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

Pro: Oximes should be used routinely in organophosphate poisoning

Thiermann, H., & Worek, F. (2022) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.15215 · Cited by 14

Drug Candidates for the Treatment of Alzheimer’s Disease: New Findings from 2021 and 2022

Motebennur, S. L., Nandeshwarappa, B. P., & Katagi, M. S. (2023) · Drugs and Drug Candidates · doi:10.3390/ddc2030030 · Cited by 14

Isolation, characterization and evaluation of oxypeucedanin and osthol from local endemic Prangos aricakensis Behçet and Yapar root as antioxidant, enzyme inhibitory, antibacterial and DNA protection: molecular docking and DFT approaches

Gökçimen, S. Ş., İpek, Y., Behçet, L., Demirtaş, İ., & Özen, T. (2024) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2024.2303387 · Cited by 14

Natural products for the treatment of chemotherapy-related cognitive impairment and prospects of nose-to-brain drug delivery

He, Y., Zhou, C., Jiang, S., Lan, W.-Q., Zhang, F., Tao, X., & Chen, W. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1292807 · Cited by 14

Risk of Pneumonia in New Users of Cholinesterase Inhibitors for Dementia

Lai, E. C., Wong, M. B., Iwata, I., Zhang, Y., Hsieh, C., Yang, Y. K., & Setoguchi, S. (2015) · Journal of the American Geriatrics Society · doi:10.1111/jgs.13380 · Cited by 14

A novel assay to determine acetylcholinesterase activity: The application potential for screening of drugs against Alzheimer's disease

Liang, P., Rong, Z., Wang, H., Shao, B., Kang, L., Qi, H. Y., & Chen, H. (2017) · Biomedical Chromatography · doi:10.1002/bmc.3971 · Cited by 14

Synthesis and biological evaluation of benzothiazin-4-ones: a possible new class of acetylcholinesterase inhibitors

Berwaldt, G. A., Gouvêa, D. P., da Silva, D. S., das Neves, A. M., Soares, M. S. P., Azambuja, J. H., Siqueira, G. M., Spanevello, R. M., & Cunico, W. J. (2018) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2018.1543286 · Cited by 14

Discovery of 9-phenylacridinediones as highly selective butyrylcholinesterase inhibitors through structure-based virtual screening

Joubert, J., & Kapp, E. (2020) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2020.127075 · Cited by 14

Characterization of molecular and kinetic properties of two acetylcholinesterases from the Colorado potato beetle, Leptinotarsa decemlineata

Yoon, K. A., Kim, J. H., Nauen, R., Alyokhin, A., Clark, J. M., & Lee, S. H. (2022) · Pesticide Biochemistry and Physiology · doi:10.1016/j.pestbp.2022.105137 · Cited by 14

Biochemical properties of 5′-nucleotidase from mouse skeletal muscle

Martı́nez-Martı́nez, A., Flores‐Flores, C., Campoy, F. J., Muñoz‐Delgado, E., Fini, C., & Vidal, C. J. (1998) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(98)00056-9 · Cited by 14

Expression and Localization of PRiMA-Linked Globular Form Acetylcholinesterase in Vertebrate Neuromuscular Junctions

Tsim, K. W. K., Leung, K. W., Mok, K., Chen, V. P., Zhu, K. Y., Zhu, J., Guo, A. J. Y., Bi, C. W. C., Zheng, Y., Lau, D. T. W., et al. (2009) · Journal of Molecular Neuroscience · doi:10.1007/s12031-009-9251-2 · Cited by 14

Biochemical and toxicological properties of two acetylcholinesterases from the common bed bug, Cimex lectularius

Hwang, C. E., Kim, Y. H., Kwon, D. H., Seong, K. M., Choi, J. Y., Je, Y. H., & Lee, S. H. (2014) · Pesticide Biochemistry and Physiology · doi:10.1016/j.pestbp.2014.02.002 · Cited by 14

(16) The effects of indole-3-acetic acid on human and horse serum butyrylcholinesterase

Bodur, E., & Çokuğraş, A. N. (2005) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2005.10.061 · Cited by 14

RNA interference of long-chain acyl-CoA synthetase 6 suppresses the neurite outgrowth of mouse neuroblastoma NB41A3 cells

Lee (2009) · Molecular Medicine Reports · doi:10.3892/mmr_00000155 · Cited by 14

Screening and analysis of acetyl-cholinesterase (AChE) inhibitors in the context of Alzheimer’s disease

