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Anti-Alzheimer's Studies on β-Sitosterol Isolated from .

Frontiers in pharmacology

Ayaz M, Junaid M, Ullah F, Subhan F, Sadiq A, Ali G, Ovais M, Shahid M, Ahmad A, Wadood A, El-Shazly M, Ahmad N, Ahmad S.
PMID: 29056913
Front Pharmacol. 2017 Oct 06;8:697. doi: 10.3389/fphar.2017.00697. eCollection 2017.

The family Polygonaceae is known for its traditional use in the management of various neurological disorders including Alzheimer's disease (AD). In search of new anti-AD drugs, β-sitosterol isolated from

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Ayaz M, Junaid M, Ullah F, et al. Anti-Alzheimer's Studies on β-Sitosterol Isolated from . Front Pharmacol. 2017;8:697doi: 10.3389/fphar.2017.00697.
Ayaz, M., Junaid, M., Ullah, F., Subhan, F., Sadiq, A., Ali, G., Ovais, M., Shahid, M., Ahmad, A., Wadood, A., El-Shazly, M., Ahmad, N., & Ahmad, S. (2017). Anti-Alzheimer's Studies on β-Sitosterol Isolated from . Frontiers in pharmacology, 8697. https://doi.org/10.3389/fphar.2017.00697
Ayaz, Muhammad, et al. "Anti-Alzheimer's Studies on β-Sitosterol Isolated from ." Frontiers in pharmacology vol. 8 (2017): 697. doi: https://doi.org/10.3389/fphar.2017.00697
Ayaz M, Junaid M, Ullah F, Subhan F, Sadiq A, Ali G, Ovais M, Shahid M, Ahmad A, Wadood A, El-Shazly M, Ahmad N, Ahmad S. Anti-Alzheimer's Studies on β-Sitosterol Isolated from . Front Pharmacol. 2017 Oct 06;8:697. doi: 10.3389/fphar.2017.00697. eCollection 2017. PMID: 29056913; PMCID: PMC5635809.
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Screening of siddha medicinal plants for its in-vitro acetylcholinesterase and butyrylcholinesterase inhibitory activity.

Pharmacognosy magazine

Kadiyala M, Ponnusankar S, Elango K.
PMID: 24991106
Pharmacogn Mag. 2014 Apr;10:S294-8. doi: 10.4103/0973-1296.133281.

BACKGROUND: The plants selected for the study were traditionally used in siddha system of medicine in neurological disorders.AIM: The aim of the following study isto screen the plant species for both acetylcholinesterase (AchE) and butyrylcholinesterase (BuchE) inhibition by in-vitro...

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Kadiyala M, Ponnusankar S, Elango K. Screening of siddha medicinal plants for its in-vitro acetylcholinesterase and butyrylcholinesterase inhibitory activity. Pharmacogn Mag. 2014;10:S294-8doi: 10.4103/0973-1296.133281.
Kadiyala, M., Ponnusankar, S., & Elango, K. (2014). Screening of siddha medicinal plants for its in-vitro acetylcholinesterase and butyrylcholinesterase inhibitory activity. Pharmacognosy magazine, 10S294-8. https://doi.org/10.4103/0973-1296.133281
Kadiyala, Madhuri, et al. "Screening of siddha medicinal plants for its in-vitro acetylcholinesterase and butyrylcholinesterase inhibitory activity." Pharmacognosy magazine vol. 10 (2014): S294-8. doi: https://doi.org/10.4103/0973-1296.133281
Kadiyala M, Ponnusankar S, Elango K. Screening of siddha medicinal plants for its in-vitro acetylcholinesterase and butyrylcholinesterase inhibitory activity. Pharmacogn Mag. 2014 Apr;10:S294-8. doi: 10.4103/0973-1296.133281. PMID: 24991106; PMCID: PMC4078355.
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Sensing activity of cholinesterases through a luminescence response of the hexarhenium cluster complex [{Re6S8}(OH)6](4.).

The Analyst

Elistratova JG, Mustafina AR, Brylev KA, Petrov KA, Shestopalov MA, Mironov YV, Babaev VM, Rizvanov IK, Masson P, Sinyashin OG.
PMID: 27169678
Analyst. 2016 Jun 20;141(13):4204-10. doi: 10.1039/c6an00581k.

