Molecular and cellular biology of cholinesterases

Amphiphilic and Nonamphiphilic Forms of Torpedo Cholinesterases: II. Electrophoretic Variants and Phosphatidylinositol Phospholipase C‐Sensitive and ‐Insensitive Forms

Bon, S., Toutant, J., Méflah, K., & Massoulié, J. (1988) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1988.tb01813.x · Cited by 70

The acetycholinesterase gene ofAnopheles stephensi

Hall, L. M. C., & Malcolm, C. A. (1991) · Cellular and Molecular Neurobiology · doi:10.1007/bf00712805 · Cited by 70

Identification of a frameshift mutation responsible for the silent phenotype of human serum cholinesterase, Gly 117 (GGT----GGAG).

Nogueira, C. P., McGuire, M. C., Graeser, C., Bartels, C. F., Arpagaus, M., van der Spek, A. F., Lightstone, H., Lockridge, O., & Du, B. N. L. (1990) · PubMed · Cited by 69

Presence of a Membrane‐Bound Acetylcholinesterase Form in a Preparation of Nerve Endings from Torpedo marmorata Electric Organ

Li, Z., & Bon, C. (1983) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1983.tb11288.x · Cited by 69

Molecular analysis of duplicated esterase genes in Drosophila melanogaster.

Collet, C., Nielsen, K. M., Russell, R. J., Karl, M., Oakeshott, J. G., & Richmond, R. C. (1990) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a040582 · Cited by 68

The Identity of the Serotonin‐Sensitive Aryl Acylamidase with Acetylcholinesterase from Human Erythrocytes, Sheep Basal Ganglia and Electric Eel

George, S. T., & Balasubramanian, A. S. (1980) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb04967.x · Cited by 67

THE SUBUNIT STRUCTURE OF MAMMALIAN ACETYLCHOLINESTERASE: CATALYTIC SUBUNITS, DISSOCIATING EFFECT OF PROTEOLYSIS AND DISULPHIDE REDUCTION ON THE POLYMERIC FORMS

Vigny, M., Bon, S., Massoulié, J., & Gisiger, V. (1979) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1979.tb05188.x · Cited by 66

Acetylcholinesterase forms in fast and slow rabbit muscle

Bacou, F., Vigneron, P., & Massoulié, J. (1982) · Nature · doi:10.1038/296661a0 · Cited by 66

The Acetylcholinesterase Activity of the Erythrocytes in Paroxysmal Nocturnal Haemoglobinuria in Relation to the Severity of the Disease

Metz, J., Bradlow, B. A., Lewis, S. M., & Dacie, J. V. (1960) · British Journal of Haematology · doi:10.1111/j.1365-2141.1960.tb06255.x · Cited by 66

Characterization of activities and forms of cholinesterases in human primary brain tumors

Razon, N., Soreq, H., Roth, E., Bartal, A., & Silman, I. (1984) · Experimental Neurology · doi:10.1016/0014-4886(84)90215-2 · Cited by 64

Fusion of sequence elements from non-anchored proteins to generate a fully functional signal for glycophosphatidylinositol membrane anchor attachment.

Moran, P., & Caras, I. W. (1991) · The Journal of Cell Biology · doi:10.1083/jcb.115.6.1595 · Cited by 62

Proposed nomenclature for human butyrylcholinesterase genetic variants identified by DNA sequencing

Du, B. N. L., Bartels, C. F., Nogueira, C. P., Arpagaus, M., & Lockridge, O. (1991) · Cellular and Molecular Neurobiology · doi:10.1007/bf00712801 · Cited by 61

A naturally occurring molecular form of human plasma cholinesterase is an albumin conjugate

Masson, P. (1989) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(89)90282-3 · Cited by 61

Axonal Transport of the Molecular Forms of Acetylcholinesterase in Chick Sciatic Nerve

Couraud, J. Y., & Giamberardino, L. D. (1980) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1980.tb07859.x · Cited by 61

Divergent Regulation of Acetylcholinesterase and Butyrylcholinesterase in Tissues of the Rat

Edwards, J. A., & Brimijoin, S. (1982) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1982.tb07918.x · Cited by 61

The p65 protein is a calmodulin-binding protein present in several types of secretory vesicles

Trifaró, J. M., Fournier, S., & Novas, M. L. (1989) · Neuroscience · doi:10.1016/0306-4522(89)90327-8 · Cited by 59

Monoclonal Antibodies to Rat Brain Acetylcholinesterase: Comparative Affinity for Soluble and Membrane‐Associated Enzyme and for Enzyme from Different Vertebrate Species

Rakonczay, Z., & Brimijoin, S. (1986) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1986.tb12959.x · Cited by 59

Acetylcholinesterase in Schistosoma mansoni is anchored to the membrane via covalently attached phosphatidylinositol

Espinoza, B., Tarrab-Hazdai, R., Silman, I., & Arnon, R. (1988) · Molecular and Biochemical Parasitology · doi:10.1016/0166-6851(88)90072-2 · Cited by 59

Amphiphilic and Nonamphiphilic Forms of Torpedo Cholinesterases: I. Solubility and Aggregation Properties

Bon, S., Toutant, J., Méflah, K., & Massoulié, J. (1988) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1988.tb01812.x · Cited by 59

An asymmetric form of muscle acetylcholinesterase contains three subunit types and two enzymic activities in one molecule.

Tsim, K. W. K., Randall, W. R., & Barnard, E. A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.4.1262 · Cited by 59

Expression of cholinesterase gene(s) in human brain tissues: translational evidence for multiple mRNA species.

Soreq, H., Zevin‐Sonkin, D., & Razon, N. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb01979.x · Cited by 58

Cholinesterases from flounder muscle

Stieger, S., Gentinetta, R., & Brodbeck, U. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb14770.x · Cited by 58

Anomalous molecular form of acetylcholinesterase in cerebrospinal fluid in histologically diagnosed Alzheimer's disease

Navaratnam, D. S., Priddle, J. D., Smith, A. D., Esiri, M. M., McDonald, B., & Robinson, J. R. (1991) · The Lancet · doi:10.1016/0140-6736(91)93391-l · Cited by 58

Collagenase Sensitivity and Aggregation Properties of Electrophorus Acetylcholinesterase

Bon, S., & Massoulié, J. (1978) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1978.tb20899.x · Cited by 58

Human cholinesterase genes localized by hybridization to chromosomes 3 and 16

Soreq, H., Zamir, R., Zevin‐Sonkin, D., & Zakut, H. V. (1987) · Human Genetics · doi:10.1007/bf00291419 · Cited by 58

Biosynthesis and secretion of catalytically active acetylcholinesterase in Xenopus oocytes microinjected with mRNA from rat brain and from Torpedo electric organ.

