The DOI matches its Crossref record; 203 of the 210 references it cites were found in a registry or an index.
Acetylcholinesterase inhibitors as Alzheimer therapy: From nerve toxins to neuroprotection
Abstract
Acetylcholinesterase is a member of the α/β hydrolase protein super family, with a significant role in acetylcholine-mediated neurotransmission. Research in the modulators of AChEs has moved from a potent poison (Sarin, Soman) in war times to the potent medicine (physostigmine) in peaceful times. Natural anti-AChE includes carbamates, glycoalkaloids, anatoxins derived from green algae; synthetic anti-AChE includes highly poisonous organophosphates used as nerve gases and insecticides. Recently, the role of anti-AChE was reassessed from neurotoxins to neuron-protective in the diseases characterized by impaired acetylcholine-mediated neurotransmission like Alzheimer's disease (AD). So, the AChE has been proven to be the most viable therapeutic target for the symptomatic treatment of AD. This review article gives a spectrum of strategies to design AChE inhibitors used in the Alzheimer therapy.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“In addition, the enzyme plays a role in the production of amyloid plaques and neurofibrillary tangles.”
From An update on the novel and approved drugs for Alzheimer disease (2022) · cites this paper as Singh et al., 2013
In the citing paper
“the positive effect of galantamine in restoring certain normal behavioral traits could result from its acetylcholinesterase inhibitor activity.”
From Galantamine Slows Down Plaque Formation and Behavioral Decline in the 5XFAD Mouse Model of Alzheimer’s Disease (2014) · cites this paper as [54]
In the citing paper
“acetylcholinesterase has been shown to promote the aggregation of β-amyloid peptide fragments by forming a complex with the growing fibrils [54].”
From Galantamine Slows Down Plaque Formation and Behavioral Decline in the 5XFAD Mouse Model of Alzheimer’s Disease (2014) · cites this paper as [54]
In the citing paper
“According to the cholinergic hypothesis, a decreased production of acetylcholine or an amplified acetylcholinesterase activity results in impairment of the cholinergic transmission, in turn leading to the loss of intellectual abilities [54].”
From Galantamine Slows Down Plaque Formation and Behavioral Decline in the 5XFAD Mouse Model of Alzheimer’s Disease (2014) · cites this paper as [54]
Citations
Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404
Memory systems of the brain: A brief history and current perspective
Squire, L. R. (2004) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2004.06.005 · Cited by 2,269
Diabetes mellitus and the risk of dementia: The Rotterdam Study
Ott, A., Stolk, R. P., van Harskamp, F., Pols, H. A. P., Hofman, A., & Breteler, M. M. B. (1999) · Neurology · doi:10.1212/wnl.53.9.1937 · Cited by 2,175
A Century of Alzheimer's Disease
Goedert, M., & Spillantini, M. G. (2006) · Science · doi:10.1126/science.1132814 · Cited by 2,153
Memantine in Moderate-to-Severe Alzheimer's Disease
Reisberg, B., Doody, R., Stöffler, A., Schmitt, F., Ferris, S., & Möbius, H. J. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa013128 · Cited by 2,043
General Nature of the Genetic Code for Proteins
