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

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 3,368

Solubilization of membranes by detergents

Helenius, A., & Simons, K. (1975) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(75)90016-7 · Cited by 2,941

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 2,740

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 2,156

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

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 1,281

The Molecular Basis of Muscular Dystrophy in the mdx 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 1,276

Structure of human pancreatic lipase

Winkler, F. K., D'Arcy, A., & Hunziker, W. H. (1990) · Nature · doi:10.1038/343771a0 · Cited by 1,245

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

Role of load bearing in acetylcholinesterase regulation in rat skeletal muscles

Pregelj, P., & Sketelj, J. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.3000 · Cited by 11

Heterologous expression of acetylcholinesterase affects proliferation and glial cytoskeleton of adherent chicken retinal cells

Keller, M., Robitzki, A. A., & Layer, P. G. (2001) · Cell and Tissue Research · doi:10.1007/s004410100444 · Cited by 11

Use of ELISA to G4 Antigen to Quantitate Neurite Outgrowth in the Chick Both In Vivo and In Vitro

Weikert, T., Rathjen, F. G., & Layer, P. G. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.62041570.x · Cited by 11

Prophylaxis against organophosphorus poisoning

Bajgar, J. (2014) · Cited by 11

Schwann Cells Modify Expression of Acetylcholinesterase and Butyrylcholinesterase at Rat Neuromuscular Junctions

Chapron, J., de la Porte, S., Delépine, L., & Koenig, J. (1997) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1997.tb01396.x · Cited by 11

Electron paramagnetic resonance reveals altered topography of the active center gorge of acetylcholinesterase after binding of fasciculin to the peripheral site

Šentjurc, M., Pečar, S., Stojan, J., Marchot, P., Radić, Z., & Grubič, Z. (1999) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00018-7 · Cited by 11

Increased Butyrylcholinesterase Levels in Microsomal Membranes of Dystrophic Lama2dy Mouse Muscle

Moral‐Naranjo, M. T., Campoy, F. J., Cabezas‐Herrera, J., & Vidal, C. J. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0731138.x · Cited by 11

20-OH-Ecdysone-induced morphogenetic movements in a Chironomus cell line are accompanied by expression of an embryonic muscarinic system

Lammerding-K�ppel, M., Spindler‐Barth, M., & Drews, U. (1994) · Development Genes and Evolution · doi:10.1007/bf00188693 · Cited by 11

In Silico Studies in Probing the Role of Kinetic and Structural Effects of Different Drugs for the Reactivation of Tabun-Inhibited AChE

Lo, R., Chandar, N. B., Kesharwani, M. K., Jain, A., & Ganguly, B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0079591 · Cited by 10

Probing the role of amino acids in oxime-mediated reactivation of nerve agent-inhibited human acetylcholinesterase

Chambers, C., Luo, C., Tong, M., Yang, Y., & Saxena, A. (2014) · Toxicology in Vitro · doi:10.1016/j.tiv.2014.11.001 · Cited by 10

Quantification of the Transcripts Encoding Different Forms of AChE in Various Cell Types: Real-Time PCR Coupled with Standards in Revealing the Copy Number

Bi, C. W. C., Luk, W. K. W., Campanari, M., Liu, Y. H., Xu, M. L., Lau, K. M., Xu, M. L., Choi, R. C. Y., Sáez‐Valero, J., & Tsim, K. W. K. (2014) · Journal of Molecular Neuroscience · doi:10.1007/s12031-013-0210-6 · Cited by 10

Ethyl nitrobenzoate: A novel scaffold for cholinesterase inhibition

Yeong, K. Y., Liew, W.-L., Murugaiyah, V., Wei, A. C., Osman, H., & Tan, S. C. (2016) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2016.11.005 · Cited by 10

Assessment of the physiological markers, oxidative stress and neurotoxic effects of nematode Anisakis sp. on the Luciobarbus callensis (Teleosts, Cyprinids) in northeast of Algeria

Abbaci, S., Mezni, A., Brahmia, S., Hamouda, B., Bensouilah, M., Al-Mekhlafi, F. A., Al-Khalifa, M. S., Wadaan, M. A., & Boulkenafet, F. I. (2022) · Journal of King Saud University - Science · doi:10.1016/j.jksus.2022.102386 · Cited by 10