Soreq, H., Parvari, R., & Silman, I. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.3.830 · Cited by 57

Acetylcholinesterase in Huntington's and Alzheimer's Diseases: Simultaneous Enzyme Assay and Immunoassay of Multiple Brain Regions

HAMMOND, P. I., & Brimijoin, S. (1988) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1988.tb10580.x · Cited by 57

Structural characterization of the asymmetric (17 + 13) S species of acetylcholinesterase from Torpedo. II. Component peptides obtained by selective proteolysis and disulfide bond reduction.

Lee, S. L., & Taylor, P. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33713-x · Cited by 56

Distribution and anchoring of molecular forms of acetylcholinesterase

Inestrosa, N. C., & Perelman, A. (1989) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(89)90067-9 · Cited by 56

Regulation by exercise of the pool of G4 acetylcholinesterase characterizing fast muscles: opposite effect of running training in antagonist muscles

Jasmin, B. J., & Gisiger, V. (1990) · Journal of Neuroscience · doi:10.1523/jneurosci.10-05-01444.1990 · Cited by 56

Intramolecular relationships in cholinesterases revealed by oocyte expression of site‐directed and natural variants of human BCHE.

Neville, L. F., Gnatt, A. L., Loewenstein, Y., Seidman, S., Ehrlich, G., & Soreq, H. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05210.x · Cited by 55

Isolation and characterization of a cDNA that encodes an agrin homolog in the marine ray

Smith, M. A., Magill, C., Rupp, F., Yao, Y.-M. M., Schilling, J. W., Snow, P. M., & McMahan, U. J. (1992) · Molecular and Cellular Neuroscience · doi:10.1016/1044-7431(92)90052-4 · Cited by 55

Expression of a cDNA encoding the glycolipid‐anchored form of rat acetylcholinesterase

Legay, C., Bon, S., & Massoulié, J. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81155-s · Cited by 55

Chicken retinospheroids as developmental and pharmacological in vitro models: acetylcholinesterase is regulated by its own and by butyrylcholinesterase activity

Layer, P. G., Weikert, T., & Willbold, E. (1992) · Cell and Tissue Research · doi:10.1007/bf00319147 · Cited by 55

On the origins of esterases.

Myers, M. A., Richmond, R. C., & Oakeshott, J. G. (1988) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a040485 · Cited by 55

Localization of the pool of G4 acetylcholinesterase characterizing fast muscles and its alteration in murine muscular dystrophy

Gisiger, V., & Stephens, H. R. (1988) · Journal of Neuroscience Research · doi:10.1002/jnr.490190110 · Cited by 54

Recombinant human acetylcholinesterase is secreted from transiently transfected 293 cells as a soluble globular enzyme

Velan, B., Kronman, C., Grosfeld, H., Leitner, M., Gozes, Y., Flashner, Y., Sery, T., Cohen, S., Ben-Aziz, R., Seidman, S., et al. (1991) · Cellular and Molecular Neurobiology · doi:10.1007/bf00712806 · Cited by 54

Minigene rescues acetylcholinesterase lethal mutations in Drosophila melanogaster

Hoffmann, F., Fournier, D., & Spierer, P. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90710-2 · Cited by 53

Exercise selectively increases G4 AChe activity in fast-twitch muscle

Fernández, H. L., & Donoso, J. A. (1988) · Journal of Applied Physiology · doi:10.1152/jappl.1988.65.5.2245 · Cited by 53

Evidence that the antigens of the Yt blood group system are located on human erythrocyte acetylcholinesterase

Spring, F. A., Gardner, B., & Anstee, D. J. (1992) · Blood · doi:10.1182/blood.v80.8.2136.2136 · Cited by 51

Site-specific mutagenesis of an essential histidine residue in pancreatic cholesterol esterase

DiPersio, L. P., Fontaine, R. N., & Hui, D. Y. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64279-x · Cited by 51

Bovine brain acetylcholinesterase primary sequence involved in intersubunit disulfide linkages.

Roberts, W. L., Doctor, B. P., Foster, J. D., & Rosenberry, T. L. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)89471-x · Cited by 51

Neurons segregate clusters of membrane-bound acetylcholinesterase along their neurites.

Rotundo, R. L., & Carbonetto, S. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.7.2063 · Cited by 51

Recommendations for Nomenclature in Cholinesterases

Massoulié, J., Sussman, J. L., Doctor, B. P., Soreq, H., Velan, B., Cygler, M., Rotundo, R. L., Avigdor Shafferman, C., Silman, I., & Taylor, P. (1992) · Springer eBooks · doi:10.1007/978-1-4615-3046-6_37 · Cited by 50

Acetylcholinesterases: Zymogens of neuropeptide processing enzymes?

Small, D. H. (1989) · Neuroscience · doi:10.1016/0306-4522(89)90054-7 · Cited by 50

Nucleus-specific translation and assembly of acetylcholinesterase in multinucleated muscle cells.

Rotundo, R. L. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.110.3.715 · Cited by 50

Manipulations of Cholinesterase Gene Expression Modulate Murine Megakaryocytopoiesis In Vitro

Patinkin, D., Seidman, S., Eckstein, F., Benseler, F., Zakut, H. V., & Soreq, H. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.11.6046 · Cited by 49

Structure of human serum cholinesterase

Lockridge, O. (1988) · BioEssays · doi:10.1002/bies.950090406 · Cited by 49

Linkage between serum cholinesterase 2 (CHE2) and γ‐crystallin gene cluster (CRYG): assignment to chromosome 2

Eiberg, H., Nielsen, L. S., Klausen, J., Dahlén, M., Kristensen, M., Bisgaard, M. L., Møller, N., & Mohr, J. (1989) · Clinical Genetics · doi:10.1111/j.1399-0004.1989.tb02951.x · Cited by 49

Amphiphilic Detergent‐Soluble Acetylcholinesterase from Torpedo marmorata: Characterization and Conversion by Proteolysis to a Hydrophilic Form

Stieger, S., & Brodbeck, U. (1985) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1985.tb07111.x · Cited by 49

Existence of an inactive pool of acetylcholinesterase in chicken brain.