Crick, F. H. C., Barnett, L., Brenner, S., & Watts-Tobin, R. J. (1961) · Nature · doi:10.1038/1921227a0 · Cited by 1,392
Oral Tetrahydroaminoacridine in Long-Term Treatment of Senile Dementia, Alzheimer Type
Summers, W. K., Majovski, L. V., Marsh, G. M., Tachiki, K. H., & Kling, A. S. (1986) · New England Journal of Medicine · doi:10.1056/nejm198611133152001 · Cited by 1,161
Inestrosa, N. C., Alvarez, A. R., Pérez, C. A., Moreno, R. D., Vicente, M., Linker, C., Casanueva, O. I., Soto, C. A., & Garrido, J. (1996) · Neuron · doi:10.1016/s0896-6273(00)80108-7 · Cited by 1,117
Microglia: Intrinsic immuneffector cell of the brain
Gehrmann, J., Matsumoto, Y., & Kreutzberg, G. W. (1995) · Brain Research Reviews · doi:10.1016/0165-0173(94)00015-h · Cited by 1,111
Research works printed but not linked: 4
- Alzheimer, 1907, Over a eigenartigo disease of the cerebral cortex, Allg. Z. Psychiat., 64, 146
- Proskurnina, 1957, Oral solution containing galanthamine and a sweetening agent, J. Gen. Chem., 22, 1899
- Bores, 1996, Galanthamine derivatives for the treatment of Alzheimer's disease, Drugs Future, 21, 621
- Zhan, 2011, Synthesis of physostigmine analogues and evaluation of their anticholinesterase activities, Bioorg. Med. Chem. Lett., 20, 1532, 10.1016/j.bmcl.2010.01.097 · DOI
Cited by
Sorted by citations
Oxindole: A chemical prism carrying plethora of therapeutic benefits
Kaur, M., Singh, M., Chadha, N., & Silakari, O. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.08.011 · Cited by 353
Sharma, P., Srivastava, P., Seth, A., Tripathi, P. N., Banerjee, A. G., & Shrivastava, S. K. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.006 · Cited by 331
Li, S., Zhang, H., Zhu, M. Z., Kuang, Z., Li, X., Xu, F., Miao, S., Zhang, Z., Lou, X., Li, H., et al. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00759 · Cited by 324
Molecular mechanisms underlying protective role of quercetin in attenuating Alzheimer's disease
Zaplatić, E., Bule, M. H., Shah, S. Z. A., Uddin, M. S., & Niaz, K. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.03.055 · Cited by 306
A critical review on the health benefits of fish consumption and its bioactive constituents
Chen, J., Jayachandran, M., Bai, W., & Xu, B. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.130874 · Cited by 336
Organophosphate pesticide exposure and neurodegeneration
Sánchez-Santed, F., Colomina, M. T., & Hernández, E. H. (2015) · Cortex · doi:10.1016/j.cortex.2015.10.003 · Cited by 258
Neuroprotective Natural Products for Alzheimer’s Disease
Chen, X., Drew, J., Berney, W., & Lei, W. (2021) · Cells · doi:10.3390/cells10061309 · Cited by 236
Fluorescent Diagnostic Probes in Neurodegenerative Diseases
Zhou, J., Jangili, P., Son, S., Ji, M. S., Won, M., & Kim, J. S. (2020) · Advanced Materials · doi:10.1002/adma.202001945 · Cited by 204
The present and future of pharmacotherapy of Alzheimer's disease: a comprehensive review
Anand, A., Patience, A. A., Sharma, N., & Khurana, N. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.09.043 · Cited by 174
Neuroprotective Effect of Cardamom Oil Against Aluminum Induced Neurotoxicity in Rats
Auti, S. T., & Kulkarni, Y. A. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.00399 · Cited by 152
Bhattacharya, S., Haertel, C., Maelicke, A., & Montag, D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089454 · Cited by 142