QSARs for Peripheral Anionic Site of Butyrylcholinesterase with Inhibitions by 4-Acyloxy-biphenyl-4′-N-butylcarbamates

Lin, G., Chen, G., Lu, C., & Yeh, S.-C. (2005) · QSAR & Combinatorial Science · doi:10.1002/qsar.200530124 · Cited by 10

Detection of carbofuran with immobilized acetylcholinesterase based on carbon nanotubes-chitosan modified electrode

Zhang, S.-P., Li, S.-Y., Ma, J., Xiong, F., & Qu, S. (2013) · Journal of Nanomaterials · doi:10.1155/2013/751236 · Cited by 11

Effect of unpredictable stress on cognition and brain acetylcholinesterase activity in adult and aged mice

Das, A., Rai, D., Dikshit, M., Palit, G., & Nath, C. (2002) · Indian Journal of Pharmacology · Cited by 10

Partial Purification and Characterization of Soluble Isoform of Butyrylcholinesterase from Rat Intestine

Yıldız, Ö., Bodur, E., Çokuğraş, A. N., & Özer, N. (2004) · The Protein Journal · doi:10.1023/b:jopc.0000020081.36183.b8 · Cited by 10

Characterization of acetylcholinesterase in Hong Kong oyster (Crassostrea hongkongensis) from South China Sea

Zha, G., Chen, V. P., Luk, W. K. W., Zou, X., Choi, R. C. Y., & Tsim, K. W. K. (2012) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2012.09.005 · Cited by 10

Untitled work

Yamauchi (2000) · doi:10.1002/1097-4547(20001115)62:4

Sensitivity of young rats to nicotine exposure: Physiological and biochemical parameters

Jósê, A. S., Franciscato, C., Sônego, F., Figueiró, M., Thiesen, F. V., García, S. C., & Pereira, M. E. (2008) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2008.03.010 · Cited by 10

Theoretical studies on the possible reaction pathway for the deacylation of the AChE-catalyzed reaction

Wang, Q. M., Jiang, H. L., Chen, K. X., Ji, R. Y., & Ye, Y.-J. (1999) · International Journal of Quantum Chemistry · doi:10.1002/(sici)1097-461x(1999)74:3 · Cited by 10

Subcellular localization of overexpressed maize AChE gene in rice plant

Yamamoto, K., & Momonoki, Y. S. (2008) · Plant Signaling & Behavior · doi:10.4161/psb.3.8.5732 · Cited by 10

Demonstration of Acetylcholinesterase Molecular Forms in a Continuous Tubular Lysosomal System of Rat Pancreatic Acinar Cells

Bendayan, M., & Gisiger, V. (2001) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215540104900104 · Cited by 9

Motor neurone acetylcholinesterase release precedes neurotoxicity caused by systemic administration of excitatory amino acids and strychnine

Rodrı́guez-Ithurralde, D., Maruri, A., & Rodrı́guez, X. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00204-4 · Cited by 10

Probing the acyl binding site of acetylcholinesterase by protein engineering

Pleiss, J., Mionetto, N., & Schmid, R. D. (1999) · Journal of Molecular Catalysis B Enzymatic · doi:10.1016/s1381-1177(98)00082-4 · Cited by 10

Examination of cross-antigenicity of acetylcholinesterase and butyrylcholinesterase using anti-acetylcholinesterase antibodies

George, K. M., Montgomery, M. A., Sandoval, L. E., & Thompson, C. M. (2002) · Toxicology Letters · doi:10.1016/s0378-4274(01)00449-0 · Cited by 10

At Least Two Receptors of Asymmetric Acetylcholinesterase Are Present at the Synaptic Basal Lamina ofTorpedoElectric Organ

Casanueva, O. I., Deprez, P. N., García‐Huidobro, T., & Inestrosa, N. C. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9303 · Cited by 10

The membrane form of acetylcholinesterase from rat brain contains a 20 kDa hydrophobic anchor