Chatel, J., Grassi, J. J., Frobert, Y., Massoulié, J., & Vallette, F. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.6.2476 · Cited by 49

Amphiphilic, glycophosphatidylinositol-specific phospholipase C (PI-PLC)-insensitive monomers and dimers of acetylcholinesterase

Bon, S., Rosenberry, T. L., & Massouli�, J. (1991) · Cellular and Molecular Neurobiology · doi:10.1007/bf00712807 · Cited by 49

Megakaryocytopoiesis in culture: Modulation by cholinergic mechanisms

Burstein, S. A., Adamson, J. W., & Harker, L. A. (1980) · Journal of Cellular Physiology · doi:10.1002/jcp.1041030205 · Cited by 49

cDNA cloning and expression in Xenopus laevis oocytes of pig renal dipeptidase, a glycosyl-phosphatidylinositol-anchored ectoenzyme

Rached, E., Hooper, N. M., James, P., Semenza, G., Turner, A. J., & Mantei, N. (1990) · Biochemical Journal · doi:10.1042/bj2710755 · Cited by 48

Heparin solubilizes asymmetric acetylcholinesterase from rat neuromuscular junction

Torres, J. C., & Inestrosa, N. C. (1983) · FEBS Letters · doi:10.1016/0014-5793(83)80162-8 · Cited by 48

X-ray crystallographic structure of dienelactone hydrolase at 2.8 Å

Pathak, D., Ngai, K. L., & Ollis, D. L. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90587-6 · Cited by 48

EFFECTS OF INACTIVATION OF BUTYRYLCHOLINESTERASE ON STEADY STATE AND REGENERATING LEVELS OF GANGLIONIC ACETYLCHOLINESTERASE

Koelle, G. B., KOELLE, W. A., & Smyrl, E. G. (1977) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1977.tb07750.x · Cited by 48

A Hidden Retinal Regenerative Capacity from the C Ciliary Margin is Reactivated In Vitro, that is Accompanied by Down‐regulation of Butyrylcholinesterase

Willbold, E., & Layer, P. G. (1992) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1992.tb00869.x · Cited by 48

Molecular Basis of Nerve Activity

(1985) · De Gruyter eBooks · doi:10.1515/9783110855630 · Cited by 48

Anionic site interactions in human butyrylcholinesterase disrupted by two single point mutations.

Neville, L. F., Gnatt, A. L., Padan, R., Seidman, S., & Soreq, H. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)45277-x · Cited by 47

Different Glycosylation in Acetylcholinesterases from Mammalian Brain and Erythrocytes

Liao, J., Heider, H., Man-chi, S., & Brodbeck, U. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb11333.x · Cited by 47

Chemical modification of Torpedo acetylcholinesterase by disulfides: appearance of a "molten globule" state

Dolginova, E. A., Roth, E., Silman, I., & Weiner, L. M. (1992) · Biochemistry · doi:10.1021/bi00163a039 · Cited by 47

Acetylcholinesterase from the motor nerve terminal accumulates on the synaptic basal lamina of the myofiber.

Anglister, L. (1991) · The Journal of Cell Biology · doi:10.1083/jcb.115.3.755 · Cited by 47

Amplification of Butyrylcholinesterase and Acetylcholinesterase Genes in Normal and Tumor Tissues: Putative Relationship to Organophosphorous Poisoning

Soreq, H., & Zakut, H. V. (1990) · Pharmaceutical Research · doi:10.1023/a:1015867021628 · Cited by 46

Depression of nigral pars compacta cell discharge by exogenous acetylcholinesterase

Greenfield, S. A., Stein, J. F., Hodgson, A. J., & Chubb, I. W. (1981) · Neuroscience · doi:10.1016/0306-4522(81)90018-x · Cited by 46

Acetylcholinesterase from Drosophila melanogaster Identification of two subunits encoded by the same gene

Fournier, D. D., Bride, J., Karch, F., & Bergé, J. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)80507-6 · Cited by 46

Molecular architecture of acetylcholinesterase collagen‐tailed forms; construction of a glycolipid‐tailed tetramer.

Duval, N., Krejci, É., Grassi, J. J., Coussen, F., Massoulié, J., & Bon, S. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05403.x · Cited by 46

Molecular species analysis of the glycosylphosphatidylinositol anchor of Torpedo marmorata acetylcholinesterase.

Bütikofer, P., Kuypers, F. A., Shackleton, C. H. L., Brodbeck, U., & Stieger, S. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30612-9 · Cited by 45

Use of the polymerase chain reaction for homology probing of butyrylcholinesterase from several vertebrates.

Arpagaus, M., Chatonnet, A., Masson, P., Newton, M., Vaughan, T. A., Bartels, C. F., Nogueira, C. P., Du, B. N. L., & Lockridge, O. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)89597-0 · Cited by 45

Quantitation of megakaryocytopoiesis in liquid culture by enzymatic determination of acetylcholinesterase

Burstein, S. A., Boyd, C. N., & Dale, G. L. (1985) · Journal of Cellular Physiology · doi:10.1002/jcp.1041220124 · Cited by 45

BEHAVIORAL AND BIOCHEMICAL DEFECTS IN TEMPERATURE-SENSITIVE ACETYLCHOLINESTERASE MUTANTS OF DROSOPHILA MELANOGASTER

Hall, J. C., Alahiotis, S., Strumpf, D. A., & White, K. (1980) · Genetics · doi:10.1093/genetics/96.4.939 · Cited by 44

Anionic subsites of the catalytic center of acetylcholinesterase from Torpedo and from cobra venom.

Kreienkamp, H., Weise, C., Raivo, R. A. B. A., Aaviksaar, A., & Hucho, F. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.14.6117 · Cited by 44

Effects of Acute and Chronic Denervation on Release of Acetylcholinesterase and Its Molecular Forms in Rat Diaphragms

Carter, J. L., & Brimijoin, S. (1981) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1981.tb01695.x · Cited by 44

Expression of alternatively terminated unusual human butyrylcholinesterase messenger RNA transcripts, mapping to chromosome 3q26-ter, in nervous system tumors.

