Molecular and cellular biology of cholinesterases

A new and rapid colorimetric determination of acetylcholinesterase activity

Ellman, G. L., Courtney, K. D., Andres, V., & Featherstone, R. M. (1961) · Biochemical Pharmacology · doi:10.1016/0006-2952(61)90145-9 · Cited by 27,221 · see citing works

A "DIRECT-COLORING" THIOCHOLINE METHOD FOR CHOLINESTERASES

Karnovsky, M. J., & ROOTS, L. (1964) · Journal of Histochemistry & Cytochemistry · doi:10.1177/12.3.219 · Cited by 3,389 · see citing works

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

Sussman, J. L., Harel, M., Frolow, F., Oefner, C., Goldman, A., Toker, L., & Silman, I. (1991) · Science · doi:10.1126/science.1678899 · Cited by 2,711 · see citing works

Solubilization of membranes by detergents.

Helenius, A., & Simons, K. (1975) · Biochimica et Biophysica Acta · doi:10.1016/0304-4157(75)90016-7 · Cited by 2,690 · see citing works

The α / β hydrolase fold

Ollis, D. L., Cheah, E., Cygler, M., Dijkstra, B. W., Frolow, F., Franken, S. M., Harel, M., Remington, S. J., Silman, I., Schrag, J. D., et al. (1992) · Protein Engineering Design and Selection · doi:10.1093/protein/5.3.197 · Cited by 2,110 · see citing works

Progress in Clinical and Biological Research

Smyth, J. F. (1979) · Journal of Clinical Pathology · doi:10.1136/jcp.32.7.742-d · Cited by 1,558 · see citing works

CELL-SURFACE ANCHORING OF PROTEINS VIA GLYCOSYL-PHOSPHATIDYLINOSITOL STRUCTURES

Ferguson, M. A. J., & Williams, A. F. (1988) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.57.070188.001441 · Cited by 1,290 · see citing works

Structure of human pancreatic lipase

Winkler, F. K., D'Arcy, A., & Hunziker, W. H. (1990) · Nature · doi:10.1038/343771a0 · Cited by 1,227 · see citing works

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 · see citing works

A Histochemical Method for Localizing Cholinesterase Activity.

Koelle, G. B., & Friedenwald, J. S. (1949) · Experimental Biology and Medicine · doi:10.3181/00379727-70-17013 · Cited by 1,192 · see citing works

The Molecular Basis of Muscular Dystrophy in the <i>mdx</i> Mouse: a Point Mutation

Sicinski, P., Geng, Y., Ryder-Cook, A. S., Barnard, E. A., Darlison, M. G., & Barnard, P. J. (1989) · Science · doi:10.1126/science.2662404 · Cited by 1,086 · see citing works

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

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

The biology of cholinesterases

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

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 · see citing works

Neurotransmitter regulation of neuronal outgrowth, plasticity and survival

Lipton, S. A., & Kater, S. B. (1989) · Trends in Neurosciences · doi:10.1016/0166-2236(89)90026-x · Cited by 724 · see citing works

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 · see citing works

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

Johnson, C. D., & Russell, R. L. (1975) · Analytical Biochemistry · doi:10.1016/0003-2697(75)90423-6 · Cited by 689 · see citing works

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

Dale, H. H. (1914) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)08268-0 · Cited by 658 · see citing works

Dissecting the catalytic triad of a serine protease

Carter, P. M., & Wells, J. A. (1988) · Nature · doi:10.1038/332564a0 · Cited by 652 · see citing works

Acetylcholine Binding by a Synthetic Receptor: Implications for Biological Recognition

Dougherty, D. A., & Stauffer, D. A. (1990) · Science · doi:10.1126/science.2274786 · Cited by 625 · see citing works

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

Kruse, J., Keilhauer, G., Faissner, A., Timpl, R., & Schachner, M. (1985) · Nature · doi:10.1038/316146a0 · Cited by 584 · see citing works

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

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

Comparison of butyrylcholinesterase and acetylcholinesterase

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

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

Herkenham, M. A., & Pert, C. B. (1981) · Nature · doi:10.1038/291415a0 · Cited by 544 · see citing works

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

Schrag, J. D., Li, Y., Wu, S., & Cygler, M. (1991) · Nature · doi:10.1038/351761a0 · Cited by 534 · see citing works

The glycosyl-phosphatidylinositol anchor of membrane proteins

Low, M. G. (1989) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(89)90014-2 · Cited by 521 · see citing works

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 · see citing works

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 · see citing works

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

Nitkin, R. M., Smith, M. A., Magill, C., Fallon, J. R., Yao, Y. M., Wallace, B. G., & McMahan, U. J. (1987) · The Journal of cell biology · doi:10.1083/jcb.105.6.2471 · Cited by 469 · see citing works

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

Glomset, J. A., Gelb, M. H., & Farnsworth, C. C. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90213-u · Cited by 468 · see citing works

Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence

Schumacher, M. A., Camp, S., Maulet, Y., Newton, M., MacPhee-Quigley, K., Taylor, S. S., Friedmann, T., & Taylor, P. (1986) · Nature · doi:10.1038/319407a0 · Cited by 430 · see citing works

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

Dotti, C. G., & Simons, K. (1990) · Cell · doi:10.1016/0092-8674(90)90240-f · Cited by 427 · see citing works

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

Han, J. H., Stratowa, C., & Rutter, W. J. (1987) · Biochemistry · doi:10.1021/bi00380a020 · Cited by 427 · see citing works

Cholinesterase is associated with the basal lamina at the neuromuscular junction

McMahan, U. J., Sanes, J. R., & Marshall, L. M. (1978) · Nature · doi:10.1038/271172a0 · Cited by 400 · see citing works

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 · see citing works

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

Grumet, M., Hoffman, S., Crossin, K. L., & Edelman, G. M. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.23.8075 · Cited by 391 · see citing works

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 · see citing works

Enzyme inhibitors as substrates

O'Brien, R. D. (1974) · Pesticide Biochemistry and Physiology · doi:10.1016/0048-3575(74)90106-0 · Cited by 347 · see citing works

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 · see citing works

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 · see citing works

Two selective inhibitors of cholinesterase

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

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Cholinesterase in embryonic development.

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

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 · see citing works

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 · see citing works

Enzymatic Detachment of Endplate Acetylcholinesterase from Muscle

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

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 · see citing works

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 · see citing works

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 · see citing works

Polarized sorting of glypiated proteins in hippocampal neurons

Dotti, C. G., Parton, R. G., & Simons, K. (1991) · Nature · doi:10.1038/349158a0 · Cited by 230 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 210 · see citing works

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 · see citing works

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 204 · see citing works

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 · see citing works

Fatty acylated proteins as components of intracellular signaling pathways

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

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 · see citing works

Cholinesterase in Embronic Development

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

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 188 · see citing works

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 185 · see citing works

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 · see citing works

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 183 · see citing works

The cholinesterases

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

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 · see citing works

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 170 · see citing works

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 · see citing works

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 165 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Neural induction of the 16S acetylcholinesterase in muscle cell cultures

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

Hydrolysis of diacetylmorphine (heroin) by human serum cholinesterase.

Lockridge, O., Mottershaw-Jackson, N., Eckerson, H. W., & Du, B. N. L. (1980) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)32246-9 · Cited by 146 · see citing works

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 · see citing works

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

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Cholinesterase activity as potential biomarker in two bivalves

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Molecular Dynamics of Acetylcholinesterase

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tanandebonyGenes Regulate a Novel Pathway for Transmitter Metabolism at Fly Photoreceptor Terminals

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