Harrad, L. E., Bourais, I., Mohammadi, H., & Amine, A. (2018) · Sensors · doi:10.3390/s18010164 · Cited by 141
Topal, G. R., Mészáros, M., Porkoláb, G., Szecskó, A., Polgár, T. F., Siklós, L., Deli, M. A., Veszelka, S., & Bozkır, A. (2020) · Pharmaceutics · doi:10.3390/pharmaceutics13010038 · Cited by 133
Jiang, Y., Gao, H., & Turdu, G. (2017) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2017.09.004 · Cited by 128
Anti-cholinesterase hybrids as multi-target-directed ligands against Alzheimer’s disease (1998–2018)
Mishra, P., Kumar, A., & Panda, G. (2019) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.01.025 · Cited by 130
Rahman, S. O., Panda, B. P., Parvez, S., Kaundal, M., Hussain, S., Akhtar, M., & Najmi, A. K. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.11.043 · Cited by 131
Aroniadou‐Anderjaska, V., Apland, J. P., Figueiredo, T. H., Furtado, M. D. A., & Braga, M. F. M. (2020) · Neuropharmacology · doi:10.1016/j.neuropharm.2020.108298 · Cited by 131
Yang, T., Xiao, T., Sun, Q. L., & Wang, K. (2017) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2017.09.001 · Cited by 127
An update on the novel and approved drugs for Alzheimer disease
Alhazmi, H. A., & Albratty, M. (2022) · Saudi Pharmaceutical Journal · doi:10.1016/j.jsps.2022.10.004 · Cited by 122
Taslımı, P., Işık, M., Türkan, F., Durgun, M., Türkeş, C., Gülçın, İ., & Beydemir, Ş. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1790422 · Cited by 115
Wang, S., Sun‐Waterhouse, D., Waterhouse, G. I. N., Zheng, L. P., Su, G., & Zhao, M. (2021) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2021.04.056 · Cited by 113
Effects of Tea Catechins on Alzheimer’s Disease: Recent Updates and Perspectives
Ide, K., Matsuoka, N., Yamada, H., Furushima, D., & Kawakami, K. (2018) · Molecules · doi:10.3390/molecules23092357 · Cited by 103
Wojtunik‐Kulesza, K. A., Oniszczuk, A., & Waksmundzka‐Hajnos, M. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.12.140 · Cited by 101
Success stories of natural product-based hybrid molecules for multi-factorial diseases
Choudhary, S., Singh, P. K., Verma, H., Singh, H., & Silakari, O. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.03.057 · Cited by 104
Borai, I. H., Ezz, M. K., Rizk, M. Z., Aly, H. F., El-Sherbiny, M., Matloub, A. A., & Fouad, G. I. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.07.038 · Cited by 98
Postu, P. A., Sadiki, F. Z., Idrissi, M. E., Cioancă, O., Trifan, A., Hăncianu, M., & Hriţcu, L. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.108673 · Cited by 92
Wang, S., Su, G., Zhang, X., Song, G., Zhang, L., Zheng, L. P., & Zhao, M. (2021) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.0c07798 · Cited by 92
In Vitro Acetylcholinesterase-Inhibitory Properties of Enzymatic Hemp Seed Protein Hydrolysates
Malomo, S., & Aluko, R. (2016) · Journal of the American Oil Chemists Society · doi:10.1007/s11746-015-2779-0 · Cited by 77
Górecki, L., Korábečný, J., Musílek, K., Maliňák, D., Nepovimová, E., Doležal, R., Jun, D., Soukup, O., & Kuča, K. (2016) · Archives of Toxicology · doi:10.1007/s00204-016-1827-3 · Cited by 89
Classics in Chemical Neuroscience: Donepezil
Brewster, J. T., Dell’Acqua, S., Thach, D. Q., & Sessler, J. L. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00517 · Cited by 94