Gnatt, A. L., Prody, C. A., Zamir, R., Lieman‐Hurwitz, J., Zakut, H. V., & Soreq, H. (1990) · PubMed · Cited by 44

Hydrophobic labeling of the membrane binding domain of acetylcholinesterase from Torpedo marmorata

Stieger, S., Brodbeck, U., Reber, B. F. X., & Brunner, J. (1984) · FEBS Letters · doi:10.1016/0014-5793(84)80252-5 · Cited by 43

Sequence determination of a peptide fragment from electric eel acetylcholinesterase, involved in the binding of quaternary ammonium

Kieffer, B. L., Goeldner, M. P., HIRTH, C. G., Aebersold, R. H., & Chang, J. (1986) · FEBS Letters · doi:10.1016/0014-5793(86)80655-x · Cited by 43

Independent spatial waves of biochemical differentiation along the surface of chicken brain as revealed by the sequential expression of acetylcholinesterase

Layer, P., Rommel, S., Bülthoff, H., & Hengstenberg, R. (1988) · Cell and Tissue Research · doi:10.1007/bf00214007 · Cited by 43

Molecular Forms of Acetylcholinesterase from Human Caudate Nucleus: Comparison of Salt‐Soluble and Detergent‐Soluble Tetrameric Enzyme Species

Gennari, K., & Brodbeck, U. (1985) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1985.tb12871.x · Cited by 43

Multidisciplinary approaches to cholinesterase functions

(1993) · International Journal of Biochemistry · doi:10.1016/0020-711x(93)90604-d · Cited by 43

Biochemistry and Pathophysiology of the Molecular Forms of Cholinesterases

Rakonczay, Z., & Brimijoin, S. (1988) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4899-1681-5_10 · Cited by 42

Autoimmune preganglionic sympathectomy induced by acetylcholinesterase antibodies.

Brimijoin, S., & Lennon, V. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.24.9630 · Cited by 42

Allelic variants of acetylcholinesterase: genetic evidence that all acetylcholinesterase forms in avian nerves and muscles are encoded by a single gene.

Rotundo, R. L., Gomez, A. M., Fernández‐Valle, C., & Randall, W. R. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.20.7805 · Cited by 42

Subcellular localization of acetycholinesterase molecular forms in endplate regions of adult mammalian skeletal muscle

Fernández, H. L., Inestrosa, N. C., & Stiles, J. R. (1984) · Neurochemical Research · doi:10.1007/bf00973035 · Cited by 41

Kinetic, equilibrium, and spectroscopic studies on dealkylation ("aging") of alkyl organophosphonyl acetylcholinesterase. Electrostatic control of enzyme topography.

Berman, H. A., & Decker, M. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67434-4 · Cited by 40

Acetylcholinesterase hydrolyses chromogranin a to yield low molecular weight peptides

Small, D. H., Ismael, Z., & Chubb, I. W. (1986) · Neuroscience · doi:10.1016/0306-4522(86)90022-9 · Cited by 40

Cell surface acetylcholinesterase molecules on multinucleated myotubes are clustered over the nucleus of origin.

Rossi, S. G., & Rotundo, R. L. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.119.6.1657 · Cited by 39

Axonal Transport and Subcellular Distribution of Molecular Forms of Acetylcholinesterase in Rabbit Sciatic Nerve

Brimijoin, S. (1979) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)11357-6 · Cited by 39

Cholinesterases: Tissue and Cellular Distribution of Molecular Forms and Their Physiological Regulation

Toutant, J.-P., & Massoulié, J. (1988) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-73220-1_9 · Cited by 38

Muscle activity pattern regulates postnatal development of acetylcholinesterase molecular forms in normal mice and mice with motor endplate disease

Yeakley, J., Janavs, J., & Reiness, C. G. (1987) · Journal of Neuroscience · doi:10.1523/jneurosci.07-12-04084.1987 · Cited by 38

Prediction of drug sensitivity in individuals with atypical serum cholinesterase based on in vitro biochemical studies

Valentino, R. J., Lockridge, O., Eckerson, H. W., & Du, B. N. L. (1981) · Biochemical Pharmacology · doi:10.1016/0006-2952(81)90392-0 · Cited by 38

Action of veratridine on acetylcholinesterase in cultures of rat muscle cells

de la Porte, S., Vigny, M., Massoulié, J., & Koenig, J. (1984) · Developmental Biology · doi:10.1016/0012-1606(84)90244-6 · Cited by 38

Peptidasic Activities Associated with Acetylcholinesterase Are Due to Contaminating Enzymes

Checler, F., & Vincent, J. (1989) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1989.tb11793.x · Cited by 38

Association of Acetylcholinesterase with the cell surface

Inestrosa, N. C., & Perelman, A. (1990) · The Journal of Membrane Biology · doi:10.1007/bf01872200 · Cited by 38

Teratogenic effects of cholinergic insecticides in chick embryos I. Diazinon treatment on acetylcholinesterase and choline acetyltransferase activities

Misawa, M., Doull, J., Kitos, P. A., & Uyeki, E. M. (1981) · Toxicology and Applied Pharmacology · doi:10.1016/0041-008x(81)90021-1 · Cited by 38

Protease Inhibitors Reduce Effects of Denervation on Muscle End‐Plate Acetylcholinesterase

Fernández, H. L., & Duell, M. J. (1980) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1980.tb07872.x · Cited by 38

Transcripts for the acetylcholine receptor and acetylcholine esterase show distribution differences in cultured chick muscle cells.

Tsim, K. W. K., Greenberg, I. B., Rimer, M., Randall, W. R., & Salpeter, M. M. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.118.5.1201 · Cited by 38

EFFECTS OF PROTECTION OF BUTYRYLCHOLINESTERASE ON REGENERATION OF GANGLIONIC ACETYLCHOLINESTERASE

KOELLE, W. A., Smyrl, E. G., Ruch, G. A., SIDDONS, V. E., & Koelle, G. B. (1977) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1977.tb07749.x · Cited by 38

Membrane-enclosed crystals in Dictyostelium discoideum cells, consisting of developmentally regulated proteins with sequence similarities to known esterases.

