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Fine Tuning of Cholinesterase and Glutathione-S-Transferase Activities by Organoruthenium(II) Complexes.

Biomedicines

Trobec T, Sepčić K, Žužek MC, Kladnik J, Podjed N, Cardoso Páscoa C, Turel I, Frangež R.
PMID: 34572429
Biomedicines. 2021 Sep 16;9(9). doi: 10.3390/biomedicines9091243.

Cholinesterases (ChEs) show increased activities in patients with Alzheimer's disease, and remain one of the main therapeutic targets for treatment of this neurodegenerative disorder. A library of organoruthenium(II) complexes was prepared to investigate the influence of their structural elements...

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Trobec T, Sepčić K, Žužek MC, et al. Fine Tuning of Cholinesterase and Glutathione-S-Transferase Activities by Organoruthenium(II) Complexes. Biomedicines. 2021;9(9)doi: 10.3390/biomedicines9091243.
Trobec, T., Sepčić, K., Žužek, M. C., Kladnik, J., Podjed, N., Cardoso Páscoa, C., Turel, I., & Frangež, R. (2021). Fine Tuning of Cholinesterase and Glutathione-S-Transferase Activities by Organoruthenium(II) Complexes. Biomedicines, 9(9), . https://doi.org/10.3390/biomedicines9091243
Trobec, Tomaž, et al. "Fine Tuning of Cholinesterase and Glutathione-S-Transferase Activities by Organoruthenium(II) Complexes." Biomedicines vol. 9,9 (2021). doi: https://doi.org/10.3390/biomedicines9091243
Trobec T, Sepčić K, Žužek MC, Kladnik J, Podjed N, Cardoso Páscoa C, Turel I, Frangež R. Fine Tuning of Cholinesterase and Glutathione-S-Transferase Activities by Organoruthenium(II) Complexes. Biomedicines. 2021 Sep 16;9(9). doi: 10.3390/biomedicines9091243. PMID: 34572429; PMCID: PMC8467340.
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Biochemical and molecular mechanisms of acaricide resistance in Dermanyssus gallinae populations from Turkey.

Pesticide biochemistry and physiology

Koç N, İnak E, Nalbantoğlu S, Alpkent YN, Dermauw W, Van Leeuwen T.
PMID: 34955178
Pestic Biochem Physiol. 2022 Jan;180:104985. doi: 10.1016/j.pestbp.2021.104985. Epub 2021 Nov 13.

The poultry red mite, Dermanyssus gallinae, is the most important blood sucking ectoparasite of egg laying hens and causes economic losses in poultry farms worldwide. Although various management methods exist, the control of poultry red mites (PRMs) mainly relies...

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Koç N, İnak E, Nalbantoğlu S, et al. Biochemical and molecular mechanisms of acaricide resistance in Dermanyssus gallinae populations from Turkey. Pestic Biochem Physiol. 2021;180:104985doi: 10.1016/j.pestbp.2021.104985.
Koç, N., İnak, E., Nalbantoğlu, S., Alpkent, Y. N., Dermauw, W., & Van Leeuwen, T. (2022). Biochemical and molecular mechanisms of acaricide resistance in Dermanyssus gallinae populations from Turkey. Pesticide biochemistry and physiology, 180104985. https://doi.org/10.1016/j.pestbp.2021.104985
Koç, Nafiye, et al. "Biochemical and molecular mechanisms of acaricide resistance in Dermanyssus gallinae populations from Turkey." Pesticide biochemistry and physiology vol. 180 (2022): 104985. doi: https://doi.org/10.1016/j.pestbp.2021.104985
Koç N, İnak E, Nalbantoğlu S, Alpkent YN, Dermauw W, Van Leeuwen T. Biochemical and molecular mechanisms of acaricide resistance in Dermanyssus gallinae populations from Turkey. Pestic Biochem Physiol. 2022 Jan;180:104985. doi: 10.1016/j.pestbp.2021.104985. Epub 2021 Nov 13. PMID: 34955178.
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Studies on the cholinesterases inhibiting compounds from the Cassiopea andromeda venom.

Bioinformation

Darabi AH, Nabipour I, Mohebbi G, Vazirizadeh A, Vatanpour H, Maryamabadi A.
PMID: 34621116
Bioinformation. 2020 Sep 30;16(9):702-709. doi: 10.6026/97320630016702. eCollection 2020.