Boschetti, N., Liao, J., & Brodbeck, U. (1994) · Neurochemical Research · doi:10.1007/bf00971586 · Cited by 10

Characterization of molecular forms of acetyl- and butyrylcholinesterase in human acoustic neurinomas

García‐Ayllón, M., Sáez‐Valero, J., Pérez, C. J. P., & Vidal, C. J. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00596-0 · Cited by 10

Spatial transcriptomics in embryonic mouse diaphragm muscle reveals regional gradients and subdomains of developmental gene expression

Kaplan, M. M., Zeidler, M., Knapp, A., Hoelzl, M., Kress, M., Fritsch, H., Krogsdam, A., & Flucher, B. E. (2024) · iScience · doi:10.1016/j.isci.2024.110018 · Cited by 9

Elevated Cholinesterase Activity and the Metabolic Syndrome—Dissecting Fatty Liver, Insulin Resistance and Dysglycaemia

Heni, M., Hummel, J., Fritsche, L., Wagner, R., Relker, L., Machann, J., Schick, F., Birkenfeld, A. L., Schleicher, E. D., Königsrainer, A., et al. (2025) · Liver International · doi:10.1111/liv.70046 · Cited by 9

Biochemical characterization of two distinct acetylcholinesterases possessing almost identical catalytic activity in the damselfly Vestalis gracilis

Kim, Y. H., Kwon, D. H., & Lee, S. H. (2013) · Journal of Asia-Pacific Entomology · doi:10.1016/j.aspen.2013.06.007 · Cited by 9

Modelling organophosphate intoxication in C. elegans highlights nicotinic acetylcholine receptor determinants that mitigate poisoning

Izquierdo, P. G., Charvet, C., Neveu, C., Green, A. C., Tattersall, J. E. H., Holden-Dye, L. M., & O'Connor, V. M. (2023) · PLoS ONE · doi:10.1371/journal.pone.0284786 · Cited by 9

Inhibition, ADME and structure based modification of IAA and IBA against acetylcholinesterase: an attempt towards new drug development for Alzheimer's disease

Dileep, K. V., Remya, C., Tintu, I., & Sadasivan, C. (2013) · Frontiers in Life Science · doi:10.1080/21553769.2013.876452 · Cited by 9

Mild Thiamine Deficiency and Chronic Ethanol Consumption Modulate Acetylcholinesterase Activity Change and Spatial Memory Performance in a Water Maze Task

Silva, I. D. F. O., Pereira, S. R. C., Fernandes, P. Á., Ribeiro, A. F., Pires, R. G. W., & Ribeiro, Â. M. (2014) · Journal of Molecular Neuroscience · doi:10.1007/s12031-014-0306-7 · Cited by 9

Association of a polymorphism of BCHE with ischemic stroke in Japanese individuals with chronic kidney disease

Yamada (2009) · Molecular Medicine Reports · doi:10.3892/mmr_00000172 · Cited by 9

Genomic structure, organization and localization of the acetylcholinesterase locus of the olive fruit fly,Bactrocera oleae

Kakani, E. G., Trakala, M., Drosopoulou, E., Mavragani-Tsipidou, P., & Mathiopoulos, K. D. (2012) · Bulletin of Entomological Research · doi:10.1017/s0007485312000478 · Cited by 9

Design, Synthesis and Bioevaluation of Two Series of 3‐[(1‐Benzyl‐1H‐1,2,3‐triazol‐4‐yl)methyl]quinazolin‐4(3H)‐ones and N‐(1‐Benzylpiperidin‐4‐yl)quinazolin‐4‐amines

Lan, T. T., Anh, D. T., Pham‐The, H., Dung, D. T. M., Park, E. J., Jang, S. D., Kwon, J. H., Kang, J. S., Thuần, N. T. D., Han, S., et al. (2020) · Chemistry & Biodiversity · doi:10.1002/cbdv.202000290 · Cited by 9

Solar light induces expression of acetylcholinesterase in skin keratinocytes: Signalling mediated by activator protein 1 transcription factor

Wu, Q., Bai, P., Xia, Y., Lai, Q. W. S., Guo, M. S., Dai, K., Zheng, B. Z.-Y., Ling, C. S. J., Dong, T. T.-X., Pi, R., et al. (2020) · Neurochemistry International · doi:10.1016/j.neuint.2020.104861 · Cited by 9