Bomblies, L., Biegelmann, E., Döring, V., Gerisch, G., Krafft-Czepa, H., Noegel, A. A., Schleicher, M., & Humbel, B. M. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.110.3.669 · Cited by 37

The binding of 18S acetylcholinesterase to sphingomyelin and the role of the collagen-like tail

Watkins, M. S., Hitt, A. S., & Bulger, J. E. (1977) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(77)91160-3 · Cited by 37

Definition, at the Molecular Level, of a Thyroglobulin—Acetylcholinesterase Shared Epitope: Study of its Pathophysiological Significance in Patients with Graves' Ophthalmopathy

Ludgate, M., Dong, Q., Dreyfus, P. A., Zakut, H. V., Taylor, P., Vassart, G., & Soreq, H. (1989) · Autoimmunity · doi:10.3109/08916938909099014 · Cited by 37

Formes moleculaires multiples de la butyrylcholinesterase du plasma humain I. Parametres moleculaires apparents et ebauche de la structure quaternaire

Masson, P. (1979) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(79)90179-x · Cited by 37

Nerve crush induced changes in molecular forms of acetylcholinesterase in soleus and extensor digitorum muscles

Groswald, D. E., & Dettbarn, W. (1983) · Experimental Neurology · doi:10.1016/0014-4886(83)90230-3 · Cited by 36

Cholinesterase and its molecular forms in pathological states

Rakonczay, Z. (1988) · Progress in Neurobiology · doi:10.1016/0301-0082(88)90017-2 · Cited by 36

An electrophysiological action of acetylcholinesterase independent of its catalytic site

Greenfield, S. A., Jack, J., Last, A. T. J., & French, M. (1988) · Experimental Brain Research · doi:10.1007/bf00248370 · Cited by 36

Acetylcholinesterase

He, Y., & Shizhen, Z. (1988) · Plastic & Reconstructive Surgery · doi:10.1097/00006534-198807000-00022 · Cited by 36

Regulation of acetylcholinesterase secretion from neuronal cell cultures.—1. Actions of nerve growth factor, cytoskeletal inhibitors and tunicamycin

Lucas, C. A., & Kreutzberg, G. W. (1985) · Neuroscience · doi:10.1016/0306-4522(85)90184-8 · Cited by 35

Conformational plasticity of butyrylcholinesterase as revealed by high pressure experiments

Masson, P., & Balny, C. (1990) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(90)90276-l · Cited by 34

Phosphatidylinositol‐specific phospholipase C induces biosynthesis of acetylcholinesterase via diacylglycerol in Schistosoma mansoni

Espinoza, B., Silman, I., Arnon, R., & Tarrab‐Hazdai, R. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb15776.x · Cited by 34

Molecular analysis of a developmentally regulated gene required for dictyostelium aggregation

Rubino, S., Mann, S. K. O., Hori, R. T., Pinko, C., & Firtel, R. (1989) · Developmental Biology · doi:10.1016/s0012-1606(89)80035-1 · Cited by 33

Synthesis in vitro of precursors of the catalytic subunits of acetylcholinesterase from Torpedo marmorata and Electrophorus electricus

Sikorav, J., Grassi, J., & Bon, S. (1984) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1984.tb08587.x · Cited by 33

ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASES; SEPARATION AND SELECTIVE MODIFICATION BY COLLAGENASE1,2

Johnson, C. D., Smith, S. P., & Russell, R. L. (1977) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1977.tb10433.x · Cited by 33

Effects of the organophosphate insecticides diazinon and parathion on bobwhite quail embryos: Skeletal defects and acetylcholinesterase activity

Meneely, G. A., & Wyttenbach, C. R. (1989) · Journal of Experimental Zoology · doi:10.1002/jez.1402520109 · Cited by 33

A 13 kDa fragment is responsible for the hydrophobic aggregation of brain G4 acetylcholinesterase

Fuentes, M.-E., Rosenberry, T. L., & Inestrosa, N. C. (1988) · Biochemical Journal · doi:10.1042/bj2561047 · Cited by 33

Expression and Tissue-specific Assembly of Human Butyrylcholine Esterase in Microinjected Xenopus laevis Oocytes

Soreq, H., Seidman, S., Dreyfus, P. A., Zevin‐Sonkin, D., & Zakut, H. V. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81664-7 · Cited by 32

Monoclonal antibodies against acetylcholinesterase from electric organs of Electrophorus and Torpedo

Musset, F., Frobert, Y., Grassi, J. J., Vigny, M., Boulla, G., Bon, S., & Massoulié, J. (1987) · Biochimie · doi:10.1016/0300-9084(87)90247-1 · Cited by 32

Expression of acetylcholinesterase during visual system development in Drosophila

Wolfgang, W. J., & Forte, M. A. (1989) · Developmental Biology · doi:10.1016/s0012-1606(89)80005-3 · Cited by 32

Promoter Elements and Transcriptional Regulation of the Acetylcholinesterase Gene

Ekström, T. J., KLUMP, W. M., Getman, D., Karin, M., & Taylor, P. (1993) · DNA and Cell Biology · doi:10.1089/dna.1993.12.63 · Cited by 32

Molecular forms of Electrophorus acetylcholinesterase the catalytic subunits: fragmentation, intra‐ and inter‐subunit disulfide bonds

Bon, S., & Massoulié, J. (1976) · FEBS Letters · doi:10.1016/0014-5793(76)80949-0 · Cited by 32

Acetylcholinesterase generates enkephalin-like immunoreactivity when it degrades the soluble proteins (Chromogranins) from adrenal chromaffin granules

Ismael, Z., Millar, T. J., Small, D. H., & Chubb, I. W. (1986) · Brain Research · doi:10.1016/0006-8993(86)90184-8 · Cited by 32

Acetylcholinesterase activity in the myotome of the early chick embryo

Miki, A., & Mizoguti, H. (1982) · Cell and Tissue Research · doi:10.1007/bf00206329 · Cited by 31

Drosophila acetylcholinesterase: Characterization of different mutants resistant to insecticides

Pralavorio, M., & Fournier, D. (1992) · Biochemical Genetics · doi:10.1007/bf00554429 · Cited by 31

Drosophila acetylcholinesterase

Fournier, D. D., Mutero, A., & Rungger, D. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb16577.x · Cited by 31

Acetylcholinesterase

Toutant, J. P., & Massoulié, J. (1987) · HAL · Cited by 31

A membrane-associated dimer of acetylcholinesterase from Xenopus skeletal muscle is solubilized by phosphatidylinositol-specific phospholipase C

Inestrosa, N. C., Fuentes, M.-E., Anglister, L., Futerman, A. H., & Silman, I. (1988) · Neuroscience Letters · doi:10.1016/0304-3940(88)90809-9 · Cited by 30

Monoclonal antibodies to human brain acetylcholinesterase: properties and applications

Rakonczay, Z., & Brimijoin, S. (1988) · Cellular and Molecular Neurobiology · doi:10.1007/bf00712914 · Cited by 30

Evolutionary origin of cholinergic macromolecules and thyroglobulin.

