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Molecular and cellular biology of cholinesterases
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“An increase of acetylcholine concentration (ACh) at the synapse by inhibiting the acetylcholinesterase (AChE) is one of the approaches to slow down the progression of AD [18,19,20,21,22,23,24,25,26].”
From Acetylcholinesterase Inhibitory Potential of Various Sesquiterpene Analogues for Alzheimer’s Disease Therapy (2021) · cites this paper as [22]
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Cites
A new and rapid colorimetric determination of acetylcholinesterase activity
Ellman, G. L., Courtney, K. D., Andres, V., & Featherstone, R. M. (1961) · Biochemical Pharmacology · doi:10.1016/0006-2952(61)90145-9 · Cited by 27,221
A "DIRECT-COLORING" THIOCHOLINE METHOD FOR CHOLINESTERASES
Karnovsky, M. J., & ROOTS, L. (1964) · Journal of Histochemistry & Cytochemistry · doi:10.1177/12.3.219 · Cited by 3,368
Solubilization of membranes by detergents
Helenius, A., & Simons, K. (1975) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(75)90016-7 · Cited by 2,941
Sussman, J. L., Harel, M., Frolow, F., Oefner, C., Goldman, A., Toker, L., & Silman, I. (1991) · Science · doi:10.1126/science.1678899 · Cited by 2,740
Ollis, D. L., Cheah, E., Cygler, M., Dijkstra, B. W., Frolow, F., Franken, S. M., Harel, M., Remington, S. J., Silman, I., Schrag, J. D., et al. (1992) · Protein Engineering Design and Selection · doi:10.1093/protein/5.3.197 · Cited by 2,156
Progress in Clinical and Biological Research
Smyth, J. F. (1979) · Journal of Clinical Pathology · doi:10.1136/jcp.32.7.742-d · Cited by 1,558
CELL-SURFACE ANCHORING OF PROTEINS VIA GLYCOSYL-PHOSPHATIDYLINOSITOL STRUCTURES
Ferguson, M. A. J., & Williams, A. F. (1988) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.57.070188.001441 · Cited by 1,281
The Molecular Basis of Muscular Dystrophy in the mdx Mouse: a Point Mutation
Sicinski, P., Geng, Y., Ryder-Cook, A. S., Barnard, E. A., Darlison, M. G., & Barnard, P. J. (1989) · Science · doi:10.1126/science.2662404 · Cited by 1,276
Structure of human pancreatic lipase
Winkler, F. K., D'Arcy, A., & Hunziker, W. H. (1990) · Nature · doi:10.1038/343771a0 · Cited by 1,245
A serine protease triad forms the catalytic centre of a triacylglycerol lipase
Brady, L., Brzozowski, A. M., Derewenda, Z. S., Dodson, E. J., Dodson, G. G., Tolley, S. P., Turkenburg, J. P., Christiansen, L., Huge‐Jensen, B., Nørskov, L., et al. (1990) · Nature · doi:10.1038/343767a0 · Cited by 1,219
Research works printed but not linked: 27
- Appleyard, 1989, Noncholinergic effects of acetylcholinesterase upon the membrane properties of mamalian cerebellar Purkinje cells, Eur. J. Neurosci., 129
- Balasubramanian, 1984, Have cholinesterases more than one function?, TINS, 9, 467
- Bartha, 1987, Characterization of ‘fetal-type’ acetylcholinesterase in hemintreated K-562 cell culture, Blood Cells, 12, 647
- Ben-Aziz, 1991, Molecular cloning and expression of an alternative human acetylcholinesterase cDNA, J. Neurochem., 57, S27A
- Brimijoin, 1991, Long lasting preganglionic sympathectomy by acetylcholinesterase antibodies, J. Neurochem., 57, S96B
- Conradi, 1990, Autoantibodies against membrane-bound acetylcholinesterase in ALS. II. Direct demonstration with ELISA-technique, J. neurol. Sci., 98S, 350
- Fernandez-Valle, 1988, Phorbol esters stimulate appearance of asymmetric acetylcholinesterase in TTX-treated quail muscle cultures, Soc. Neurosci. Abstr., 14, 1163
- Fisher, 1992, Expression and recognition of biologically active human acetylcholinesterase from E. coli, Molec. cell. Neurobiol.
- Gnatt, 1990, Expression of alternatively terminated unusual cholinesterase transcripts, mapping to chromosome 3q26-ter in nervous system tumors, Cancer Res., 50, 1983
- Henderson, 1986, Is there a link between choline acetyltransferase-containing neurons and butyrylcholinesterase in rat cerebral cortex?, TINS, 9, 20
- Hutchinson, 1992, Congenital myasthenic syndrome secondary to endplate acetylcholinesterase deficiency, Ann. N.Y. Acad. Sci.