Khan, M. B., Palaka, B. K., Sapam, T. D., Subbarao, N., & Ampasala, D. R. (2018) · Bioinformation · doi:10.6026/97320630014414 · Cited by 14

The structural and biochemical impacts of monomerizing human acetylcholinesterase

Bester, S. M., Adipietro, K. A., Funk, V. L., Myslinski, J. M., Keul, N. D., Cheung, J., Wilder, P. T., Wood, Z. A., Weber, D. J., Height, J. J., et al. (2019) · Protein Science · doi:10.1002/pro.3625 · Cited by 14

Butyrylcholinesterase Is Complexed with Transferrin in Chicken Serum

Weitnauer, E., Ebert, C., Hucho, F., Robitzki, A. A., Weise, C., & Layer, P. G. (1999) · Journal of Protein Chemistry · doi:10.1023/a:1020632207361 · Cited by 14

Dissociation of Transcription, Translation, and Assembly of Collagen-tailed Acetylcholinesterase in Skeletal Muscle

Ruiz, C. A., & Rotundo, R. L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.030049 · Cited by 14

Pilocarpine-Induced Seizures Produce Alterations on Choline Acetyltransferase and Acetylcholinesterase Activities and Deficit Memory in Rats

Santos, Í. M. D. S., Feitosa, C. M., & de Freitas, R. M. (2009) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-009-9481-4 · Cited by 14

Molecular forms of tegumental and muscle acetylcholinesterases of Schistosoma

Camacho, M., Alsford, S., & Agnew, A. (1996) · Parasitology · doi:10.1017/s0031182000084766 · Cited by 14

Reversal of signal-mediated cellular retention by subunit assembly of human acetylcholinesterase.

Velan, B., Kronman, C., Flashner, Y., & Avigdor Shafferman, C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31705-2 · Cited by 14

Absence of a Protective Effect of the Oxime 2-PAM toward Paraoxon-Poisoned Honey Bees: Acetylcholinesterase Reactivation Not at Fault

Polyzou, A., Froment, M.-T., Masson, P., & Belzunces, L. (1998) · Toxicology and Applied Pharmacology · doi:10.1006/taap.1998.8483 · Cited by 14

Monomers and dimers of acetylcholinesterase in human meningioma are anchored to the membrane by glycosylphosphatidylinositol

Sáez‐Valero, J., & Vidal, C. J. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(94)11791-g · Cited by 14

Acetyl‐ and butyrylcholinesterase activities in the rat retina and retinal pigment epithelium

Sánchez‐Chávez, G., Vidal, C. J., & Salceda, R. (1995) · Journal of Neuroscience Research · doi:10.1002/jnr.490410512 · Cited by 14

Synthesis, molecular docking and biochemical analysis of aminoalkylated naphthalene-based chalcones as acetylcholinesterase inhibitors

Aljohani, G. F., Ali, A. A.-S., Al‐Raqa, S. Y., Amran, S. I., & Basar, N. (2021) · Journal of Taibah University for Science · doi:10.1080/16583655.2021.2005921 · Cited by 13

Nematicidal Coumarins from Cnidium monnieri Fruits and Angelica dahurica Roots and Their Physiological Effect on Pine Wood Nematode (Bursaphelenchus xylophilus)

Feng, J., Qin, C., Liu, X., Li, R., Wang, C., Li, C., Du, G., & Guo, Q. (2023) · Molecules · doi:10.3390/molecules28104109 · Cited by 13

Recent development and strategies towards target interactions: Synthesis, characterization and in silico analysis of benzimidazole based thiadiazole as potential anti-Alzheimer agents

Khan, S. A., Hussain, R., Iqbal, T., Rahim, F., & Khan, Y. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.150201 · Cited by 13

Plasma Cholinesterase Activity in Alzheimer's Disease

Hosoi, M., Hori, K., Konishi, K., Tani, M., Tomioka, H., Kitajima, Y., Akashi, N., Inamoto, A., Minami, S., Izuno, T., et al. (2015) · Neurodegenerative Diseases · doi:10.1159/000381532 · Cited by 13

Impact of the pinewood nematode on naturally-emitted volatiles and scCO2 extracts from Pinus pinaster branches: a comparison with P. pinea