Mori, N., Itoh, N., & Salvaterra, P. M. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.9.2813 · Cited by 30

Comparison of the Molecular Forms of the Cholinesterases in Tissues of Normal and Dystrophic Chickens

Lyles, J. M., Silman, I., Giamberardino, L. D., Couraud, J.-Y., & Barnard, E. A. (1982) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1982.tb05342.x · Cited by 30

Regulation of Acetylcholinesterase Synthesis and Assembly by Muscle Activity

Fernández‐Valle, C., & Rotundo, R. L. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71639-6 · Cited by 29

Immunology and Molecular Biology of The Cholinesterases: Current Results and Prospects

Brimijoin, S., & Rakonczay, Z. (1986) · International review of neurobiology · doi:10.1016/s0074-7742(08)60112-9 · Cited by 29

Monoclonal antibodies against chicken brain acetylcholinesterase. Their use in immunopurification and immunochemistry to demonstrate allelic variants of the enzyme

Randall, W. R., Tsim, K. W. K., Lai, J. Y., & Barnard, E. A. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb10998.x · Cited by 29

Differences in structure and distribution of the molecular forms of acetylcholinesterase.

Abramson, S. N., Ellisman, M. H., Deerinck, T. J., Maulet, Y., Gentry, M. K., Doctor, B. P., & Taylor, P. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.108.6.2301 · Cited by 29

MOLECULAR FORMS OF ACETYLCHOLINESTERASE IN ALZHEIMERʼS DISEASE

Younkin, L. H., Lockett, G., Usiak, M., Younkin, S. G., & Roessmann, U. (1986) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-198605000-00190 · Cited by 29

Interrelationships between ganglionic acetylcholinesterase and nonspecific cholinesterase of the cat and rat.

Koelle, G. B., Rickard, K. K., & Ruch, G. A. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.11.6012 · Cited by 29

Solubilization of Collagen‐Tailed Acetylcholinesterase from Chick Retina: Effect of Different Extraction Procedures

Gómez‐Barriocanal, J., Barat, A., Escudero, E., Rodríguez‐Borrajo, C., & Ramı́rez, G. (1981) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1981.tb04674.x · Cited by 29

Monoclonal Antibodies Specific for the Different Subunits of Asymmetric Acetylcholinesterase from Chick Muscle

Tsim, K. W. K., Randall, W. R., & Barnard, E. A. (1988) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1988.tb04840.x · Cited by 29

Acetylcholinesterase (AChE) and pseudocholinesterase (BuChE) activity distribution pattern in early developing chick limbs

Falugi, C., & Raineri, M. (1985) · Development · doi:10.1242/dev.86.1.89 · Cited by 29

Subcellular distribution of acetylcholinesterase forms in chromaffin cells

Bon, S., Bader, M. F., Aunis, D., Massoulié, J., & Henry, J. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb15567.x · Cited by 28

Cholinoceptive properties of human primordial, preantral, and antral oocytes: In situ hybridization and biochemical evidence for expression of cholinesterase genes

Malinger, G., Zakut, H. V., & Soreq, H. (1989) · Journal of Molecular Neuroscience · doi:10.1007/bf02896891 · Cited by 28

Evolution of an active-site codon in serine proteases

Irwin, D. M. (1988) · Nature · doi:10.1038/336429b0 · Cited by 28

Aspartate‐70 to glycine substitution confers resistance to naturally occurring and synthetic anionic‐site ligands on inovo produced human butyrylcholinesterase

Neville, L. F., Gnatt, A. L., Loewenstein, Y., & Soreq, H. (1990) · Journal of Neuroscience Research · doi:10.1002/jnr.490270404 · Cited by 28

Simple general acid-base catalysis of physiological acetylcholinesterase reactions

Pryor, A. N., Selwood, T., Leu, L.-S., Andracki, M. A., Lee, B. H., Rao, M., Rosenberry, T. L., Doctor, B. P., Silman, I., & Quinn, D. M. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00036a043 · Cited by 28

Non‐specific cholinesterase activity of the developing peripheral nerves and its possible function in cells in intimate contact with growing axons of chick embryo

Dubový, P., & Haninec, P. (1990) · International Journal of Developmental Neuroscience · doi:10.1016/0736-5748(90)90051-3 · Cited by 28

Pressure ejection of acetylcholinesterase within the guinea-pig substantia nigra has non-classical actions on the pars compacta cells independent of selective receptor and ion channel blockade

Greenfield, S. A., Nedergaard, S., Webb, C., & French, M. (1989) · Neuroscience · doi:10.1016/0306-4522(89)90329-1 · Cited by 28

Characterization of the association of Electrophorus electricus acetylcholinesterase with sphingomyelin liposomes. Relevance to collagen-sphingomyelin interactions

Cohen, R., & Barenholz, Y. (1984) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(84)90452-8 · Cited by 28

Evidence for a single butyrylcholinesterase gene in individuals carrying the C5 plasma cholinesterase variant (CHE2)

Masson, P., Chatonnet, A., & Lockridge, O. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)80167-h · Cited by 28

Butyrylcholinesterase from Chicken Brain Is Smaller than That from Serum: Its Purification, Glycosylation, and Membrane Association

Treskatis, S., Ebert, C., & Layer, P. G. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb10969.x · Cited by 28

Clonal analysis of vertebrate myogenesis

Linkhart, T. A., & Hauschka, S. D. (1979) · Developmental Biology · doi:10.1016/0012-1606(79)90310-5 · Cited by 27

Genetic Linkage Studies of Transf errin, Pseudocholinesterase, and Chromosome 1 Loci

Sparkes, R. S., Field, L. L., Sparkes, M. C., Crist, M. L., Spence, M. A., James, K., & Garry, P. J. (1984) · Human Heredity · doi:10.1159/000153442 · Cited by 27

In vivo gene amplification in non-cancerous cells: cholinesterase genes and oncogenes amplify in thrombocytopenia associated with lupus erythematosus

Zakut, H. V., Lapidot-Lifson, Y., Beeri, R., Ballin, A., & Soreq, H. (1992) · Mutation Research/Reviews in Genetic Toxicology · doi:10.1016/0165-1110(92)90013-y · Cited by 27

ACETYLCHOLINESTERASE: MULTIPLE FUNCTIONS?

