90031-2 · Cited by 221

Acetylcholinesterase may have novel functions in the brain

Greenfield, S. A. (1984) · Trends in Neurosciences · doi:10.1016/s0166-2236(84)80055-7 · Cited by 216

Molecular forms of acetylcholinesterase in senile dementia of Alzheimer type: Selective loss of the intermediate (10S) form

Atack, J. R., Perry, E. K., Bonham, J. R., Perry, R. H., Tomlinson, B. E., Blessed, G., & FAIRBAIRN, A. F. (1983) · Neuroscience Letters · doi:10.1016/0304-3940(83)90302-6 · Cited by 211

Molecular cloning and construction of the coding region for human acetylcholinesterase reveals a G + C-rich attenuating structure.

Soreq, H., Ben-Aziz, R., Prody, C. A., Seidman, S., Gnatt, A. L., Neville, L., Lieman‐Hurwitz, J., Lev-Lehman, E., Ginzberg, D., & Lapidot-Lifson, Y. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.24.9688 · Cited by 208

Crystal structure of haloalkane dehalogenase: an enzyme to detoxify halogenated alkanes.

Franken, S. M., Rozeboom, H. J., Kalk, K. H., & Dijkstra, B. W. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07647.x · Cited by 206

DNA mutation associated with the human butyrylcholinesterase K-variant and its linkage to the atypical variant mutation and other polymorphic sites.

Bartels, C. F., Jensen, F. S., Lockridge, O., van der Spek, A. F., Rubinstein, H. M., LUBRANO, T., & Du, B. N. L. (1992) · PubMed · Cited by 203

Fatty acylated proteins as components of intracellular signaling pathways

James, G. L., & Olson, E. N. (1990) · Biochemistry · doi:10.1021/bi00463a001 · Cited by 203

cDNA that encodes active agrin

Tsim, K. W. K., Rüegg, M. A., Escher, G., Kröger, S., & McMahan, U. J. (1992) · Neuron · doi:10.1016/0896-6273(92)90089-v · Cited by 200

Cholinesterase in Embronic Development

Drews, U. (1975) · Progress in Histochemistry and Cytochemistry · doi:10.1016/s0079-6336(75)80008-8 · Cited by 197

Molecular forms of acetylcholinesterase in brain, nerve and muscle: Nature, localization and dynamics

Brimijoin, S. (1983) · Progress in Neurobiology · doi:10.1016/0301-0082(83)90015-1 · Cited by 196

Non‐lytic release of acetylcholinesterase from erythrocytes by A phosphatidylinositol‐specific phospholipase C

Low, M. G., & FINEAN, J. B. (1977) · FEBS Letters · doi:10.1016/0014-5793(77)80905-8 · Cited by 193

Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding.

Avigdor Shafferman, C., Kronman, C., Flashner, Y., Leitner, M., Grosfeld, H., Ordentlich, A., Gozes, Y., Cohen, S., Ariel, N., & Barak, D. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)37091-7 · Cited by 192

Primary sequence of a motor neuron-selective adhesive site in the synaptic basal lamina protein s-laminin

Hunter, D. D., Porter, B. E., Bulock, J. W., Adams, S. P., Merlie, J. P., & Sanes, J. R. (1989) · Cell · doi:10.1016/0092-8674(89)90613-2 · Cited by 192

Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligands

Nolte, H.-J., Rosenberry, T. L., & Neumann, E. (1980) · Biochemistry · doi:10.1021/bi00557a011 · Cited by 190

Segmental pattern of development of the hindbrain and spinal cord of the zebrafish embryo

Hanneman, E. H., Trevarrow, B., Metcalfe, W. K., Kimmel, C. B., & Westerfield, M. (1988) · Development · doi:10.1242/dev.103.1.49 · Cited by 187

Identification of the structural mutation responsible for the dibucaine-resistant (atypical) variant form of human serum cholinesterase.

McGuire, M. C., Nogueira, C. P., Bartels, C. F., Lightstone, H., Hajra, A. K., van der Spek, A. F., Lockridge, O., & Du, B. N. L. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.3.953 · Cited by 186

Acetylcholinesterase from bovine caudate nucleus is attached to membranes by a novel subunit distinct from those of acetylcholinesterases in other tissues.

Inestrosa, N. C., Roberts, W. L., Marshall, T. L., & Rosenberry, T. L. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61212-8 · Cited by 183

Modes of attachment of acetylcholinesterase to the surface membrane

Silman, I., & Futerman, A. H. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb13662.x · Cited by 181

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Taylor, P. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64277-6 · Cited by 176

Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues.