Gaspar, M. C., Agostinho, B., Fonseca, L., Abrantes, I., de Sousa, H. C., & Braga, M. E. M. (2020) · The Journal of Supercritical Fluids · doi:10.1016/j.supflu.2020.104784 · Cited by 13

Structure–activity relationship, in vitro and in vivo evaluation of novel dienyl sulphonyl fluorides as selective BuChE inhibitors for the treatment of Alzheimer's disease

Wu, C., Zhang, G., Zhang, Z.-W., Jiang, X., Zhang, Z., Li, H., Qin, H., & Tang, W. (2021) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2021.1959571 · Cited by 14

Mechanisms of Congenital Myasthenia Caused by Three Mutations in the COLQ Gene

Luo, X., Wang, C., Lin, L., Yuan, F., Wang, S., Wang, Y., Wang, A., Wang, C., Wu, S., Lan, X., et al. (2021) · Frontiers in Pediatrics · doi:10.3389/fped.2021.679342 · Cited by 13

Changes of Acetylcholinesterase Activity in Brain Areas and Liver of Sucrose- and Ethanol-Fed Rats

Ruano, M. J., Sánchez-Martín, M. M., Alonso, J. M., & Hueso, P. (2000) · Neurochemical Research · doi:10.1023/a:1007555924661 · Cited by 13

Cholinesterase activity in the tissues of bivalves Noah's ark shell (Arca noae) and warty venus (Venus verrucosa): Characterisation and in vitro sensitivity to organophosphorous pesticide trichlorfon

Perić, L., Ribarić, L., & Nerlović, V. (2013) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2013.05.002 · Cited by 13

The effect of esterases on 17α-hydroxyprogesterone caproate

Yan, R., Fokina, V. M., Hankins, G. D. V., Ahmed, M. S., & Nanovskaya, T. N. (2008) · American Journal of Obstetrics and Gynecology · doi:10.1016/j.ajog.2007.07.038 · Cited by 13

Structure-toxicity relationships of thiono and seleno phosphoramidate compounds: new type of acetylcholinesterase inhibitors

Dehghanpour, S., Rasmi, Y., & Bagheri, M. (2007) · Molecular Diversity · doi:10.1007/s11030-007-9056-6 · Cited by 13

Molecular Characterization of Monoclonal Antibodies that Inhibit Acetylcholinesterase by Targeting the Peripheral Site and Backdoor Region

Bourne, Y., Renault, L. L. R., Essono, S., Mondielli, G., Lamourette, P., Boquet, D., Grassi, J. J., & Marchot, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077226 · Cited by 13

Antimalarials Inhibit Human Erythrocyte Membrane Acetylcholinesterase

Katewa, S. D., & Katyare, S. S. (2005) · Drug and Chemical Toxicology · doi:10.1080/01480540500262912 · Cited by 13

Cloning and Sequencing of Putative Acetylcholinesterase cDNAs from the American Dog Tick, Dermacentor variabilis, and the Brown Dog Tick, Rhipicephalus sanguineus (Acari: Ixodidae)

Xu, G., Fang, Q. Q., Keirans, J. E., & Durden, L. A. (2003) · Journal of Medical Entomology · doi:10.1603/0022-2585-40.6.890 · Cited by 13

Radioligand Binding at Muscarinic Receptors

El‐Fakahany, E. E., & Jakubík, J. (2015) · Neuromethods · doi:10.1007/978-1-4939-2858-3_3 · Cited by 13

Effects of monocrotophos pesticide on cholinergic and dopaminergic neurotransmitter systems during early development in the sea urchin Hemicentrotus pulcherrimus

Zhang, X., Li, S., Wang, C., Tian, H., Wang, W., & Ru, S. (2017) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2017.05.003 · Cited by 13

Monitoring of Blood Cholinesterase Activity in Workers Exposed to Nerve Agents

Jun, D., Bajgar, J., Kuča, K., & Kassa, J. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800159-2.00065-8 · Cited by 13

Congenital myasthenic syndromes

Ohno, K., & Engel, A. G. (2003) · European Journal of Paediatric Neurology · doi:10.1016/s1090-3798(03)00078-3 · Cited by 13

In vivo and in vitro studies of glycine- and glutamate-evoked acetylcholinesterase release from spinal motor neurones: implications for amyotrophic lateral sclerosis/motor neurone disease pathogenesis

Rodrı́guez-Ithurralde, D., Olivera, S., Vincent, O., & Maruri, A. (1997) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(97)00245-1 · Cited by 13

