Cholinesterases are fundamental players in the peripheral and central nervous systems [...].

Biomedical Research Center University Hospital Hradec Kralove Sokolska 581 500 05 Hradec Kralove Czech Republic

Faculty of Military Health Sciences University of Defence Trebesska 1575 500 05 Hradec Kralove Czech Republic

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De Boer D., Nguyen N., Mao J., Moore J., Sorin E.J. A Comprehensive Review of Cholinesterase Modeling and Simulation. Biomolecules. 2021;11:580. doi: 10.3390/biom11040580. PubMed DOI PMC

Jończyk J., Kukułowicz J., Łątka K., Malawska B., Jung Y.-S., Musilek K., Bajda M. Molecular Modeling Studies on the Multistep Reactivation Process of Organophosphate-Inhibited Acetylcholinesterase and Butyrylcholinesterase. Biomolecules. 2021;11:169. doi: 10.3390/biom11020169. PubMed DOI PMC

Lushchekina S.V., Inidjel G., Martinez N., Masson P., Trovaslet-Leroy M., Nachon F., Koza M.M., Seydel T., Peters J. Impact of Sucrose as Osmolyte on Molecular Dynamics of Mouse Acetylcholinesterase. Biomolecules. 2020;10:1664. doi: 10.3390/biom10121664. PubMed DOI PMC

Zueva I.V., Lushchekina S.V., Pottie I.R., Darvesh S., Masson P. 1-(3-Tert-Butylphenyl)-2,2,2-Trifluoroethanone as a Potent Transition-State Analogue Slow-Binding Inhibitor of Human Acetylcholinesterase: Kinetic, MD and QM/MM Studies. Biomolecules. 2020;10:1608. doi: 10.3390/biom10121608. PubMed DOI PMC

Konecny J., Misiachna A., Hrabinova M., Pulkrabkova L., Benkova M., Prchal L., Kucera T., Kobrlova T., Finger V., Kolcheva M., et al. Pursuing the Complexity of Alzheimer’s Disease: Discovery of Fluoren-9-Amines as Selective Butyrylcholinesterase Inhibitors and N-Methyl-d-Aspartate Receptor Antagonists. Biomolecules. 2021;11:3. doi: 10.3390/biom11010003. PubMed DOI PMC

Calas A.-G., Hanak A.-S., Jaffré N., Nervo A., Dias J., Rousseau C., Courageux C., Brazzolotto X., Villa P., Obrecht A., et al. Efficacy Assessment of an Uncharged Reactivator of NOP-Inhibited Acetylcholinesterase Based on Tetrahydroacridine Pyridine-Aldoxime Hybrid in Mouse Compared to Pralidoxime. Biomolecules. 2020;10:858. doi: 10.3390/biom10060858. PubMed DOI PMC

Amat-ur-Rasool H., Symes F., Tooth D., Schaffert L.-N., Elmorsy E., Ahmed M., Hasnain S., Carter W.G. Potential Nutraceutical Properties of Leaves from Several Commonly Cultivated Plants. Biomolecules. 2020;10:1556. doi: 10.3390/biom10111556. PubMed DOI PMC

Al Mamun A., Maříková J., Hulcová D., Janoušek J., Šafratová M., Nováková L., Kučera T., Hrabinová M., Kuneš J., Korábečný J., et al. Amaryllidaceae Alkaloids of Belladine-Type from Narcissus Pseudonarcissus Cv. Carlton as New Selective Inhibitors of Butyrylcholinesterase. Biomolecules. 2020;10:800. doi: 10.3390/biom10050800. PubMed DOI PMC

Audira G., Ngoc Anh N.T., Ngoc Hieu B.T., Malhotra N., Siregar P., Villalobos O., Villaflores O.B., Ger T.-R., Huang J.-C., Chen K.H.-C., et al. Evaluation of the Adverse Effects of Chronic Exposure to Donepezil (An Acetylcholinesterase Inhibitor) in Adult Zebrafish by Behavioral and Biochemical Assessments. Biomolecules. 2020;10:1340. doi: 10.3390/biom10091340. PubMed DOI PMC

Al-Hamed F.S., Maria O.M., Phan J., Al Subaie A., Gao Q., Mansour A., Abu Nada L., Boukhatem I., Elkashty O.A., Tran S.D., et al. Postoperative Administration of the Acetylcholinesterase Inhibitor, Donepezil, Interferes with Bone Healing and Implant Osseointegration in a Rat Model. Biomolecules. 2020;10:1318. doi: 10.3390/biom10091318. PubMed DOI PMC