Amphiphilic properties of acetylcholinesterase monomers in mouse plasma

García‐Ayllón, M., Gómez, J. L., & Vidal, C. J. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00252-9 · Cited by 9

Characterization of acetylcholinesterase from the gut of sea cucumber Stichopus japonicus

Wu, H.-T., Li, D.-M., Zhu, B., Du, Y., Chai, X.-Q., & Murata, Y. (2013) · Fisheries Science · doi:10.1007/s12562-012-0588-z · Cited by 9

In silico Exploration of Bioactive Phytochemicals Against Neurodegenerative Diseases Via Inhibition of Cholinesterases

Mahomoodally, M. F., Abdallah, H. H., Suroowan, S., Jugreet, S., Zhang, Y., & Hu, X. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666200316125517 · Cited by 9

Monitoring of Blood Cholinesterase Activity in Workers Exposed to Nerve Agents

Jun, D., Bajgar, J., Kuča, K., & Kassa, J. (2009) · Elsevier eBooks · doi:10.1016/b978-012374484-5.00058-4 · Cited by 9

Chapter 4 Biosynthesis and integration of acetylcholinesterase in the cholinergic synapse

Massoulié, J., Legay, C., Anselmet, A., Krejci, É., Coussen, F., & Bon, S. (1996) · Progress in brain research · doi:10.1016/s0079-6123(08)62088-9 · Cited by 9

Enzimas polifuncionales: El caso de la acetilcolinesterasa

Sánchez‐Chávez, G., & Salceda, R. (2008) · REB. Revista de educación bioquímica · Cited by 9

Differential inhibition of rat brain acetylcholinesterase molecular forms by 7-methoxytacrine in vitro

Bajgar, J. (1995) · Toxicology Letters · doi:10.1016/0378-4274(95)03341-h · Cited by 9

Two new mutations of the human BCHE gene (IVS3-14T>C and L574fsX576)

Parmo-Folloni, F., Nunes, K., Lepienski, L. M., Mikami, L. R., de Souza, R. L. R., Tsuneto, L. T., Petzl‐Erler, M. L., & Chautard‐Freire‐Maia, E. A. (2008) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2008.04.038 · Cited by 9

Use of peptide nucleic acid probes for detecting DNA single-base mutations by capillary electrophoresis

Basile, A., Giuliani, A., Pirri, G., & Chiari, M. (2002) · Electrophoresis · doi:10.1002/1522-2683(200203)23:6 · Cited by 23

Comparative Expression of Homologous Proteins

Morel, N., & Massoulié, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.10.7304 · Cited by 9

Structural Bioinformatics and QSAR Analysis Applied to the Acetylcholinesterase and Bispyridinium Aldoximes

Mager, P. P., & Weber, A. (2003) · Drug design and discovery · doi:10.1080/10559610390484168 · Cited by 9

Monoclonal antibodies against a C-terminal peptide of human brain acetylcholinesterase distinguish between erythrocyte and brain acetylcholinesterases

Boschetti, N., Brodbeck, U., Jensen, S., Koch, C., & Nørgaard‐Pedersen, B. (1996) · Clinical Chemistry · doi:10.1093/clinchem/42.1.19 · Cited by 9

Kinetics of Muscarinic Reduction ofIsAHPin Hippocampal Neurons: Effects of Acetylcholinesterase Inhibitors

Zhang, Y., Carlen, P. L., & Zhang, L. (1997) · Journal of Neurophysiology · doi:10.1152/jn.1997.78.6.2999 · Cited by 9

Biodegradation and valorisation of plastic based food packets: a microbial solution for sustainability and circular economy

Ganguly, A., Kaibarta, R., Das, S., Kundu, R., Paramanik, S., Mohapatra, S. D., Mukherjee, S. K., Mitra, D., & Chattaraj, S. (2025) · Discover Sustainability · doi:10.1007/s43621-025-01257-y · Cited by 8