Cholinesterase activities in the adductor muscle of the Antarctic scallop Adamussium colbecki

Bonacci, S., Corsi, I., & Focardi, S. E. (2006) · Antarctic Science · doi:10.1017/s0954102006000022 · Cited by 13

Identification of inactive ecto‐5′‐nucleotidase in normal mouse muscle and its increased activity in dystrophic Lama2dy mice

García‐Ayllón, M., Campoy, F. J., Vidal, C. J., & Muñoz‐Delgado, E. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.10014 · Cited by 13

RanBPM is an acetylcholinesterase-interacting protein that translocates into the nucleus during apoptosis

Gong, X., Ye, W., Zhou, H., Ren, X., Li, Z., Zhou, W., Wu, J., Gong, Y., Ouyang, Q., Zhao, X., et al. (2009) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmp082 · Cited by 13

Rivastigmine and Parkinson dementia complex

Moretti, R., Torre, P., Vilotti, C., Antonello, R. M., & Pizzolato, G. (2007) · Expert Opinion on Pharmacotherapy · doi:10.1517/14656566.8.6.817 · Cited by 13

The Prevalence of Anti-acetylcholinesterase Antibodies in Autoimmune Disease

Geen, J., Howells, R. C., Ludgate, M. E., Hullin, D. A., & Hogg, S. I. (2004) · Autoimmunity · doi:10.1080/08916930400021360 · Cited by 13

Acetylcholinesterase in Dendrobaena veneta (Oligochaeta: Opisthopora) is Present with Forms Sensitive and Insensitive to Phosphatidylinositol Phospholipase C

Talesa, V. N., Romani, R., Rosi, G., & Giovannini, E. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0538z.x · Cited by 13

Molecular modeling of the collagen-like tail of asymmetric acetylcholinesterase

Deprez, P. N., & Inestrosa, N. C. (2000) · Protein Engineering Design and Selection · doi:10.1093/protein/13.1.27 · Cited by 13

Protein fold recognition score functions: Unusual construction strategies

Ayers, D., Huber, T., & Torda, A. E. (1999) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(19990901)36:4 · Cited by 5

Characterization of a null mutation in ace‐1, the gene encoding class A acetylcholinesterase in the nematode Caenorhabditis elegans

Talesa, V. N., Culetto, E., Schirru, N., Bernardi, H., Fédon, Y., Toutant, J., & Arpagaus, M. (1995) · FEBS Letters · doi:10.1016/0014-5793(94)01343-y · Cited by 13

Neuromuscular transmission and its pharmacological blockade. Part 1: Neuromuscular transmission and general aspects of its blockade.

Booij, L. H. D. J. (1997) · Pharmacy World & Science · doi:10.1023/a:1008694726564 · Cited by 13

Biochemical determination of insecticides via cholinesterases. 1. Acetylcholinesterase from rat brain: functional expression using a baculovirus system, and biochemical characterization

Mionetto, N., Morel, N., Massoulié, J., & Schmid, R. D. (1997) · Biotechnology Techniques · doi:10.1023/a:1018425224892 · Cited by 13

Modulation of Acetylcholinesterase and Voltage‐Gated Na+ Channels in Choline Acetyltransferase‐ Transfected Neuroblastoma Clones

Jaco, A. D., Ajmone‐Cat, M. A., Baldelli, P., Carbone, E., Augusti-Tocco, G., & Biagioni, S. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0751123.x · Cited by 13

Differential reactivation by HI-6 in vivo of paraoxon-inhibited rat brain acetylcholinesterase molecular forms

Bajgar, J. (1995) · Neurochemistry International · doi:10.1016/0197-0186(94)00151-j · Cited by 13

Global marine plastic pollution: Sources, distribution, implications on human health and mitigation strategies

Fulke, A. B., Bhanushali, S., & Jadhav, H. S. (2025) · Continental Shelf Research · doi:10.1016/j.csr.2025.105578 · Cited by 18

The relationship between total cholinesterase activity and mortality in four butterfly species

Bargar, T. A. (2012) · Environmental Toxicology and Chemistry · doi:10.1002/etc.1927 · Cited by 12

Benzimidazolone conjugated biscoumarins: Synthesis, molecular docking studies, urease, lipase, and acetylcholinesterase inhibitory activities

Güven, O., Menteşe, E., Sökmen, B. B., Emirik, M., & Akyüz, G. (2025) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2025.142362 · Cited by 12