- Hutchinson, 1992, The syndrome of endplate acetylcholinesterase deficiency: clinical, electrophysiological morphological, biochemical and molecular genetic observations, Brain
- Jasmin, 1991, Analysis of acetylcholinesterase gene expression at the avian neuromuscular junction by quantitative PCR, J. Cell Biol., 115, 30a
- Jasmin, 1992, Acetylcholinesterase mRNA levels increase in parallel with enzyme activity in overloaded skeletal muscle, Soc. Neurosci. Abstr., 18, 1556
- Kaupmann, 1985, N-acetylgalactosamine specific lectin binding in mammalian muscle: dependence on development, mutations and species, Abstracts Eur. J. Cell Biol., 39, 19
- 1963, Vol. 15
- Layer, 1985, Development of embryonic cholinesterases and cell proliferation in chick brain and retina, J. Neurochem., 44, S129
- Lee, 1992, Discordant expression of acetylcholinesterase activity and mRNA levels in single neuromuscular junctions of normal muscle, Soc. Neurosci. Abstr., 18, 1556
- Li, 1992, Tissue specific expression and alternative message processing of the mammalian acetylcholinesterase gene, J. biol. Chem.
- MacPhee-Quigley, 1988, Expression of active, glycosylated acetylcholinesterase using the insect vector Baculovirus system, FASEB J., 2, A361
- Marnay, 1937, Cholinestérase dans l'organe électrique de la Torpille, Compt. Rend. Soc. Biol., 126, 573
- Marnay, 1937, Cholinestérase dans le muscle strié, Compt. Rend. Soc. Biol., 124, 942
- Rama-Sastry, 1979, Cholinergic system in nonnervous tissue, Pharmac. Rev., 30, 65
- Randall, 1988, Expression of multiple acetylcholinesterase transcripts in quail myotubes is regulated by muscle activity, Soc. Neurosci. Abstr., 14, 1163
- Roshchina, 1988, Characterization of pea chloroplast cholinesterase: effect of inhibitors of animal enzymes, Photosynthetica, 22, 20
- Small, 1991, Protease activity is recovered in association with a minor species of serum acetylcholinesterase: implications for Alzheimer's disease (AD), J. Neurochem., 57, S27D
- Soreq, 1990, Vol. 13
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Silveyra, M. X., Cuadrado‐Corrales, N., Marcos, A., Jiménez, M. S. B., Rábano, A., Calero, M., & Sáez‐Valero, J. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03514.x · Cited by 33
Mechanical stimulation increases expression of acetylcholinesterase in cultured myotubes
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Sáez‐Valero, J., CEBALLOS, M. L. D., Small, D. H., & Felipe, C. D. (2002) · Neuroscience Letters · doi:10.1016/s0304-3940(02)00282-3 · Cited by 35
Choi, R. C. Y., Siow, N. L., Zhu, S. Q., Wan, D. C., Wong, Y. H., & Tsim, K. W. K. (2001) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2001.0968 · Cited by 33
Belbeoc'h, S., Falasca, C., Leroy, J., Ayon, A., Massoulié, J., & Bon, S. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04052.x · Cited by 33
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Arredondo, J., Lara, M., Ng, F., Gochez, D. A., Lee, D. C., Logia, S. P., Nguyen, J., & Maselli, R. A. (2013) · Human Genetics · doi:10.1007/s00439-013-1391-3 · Cited by 32
Chen, J., Lin, K., Prasad, S., & Schmidtke, D. W. (2023) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2023.115340 · Cited by 32
Anglister, L., Eichler, J., Szabo, M., Haesaert, B., & Salpeter, M. M. (1998) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(98)00015-6 · Cited by 32
da Silva, A. C., Balz, D., de Souza, J. B. D., Morsch, V. M., Correa, M. C. J. M., Zanetti, G. D., Manfron, M. P., & Schetinger, M. R. C. (2005) · Phytomedicine · doi:10.1016/j.phymed.2005.01.011 · Cited by 32
Vallianou, N. G., Evangelopoulos, A. A., Bountziouka, V. P., Bonou, M. S., Katsagoni, C. N., Vogiatzakis, E. D., Avgerinos, P. C., Barbetseas, J. D., & Panagiotakos, D. B. (2014) · Journal of Cardiovascular Medicine · doi:10.2459/jcm.0b013e3283627700 · Cited by 32
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Mendelson, I., Kronman, C., Ariel, N., Avigdor Shafferman, C., & Velan, B. (1998) · Biochemical Journal · doi:10.1042/bj3340251 · Cited by 32
Direct Detection of Molecular Biorecognition by Dipole Sensing Mechanism