Hybrids: a new paradigm to treat Alzheimer’s disease
Singh, M., Kaur, M., Chadha, N., & Silakari, O. (2015) · Molecular Diversity · doi:10.1007/s11030-015-9628-9 · Cited by 85
Tahir, S., Ramzan, M. S., Hassan, A., Sadiq, A., Jan, M. S., Khan, F. A., Ullah, F., Ahmad, H., Bibi, M., Mahmood, T., et al. (2018) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2018.10.035 · Cited by 84
Hùng, N. H., Quân, P. M., Satyal, P., Đài, Đ. N., Hoa, V. V., Ngo, G. H., An, N. T. G., Hà, N. T. T., Huong, L. T., Hien, V. T., et al. (2022) · Molecules · doi:10.3390/molecules27207092 · Cited by 86
Ghumatkar, P. J., Patil, S. P., Jain, P. D., Tambe, R., & Sathaye, S. S. (2015) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2015.06.005 · Cited by 87
Arylidene indanone scaffold: medicinal chemistry and structure–activity relationship view
Menezes, J. C. J. M. D. S. (2017) · RSC Advances · doi:10.1039/c6ra28613e · Cited by 83
Palanimuthu, D., Poon, R., Sahni, S., Anjum, R., Hibbs, D. E., Lin, H.-Y. J., Bernhardt, P. V., Kalinowski, D. S., & Richardson, D. R. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.08.021 · Cited by 82
Işık, M., Demir, Y., Durgun, M., Türkeş, C., Necip, A., & Beydemir, Ş. (2019) · Chemical Papers · doi:10.1007/s11696-019-00988-3 · Cited by 77
Current pharmacotherapy and putative disease-modifying therapy for Alzheimer’s disease
Kulshreshtha, A., & Piplani, P. (2016) · Neurological Sciences · doi:10.1007/s10072-016-2625-7 · Cited by 76
Manzoor, S., Prajapati, S. K., Majumdar, S., Raza, M. K., Gabr, M. T., Kumar, S., Pal, K., Rashid, H. U., Kumar, S., Krishnamurthy, S., et al. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113224 · Cited by 79
Roldán-Peña, J. M., Alejandre-Ramos, D., López, Ó., Maya, I., Lagunes, I., Padrón, J. M., Peña‐Altamira, E., Bartolini, M., Monti, B., Bolognesi, M. L., et al. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.06.048 · Cited by 75
Sánchez-Martínez, J. D., Valdés, A., Gallego, R., Suárez-Montenegro, Z. J., Alarcón, M., Ibáñez, E., Álvarez‐Rivera, G., & Cifuentes, A. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.924596 · Cited by 81
Pudlo, M., Luzet, V., Ismaïli, L., Tomassoli, I., Iutzeler, A., & Refouvelet, B. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2014.02.046 · Cited by 73
Chowdhury, A. A., Gawali, N. B., Munshi, R., & Juvekar, A. R. (2017) · Metabolic Brain Disease · doi:10.1007/s11011-017-0147-5 · Cited by 76
Huang, G., Kling, B., Darras, F. H., Heilmann, J., & Decker, M. W. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.05.002 · Cited by 72
Taveira, M., Sousa, C., Valentão, P., Ferreres, F., Teixeira, J. P., & Andrade, P. B. (2013) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2013.12.013 · Cited by 70
Heo, J. H., Eom, B. H., Ryu, H. W., Kang, M.-G., Park, J. E., Kim, D.-Y., Kim, J., Park, D., Oh, S., & Kim, H. (2020) · Scientific Reports · doi:10.1038/s41598-020-78782-5 · Cited by 68
Ameliorative Effect of Silymarin on Scopolamine-induced Dementia in Rats
El‐Marasy, S. A., Abd‐Elsalam, R. M., & Ahmed-Farid, O. A.-H. (2018) · Open Access Macedonian Journal of Medical Sciences · doi:10.3889/oamjms.2018.257 · Cited by 66
Ahnaou, A., Huysmans, H., Jacobs, T., & Drinkenburg, W. H. I. M. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.08.015 · Cited by 64