Cholinesterase inhibitors find application in the combat and care of several diseases, especially AD. Jellyfish venoms are the most promising sources of potent cholinesterase inhibitors. Therefore, it is of interest to study cholinesterases inhibiting compounds from the Cassiopea andromeda...

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Darabi AH, Nabipour I, Mohebbi G, et al. Studies on the cholinesterases inhibiting compounds from the Cassiopea andromeda venom. Bioinformation. 2020;16(9):702-709doi: 10.6026/97320630016702.
Darabi, A. H., Nabipour, I., Mohebbi, G., Vazirizadeh, A., Vatanpour, H., & Maryamabadi, A. (2020). Studies on the cholinesterases inhibiting compounds from the Cassiopea andromeda venom. Bioinformation, 16(9), 702-709. https://doi.org/10.6026/97320630016702
Darabi, Amir Hossein, et al. "Studies on the cholinesterases inhibiting compounds from the Cassiopea andromeda venom." Bioinformation vol. 16,9 (2020): 702-709. doi: https://doi.org/10.6026/97320630016702
Darabi AH, Nabipour I, Mohebbi G, Vazirizadeh A, Vatanpour H, Maryamabadi A. Studies on the cholinesterases inhibiting compounds from the Cassiopea andromeda venom. Bioinformation. 2020 Sep 30;16(9):702-709. doi: 10.6026/97320630016702. eCollection 2020. PMID: 34621116; PMCID: PMC8457019.
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Cholinesterases in Tripartite Neuromuscular Synapse.

Frontiers in molecular neuroscience

Petrov KA, Proskurina SE, Krejci E.
PMID: 35002624
Front Mol Neurosci. 2021 Dec 23;14:811220. doi: 10.3389/fnmol.2021.811220. eCollection 2021.

The neuromuscular junction (NMJ) is a tripartite synapse in which not only presynaptic and post-synaptic cells participate in synaptic transmission, but also terminal Schwann cells (TSC). Acetylcholine (ACh) is the neurotransmitter that mediates the signal between the motor neuron...

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Petrov KA, Proskurina SE, Krejci E. Cholinesterases in Tripartite Neuromuscular Synapse. Front Mol Neurosci. 2021;14:811220doi: 10.3389/fnmol.2021.811220.
Petrov, K. A., Proskurina, S. E., & Krejci, E. (2021). Cholinesterases in Tripartite Neuromuscular Synapse. Frontiers in molecular neuroscience, 14811220. https://doi.org/10.3389/fnmol.2021.811220
Petrov, Konstantin A, et al. "Cholinesterases in Tripartite Neuromuscular Synapse." Frontiers in molecular neuroscience vol. 14 (2021): 811220. doi: https://doi.org/10.3389/fnmol.2021.811220
Petrov KA, Proskurina SE, Krejci E. Cholinesterases in Tripartite Neuromuscular Synapse. Front Mol Neurosci. 2021 Dec 23;14:811220. doi: 10.3389/fnmol.2021.811220. eCollection 2021. PMID: 35002624; PMCID: PMC8733319.
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Combination of donepezil and gallic acid improves antioxidant status and cholinesterases activity in aluminum chloride-induced neurotoxicity in Wistar rats.

Metabolic brain disease

Obafemi TO, Owolabi OV, Omiyale BO, Afolabi BA, Ojo OA, Onasanya A, Adu IAI, Rotimi D.
PMID: 33978901
Metab Brain Dis. 2021 Dec;36(8):2511-2519. doi: 10.1007/s11011-021-00749-w. Epub 2021 May 12.

The present study compared the effect of donepezil only and combination of donepezil and gallic acid on oxidative status and cholinesterase activity in the brain of Wistar rats administered AlCl