2-Mercaptobenzimidazole clubbed hydrazone for Alzheimer’s therapy: In vitro, kinetic, in silico, and in vivo potentials

Begum, F., Rehman, N. U., Khan, A., Iqbal, S., Paracha, R. Z., Uddin, J., Al‐Harrasi, A., & Lodhi, M. A. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.946134 · Cited by 8

Glyphosate is Harmful to Early Life Stages of the Viviparous Fish Jenynsia Multidentata: Biochemical and Locomotor Effects

Moraes, J. S., Silva, D. G. D. C., Vaz, B. D. S., Mizuschima, C. W., & Martins, C. D. M. G. (2023) · Archives of Environmental Contamination and Toxicology · doi:10.1007/s00244-023-01015-z · Cited by 8

Development of Thiazolidinone-Based Pyrazine Derivatives: Synthesis, Molecular Docking Simulation, and Bioevaluation for Anti-Alzheimer and Antibacterial Activities

Jehangir, U., Khan, S., Hussain, R., Khan, Y., Ali, F., Sardar, A., Aslam, S., & Afshari, M. (2024) · Journal of Chemistry · doi:10.1155/2024/8426930 · Cited by 8

Ecotoxicity threshold values for 4-hydroxychlorothalonil, carbendazim, dimethoate and methoxyfenozide in fresh and marine waters: Part 1. Derivation of threshold values

Mitchell, H. C., Warne, M. S. J., Mann, R. M., King, O. C., & Turner, R. D. R. (2024) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2024.174578 · Cited by 8

Toothpastes for children and their detergent contents affect molecular mechanisms of odontogenesis in zebrafish embryos

Karaman, G. E., Ünal, İ., Beler, M., Üstündağ, F. D., Cansız, D., Üstündağ, Ü. V., Emekli‐Alturfan, E., & Akyüz, S. (2022) · Drug and Chemical Toxicology · doi:10.1080/01480545.2022.2150208 · Cited by 9

Synthesis and Molecular Docking Study of Bis-Indolylmethane Thiourea Derivatives as Anti-Alzheimer Agents

Ullah, H., Bibi, U., Hussain, A., Sarfraz, M., Rahim, F., Hayat, S., Zada, H., Khan, F., & Wadood, A. (2023) · Russian Journal of Organic Chemistry · doi:10.1134/s1070428023010207 · Cited by 8

EVIDENCES FOR THE PROMISING THERAPEUTIC POTENTIAL OF BOSWELLIA SERRATA AGAINST ALZHEIMER'S DISEASE: PRE-CLINICAL STUDY

Ahmed, H. H., Mohamed, E. M., & El-dsoki, S. M. (2014) · International Journal of Pharmacy and Pharmaceutical Sciences · Cited by 8

Some New Carbacylamidophosphates as Inhibitors of Acetylcholinesterase and Butyrylcholinesterase

Gholivand, K., Alizadehgan, A. M., Mojahed, F., Dehghan, G., Mohammadirad, A., & Abdollahi, M. R. (2008) · Zeitschrift für Naturforschung C · doi:10.1515/znc-2008-3-414 · Cited by 8

Acetyl- and butyrylcholinesterase molecular forms in normal and streptozotocin-diabetic rat retinal pigment epithelium

Sánchez‐Chávez, G., & Salceda, R. (2001) · Neurochemistry International · doi:10.1016/s0197-0186(01)00022-5 · Cited by 8

Streptozotocin-induced diabetes alters the oligomerization pattern of acetylcholinesterase in rat skeletal muscle

Kiss, G., Somogyi, J., Csermely, P., Szel�nyi, J., & V�r, �. (2001) · Diabetologia · doi:10.1007/s001250051602 · Cited by 8

LA ESTRUCTURA Y FUNCIÓN DE LAS COLINESTERASAS: BLANCO DE LOS PLAGUICIDAS

Departamento de Ciencias de la Salud, D. D. C. B. Y. D. L. S., López-Durán, R. M., Quintana, R. V., Facultad de Agrobiología, U. A. D. T., Sánchez-Alarcón, J., Facultad de Agrobiología, U. A. D. T., Pérez-Aguilar, B., Departamento de Ciencias de la Salud, D. D. C. B. Y. D. L. S., Salinas-Arreortua, N., Departamento de Ciencias de la Salud, D. D. C. B. Y. D. L. S., et al. (2018) · Revista Internacional de Contaminación Ambiental · doi:10.20937/rica.2018.34.esp02.06 · Cited by 8

