1. Vogel, J.W., Iturria-Medina, Y., Strandberg, O.T., Smith, R., Levitis, E., Evans, A.C. and Hansson, O., 2020. Spread of pathological tau proteins through communicating neurons in human Alzheimer’s disease. Nature Communications. 11(1): 2612. doi: 10.1038/s41467-020-15701-2 [DOI]

2. Breijyeh, Z. and Karaman, R., 2020. Comprehensive Review on Alzheimer's Disease: Causes and Treatment. Molecules. 25(24): 5789. doi: 10.3390/molecules25245789 [DOI]

3. Mufson, E.J., Counts, S.E., Perez, S.E. and Ginsberg, S.D., 2008. Cholinergic system during the progression of Alzheimer’s disease: therapeutic implications. Expert Review of Neurotherapeutics. 8(11): 1703-1718. doi: 10.1586/14737175.8.11.1703 [DOI]

4. Hasselmo, M.E., 2006. The role of acetylcholine in learning and memory. Current Opinion in Neurobiology. 16(6): 710-715. doi: 10.1016/j.conb.2006.09.002 [DOI]

5. Galimberti, D. and Scarpini, E., 2016. Old and new acetylcholinesterase inhibitors for Alzheimer's disease. Expert Opinion on investigational Drugs. 25(10): 1181-1187. doi: 10.1080/13543784.2016.1216972 [DOI]

6. Sharma, K., 2019. Cholinesterase inhibitors as Alzheimer's therapeutics (Review). Molecular Medicine Reports. 20(2): 1479-1487. doi: 10.3892/mmr.2019.1037 4 [DOI]

7. De Boer, D., Nguyen, N., Mao, J., Moore, J. and Sorin, E.J., 2021. A Comprehensive Review of Cholinesterase Modeling and Simulation. Biomolecules. 11(4): 580. doi: 10.3390/biom11040580 [DOI]

8. Zare-Zardini, H., Tolueinia, B., Hashemi, A., Ebrahimi, L. and Fesahat, F., 2013. Antioxidant and cholinesterase inhibitory activity of a new peptide from Ziziphus jujuba fruits. American Journal of Alzheimer's Disease & Other Dementias®. 28(7): 702-709. doi: 10.1177/1533317513500839 [DOI]

9. Tahmasebi, E., Dastan, D. and Ebadi, A., 2020. Design, synthesis and biological evaluation of anticholinesterase peptides: Fragment-based vs. template-based peptide design. Bioorganic Chemistry. 105: 104351. doi: 10.1016/j.bioorg.2020.104351 [DOI]

10. Deveci, E., Cayan, F., Tel-Cayan, G. and Duru, M.E., 2019. Structural characterization and determination of biological activities for different polysaccharides extracted from tree mushroom species. Journal of Food Biochemistry. 43(9): e12965. doi: 10.1111/jfbc.12965 [DOI]

11. Prasasty, V., Radifar, M. and Istyastono, E., 2018. Natural Peptides in Drug Discovery Targeting Acetylcholinesterase. Molecules. 23(9): 2344. doi: 10.3390/molecules23092344 [DOI]

12. Moghadasi, Z., 2017. In vitro study on cytotoxic effect of methanolic extract from carpet anemone tentacles against brain and colon cell lines. Journal of Animal Environment. 9(3): 379-384. GSID: B32MFesl63cJ. (In Persian)

13. Pishgouii, F., Lotfi, S. and Sedaghati, E., 2023. Anti AChE and Anti-BuChE Screening of the Fermentation Broth Extracts from Twelve Aspergillus Isolates and GC-MS and Molecular Docking Studies of the Most Active Extracts. Applied Biochemistry and Biotechnology. 195: 5199-5216. doi: 10.1007/s12010-023-04548-0 [DOI]

14. Klose, J., Griehl, C., Rossner, S. and Schilling, S., 2022. Natural Products from Plants and Algae for Treatment of Alzheimer's Disease: A Review. Biomolecules. 12(5): 1-27. doi: 10.3390/biom12050694 [DOI]

15. Fonar, G., Polis, B., Sams, D.S., Levi, A., Malka, A., Bal, N., Maltsev, A., Elliott, E. and Samson, A.O., 2021. Modified Snake alpha-Neurotoxin Averts beta Amyloid Binding to alpha7 Nicotinic Acetylcholine Receptor and Reverses Cognitive Deficits in Alzheimer's Disease Mice. Molecular Neurobiology. 58(5): 2322-2341. doi: 10.1007/s12035-020-02270-0 [DOI]

16. Bellik, Y., 2015. Bee venom: its potential use in alternative medicine. Anti-Infective Agents. 13(1): 3-16. doi: 10.2174/2211352513666150318234624 [DOI]

17. Badawi, J.K., 2021. Bee venom components as therapeutic tools against prostate cancer. Toxins. 13(5): 337. doi: 10.3390/toxins13050337 [DOI]

18. Ye, M., Chung, H.S., Lee, C., Yoon, M.S., Yu, A.R., Kim, J.S., Hwang, D.S., Shim, I. and Bae, H., 2016. Neuroprotective effects of bee venom phospholipase A2 in the 3xTg AD mouse model of Alzheimer’s disease. Journal of Neuroinflammation. 13: 1-12. doi: 10.1186/s12974-016-0476-z [DOI]