Singh, V., Kahol, A., Singh, I. P., Saraf, I., & Shri, R. (2016) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2016.10.026 · Cited by 64
Natural Peptides in Drug Discovery Targeting Acetylcholinesterase
Prasasty, V. D., Radifar, M., & Istyastono, E. P. (2018) · Molecules · doi:10.3390/molecules23092344 · Cited by 65
Mechanisms of Non-coenzyme Action of Thiamine: Protein Targets and Medical Significance
Aleshin, V. A., Mkrtchyan, G. V., & Bunik, V. I. (2019) · Biochemistry (Moscow) · doi:10.1134/s0006297919080017 · Cited by 61
Knez, D., Brus, B., Coquelle, N., Sosič, I., Šink, R., Brazzolotto, X., Mravljak, J., Colletier, J., & Gobec, S. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.06.010 · Cited by 60
Liu, Y., Feng, Y.-D., Lu, X. L., Nie, J., Li, W., Wang, L., Tian, L.-J., & Liu, Q. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.06.007 · Cited by 58
Darras, F. H., Wehle, S., Huang, G., Sotriffer, C., & Decker, M. W. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2014.06.045 · Cited by 58
Chowdhury, A. A., Gawali, N. B., Shinde, P., Munshi, R., & Juvekar, A. R. (2018) · Cytokine · doi:10.1016/j.cyto.2018.04.018 · Cited by 57
Volatile terpenoids as potential drug leads in Alzheimer’s disease
Wojtunik‐Kulesza, K. A., Targowska‐Duda, K. M., Klimek, K., Ginalska, G., Jóźwiak, K., Waksmundzka‐Hajnos, M., & Ciesla, L. M. (2017) · Open Chemistry · doi:10.1515/chem-2017-0040 · Cited by 55
Kamli, M. R., Sharaf, A. A. M., Sabir, J. S. M., & Rather, I. A. (2022) · Plants · doi:10.3390/plants11040514 · Cited by 55
Fat-soluble vitamins in patients with chronic pancreatitis (pancreatic insufficiency).
Nakamura, T., Takebe, K., Imamura, K., Tando, Y., Yamada, N., Arai, Y., Terada, A., Ishii, M., Kikuchi, H., & Suda, T. (1996) · PubMed · Cited by 52
van Greunen, D. G., Cordier, W., Nell, M. J., van der Westhuyzen, C. W., Steenkamp, V., Panayides, J., & Riley, D. L. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.10.036 · Cited by 51
Sośnicki, J. G., & Idzik, T. J. (2019) · Synthesis · doi:10.1055/s-0037-1611844 · Cited by 51
Fouad, G. I. (2020) · Neurochemical Research · doi:10.1007/s11064-020-02996-2 · Cited by 51
Zaib, S., Munir, R., Younas, M. T., Kausar, N., Ibrar, A., Aqsa, S., Shahid, N., Asif, T. T., Alsaab, H. O., & Khan, I. A. (2021) · Molecules · doi:10.3390/molecules26216573 · Cited by 49
Food‐derived Acetylcholinesterase Inhibitors as Potential Agents against Alzheimer’s Disease
Aluko, R. E. (2021) · eFood · doi:10.2991/efood.k.210318.001 · Cited by 52
Ganeshpurkar, A., Singh, R., Gore, P., Kumar, D., Gutti, G., Kumar, A., & Singh, S. K. (2019) · Molecular Simulation · doi:10.1080/08927022.2019.1682572 · Cited by 48
Zang, C., Bao, X.-Q., Li, L., Yang, H., Wang, L., Yu, Y., Wang, X., Yao, X., & Zhang, D. (2018) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x18500192 · Cited by 47
Saeedi, M., Maleki, A., Iraji, A., Hariri, R., Akbarzadeh, T., Edraki, N., Firuzi, O., & Mirfazli, S. S. (2020) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2020.129828 · Cited by 47
Liu, Y., Uras, G., Onuwaje, I., Li, W., Yao, H., Xu, S., Li, X., Li, X., Phillips, J. B., Allen, S., et al. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114305 · Cited by 46
Shou, J., & Shaw, P. (2022) · Cells · doi:10.3390/cells11050796 · Cited by 48