The present work describes a new method to sense cholinesterase-catalyzed hydrolysis of acetylcholine (ACh) through a luminescence response of the hexarhenium cluster complex [{Re6S8}(OH)6](4-). A proton released from acetylcholinesterase (AChE)- or butyrylcholinesterase (BuChE)-catalyzed hydrolysis of ACh results in time-resolved...

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Elistratova JG, Mustafina AR, Brylev KA, et al. Sensing activity of cholinesterases through a luminescence response of the hexarhenium cluster complex [{Re6S8}(OH)6](4.). Analyst. 2016;141(13):4204-10doi: 10.1039/c6an00581k.
Elistratova, J. G., Mustafina, A. R., Brylev, K. A., Petrov, K. A., Shestopalov, M. A., Mironov, Y. V., Babaev, V. M., Rizvanov, I. K., Masson, P., & Sinyashin, O. G. (2016). Sensing activity of cholinesterases through a luminescence response of the hexarhenium cluster complex [{Re6S8}(OH)6](4.). The Analyst, 141(13), 4204-10. https://doi.org/10.1039/c6an00581k
Elistratova, Julia G, et al. "Sensing activity of cholinesterases through a luminescence response of the hexarhenium cluster complex [{Re6S8}(OH)6](4.)." The Analyst vol. 141,13 (2016): 4204-10. doi: https://doi.org/10.1039/c6an00581k
Elistratova JG, Mustafina AR, Brylev KA, Petrov KA, Shestopalov MA, Mironov YV, Babaev VM, Rizvanov IK, Masson P, Sinyashin OG. Sensing activity of cholinesterases through a luminescence response of the hexarhenium cluster complex [{Re6S8}(OH)6](4.). Analyst. 2016 Jun 20;141(13):4204-10. doi: 10.1039/c6an00581k. PMID: 27169678.
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Postponed effect of neostigmine on oxidative homeostasis.

Interdisciplinary toxicology

Pohanka M.
PMID: 26109890
Interdiscip Toxicol. 2014 Sep;7(3):134-8. doi: 10.2478/intox-2014-0018. Epub 2014 Dec 30.

Cholinesterases are enzymes able to hydrolyze the neurotransmitter acetylcholine and thus to terminate transmission. Once the enzymes are inhibited, excitotoxicity can appear in the adjacent cells. It is well known that oxidative stress is involved in the toxicity of...

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Pohanka M. Postponed effect of neostigmine on oxidative homeostasis. Interdiscip Toxicol. 2014;7(3):134-8doi: 10.2478/intox-2014-0018.
Pohanka, M. (2014). Postponed effect of neostigmine on oxidative homeostasis. Interdisciplinary toxicology, 7(3), 134-8. https://doi.org/10.2478/intox-2014-0018
Pohanka, Miroslav. "Postponed effect of neostigmine on oxidative homeostasis." Interdisciplinary toxicology vol. 7,3 (2014): 134-8. doi: https://doi.org/10.2478/intox-2014-0018
Pohanka M. Postponed effect of neostigmine on oxidative homeostasis. Interdiscip Toxicol. 2014 Sep;7(3):134-8. doi: 10.2478/intox-2014-0018. Epub 2014 Dec 30. PMID: 26109890; PMCID: PMC4434106.
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THE CONTROVERSY ON CHOLINESTERASES.

Science (New York, N.Y.)

Glick D.
PMID: 17813945
Science. 1945 Jul 27;102(2639):100-1. doi: 10.1126/science.102.2639.100.

No abstract available.

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Glick D. THE CONTROVERSY ON CHOLINESTERASES. Science. 1945;102(2639):100-1doi: 10.1126/science.102.2639.100.
Glick, D. (1945). THE CONTROVERSY ON CHOLINESTERASES. Science (New York, N.Y.), 102(2639), 100-1. https://doi.org/10.1126/science.102.2639.100
Glick, D. "THE CONTROVERSY ON CHOLINESTERASES." Science (New York, N.Y.) vol. 102,2639 (1945): 100-1. doi: https://doi.org/10.1126/science.102.2639.100
Glick D. THE CONTROVERSY ON CHOLINESTERASES. Science. 1945 Jul 27;102(2639):100-1. doi: 10.1126/science.102.2639.100. PMID: 17813945.
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THE CHOLINESTERASES IN THE LIGHT OF RECENT FINDINGS.