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Obafemi TO, Owolabi OV, Omiyale BO, et al. Combination of donepezil and gallic acid improves antioxidant status and cholinesterases activity in aluminum chloride-induced neurotoxicity in Wistar rats. Metab Brain Dis. 2021;36(8):2511-2519doi: 10.1007/s11011-021-00749-w.
Obafemi, T. O., Owolabi, O. V., Omiyale, B. O., Afolabi, B. A., Ojo, O. A., Onasanya, A., Adu, I. A. I., & Rotimi, D. (2021). Combination of donepezil and gallic acid improves antioxidant status and cholinesterases activity in aluminum chloride-induced neurotoxicity in Wistar rats. Metabolic brain disease, 36(8), 2511-2519. https://doi.org/10.1007/s11011-021-00749-w
Obafemi, Tajudeen O, et al. "Combination of donepezil and gallic acid improves antioxidant status and cholinesterases activity in aluminum chloride-induced neurotoxicity in Wistar rats." Metabolic brain disease vol. 36,8 (2021): 2511-2519. doi: https://doi.org/10.1007/s11011-021-00749-w
Obafemi TO, Owolabi OV, Omiyale BO, Afolabi BA, Ojo OA, Onasanya A, Adu IAI, Rotimi D. Combination of donepezil and gallic acid improves antioxidant status and cholinesterases activity in aluminum chloride-induced neurotoxicity in Wistar rats. Metab Brain Dis. 2021 Dec;36(8):2511-2519. doi: 10.1007/s11011-021-00749-w. Epub 2021 May 12. PMID: 33978901.
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Novel bipharmacophoric inhibitors of the cholinesterases with affinity to the muscarinic receptors M.

MedChemComm

Messerer R, Dallanoce C, Matera C, Wehle S, Flammini L, Chirinda B, Bock A, Irmen M, Tränkle C, Barocelli E, Decker M, Sotriffer C, De Amici M, Holzgrabe U.
PMID: 30108847
Medchemcomm. 2017 Apr 27;8(6):1346-1359. doi: 10.1039/c7md00149e. eCollection 2017 Jun 01.

A set of hybrid compounds composed of the fragment of allosteric modulators of the muscarinic receptor,

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Messerer R, Dallanoce C, Matera C, et al. Novel bipharmacophoric inhibitors of the cholinesterases with affinity to the muscarinic receptors M. Medchemcomm. 2017;8(6):1346-1359doi: 10.1039/c7md00149e.
Messerer, R., Dallanoce, C., Matera, C., Wehle, S., Flammini, L., Chirinda, B., Bock, A., Irmen, M., Tränkle, C., Barocelli, E., Decker, M., Sotriffer, C., De Amici, M., & Holzgrabe, U. (2017). Novel bipharmacophoric inhibitors of the cholinesterases with affinity to the muscarinic receptors M. MedChemComm, 8(6), 1346-1359. https://doi.org/10.1039/c7md00149e
Messerer, Regina, et al. "Novel bipharmacophoric inhibitors of the cholinesterases with affinity to the muscarinic receptors M." MedChemComm vol. 8,6 (2017): 1346-1359. doi: https://doi.org/10.1039/c7md00149e
Messerer R, Dallanoce C, Matera C, Wehle S, Flammini L, Chirinda B, Bock A, Irmen M, Tränkle C, Barocelli E, Decker M, Sotriffer C, De Amici M, Holzgrabe U. Novel bipharmacophoric inhibitors of the cholinesterases with affinity to the muscarinic receptors M. Medchemcomm. 2017 Apr 27;8(6):1346-1359. doi: 10.1039/c7md00149e. eCollection 2017 Jun 01. PMID: 30108847; PMCID: PMC6072511.
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Cholinesterase activity as potential biomarker in two bivalves.

Environmental toxicology and pharmacology

Mora P, Michel X, Narbonne JF.
PMID: 21781933
Environ Toxicol Pharmacol. 1999 Oct;7(4):253-60. doi: 10.1016/s1382-6689(99)00019-8.

In this study, the pH, temperature and substrate specificity for cholinesterases (ChE) assay in two bivalves was optimized: the Spanish mussel Mytilus galloprovincialis and the Asiatic clam Corbicula fluminea. The optimal values found are pH 7, 25°C, 2 mM...

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Mora P, Michel X, Narbonne JF. Cholinesterase activity as potential biomarker in two bivalves. Environ Toxicol Pharmacol. 1999;7(4):253-60doi: 10.1016/s1382-6689(99)00019-8.
Mora, P., Michel, X., & Narbonne, J. F. (1999). Cholinesterase activity as potential biomarker in two bivalves. Environmental toxicology and pharmacology, 7(4), 253-60. https://doi.org/10.1016/s1382-6689(99)00019-8
Mora, P, et al. "Cholinesterase activity as potential biomarker in two bivalves." Environmental toxicology and pharmacology vol. 7,4 (1999): 253-60. doi: https://doi.org/10.1016/s1382-6689(99)00019-8
Mora P, Michel X, Narbonne JF. Cholinesterase activity as potential biomarker in two bivalves. Environ Toxicol Pharmacol. 1999 Oct;7(4):253-60. doi: 10.1016/s1382-6689(99)00019-8. PMID: 21781933.
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CHOLINESTERASES.