Zhan, G., Liu, J., Zhou, J., Sun, B., Aisa, H. A., & Yao, G. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.10.057 · Cited by 45
Recent Advances in Multi-target Anti-Alzheimer Disease Compounds (2013 Up to the Present)
Wang, N., Qiu, P., Cui, W., Yan, X., Zhang, B., & He, S. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867326666181203124102 · Cited by 45
Plant‐derived bioactive peptides: A comprehensive review
Kadam, D., Kadam, A., Köksel, F., & Aluko, R. E. (2024) · Sustainable Food Proteins · doi:10.1002/sfp2.1036 · Cited by 47
Singh, R. S., Singh, T., & Singh, A. K. (2019) · Elsevier eBooks · doi:10.1016/b978-0-444-64114-4.00009-1 · Cited by 45
Potential of flavonoids as anti-Alzheimer’s agents: bench to bedside
Kaur, R., Sood, A., Lang, D. K., Bhatia, S., Al‐Harrasi, A., Aleya, L., & Behl, T. (2022) · Environmental Science and Pollution Research · doi:10.1007/s11356-021-18165-z · Cited by 45
Molecular Insights into Therapeutic Potentials of Hybrid Compounds Targeting Alzheimer’s Disease
Jana, A., Bhattacharjee, A., Das, S. S., Srivastava, A., Choudhury, A., Bhattacharjee, R., De, S., Perveen, A., Iqbal, D., Gupta, P. K., et al. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02779-6 · Cited by 46
Wang, S., Su, G., Fan, J., Xiao, Z., Zheng, L. P., Zhao, M., & Wu, J. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c05104 · Cited by 43
Botić, T., Defant, A., Zanini, P., Žužek, M. C., Frangež, R., Janussen, D., Kersken, D., Knez, Ž., Mancini, I., & Sepčić, K. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.05.019 · Cited by 43
Therapeutic Effects of Natural Drugs on Alzheimer’s Disease
Ma, Y., Yang, M., Li, X., Yue, J.-W., Chen, J., Yang, M.-W., Huang, X., Zhu, L., Hong, F., & Yang, S. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01355 · Cited by 43
Taha, M., Alshamrani, F., Rahim, F., Anouar, E. H., Uddin, N., Chigurupati, S., Almandil, N. B., Farooq, R. K., Iqbal, N., Aldubayan, M. A., et al. (2021) · Journal of King Saud University - Science · doi:10.1016/j.jksus.2021.101401 · Cited by 43
Chauhan, N., Narang, J., & Jain, U. (2015) · The Analyst · doi:10.1039/c4an01873g · Cited by 42
Lee, M., Im, W., & Kim, M. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105374 · Cited by 44
Gene Therapy for Huntington’s Disease: The Final Strategy for a Cure?
Byun, S., Lee, M., & Kim, M. (2021) · Journal of Movement Disorders · doi:10.14802/jmd.21006 · Cited by 42
Yerdelen, K. Ö., & Tosun, E. (2014) · Medicinal Chemistry Research · doi:10.1007/s00044-014-1152-4 · Cited by 40
Asen, N. D., & Aluko, R. E. (2022) · Journal of Food Biochemistry · doi:10.1111/jfbc.14289 · Cited by 41
Bhattacharya, S., Maelicke, A., & Montag, D. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-142421 · Cited by 39
Synthesis and biological evaluation of 3-arylcoumarins as potential anti-Alzheimer's disease agents
Yang, J. W., Zhang, P., Hu, Y., Liu, T., Sun, J., & Wang, X. (2019) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2019.1574297 · Cited by 39
Kinetics of acetylcholinesterase inhibition by hemp seed protein‐derived peptides
Malomo, S. A., & Aluko, R. E. (2019) · Journal of Food Biochemistry · doi:10.1111/jfbc.12897 · Cited by 42
Paudel, P., Seong, S. H., Zhou, Y., Park, H. J., Jung, H. A., & Choi, J. S. (2019) · ACS Omega · doi:10.1021/acsomega.9b01557 · Cited by 40