Science (New York, N.Y.)

Mendel B, Rudney H.
PMID: 17734192
Science. 1944 Dec 01;100(2605):499-500. doi: 10.1126/science.100.2605.499.

No abstract available.

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Mendel B, Rudney H. THE CHOLINESTERASES IN THE LIGHT OF RECENT FINDINGS. Science. 1944;100(2605):499-500doi: 10.1126/science.100.2605.499.
Mendel, B., & Rudney, H. (1944). THE CHOLINESTERASES IN THE LIGHT OF RECENT FINDINGS. Science (New York, N.Y.), 100(2605), 499-500. https://doi.org/10.1126/science.100.2605.499
Mendel, B, and Rudney, H. "THE CHOLINESTERASES IN THE LIGHT OF RECENT FINDINGS." Science (New York, N.Y.) vol. 100,2605 (1944): 499-500. doi: https://doi.org/10.1126/science.100.2605.499
Mendel B, Rudney H. THE CHOLINESTERASES IN THE LIGHT OF RECENT FINDINGS. Science. 1944 Dec 01;100(2605):499-500. doi: 10.1126/science.100.2605.499. PMID: 17734192.
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Cholinesterases from Plant Tissues: II. Inhibition of Bean Cholinesterase by 2-Isopropyl-4-dimethylamino-5-methylphenyl-1-piperidine Carboxylate Methyl Chloride (AMO-1618).

Plant physiology

Riov J, Jaffe MJ.
PMID: 16658537
Plant Physiol. 1973 Sep;52(3):233-5. doi: 10.1104/pp.52.3.233.

2-Isopropyl-4-dimethylamino-5-methylphenyl-1-piperidine carboxylate methyl chloride (AMO-1618) inhibits the activity of a cholinesterase isolated from mung bean (Phaseolus aureus) roots at concentrations comparable to those which retard growth and inhibit development of secondary roots of bean seedlings. Fifty per cent inhibition...

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Riov J, Jaffe MJ. Cholinesterases from Plant Tissues: II. Inhibition of Bean Cholinesterase by 2-Isopropyl-4-dimethylamino-5-methylphenyl-1-piperidine Carboxylate Methyl Chloride (AMO-1618). Plant Physiol. 1973;52(3):233-5doi: 10.1104/pp.52.3.233.
Riov, J., & Jaffe, M. J. (1973). Cholinesterases from Plant Tissues: II. Inhibition of Bean Cholinesterase by 2-Isopropyl-4-dimethylamino-5-methylphenyl-1-piperidine Carboxylate Methyl Chloride (AMO-1618). Plant physiology, 52(3), 233-5. https://doi.org/10.1104/pp.52.3.233
Riov, J, and Jaffe, M J. "Cholinesterases from Plant Tissues: II. Inhibition of Bean Cholinesterase by 2-Isopropyl-4-dimethylamino-5-methylphenyl-1-piperidine Carboxylate Methyl Chloride (AMO-1618)." Plant physiology vol. 52,3 (1973): 233-5. doi: https://doi.org/10.1104/pp.52.3.233
Riov J, Jaffe MJ. Cholinesterases from Plant Tissues: II. Inhibition of Bean Cholinesterase by 2-Isopropyl-4-dimethylamino-5-methylphenyl-1-piperidine Carboxylate Methyl Chloride (AMO-1618). Plant Physiol. 1973 Sep;52(3):233-5. doi: 10.1104/pp.52.3.233. PMID: 16658537; PMCID: PMC366475.
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Cholinesterases from plant tissue: v. Cholinesterase is not pectin esterase.

Plant physiology

Fluck RA, Jaffe MJ.
PMID: 16658976
Plant Physiol. 1974 Nov;54(5):797-8. doi: 10.1104/pp.54.5.797.

Several properties of the cholinesterase from Phaseolus aureus Roxb. and of pectin (methyl) esterases from both Phaseolus aureus and Lycopersicon esculentum (L.) Mill. are contrasted. Cholinesterase activity is inhibited by all of the concentrations of NaCl tested, from 0.05...