Three N-Glycosylation Sites of Human Acetylcholinesterase Shares Similar Glycan Composition

Xu, M. L., Luk, W. K. W., Lau, K. M., Bi, C. W. C., Cheng, A. W. M., Gong, A. G. W., Lin, H., & Tsim, K. W. K. (2015) · Journal of Molecular Neuroscience · doi:10.1007/s12031-015-0629-z · Cited by 12

Effect of different buffers on kinetic properties of human acetylcholinesterase and the interaction with organophosphates and oximes

Wille, T., Thiermann, H., & Worek, F. (2010) · Archives of Toxicology · doi:10.1007/s00204-010-0578-9 · Cited by 12

Polypyridylruthenium(II) complexes exert in vitro and in vivo nematocidal activity and show significant inhibition of parasite acetylcholinesterases

Sundaraneedi, M. K., Eichenberger, R. M., Al-Hallaf, R., Dai, Y., Sotillo, J., Rajan, S., Wangchuk, P., Giacomin, P., Keene, F. R., Loukas, A. C., et al. (2017) · International Journal for Parasitology Drugs and Drug Resistance · doi:10.1016/j.ijpddr.2017.11.005 · Cited by 12

Nematicidal activity of tirotundin and parthenolide isolated from Tithonia diversifolia and Chrysanthemum parthenium

Lan, M., Gao, X., Duan, X., Li, H., Yu, H., Li, J., Zhao, Y., Hao, X., Zhao, Y., Ding, X., et al. (2022) · Journal of Environmental Science and Health Part B · doi:10.1080/03601234.2021.2022945 · Cited by 12

Synthesis of indole derivatives as Alzheimer inhibitors and their molecular docking study

Homoud, Z. A., Taha, M., Rahim, F., Iqbal, N., Nawaz, M., Farooq, R. K., Wadood, A., Alomari, M., Islam, I., Algheribe, S., et al. (2022) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2022.2148126 · Cited by 12

Femtosecond quantum fluid dynamics of helium atom under an intense laser field

Dey, B. K., & Deb, B. (1998) · International Journal of Quantum Chemistry · doi:10.1002/(sici)1097-461x(1998)70:3 · Cited by 28

Correlation between antibutyrylcholinesterasic and antioxidant activities of three aqueous extracts from Tunisian Rhus pentaphyllum

Mansour, H. B., Sonia, Y., Mbarek, S., Houas, I., Delai, A., & Dridi, D. (2011) · Annals of Clinical Microbiology and Antimicrobials · doi:10.1186/1476-0711-10-32 · Cited by 12

Nematicidal effect against Bursaphelenchus xylophilus of harmine quaternary ammonium derivatives, inhibitory activity and molecular docking studies on acetylcholinesterase

Xia, Y., Qi, Y.-M., Yu, X.-H., Wang, B.-F., Cao, R., & Jiang, D. (2018) · European Journal of Plant Pathology · doi:10.1007/s10658-018-1559-8 · Cited by 12

So alike yet so different. Differential expression of the long non-coding RNAs NORAD and HCG11 in breast cancer subtypes

Mathias, C., Pedroso, G. A., Pabst, F. R., de Lima, R. S., Kuroda, F., Cavalli, I. J., de Oliveira, J. C., Ribeiro, E. M. D. S. F., & Gradia, D. F. (2021) · Genetics and Molecular Biology · doi:10.1590/1678-4685-gmb-2020-0153 · Cited by 12

Molecular properties of acetylcholinesterase in mouse spleen

Nieto, S. (2004) · Neurochemistry International · doi:10.1016/j.neuint.2003.11.019 · Cited by 12

Correlation between dopaminergic neurons, acetylcholinesterase and nicotinic acetylcholine receptors containing the α3- or α5-subunit in the rat substantia nigra

Emmett, S. R., & Greenfield, S. A. (2005) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2005.04.004 · Cited by 12

Choline acetyltransferase and acetylcholinesterase activities are reduced in rat striatum and frontal cortex after pilocarpine-induced seizures

Sales, I. M. S., de Freitas, R. L. M., Saldanha, G. B., de Souza, G. F., & de Freitas, R. M. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.11.048 · Cited by 12

Desensitization of the post-synaptic membrane of neuromuscular synapses induced by spontaneous quantum secretion of mediator