Zhao, L., Yang, G. H., Li, L., Zhu, C., Ma, Y., & Qu, F. (2020) · Analytica Chimica Acta · doi:10.1016/j.aca.2020.10.024 · Cited by 38
Mitić, M., & Pašti, T. D. L. (2021) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1080/17425255.2021.1931681 · Cited by 39
Elmaidomy, A. H., Abdelmohsen, U. R., Alsenani, F., Aly, H. F., Shams, S. G. E., Younis, E. A., Ahmed, K. A., Sayed, A. M., Owis, A. I., Afifi, N., et al. (2022) · RSC Advances · doi:10.1039/d2ra01340a · Cited by 38
RetractedChowdhury, A. A., Gawali, N. B., Bulani, V. D., Kothavade, P. S., Mestry, S. N., Deshpande, P. S., & Juvekar, A. R. (2017) · Pharmacological Reports · doi:10.1016/j.pharep.2017.09.006 · Cited by 37
Chauhan, N., Balayan, S., & Jain, U. (2020) · Synthetic Metals · doi:10.1016/j.synthmet.2020.116354 · Cited by 37
Qi, C., Qiao, Y., Gao, W., Liu, M., Zhou, Q. Y., Chen, C., Lai, Y., Xue, Y., Zhang, J., Li, D., et al. (2018) · Organic & Biomolecular Chemistry · doi:10.1039/c8ob02741b · Cited by 36
van Greunen, D. G., van der Westhuizen, C. J., Cordier, W., Nell, M. J., Stander, A., Steenkamp, V., Panayides, J., & Riley, D. L. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.06.088 · Cited by 36
Rat hormone sensitive lipase inhibition by cyclipostins and their analogs
Vasilieva, E., Dutta, S., Malla, R. K., Martin, B. P., Spilling, C. D., & Dupureur, C. M. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.01.028 · Cited by 34
Singh, M., & Silakari, O. (2016) · RSC Advances · doi:10.1039/c6ra17678j · Cited by 34
Namdaung, U., Athipornchai, A., Khammee, T., Kuno, M., & Suksamrarn, S. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.10.019 · Cited by 34
Iranshahy, M., & Javadi, B. (2019) · PubMed Central · doi:10.22038/ijbms.2019.36505.8694 · Cited by 34
Fernández‐Bolaños, J. G., & López, Ó. (2022) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2022.2083956 · Cited by 35
Abdelwahab, H. E., Ibrahim, H. Z., & Omar, A. Z. (2022) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2022.134137 · Cited by 34
Metadata
- Authors
- Singh, M., Kaur, M., Kukreja, H., Chugh, R., Silakari, O., & Singh, D.
- Affiliations
- Panjab University (IN)
- Corresponding author
- Singh, Dhandeep
- Venue
- European Journal of Medicinal Chemistry
- Publisher
- Elsevier BV
- Published
- 2013-12
- Volume
- 70
- Pages
- 165-188
- ISSN
- 0223-5234 (ISSN-L)
- OpenAlex
- W1994264985
- Cited by
- 364
- References
- 210
- Citations by year
- 2026: 12 · 2025: 30 · 2024: 31 · 2023: 34 · 2022: 35 · 2021: 29 · 2020: 32 · 2019: 36 · 2018: 30 · 2017: 31 · 2016: 21 · 2015: 23 · 2014: 17 · 2013: 1
- FWCI
- 2.90
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- European Journal of Medicinal Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Pharmacology (medical) › Cholinesterase and Neurodegenerative Diseases
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Pesticide Exposure and Toxicity
- Keywords
- acetylcholinesterase inhibitors, Alzheimer's disease, acetylcholinesterase, cholinergic neurotransmission, organophosphorus nerve agents, carbamate insecticides, physostigmine, glycoalkaloids, anatoxin, neuroprotection, drug design strategies, alpha/beta hydrolase superfamily
- MeSH terms
- Acetylcholinesterase, Alzheimer Disease, Animals, Cholinesterase Inhibitors, Humans, Drug Design, Molecular Structure
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review