Science (New York, N.Y.)

Alles GA, Hawes RC.
PMID: 17806413
Science. 1944 Jul 28;100(2587):75. doi: 10.1126/science.100.2587.75.

No abstract available.

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Alles GA, Hawes RC. CHOLINESTERASES. Science. 1944;100(2587):75doi: 10.1126/science.100.2587.75.
Alles, G. A., & Hawes, R. C. (1944). CHOLINESTERASES. Science (New York, N.Y.), 100(2587), 75. https://doi.org/10.1126/science.100.2587.75
Alles, G A, and Hawes, R C. "CHOLINESTERASES." Science (New York, N.Y.) vol. 100,2587 (1944): 75. doi: https://doi.org/10.1126/science.100.2587.75
Alles GA, Hawes RC. CHOLINESTERASES. Science. 1944 Jul 28;100(2587):75. doi: 10.1126/science.100.2587.75. PMID: 17806413.
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Cholinesterases from plant tissues: I. Purification and characterization of a cholinesterase from mung bean roots.

Plant physiology

Riov J, Jaffe MJ.
PMID: 16658363
Plant Physiol. 1973 Mar;51(3):520-8. doi: 10.1104/pp.51.3.520.

A cholinesterase was purified 36-fold from mung bean (Phaseolus aureus) roots by a combination of differential extraction media and gel filtration. The enzyme could be effectively extracted only by high salt concentration, indicating that it is probably membrane-bound. Methods...

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Riov J, Jaffe MJ. Cholinesterases from plant tissues: I. Purification and characterization of a cholinesterase from mung bean roots. Plant Physiol. 1973;51(3):520-8doi: 10.1104/pp.51.3.520.
Riov, J., & Jaffe, M. J. (1973). Cholinesterases from plant tissues: I. Purification and characterization of a cholinesterase from mung bean roots. Plant physiology, 51(3), 520-8. https://doi.org/10.1104/pp.51.3.520
Riov, J, and Jaffe, M J. "Cholinesterases from plant tissues: I. Purification and characterization of a cholinesterase from mung bean roots." Plant physiology vol. 51,3 (1973): 520-8. doi: https://doi.org/10.1104/pp.51.3.520
Riov J, Jaffe MJ. Cholinesterases from plant tissues: I. Purification and characterization of a cholinesterase from mung bean roots. Plant Physiol. 1973 Mar;51(3):520-8. doi: 10.1104/pp.51.3.520. PMID: 16658363; PMCID: PMC366299.
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Comparative Study of White and Steamed Black Panax ginseng, P. quinquefolium, and P. notoginseng on Cholinesterase Inhibitory and Antioxidative Activity.

Journal of ginseng research

Lee MR, Yun BS, Sung CK.
PMID: 23717109
J Ginseng Res. 2012 Jan;36(1):93-101. doi: 10.5142/jgr.2012.36.1.93.

This study evaluated the anti-cholinesterases (ChEs) and antioxidant activities of white ginseng (WG) and black ginseng (BG) roots of Panax ginseng (PG), P. quinquefolium (PQ), and P. notoginseng (PN). Ginsenosides Rg1, Re, Rf, Rb1, Rc, Rb2, and Rd were...

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Lee MR, Yun BS, Sung CK. Comparative Study of White and Steamed Black Panax ginseng, P. quinquefolium, and P. notoginseng on Cholinesterase Inhibitory and Antioxidative Activity. J Ginseng Res. 2012;36(1):93-101doi: 10.5142/jgr.2012.36.1.93.
Lee, M. R., Yun, B. S., & Sung, C. K. (2012). Comparative Study of White and Steamed Black Panax ginseng, P. quinquefolium, and P. notoginseng on Cholinesterase Inhibitory and Antioxidative Activity. Journal of ginseng research, 36(1), 93-101. https://doi.org/10.5142/jgr.2012.36.1.93
Lee, Mi Ra, et al. "Comparative Study of White and Steamed Black Panax ginseng, P. quinquefolium, and P. notoginseng on Cholinesterase Inhibitory and Antioxidative Activity." Journal of ginseng research vol. 36,1 (2012): 93-101. doi: https://doi.org/10.5142/jgr.2012.36.1.93
Lee MR, Yun BS, Sung CK. Comparative Study of White and Steamed Black Panax ginseng, P. quinquefolium, and P. notoginseng on Cholinesterase Inhibitory and Antioxidative Activity. J Ginseng Res. 2012 Jan;36(1):93-101. doi: 10.5142/jgr.2012.36.1.93. PMID: 23717109; PMCID: PMC3659564.
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Plasma and whole brain cholinesterase activities in three wild bird species in Mosul, IRAQ: In vitro inhibition by insecticides.