Giniatullin, R. A., & Magazanik, L. G. (1998) · Neuroscience and Behavioral Physiology · doi:10.1007/bf02464803 · Cited by 12

Exposure to Diazinon Alters In Vitro Retinogenesis: Retinospheroid Morphology, Development of Chicken Retinal Cell Types, and Gene Expression

Paraoanu, L. E., Mocko, J. B., Becker-Röck, M., Smidek-Huhn, J., & Layer, P. G. (2005) · Toxicological Sciences · doi:10.1093/toxsci/kfj003 · Cited by 12

Raman spectroscopic study of conjugates of butyrylcholinesterase with organophosphates

Aslanian, D., Gróf, P., Renault, F., & Masson, P. (1995) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(95)00035-s · Cited by 12

The rate of thermal inactivation of Torpedo acetylcholinesterase is not reduced in the C231 S mutant

Wilson, E. J., Massoulié, J., Bon, S., & Rosenberry, T. L. (1996) · FEBS Letters · doi:10.1016/0014-5793(95)01504-3 · Cited by 12

Molecular dynamics study of active-site interactions with tetracoordinate transients in acetylcholinesterase and its mutants

Enyedy, I. J., Kovach, I. M., & Bencsura, Á. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530645 · Cited by 12

Pharmacodynamics—a pharmacognosy perspective

Campbell, J. E., Thomas-Brown, P. G., & Cohall, D. (2023) · Elsevier eBooks · doi:10.1016/b978-0-443-18657-8.00025-6 · Cited by 11

Structure based design, synthesis of novel fused triazole-thiazole derivatives and their comparative study on Alzheimer disease along with in silico modeling

Khan, S. A., Iqbal, T., Hussain, R., Khan, Y., Ullah, H., Jamal, U., Muqadas, Iqbal, R., Alfarraj, S. A., & Alharbi, S. A. (2024) · Results in Chemistry · doi:10.1016/j.rechem.2024.101590 · Cited by 11

Insights into the Therapeutic Potential of Heparinized Collagen Scaffolds Loading Human Umbilical Cord Mesenchymal Stem Cells and Nerve Growth Factor for the Repair of Recurrent Laryngeal Nerve Injury

Pan, Y., Jiao, G., Yang, J., Guo, R., Li, J., & Wang, C. (2017) · Tissue Engineering and Regenerative Medicine · doi:10.1007/s13770-017-0032-7 · Cited by 11

Kinetic and toxicological effects of synthesized palladium(II) complex on snake venom (Bungarus sindanus) acetylcholinesterase

Ahmed, M., Khan, S. Z., Sher, N., Rehman, Z., Mushtaq, N., & Khan, R. A. (2021) · The Journal of venomous animals and toxins including tropical diseases · doi:10.1590/1678-9199-jvatitd-2020-0047 · Cited by 11

Benzoxazole based thiazole hybrid analogs: Synthesis, in vitro cholinesterase inhibition, and molecular docking studies

Hussain, R., Rahim, F., Rehman, W. U., Shah, S. A. A., Khan, S., Khan, I., Rasheed, L., Imran, S., Wadood, A., & Abdellattif, M. H. (2022) · Computational Toxicology · doi:10.1016/j.comtox.2022.100253 · Cited by 11

Thiosemicarbazone derivatives as potential inhibitors of acetylcholinesterase, butyrylcholinesterase and their molecular docking studies

Al-Zahrani, A. A., Awwad, N. S., Ibrahium, H. A., Hayat, S., Ullah, H., Javed, Z., Rahim, F., Khan, M. S., Zada, H., Rab, A., et al. (2023) · Chemical Data Collections · doi:10.1016/j.cdc.2023.101014 · Cited by 11

The immunotoxicity mechanism of NH4Cl exposure to Litopenaeus vannamei based on the cerebral ganglion-eyestalk-haemocytes axis

Tong, R., Li, Y., Yu, X., Zhang, N., Liao, Q., & Pan, L. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.166876 · Cited by 11

Organophosphate-resistant forms of acetylcholinesterases in two scallops—the Antarctic Adamussium colbecki and the Mediterranean Pecten jacobaeus

Romani, R., Corsi, I., Bonacci, S., Focardi, S. E., Medio, G. E. D., Santis, A. D., Incarnato, F., Giovannini, E., & Rosi, G. (2006) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2006.07.005 · Cited by 11

Resistance to common organophosphate and carbamate insecticides in Aphis pomi (Hemiptera: Aphididae)