Chubb, I. W. (1984) · De Gruyter eBooks · doi:10.1515/9783110848496-030 · Cited by 27

Gene Amplification in Mammalian Cells

Kellems, R. E. (2020) · CRC Press eBooks · doi:10.1201/9781003066989 · Cited by 27

Identical N‐terminal peptide sequences of asymmetric forms and of low‐salt‐soluble and detergent‐soluble amphiphilic dimers of Torpedo acetylcholinesterase

Bon, S., Chang, J., & Strosberg, A. D. (1986) · FEBS Letters · doi:10.1016/0014-5793(86)81112-7 · Cited by 26

Yeast KEX1 protease cleaves a prohormone processing intermediate in mammalian cells.

Thomas, L., Cooper, A. A., Bussey, H., & Thomas, G. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38519-9 · Cited by 26

Effects of persistent selective suppression of ganglionic butyrylcholinesterase on steady state and regenerating levels of acetylcholinesterase: implications regarding function of butyrylcholinesterase and regulation of protein synthesis.

KOELLE, W. A., Koelle, G. B., & Smyrl, E. G. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.8.2936 · Cited by 26

Molecular forms of acetylcholinesterase in synaptic and extrasynaptic regions of avian tonic muscle

Jedrzejczyk, J., Silman, I., Lai, J. Y., & Barnard, E. A. (1984) · Neuroscience Letters · doi:10.1016/0304-3940(84)90113-7 · Cited by 26

Disappearance of the ‘endplate’ form of acetylcholinesterase from a slow tonic muscle

Lyles, J. M., & Barnard, E. A. (1980) · FEBS Letters · doi:10.1016/0014-5793(80)81299-3 · Cited by 26

Interactions between intrinsic regulation and neural modulation of acetylcholinesterase in fast and slow skeletal muscles

Sketelj, J., Črne‐Finderle, N., Ribarič, S., & Brzin, M. (1991) · Cellular and Molecular Neurobiology · doi:10.1007/bf00712799 · Cited by 26

The development of acetylcholinesterase activity in the embryonic nervous system of the frog, Xenopus laevis

Moody, S. A., & Stein, D. B. (1988) · Developmental Brain Research · doi:10.1016/0165-3806(88)90026-0 · Cited by 26

Reciprocal regulation of acetylcholinesterase and butyrylcholinesterase in mammalian skeletal muscle

Berman, H. A., Decker, M. M., & Jo, S. A. (1987) · Developmental Biology · doi:10.1016/0012-1606(87)90113-8 · Cited by 26

Chapter 9 Identification and Analysis of Glycoinositol Phospholipid Anchors in Membrane Proteins

Rosenberry, T. L., Toutant, J., Haas, R., & Roberts, W. L. (1989) · Methods in cell biology · doi:10.1016/s0091-679x(08)61173-5 · Cited by 26

Acetylcholinesterase antibodies and thyroid autoimmunity.

Weetman, A. P., Tse, C. K., Randall, W. R., Tsim, K. W. K., & Barnard, E. A. (1988) · PubMed Central · Cited by 25

Different membrane‐bound forms of acetylcholinesterase are present at the cell surface of hepatocytes

Perelman, A., & Brandan, E. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb14818.x · Cited by 25

Selective Complexing of Acetylcholinesterase in Brain by Intravenously Administered Monoclonal Antibody

Brimijoin, S., Balm, M., HAMMOND, P. I., & Lennon, V. A. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb13306.x · Cited by 25

An evaluation of the hydrophobic interactions of chick muscle acetylcholinesterase by charge shift electrophoresis and gradient centrifugation

Toutant, J. (1986) · Neurochemistry International · doi:10.1016/0197-0186(86)90039-2 · Cited by 25

Evolutionary origin of thyroglobulin by duplication of esterase gene

Takagi, Y., Omura, T., & Gō, M. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80435-6 · Cited by 25

Acetylcholinesterase in the development of chick dorsal root ganglia

Biagioni, S., Odorisio, T., Poiana, G., Scarsella, G., & Augusti-Tocco, G. (1989) · International Journal of Developmental Neuroscience · doi:10.1016/0736-5748(89)90031-2 · Cited by 25

Influence of denervation on the molecular forms of junctional and extrajunctional acetylcholinesterase in fast and slow muscles of the rat

Sketelj, J., Črne‐Finderle, N., & Brzin, M. (1992) · Neurochemistry International · doi:10.1016/0197-0186(92)90193-u · Cited by 25

Regulation of acetylcholinesterase in chick muscle cultures after treatment with diisopropylphosphorofluoridate: Ribonucleic acid and protein synthesis

Walker, C. R., & Wilson, B. W. (1976) · Neuroscience · doi:10.1016/0306-4522(76)90103-2 · Cited by 24

Assignment of the YT blood group locus to chromosome 7q

Zelinski, T. A., White, L., Coghlan, G., & Philipps, S. (1991) · Genomics · doi:10.1016/0888-7543(91)90113-s · Cited by 24

Complete sequence of rabbit butyrylcholinesterase

Jbilo, O., & Chatonnet, A. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.13.3990 · Cited by 24

The effects of the organophosphate insecticide malathion on very young chick embryos: Malformations detected by histological examination

Wyttenbach, C. R., & Thompson, S. C. (1985) · American Journal of Anatomy · doi:10.1002/aja.1001740208 · Cited by 24

Formation of neuroblastic layers in chicken retinospheroids: the fibre layer of Chievitz secludes AChE-positive cells from mitotic cells

Willbold, E., & Layer, P. G. (1992) · Cell and Tissue Research · doi:10.1007/bf00319146 · Cited by 24

Cellular expression of a cloned, hydrophilic, murine acetylcholinesterase. Evidence of palmitoylated membrane-bound forms.

Randall, W. R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32725-4 · Cited by 23

The monoclonal antibody 2G8 is carbohydrate‐specific and distinguishes between different forms of vertebrate cholinesterases

Liao, J., Heider, H., Man-chi, S., Stieger, S., & Brodbeck, U. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb15986.x · Cited by 23

Site‐directed mutagenesis of active‐site‐related residues in Torpedo acetylcholinesterase Presence of a glutamic acid in the catalytic triad

Duval, N., Bon, S., Silman, I., Sussman, J. L., & Massoulié, J. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80821-w · Cited by 23

Effects of high pressure on the single-turnover kinetics of the carbamylation of cholinesterase

Masson, P., & Balny, C. (1988) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(88)90073-8 · Cited by 23

Acetylcholinesterase from the Skeletal Muscle of the Lamprey Petromyzon marinus Exists in Globular and Asymmetric Forms

Pezzementi, L., Reinheimer, E. J., & Pezzementi, M. L. (1987) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1987.tb05733.x · Cited by 23

Acetylcholinesterase has a non-cholinergic neuromodulatory action in the guinea-pig substantia nigra

Last, A. T. J., & Greenfield, S. A. (1987) · Experimental Brain Research · doi:10.1007/bf00248567 · Cited by 23

Synaptic acetylcholinesterase of chicken muscle changes during development from a hybrid to a homogeneous enzyme.

