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Anthelmintic and Hepatoprotective Activities of the Green-Synthesized Zinc Oxide Nanoparticles Against Parascaris equorum Infection in Rats

Ali, S. B., Mohamed, A. S., Fahmy, S. R., Garhy, M. E., Mousa, M. R., & Abdel‐Ghaffar, F. (2023) · Acta Parasitologica · doi:10.1007/s11686-023-00728-4 · Cited by 20 · see citing works

Non-conventional compounds with potential therapeutic effects against Alzheimer’s disease

de Castro, A. A., Soares, F. V., Pereira, A. F., Polisel, D. A., Caetano, M. S., Leal, D. H. S., da Cunha, E. F. F., Nepovimová, E., Kuča, K., & Ramalho, T. C. (2019) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2019.1608823 · Cited by 20 · see citing works

Theoretical and Practical Aspects of Albumin Esterase Activity

Belinskaia, D. A., & Goncharov, N. V. (2020) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162020030036 · Cited by 20 · see citing works

Preclinical and first-in-human evaluation of PRX-105, a PEGylated, plant-derived, recombinant human acetylcholinesterase-R

Atsmon, J., Brill‐Almon, E., Nadri-Shay, C., Chertkoff, R., Alon, S., Shaikevich, D., Volokhov, I., Haim, K. Y., Bartfeld, D., Shulman, A., et al. (2015) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2015.06.004 · Cited by 20 · see citing works

Differentiated SH-SY5Y neuroblastoma cells as a model for evaluation of nerve agent-associated neurotoxicity

Pulkrabkova, L., Múčková, Ľ., Hrabinová, M., Sorf, A., Kobrlová, T., Jošt, P., Bezděková, D., Korábečný, J., Jun, D., & Soukup, O. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03525-0 · Cited by 19 · see citing works

Energy Landscapes of Human Acetylcholinesterase and Its Huperzine A-Inhibited Counterpart

Trapp, M., Trovaslet, M., Nachon, F., Koza, M. M., van Eijck, L., Hill, F. R., Weik, M., Masson, P., Tehei, M., & Peters, J. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp304704h · Cited by 19 · see citing works

Activity and molecular dynamics relationship within the family of human cholinesterases

Peters, J., Trovaslet, M., Trapp, M., Nachon, F., Hill, F. R., Royer, E., Gabel, F., van Eijck, L., Masson, P., & Tehei, M. (2012) · Physical Chemistry Chemical Physics · doi:10.1039/c2cp23817a · Cited by 19 · see citing works

New therapeutic approaches and novel alternatives for organophosphate toxicity

Katz, F. S., Pecic, S., Schneider, L., Zhu, Z., Hastings-Robinson, A., Luzac, M., Macdonald, J., Landry, D. W., & Stojanović, M. N. (2018) · Toxicology Letters · doi:10.1016/j.toxlet.2018.03.028 · Cited by 18 · see citing works

Fluorosulfate-containing pyrazole heterocycles as selective BuChE inhibitors: structure-activity relationship and biological evaluation for the treatment of Alzheimer’s disease

Li, H., Wu, C., Zhang, S., Yang, J.-G., Qin, H., & Tang, W. (2022) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2022.2103553 · Cited by 18 · see citing works

Understanding the non-catalytic behavior of human butyrylcholinesterase silent variants: Comparison of wild-type enzyme, catalytically active Ala328Cys mutant, and silent Ala328Asp variant

Lushchekina, S. V., Nemukhin, A. V., Varfolomeev, S. D., & Masson, P. (2016) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2016.04.007 · Cited by 18 · see citing works

Activity and polymorphisms of butyrylcholinesterase in a Polish population

Jasiecki, J., Jońca, J., Żuk, M., Szczoczarz, A., Janaszak‐Jasiecka, A., Lewandowski, K. K., Waleron, K., & Wasąg, B. (2016) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2016.04.030 · Cited by 17 · see citing works

Proteomic analysis of adducted butyrylcholinesterase for biomonitoring organophosphorus exposures

Marsillach, J., Hsieh, E. J., Richter, R. J., MacCoss, M. J., & Furlong, C. E. (2012) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2012.10.019 · Cited by 17 · see citing works

Effects of chlorpyrifos on soil carboxylesterase activity at an aggregate-size scale

Sanchez-Hernandez, J. C., & Sandoval, M. (2017) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2017.04.032 · Cited by 17 · see citing works

Dimerization of human butyrylcholinesterase expressed in bacterium for development of a thermally stable bioscavenger of organophosphorus compounds

Cai, Y., Zhou, S., Stewart, M. J., Zheng, F., & Zhan, C. (2019) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2019.108756 · Cited by 16 · see citing works

Different sensitivities of rat skeletal muscles and brain to novel anti‐cholinesterase agents, alkylammonium derivatives of 6‐methyluracil (ADEMS)

Petrov, K. A., Iagodina, L. O., Valeeva, G. R., Ивановна, Л. Н., Nikitashina, A. D., Rizvanov, A. A., Васильевич, З. В., Bukharaeva, E. A., Reznik, V. S., Nikolsky, E. E., et al. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01211.x · Cited by 16 · see citing works

Correction: Evolution of Acetylcholinesterase and Butyrylcholinesterase in the Vertebrates: An Atypical Butyrylcholinesterase from the Medaka Oryzias latipes

Pezzementi, L., Nachon, F., & Chatonnet, A. (2011) · PLoS ONE · doi:10.1371/annotation/938a4e59-a5d1-448c-b7c1-632bf9e7e8ef · Cited by 16 · see citing works

Optical imaging probes for selective detection of butyrylcholinesterase

Dirak, M., Chan, J., & Kölemen, S. (2024) · Journal of Materials Chemistry B · doi:10.1039/d3tb02468g · Cited by 15 · see citing works

Determination of binding points of methylene blue and cationic phenoxazine dyes on human butyrylcholinesterase

Sezgin, Z., Biberoğlu, K., Chupakhin, V., Махаева, Г. Ф., & Tacal, Ö. (2013) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2013.01.003 · Cited by 15 · see citing works

Reactivation of organophosphate-inhibited serum butyrylcholinesterase by novel substituted phenoxyalkyl pyridinium oximes and traditional oximes

Nichols, R. H., & Chambers, J. E. (2021) · Toxicology · doi:10.1016/j.tox.2021.152719 · Cited by 8 · see citing works

Enhancing inhibitor- and enzyme-based strategies for prophylaxis against organophosphate toxicity

Hester, K. (2019) · SHAREOK (University of Oklahoma; Oklahoma State University; Central Oklahoma University)

Progress towards BChE tethered with a reactivating ligand: a pseudo-catalytic nerve agent bioscavenger (Poster)

de Koning, M. C., Nachon, F., Worek, F., Brazzolotto, X., Berthoin, L., Trovaslet-Leroy, M., Noort, D., van Grol, M., Alkema, D. P. W., & Muns, J. A. (2012)

Why acetylcholinesterase reactivators do not work in butyrylcholinesterase

Wiesner, J., Křı́ž, Z., Kuča, K., Jun, D., & Koča, J. (2009) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756360903179427 · Cited by 16 · see citing works

Reactivators of butyrylcholinesterase inhibited by organophosphorus compounds

Kohoutova, Z., Prchalová, E., Knittelova, K., Musílek, K., & Maliňák, D. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107526 · Cited by 6 · see citing works