Tamaš, N., Dojnov, B., Margetić, A., Vujčić, M. T., Špirović‐Trifunović, B., Miletić, N., Stević, M. Ž., & Vujčić, Z. (2015) · Fruits · doi:10.1051/fruits/2015005 · Cited by 11

Specific Cholinesterase Inhibitors: A Potential Tool to Assist in Management of Alzheimer Disease

Grieg, N. H., Kamal, M. A., Jabir, N. R., Tabrez, S. S. M., Nasim, F., Abuzenadah, A. M., & Aliev, G. M. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-803959-5.50006-4 · Cited by 11

Effect of Acetylcholinesterase and Butyrylcholinesterase on Intrauterine Insemination, Contribution to Inflammations, Oxidative Stress and Antioxidant Status; A Preliminary Report.

Haghnazari, L., Vaisi‐Raygani, A., Keshvarzi, F., Ferdowsi, F., Goodarzi, M., Rahimi, Z., Baniamerian, H., Tavilani, H., Vaisi-Raygani, H., Vaisi‐Raygani, H., et al. (2016) · Europe PMC (PubMed Central) · Cited by 11

Monoclonal Antibodies against Acetylcholinesterase of Schistosoma monsoni : Production and Characterization

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Impact of detergents on the activity of acetylcholinesterase and on the effectiveness of its inhibitors

Zimmermann, M., Westwell, M. S., & Greenfield, S. A. (2008) · Biological Chemistry · doi:10.1515/bc.2009.005 · Cited by 11

Acetylcholinesterase and butyrylcholinesterase activities in obese Beagle dogs before and after weight loss

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An analysis of acetylcholinesterase sequence for predicting mechanisms of its non-catalytic actions

Srivatsan, M. (2006) · Bioinformation · doi:10.6026/97320630001281 · Cited by 11

Three-dimensional mapping of cholinergic molecules by confocal laser scanning microscopy in sea urchin larvae

Falugi, C., Diaspro, A., Angelini, C., Pedrotti, M., Raimondo, M., & Robello, M. (2002) · Micron · doi:10.1016/s0968-4328(01)00018-x · Cited by 11

Characterization of Acetylcholinesterase in Caco-2 Cells

Plageman, L. R., Pauletti, G. M., & Skau, K. A. (2002) · Experimental Biology and Medicine · doi:10.1177/153537020222700712 · Cited by 11

Diversity and Processing of Acetylcholinesterase

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Cholinesterase in Helix pomatia (Gastropoda: Stylommatophora): presence of a soluble (hemolymph) and a membrane-bound form

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Amphiphilic properties of molecular forms of acetylcholinesterase in normal and dystrophic muscle

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Differential effect of pressure and temperature on the catalytic behaviour of wild‐type human butyrylcholinesterase and its D70G mutant

Weingand-Ziadé, A., Renault, F., & Masson, P. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00609.x · Cited by 11

Monoclonal antibodies against brain acetycholinesterases which recognize the subunits bearing the hydrophobic anchor

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Changes in acetylcholinesterase during pupal development ofApis mellifera queen

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Over-expression of acetylcholinesterase stimulates the expression of agrin in NG108–15 cells

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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

Khan, S., Ullah, H., Hussain, R., Khan, Y., Khan, M. U., Khan, M., Sattar, A., & Khan, M. S. (2023) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2023.135351 · Cited by 98

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

Hussain, R., Ullah, H., Rahim, F., Sarfraz, M., Taha, M., Iqbal, R., Rehman, W. U., Khan, S., Shah, S. A. A., Hyder, S., et al. (2022) · Molecules · doi:10.3390/molecules27186087 · Cited by 77

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

Ullah, H., Rahim, F., Zada, H., Hayat, S., Khan, F., & Khan, M. S. (2023) · Chemical Data Collections · doi:10.1016/j.cdc.2023.101048 · Cited by 10

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

Jehangir, U., Khan, S., Hussain, R., Khan, Y., Rahim, F., Iqbal, T., Aziz, T. A., & Alasmari, A. F. (2024) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2024.137585 · Cited by 19

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

Othman, M. S., Naz, H., Rahim, F., Ullah, H., Hussain, R., Taha, M., Khan, S., Fareid, M. A., Aboelnaga, S. M. H., Altaleb, A. T., et al. (2024) · Results in Chemistry · doi:10.1016/j.rechem.2024.101717 · Cited by 7