Tsim, K. W. K., Randall, W. R., & Barnard, E. A. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03091.x · Cited by 23

Multiple Forms of a Cholinesterase from Body Muscle of Plaice (Pleuronectes platessa) and Possible Role of Sialic Acid in Cholinesterase Reaction Specificity.

Brodbeck, U., Gentinetta, R., Lundin, S. J., Husebye, S., Klæboe, P., & Swahn, C. (1973) · Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry · doi:10.3891/acta.chem.scand.27-0561 · Cited by 22

Expression of the A12 form of acetylcholinesterase by developing avian leg muscle cells in vivo and during differentiation in primary cell cultures

Toutant, J., Toutant, M., Fiszman, M. Y., & Massoulié, J. (1983) · Neurochemistry International · doi:10.1016/0197-0186(83)90101-8 · Cited by 22

Human acetylcholinesterase and butyrylcholinesterase are encoded by two distinct genes

Gnatt, A. L., Ginzberg, D., Lieman‐Hurwitz, J., Zamir, R., Zakut, H. V., & Soreq, H. (1991) · Cellular and Molecular Neurobiology · doi:10.1007/bf00712802 · Cited by 22

TWO CLASSES OF COLLAGEN-TAILED MOLECULAR FORMS OF ACETYLCHOLINESTERASE

Ramı́rez, G., Gómez‐Barriocanal, J., Barat, A., & Rodríguez‐Borrajo, C. (1984) · De Gruyter eBooks · doi:10.1515/9783110848496-012 · Cited by 22

Studies on the Topography of the Catalytic Site of Acetylcholinesterase Using Polyclonal and Monoclonal Antibodies

Ogert, R. A., Gentry, M. K., Richardson, E. C., Al, C. D. D., Abramson, S. N., Alving, C. R., Taylor, P., & Doctor, B. P. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb04556.x · Cited by 21

A small hydrophobic domain that localizes human erythrocyte acetylcholinesterase in liposomal membranes is cleaved by papain digestion

Kim, B. H., & Rosenberry, T. L. (1985) · Biochemistry · doi:10.1021/bi00335a029 · Cited by 21

Swimming training increases the G4 acetylcholinesterase content of both fast ankle extensors and flexors

Gisiger, V., Sheker, S., & Gardiner, P. F. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80133-n · Cited by 21

Amphiphilic forms of butyrylcholinesterase in mucosal cells of rat intestine

Sine, J.-P., Toutant, J., Weigel, P., & Colas, B. (1992) · Biochemistry · doi:10.1021/bi00159a033 · Cited by 21

Neonatal enucleations reduce specific activity of acetylcholinesterase but not choline acetyltransferase in developing rat visual cortex

Robertson, R. T., Höhmann, C. F., Bruce, J. L., & Coyle, J. T. (1988) · Developmental Brain Research · doi:10.1016/0165-3806(88)90034-x · Cited by 21

Monoclonal Antibodies Allow Precipitation of Esterasic but Not Peptidasic Activities Associated with Butyrylcholinesterase

Checler, F., Grassi, J. J., Masson, P., & Vincent, J. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb04555.x · Cited by 21

Glycolipid-anchored acetylcholinesterases from rabbit lymphocytes and erythrocytes differ in their sensitivity to phosphatidylinositol-specific phospholipase C

RICHIER, P., Arpagaus, M., & Toutant, J.-P. (1992) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(92)90257-m · Cited by 21

Cholinesterase Genes: Multileveled Regulation

Soreq, H., & Zakut, H. V. (1990) · Medical Entomology and Zoology · Cited by 20

Contraction wave in the chick blastoderm induced by muscarinic stimulation

Drews, U., & Mengis, W. (1990) · Anatomy and Embryology · doi:10.1007/bf00178909 · Cited by 20

Selective Increase of Tetrameric (G4) Acetylcholinesterase Activity in Rat Hindlimb Skeletal Muscle Term Denervation

Gregory, E. J., Hodges-Savola, C. A., & Fernández, H. L. (1989) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1989.tb08532.x · Cited by 20

Regulation of the Expression of Acetylcholinesterase by Muscular Activity in Avian Primary Cultures

Vallett, F., & Massoulié, J. (1991) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1991.tb02046.x · Cited by 20

Expression of the Ca2+ mobilizing muscarinic system in the chick embryo correlates with morphogenesis

Oettling, G., Schmidt, H., Show-Klett, A., & Drews, U. (1988) · Cell Differentiation · doi:10.1016/0045-6039(88)90039-5 · Cited by 19

Muscular differentiation of chicken myotubes in a simple defined synthetic culture medium and in serum supplemented media: Expression of the molecular forms of acetylcholinesterase

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Microplastics in Wild Fish from North East Atlantic Ocean and Its Potential for Causing Neurotoxic Effects, Lipid Oxidative Damage, and Human Health Risks Associated with Ingestion Exposure

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Synthesis, in vitro bio-evaluation, and molecular docking study of thiosemicarbazone-based isatin/bis-Schiff base hybrid analogues as effective cholinesterase inhibitors

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Multipotent Cholinesterase Inhibitors for the Treatment of Alzheimer’s Disease: Synthesis, Biological Analysis and Molecular Docking Study of Benzimidazole-Based Thiazole Derivatives

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Synthesis, molecular docking, and bioactivity study of isoquinoline-sulfonamide hybrid analogues: A promising acetylcholinesterase and butyrylcholinesterase inhibitor candidate

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In vitro and in silico correlation of bis-thiazole based Schiff base hybrids analogues: A computational approach develop to promising acetylcholinesterase and butyrylcholinesterase inhibitors

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New Cholinesterase inhibitors based on 1,2,4-triazole bearing benzenesulfonohydrazide skeleton: Synthesis, in vitro and in silico studies

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