Differentiation of erythroblast requires the dimeric form of acetylcholinesterase: Interference with erythropoietin receptor

Xu, M. L., Luk, W. K. W., Liu, E. Y. L., Kong, X. P., Wu, Q. Y., Xia, Y., Dong, T. T.-X., & Tsim, K. W. K. (2019) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2019.06.006 · Cited by 8

Synthesis of 1‐[(1R)‐1‐(6‐fluoro‐1,3‐benzothiazol‐2‐yl)ethyl]‐3‐substituted phenyl ureas and their inhibition activity to acetylcholinesterase and butyrylcholinesterase

Pejchal, V., Štěpánková, Š., & Drabina, P. (2010) · Journal of Heterocyclic Chemistry · doi:10.1002/jhet.502 · Cited by 8

Novel cholinesterase paralogs of Schistosoma mansoni have perceived roles in cholinergic signalling and drug detoxification and are essential for parasite survival

Tedla, B., Sotillo, J., Pickering, D., Eichenberger, R. M., Ryan, S. M., Becker, L., Loukas, A. C., & Pearson, M. S. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1008213 · Cited by 8

Rescue and Stabilization of Acetylcholinesterase in Skeletal Muscle by N-terminal Peptides Derived from the Noncatalytic Subunits

Ruiz, C. A., Rossi, S. G., & Rotundo, R. L. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.653741 · Cited by 8

Isolation of Acetylcholinesterase from Apoptotic Human Lung Fibroblast Cells by Antibody Affinity Chromatography

Jin, Q.-H., Shi, Y., He, H. Y., Ng, K. K. W., Jiang, H. L., Yang, L., Jiang, Z.-Q., & Zhang, X. (2002) · BioTechniques · doi:10.2144/oct0211 · Cited by 8

Sequence comparison ofACE-1, the gene encoding acetylcholinesterase of class A, in the two nematodesCaenorhabditis elegansandCaenorhabditis briggsae

Grauso, M., Culetto, E., Bergé, J., Toutant, J., & Arpagaus, M. (1996) · DNA sequence · doi:10.3109/10425179609008446 · Cited by 8

Age-related changes in activity of fischer 344 rat brain acetylcholinesterase molecular forms

Skau, K. A., & Triplett, C. G. (1998) · Molecular and Chemical Neuropathology · doi:10.1007/bf02815113 · Cited by 8

Acetylcholinesterase at high catalytic efficiency and substrate specificity in the optic lobe of Eledone moschata (Cephalopoda: Octopoda): biochemical characterization and histochemical localization

Talesa, V. N., Romani, R., Calvitti, M., Rosi, G., & Giovannini, E. (1998) · Neurochemistry International · doi:10.1016/s0197-0186(98)00017-5 · Cited by 8

The aryl acylamidase activity is much more sensitive to Alzheimer drugs than the esterase activity of acetylcholinesterase in chicken embryonic brain

Rajesh, R. V., Loganathan, C., Layer, P. G., & Boopathy, R. (2009) · Biochimie · doi:10.1016/j.biochi.2009.07.004 · Cited by 8

Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method

Pavelkić, V. M., Krinulović, K., Savić, J., & Ilić, M. (2008) · Russian Journal of Physical Chemistry A · doi:10.1134/s0036024408050312 · Cited by 8

Expression of acetylcholinesterase gene during in vitro differentiation of rabbit muscle satellite cells

Barjot, C., Jbilo, O., Chatonnet, A., & Bacou, F. (1993) · Neuromuscular Disorders · doi:10.1016/0960-8966(93)90093-y · Cited by 8

Differential interaction of the monoclonal antibody AE-1 with acetylcholinesterase oligomers and monomers from rabbit muscle microsomes, human brain and fetal bovine serum

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Acetylcholinesterase and inhibitors: effects upon normal and regenerating nerves of the rat

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