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Fluck RA, Jaffe MJ. Cholinesterases from plant tissue: v. Cholinesterase is not pectin esterase. Plant Physiol. 1974;54(5):797-8doi: 10.1104/pp.54.5.797.
Fluck, R. A., & Jaffe, M. J. (1974). Cholinesterases from plant tissue: v. Cholinesterase is not pectin esterase. Plant physiology, 54(5), 797-8. https://doi.org/10.1104/pp.54.5.797
Fluck, R A, and Jaffe, M J. "Cholinesterases from plant tissue: v. Cholinesterase is not pectin esterase." Plant physiology vol. 54,5 (1974): 797-8. doi: https://doi.org/10.1104/pp.54.5.797
Fluck RA, Jaffe MJ. Cholinesterases from plant tissue: v. Cholinesterase is not pectin esterase. Plant Physiol. 1974 Nov;54(5):797-8. doi: 10.1104/pp.54.5.797. PMID: 16658976; PMCID: PMC366607.
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Multienzyme electrochemical array sensor for determination of phenols and pesticides.

Talanta

Solná R, Sapelnikova S, Skládal P, Winther-Nielsen M, Carlsson C, Emnéus J, Ruzgas T.
PMID: 18969806
Talanta. 2005 Jan 30;65(2):349-57. doi: 10.1016/j.talanta.2004.07.005.

The screen-printed four-electrode system was used as the amperometric transducer for determination of phenols and pesticides using immobilised tyrosinase, peroxidase, acetylcholinesterase and butyrylcholinesterase. Acetylthiocholine chloride was chosen as substrate for cholinesterases to measure inhibition by pesticides, hydrogen peroxide served...

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Solná R, Sapelnikova S, Skládal P, et al. Multienzyme electrochemical array sensor for determination of phenols and pesticides. Talanta. 2005;65(2):349-57doi: 10.1016/j.talanta.2004.07.005.
Solná, R., Sapelnikova, S., Skládal, P., Winther-Nielsen, M., Carlsson, C., Emnéus, J., & Ruzgas, T. (2005). Multienzyme electrochemical array sensor for determination of phenols and pesticides. Talanta, 65(2), 349-57. https://doi.org/10.1016/j.talanta.2004.07.005
Solná, R, et al. "Multienzyme electrochemical array sensor for determination of phenols and pesticides." Talanta vol. 65,2 (2005): 349-57. doi: https://doi.org/10.1016/j.talanta.2004.07.005
Solná R, Sapelnikova S, Skládal P, Winther-Nielsen M, Carlsson C, Emnéus J, Ruzgas T. Multienzyme electrochemical array sensor for determination of phenols and pesticides. Talanta. 2005 Jan 30;65(2):349-57. doi: 10.1016/j.talanta.2004.07.005. PMID: 18969806.
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Cholinesterases from Plant Tissues: III. Distribution and Subcellular Localization in Phaseolus aureus Roxb.

Plant physiology

Fluck RA, Jaffe MJ.
PMID: 16658783
Plant Physiol. 1974 May;53(5):752-8. doi: 10.1104/pp.53.5.752.

The distribution and localization of cholinesterase in Phaseolus aureus, Glycine max, and Pisum sativum is described. The enzyme is present in roots, leaves, stems, root callus tissue, root cells suspension cultures, and root nodules. Cholinesterase in roots is found...

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Fluck RA, Jaffe MJ. Cholinesterases from Plant Tissues: III. Distribution and Subcellular Localization in Phaseolus aureus Roxb. Plant Physiol. 1974;53(5):752-8doi: 10.1104/pp.53.5.752.
Fluck, R. A., & Jaffe, M. J. (1974). Cholinesterases from Plant Tissues: III. Distribution and Subcellular Localization in Phaseolus aureus Roxb. Plant physiology, 53(5), 752-8. https://doi.org/10.1104/pp.53.5.752
Fluck, R A, and Jaffe, M J. "Cholinesterases from Plant Tissues: III. Distribution and Subcellular Localization in Phaseolus aureus Roxb." Plant physiology vol. 53,5 (1974): 752-8. doi: https://doi.org/10.1104/pp.53.5.752
Fluck RA, Jaffe MJ. Cholinesterases from Plant Tissues: III. Distribution and Subcellular Localization in Phaseolus aureus Roxb. Plant Physiol. 1974 May;53(5):752-8. doi: 10.1104/pp.53.5.752. PMID: 16658783; PMCID: PMC541439.
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Microscopic localization of cholinesterases in the nervous systems of the lobsters, Panulirus argus and Homarus americanus.