Prody, C. A., Zevin‐Sonkin, D., Gnatt, A. L., Goldberg, O., & Soreq, H. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.11.3555 · Cited by 172

Molecular cloning of mouse acetylcholinesterase: Tissue distribution of alternatively spliced mRNA species

Rachinsky, T. L., Camp, S., Li, Y., Ekström, T. J., Newton, M., & Taylor, P. (1990) · Neuron · doi:10.1016/0896-6273(90)90168-f · Cited by 171

Cellular localization of the molecular forms of acetylcholinesterase in rat diaphragm.

Younkin, S. G., Rosenstein, C., Collins, P. L., & Rosenberry, T. L. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33494-x · Cited by 166

Agrin-induced specializations contain cytoplasmic, membrane, and extracellular matrix-associated components of the postsynaptic apparatus

Wallace, B. (1989) · Journal of Neuroscience · doi:10.1523/jneurosci.09-04-01294.1989 · Cited by 163

Acetylcholinesterase mutants in drosophila and their effects on the structure and function of the cental nervous system

Greenspan, R. J., Finn, J. A., & Hall, J. C. (1980) · The Journal of Comparative Neurology · doi:10.1002/cne.901890409 · Cited by 163

Role of the peripheral anionic site on acetylcholinesterase: inhibition by substrates and coumarin derivatives.

Radić, Z., Reiner, E., & Taylor, P. (1991) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10932-2 · Cited by 160

Minnesota multiphasic personality inventory-rated depression and the incidence of breast cancer

Hahn, R. C., & Petitti, D. B. (1988) · Cancer · doi:10.1002/1097-0142(19880215)61:4 · Cited by 157

Enzyme immunoassays of adenosine cyclic 3',5'-monophosphate and guanosine cyclic 3',5'-monophosphate using acetylcholinesterase

Pradelles, P., Grassi, J. J., Chabardès, D., & Guiso, N. (1989) · Analytical Chemistry · doi:10.1021/ac00180a014 · Cited by 154

A noncholinergic action of acetylcholinesterase (AChE) in the brain: From neuronal secretion to the generation of movement

Greenfield, S. A. (1991) · Cellular and Molecular Neurobiology · doi:10.1007/bf00712800 · Cited by 152

Regulation of acetylcholinesterase appearance at neuromuscular junctions in vitro

Rubin, L. L., Schuetze, S. M., Weill, C. L., & Fischbach, G. D. (1980) · Nature · doi:10.1038/283264a0 · Cited by 152

Anchorage of collagen-tailed acetylcholinesterase to the extracellular matrix is mediated by heparan sulfate proteoglycans.

Brandan, E., Maldonado, M., Garrido, J., & Inestrosa, N. C. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.3.985 · Cited by 152

A morphogenic role for transiently expressed acetylcholinesterase in developing thalamocortical systems?

Robertson, R. T. (1987) · Neuroscience Letters · doi:10.1016/0304-3940(87)90531-3 · Cited by 147

Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid.

Krejci, É., Duval, N., Chatonnet, A., Vincens, P., & Massoulié, J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.15.6647 · Cited by 147

Neural induction of the 16S acetylcholinesterase in muscle cell cultures

Koenig, J., & Vigny, M. (1978) · Nature · doi:10.1038/271075a0 · Cited by 146

Hydrolysis of diacetylmorphine (heroin) by human serum cholinesterase.

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Complex alternative splicing of acetylcholinesterase transcripts in Torpedo electric organ; primary structure of the precursor of the glycolipid‐anchored dimeric form.

Sikorav, J., Duval, N., Anselmet, A., Bon, S., Krejci, É., Legay, C., Osterlund, M., Reimund, B., & Massoulié, J. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03161.x · Cited by 145

Comparative localization of acetylcholinesterase and pseudocholinesterase during morphogenesis of the chicken brain.

Layer, P. G. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.20.6413 · Cited by 145

Distribution of the molecular forms of acetylcholinesterase in human brain: Alterations in dementia of the Alzheimer type

Fishman, E. B., Siek, G. C., MacCallum, R. D., Bird, E. D., Volicer, L., & Marquis, J. K. (1986) · Annals of Neurology · doi:10.1002/ana.410190305 · Cited by 145

Characterization of amplification core and esterase B1 gene responsible for insecticide resistance in Culex.

Mouchès, C., Pauplin, Y., Agarwal, M., Lemieux, L., Herzog, M., Abadon, M., Beyssat-Arnaouty, V., Hyrien, O., Vincent, B. R. D. S., & Georghiou, G. P. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.7.2574 · Cited by 144

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Primary structure of a collagenic tail peptide of Torpedo acetylcholinesterase: co‐expression with catalytic subunit induces the production of collagen‐tailed forms in transfected cells.

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