19. Zhang, S., Liu, Y., Ye, Y., Wang, X.R., Lin, L.T., Xiao, L.Y., Zhou, P., Shi, G.X. and Liu, C.Z., 2018. Bee venom therapy: Potential mechanisms and therapeutic applications. Toxicon. 148: 64-73. doi: 10.1016/j.toxicon.2018.04.012 [DOI]

20. Hwang, D.S., Kim, S.K. and Bae, H., 2015. Therapeutic effects of bee venom on immunological and neurological diseases. Toxins. 7(7): 2413-2421. doi: 10.3390/toxins7072413 [DOI]

21. Shawrang, P., Abbasi, F., Motamedi sede, F. and Sadeghi, M., 2023. Antimicrobial and anti-inflammatory properties of gamma irradiated honey bee venom. Journal of Animal Environment. 15(3): 321-328. doi: 10.22034/AEJ.2022.362124.2884 (In Persian) [DOI]

22. Abd El-Wahed, A.A., Khalifa, S.A.M., Sheikh, B.Y., Farag, M.A., Saeed, A., Larik, F.A., Koca-Caliskan, U., AlAjmi, M.F., Hassan, M., Wahabi, H.A., Hegazy, M.-E.F., Algethami, A.F., Büttner, S. and El-Seedi, H.R., 2019. Chapter 13 - Bee Venom Composition: From Chemistry to Biological Activity. In: Atta ur R, editor. Studies in Natural Products Chemistry. 60: 459-484. doi: 10.1016/B978-0-444-64181-6.00013-9 [DOI]

23. Proulx, É., Power, S., Oliver, D., Sargin, D., McLaurin, J. and Lambe, E., 2020. Apamin improves prefrontal nicotinic impairment in mouse model of Alzheimer’s disease. Cerebral Cortex. 30(2): 563-574. doi: 10.1093/cercor/bhz107 [DOI]

24. Gu, H., Han, S.M. and Park, K.-K., 2020. Therapeutic effects of apamin as a bee venom component for non neoplastic disease. Toxins. 12(3): 195. doi: 10.3390/toxins12030195 [DOI]

25. Kim, K.H., Lee, S.Y., Shin, J., Hwang, J.T., Jeon, H.N. and Bae, H., 2019. Dose-dependent neuroprotective effect of standardized bee venom phospholipase A2 against MPTP-induced Parkinson’s disease in mice. Frontiers in Aging Neuroscience. 11: 80. doi: 10.3389/fnagi.2019.00080 [DOI]

26. Wehbe, R., Frangieh, J., Rima, M., El Obeid, D., Sabatier, J.M. and Fajloun, Z., 2019. Bee venom: Overview of main compounds and bioactivities for therapeutic interests. Molecules. 24(16): 2997. doi: 10.3390/molecules24162997 [DOI]

27. Ku, Y.H., Kang, J.H. and Lee, H., 2020. Effect of bee venom on an experimental cellular model of Alzheimer’s disease. The American Journal of Chinese Medicine. 48(08): 1803-1819. doi: 10.1142/S0192415X20500895 [DOI]

28. Ellman, G.L., Courtney, K.D., Andres, V.Jr. and Feather Stone, R.M., 1961. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochemical Pharmacology. 7: 88-95. doi: 10.1016/0006-2952(61)90145-9 [DOI]

29. Honorato, R.V., Koukos, P.I., Jimenez-Garcia, B., Tsaregorodtsev, A., Verlato, M., Giachetti, A., Rosato, A. and Bonvin, A., 2021. Structural Biology in the Clouds: The WeNMR-EOSC Ecosystem. Frontiers in Molecular Biosciences. 8: 729513. doi: 10.3389/fmolb.2021.729513 [DOI]

30. Burley, S.K., Bhikadiya, C., Bi, C., Bittrich, S., Chen, L., Crichlow, G.V., Christie, C.H., Dalenberg, K., Di Costanzo, L., Duarte, J.M., Dutta, S., Feng, Z., Ganesan, S., Goodsell, D.S., Ghosh, S., Green, R.K., Guranovic, V., Guzenko, D., Hudson, B.P., Lawson, C.L., Liang, Y., Lowe, R., Namkoong, H., Peisach, E., Persikova, I., Randle, C., Rose, A., Rose, Y., Sali, A., Segura, J., Sekharan, M., Shao, C., Tao, Y.P., Voigt, M., Westbrook, J.D., Young, J.Y., Zardecki, C. and Zhuravleva, M., 2021. RCSB Protein Data Bank: powerful new tools for exploring 3D structures of biological macromolecules for basic and applied research and education in fundamental biology, biomedicine, biotechnology, bioengineering and energy sciences. Nucleic Acids Research. 49(D1): D437-D451. doi: 10.1093/nar/gkaa1038 [DOI]