Tissue & cell

Maynard EA.
PMID: 18631552
Tissue Cell. 1971;3(2):215-50. doi: 10.1016/s0040-8166(71)80020-4.

Using acetylthiocholine as substrate, microscopically localizable cholinesterase (ChE) activity is demonstrated in neural and glial elements of central and peripheral nervous systems of the lobsters, Panulirus argus and Homarus americanus. Moderate to very intense ChE activity occurs in all...

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Maynard EA. Microscopic localization of cholinesterases in the nervous systems of the lobsters, Panulirus argus and Homarus americanus. Tissue Cell. 1971;3(2):215-50doi: 10.1016/s0040-8166(71)80020-4.
Maynard, E. A. (1971). Microscopic localization of cholinesterases in the nervous systems of the lobsters, Panulirus argus and Homarus americanus. Tissue & cell, 3(2), 215-50. https://doi.org/10.1016/s0040-8166(71)80020-4
Maynard, E A. "Microscopic localization of cholinesterases in the nervous systems of the lobsters, Panulirus argus and Homarus americanus." Tissue & cell vol. 3,2 (1971): 215-50. doi: https://doi.org/10.1016/s0040-8166(71)80020-4
Maynard EA. Microscopic localization of cholinesterases in the nervous systems of the lobsters, Panulirus argus and Homarus americanus. Tissue Cell. 1971;3(2):215-50. doi: 10.1016/s0040-8166(71)80020-4. PMID: 18631552.
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In Vitro Comparison of Two Most Promising H-Oximes (HI-6 and HLö-7) and Currently Commercially Available Reactivators Pralidoxime and Obidoxime in Reactivation of Cyclosarin-Inhibited Human Cholinesterases.

Toxicology mechanisms and methods

Kuca K, Cabal J, Jun D, Koleckar V.
PMID: 20020898
Toxicol Mech Methods. 2008;18(4):329-33. doi: 10.1080/15376510701380323.

ABSTRACT This study describes the evaluation of the in vitro ability of two acetylcholinesterase (EC 3.1.1.7) reactivators, HI-6 and HLö-7, very promising at present, to reactivate human brain cholinesterases inhibited by the nerve agent cyclosarin. The results obtained (percentage...

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Kuca K, Cabal J, Jun D, et al. In Vitro Comparison of Two Most Promising H-Oximes (HI-6 and HLö-7) and Currently Commercially Available Reactivators Pralidoxime and Obidoxime in Reactivation of Cyclosarin-Inhibited Human Cholinesterases. Toxicol Mech Methods. 2008;18(4):329-33doi: 10.1080/15376510701380323.
Kuca, K., Cabal, J., Jun, D., & Koleckar, V. (2008). In Vitro Comparison of Two Most Promising H-Oximes (HI-6 and HLö-7) and Currently Commercially Available Reactivators Pralidoxime and Obidoxime in Reactivation of Cyclosarin-Inhibited Human Cholinesterases. Toxicology mechanisms and methods, 18(4), 329-33. https://doi.org/10.1080/15376510701380323
Kuca, Kamil, et al. "In Vitro Comparison of Two Most Promising H-Oximes (HI-6 and HLö-7) and Currently Commercially Available Reactivators Pralidoxime and Obidoxime in Reactivation of Cyclosarin-Inhibited Human Cholinesterases." Toxicology mechanisms and methods vol. 18,4 (2008): 329-33. doi: https://doi.org/10.1080/15376510701380323
Kuca K, Cabal J, Jun D, Koleckar V. In Vitro Comparison of Two Most Promising H-Oximes (HI-6 and HLö-7) and Currently Commercially Available Reactivators Pralidoxime and Obidoxime in Reactivation of Cyclosarin-Inhibited Human Cholinesterases. Toxicol Mech Methods. 2008;18(4):329-33. doi: 10.1080/15376510701380323. PMID: 20020898.
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Showing 1 to 12 of 162 entries