Interdisciplinary toxicology

Alias AS, Al-Zubaidy MH, Mousa YJ, Mohammad FK.
PMID: 22058655
Interdiscip Toxicol. 2011 Sep;4(3):144-8. doi: 10.2478/v10102-011-0022-x.

Plasma and brain cholinesterase activities were determined in three wild bird species to assess their exposure to organophosphate and carbamate insecticides which are used in agriculture and public health. In the present study, we used an electrometric method for...

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Alias AS, Al-Zubaidy MH, Mousa YJ, et al. Plasma and whole brain cholinesterase activities in three wild bird species in Mosul, IRAQ: In vitro inhibition by insecticides. Interdiscip Toxicol. 2011;4(3):144-8doi: 10.2478/v10102-011-0022-x.
Alias, A. S., Al-Zubaidy, M. H., Mousa, Y. J., & Mohammad, F. K. (2011). Plasma and whole brain cholinesterase activities in three wild bird species in Mosul, IRAQ: In vitro inhibition by insecticides. Interdisciplinary toxicology, 4(3), 144-8. https://doi.org/10.2478/v10102-011-0022-x
Alias, Ashraf S, et al. "Plasma and whole brain cholinesterase activities in three wild bird species in Mosul, IRAQ: In vitro inhibition by insecticides." Interdisciplinary toxicology vol. 4,3 (2011): 144-8. doi: https://doi.org/10.2478/v10102-011-0022-x
Alias AS, Al-Zubaidy MH, Mousa YJ, Mohammad FK. Plasma and whole brain cholinesterase activities in three wild bird species in Mosul, IRAQ: In vitro inhibition by insecticides. Interdiscip Toxicol. 2011 Sep;4(3):144-8. doi: 10.2478/v10102-011-0022-x. PMID: 22058655; PMCID: PMC3203916.
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Transplantation of dorsal root ganglion into the olfactory bulb of neonatal rats: a histochemical study.

Restorative neurology and neuroscience

Sekerková G, Malatová Z, Orendáčová J, Zigová T.
PMID: 21551726
Restor Neurol Neurosci. 1993 Jan 01;6(1):1-8. doi: 10.3233/RNN-1993-6101.

We have transplanted encapsulated dorsal root ganglia (DRG) from adult Wistar albino rats unilaterally into partially bulbectomized (n = 20) neonatal (P3-5) rats of the same strain. Three months postoperatively the animals were perfused and their brains processed by...

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Sekerková G, Malatová Z, Orendáčová J, et al. Transplantation of dorsal root ganglion into the olfactory bulb of neonatal rats: a histochemical study. Restor Neurol Neurosci. 1993;6(1):1-8doi: 10.3233/RNN-1993-6101.
Sekerková, G., Malatová, Z., Orendáčová, J., & Zigová, T. (1993). Transplantation of dorsal root ganglion into the olfactory bulb of neonatal rats: a histochemical study. Restorative neurology and neuroscience, 6(1), 1-8. https://doi.org/10.3233/RNN-1993-6101
Sekerková, G, et al. "Transplantation of dorsal root ganglion into the olfactory bulb of neonatal rats: a histochemical study." Restorative neurology and neuroscience vol. 6,1 (1993): 1-8. doi: https://doi.org/10.3233/RNN-1993-6101
Sekerková G, Malatová Z, Orendáčová J, Zigová T. Transplantation of dorsal root ganglion into the olfactory bulb of neonatal rats: a histochemical study. Restor Neurol Neurosci. 1993 Jan 01;6(1):1-8. doi: 10.3233/RNN-1993-6101. PMID: 21551726.
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