31. Waterhouse, A., Bertoni, M., Bienert, S., Studer, G., Tauriello, G., Gumienny, R., Heer, F.T., de Beer, T.A.P., Rempfer, C., Bordoli, L., Lepore, R. and Schwede, T., 2018. SWISS-MODEL: homology modelling of protein structures and complexes. Nucleic Acids Research. 46(W1): W296-W303. doi: 10.1093/nar/gky427 [DOI]

32. Laskowski, R.A. and Swindells, M.B., 2011. LigPlot+: multiple ligand-protein interaction diagrams for drug discovery. Journal of Chemical Information and Modeling. 51(10): 2778-2786. doi: 10.1021/ci200227u [DOI]

33. Van Zundert, G., Rodrigues, J., Trellet, M., Schmitz, C., Kastritis, P., Karaca, E., Melquiond, A., van Dijk, M., De Vries, S. and Bonvin, A., 2016. The HADDOCK 2.2 web server: user-friendly integrative modeling of biomolecular complexes. Journal of Molecular Biology. 428(4): 720-725. doi: 10.1016/j.jmb.2015.09.014 [DOI]

34. Wallace, A.C., Laskowski, R.A. and Thornton, J.M., 1995. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Engineering, Design and Selection. 8(2): 127-134. doi: 10.1016/j.jmb.2015.09.014 [DOI]

35. Shi, P., Xie, S., Yang, J., Zhang, Y., Han, S., Su, S. and Yao, H., 2022. Pharmacological effects and mechanisms of bee venom and its main components: recent progress and perspective. Frontiers in Pharmacology. 13: 1001553. doi: 10.3389/fphar.2022.1001553 [DOI]

36. Yoo, S.S., Han, S.B., Yun, J., Yeo, I.J. and Ham, H.J., 2023. Bee Venom Phospholipase A2 Reduces Tau Phosphorylation through Inhibition of GSK3β Expression. Journal of Biotechnology and Biomedicine. 6: (2). 202-213. doi: 10.26502/jbb.2642-91280084 [DOI]

37. Elumalai, V., Trobec, T., Grundner, M., Labriere, C., Frangež, R., Sepčić, K., Hansen, J.H. and Svenson, J., 2022. Development of potent cholinesterase inhibitors based on a marine pharmacophore. Organic & Biomolecular Chemistry. 20(28): 5589-5601. doi: 10.1039/D2OB01064J [DOI]

38. Asen, N.D., Okagu, O.D., Udenigwe, C.C. and Aluko, R.E., 2022. In vitro inhibition of acetylcholinesterase activity by yellow field pea (Pisum sativum) protein derived peptides as revealed by kinetics and molecular docking. Frontiers in Nutrition 9: 1021893. doi: 10.3389/ fnut.2022.1021893 [DOI]

39. Sanchis, I., Spinelli, R., Dias, J., Brazzolotto, X., Rietmann, A., Aimaretti, F. and Siano, A.S., 2023. Inhibition of Human Cholinesterases and in vitro beta Amyloid Aggregation by Rationally Designed Peptides. ChemMedChem. 18(12): e202200691. doi: 10.1002/cmdc.202200691 [DOI]

40. Ji, D., Ma, J., Dai, J., Xu, E., Harris, P., Brimble, M. and Agyei, D., 2022. Anticholinesterase Inhibition, Drug Likeness Assessment, and Molecular Docking Evaluation of Milk Protein-Derived Opioid Peptides for the Control of Alzheimer’s Disease. Dairy. 3(3): 422-437. doi: 10.3390/dairy3030032 [DOI]

41. Sanchis, I., Spinelli, R., Aschemacher, N. and Siano, A.S., 2022. Rational design and synthesis of modified natural peptides from Boana pulchella (anura) as acetylcholinesterase inhibitors and antioxidants. Amino Acids. 54(2): 181-192. doi: 10.1007/s00726-021-03096-3 [DOI]

42. Kulshreshtha, A. and Piplani, P., 2016. Current pharmacotherapy and putative disease-modifying therapy for Alzheimer's disease. Neurological Sciences. 37: 1403-1435. doi: 10.1007/s10072-016-2625-7 [DOI]

43. Johnson, G. and Moore, S.W., 2006. The peripheral anionic site of acetylcholinesterase: structure, functions and potential role in rational drug design. Current Pharmaceutical Design. 12(2): 217-225. doi: 10.2174/138161206775193127 [DOI]

44. Dvir, H., Silman, I., Harel, M., Rosenberry, T.L. and Sussman, J.L., 2010. Acetylcholinesterase: from 3D structure to function. Chemico-Biological Interactions. 187(1-3): 10-22. doi: 10.1016/j.cbi.2010.01.042 [DOI]

45. Agatonovic-Kustrin, S., Kettle, C. and Morton, D.W., 2018. A molecular approach in drug development for Alzheimer's disease. Biomedicine & Pharmacotherapy. 106: 553-565. doi: 10.1016/j.biopha.2018.06.147 [DOI]

46. Macdonald, I.R., Martin, E., Rosenberry, T.L. and Darvesh, S., 2012. Probing the peripheral site of human butyrylcholinesterase. Biochemistry. 51(36): 7046-7053. doi: 10.1021/bi300955k [DOI]