Goykhman, I., Korbakov, N., Bartic, C., Borghs, G., Spira, M. E., Shappir, J., & Yitzchaik, S. (2009) · Journal of the American Chemical Society · doi:10.1021/ja809051p · Cited by 32
Zhang, D., Suen, J. K., Zhang, Y. J., Song, Y., Radić, Z., Taylor, P., Holst, M., Bajaj, C., Baker, N., & McCammon, J. A. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.053850 · Cited by 32
Targeting acetylcholinesterase to the neuromuscular synapse
Rotundo, R. L., Rossi, S. G., Kimbell, L. M., Ruiz, C. A., & Marrero, E. (2005) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2005.10.007 · Cited by 32
Effect of long-term aluminum feeding on kinetics attributes of tissue cholinesterases
Dave, K. R., Syal, A. R., & Katyare, S. S. (2002) · Brain Research Bulletin · doi:10.1016/s0361-9230(02)00786-4 · Cited by 32
Schwarz, M., Loewenstein, Y., Glick, D., Liao, J., Nørgaard‐Pedersen, B., & Soreq, H. (1995) · Molecular Brain Research · doi:10.1016/0169-328x(95)00040-y · Cited by 32
PRITCHARD, D. I., Brown, A., & Toutant, J. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb19943.x · Cited by 32
Congenital Myasthenic Syndromes in 2012
Engel, A. G. (2011) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-011-0234-7 · Cited by 31
Wester, J. C., & Contreras, D. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.1644-13.2013 · Cited by 31
Forget‐Leray, J., & Bocquené, G. (1999) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/s0305-0491(99)00073-5 · Cited by 31
Bulut, S., Bodur, E., Çolak, R., & Turnagöl, H. (2012) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2012.09.022 · Cited by 31
Mehlert, A., Varon, L. E., Silman, I., Homans, S. W., & Ferguson, M. A. J. (1993) · Biochemical Journal · doi:10.1042/bj2960473 · Cited by 31
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Dziri, L., Puppala, K., & Leblanc, R. M. (1997) · Journal of Colloid and Interface Science · doi:10.1006/jcis.1997.5069 · Cited by 31
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Bon, S., Ayon, A., Leroy, J., & Massoulié, J. (2003) · Neurochemical Research · doi:10.1023/a:1022821306722 · Cited by 31
Self-citationAcetylcholinesterase at the neuromuscular junction
Rotundo, R. L. (2020) · Neuroscience Letters · doi:10.1016/j.neulet.2020.135157 · Cited by 30
Naz, H., Othman, M. S., Rahim, F., Hussain, R., Khan, S., Taha, M., Hafez, M. M., Abdel-Hafez, L. J. M., Ullah, H., Khan, I. U., et al. (2024) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2024.138592 · Cited by 30
Guo, Q., Du, G., He, H., Xu, H., Guo, D., & Li, R. (2015) · Natural Product Research · doi:10.1080/14786419.2015.1094804 · Cited by 30
Pejchal, V., Štěpánková, Š., Pejchalová, M., Královec, K., Havelek, R., Růžičková, Z., Ajani, H., Lo, R., & Lepšı́k, M. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.02.033 · Cited by 34
Sundaramoorthy, P. M. K., & Packiam, K. K. (2020) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-020-02922-7 · Cited by 31
Rossi, S. G., Vazquez, A. E., & Rotundo, R. L. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-03-00919.2000 · Cited by 30
Amat-ur-Rasool, H., & Ahmed, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0136509 · Cited by 30
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Angelini, C., Amaroli, A., Falugi, C., Bella, G. D., & Matranga, V. (2003) · Marine Biology · doi:10.1007/s00227-003-1120-x · Cited by 30
Tripathi, R. K. P., Rai, G. K., & Ayyannan, S. R. (2016) · ChemMedChem · doi:10.1002/cmdc.201600128 · Cited by 30
Sanjeewa, K. K. A., Lee, W., Kim, J., & Jeon, Y. (2017) · Journal of Applied Phycology · doi:10.1007/s10811-017-1213-4 · Cited by 30
Heim, J., Schmidt‐Dannert, C., Atomi, H., & Schmid, R. D. (1998) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(97)00196-6 · Cited by 30
Wan, D. C., Choi, R. C. Y., Siow, N. L., & Tsim, K. W. K. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01200-3 · Cited by 30
Sarkaratı, B., Çokuğraş, A. N., & Tezcan, E. F. (1999) · Comparative Biochemistry and Physiology Part C Pharmacology Toxicology and Endocrinology · doi:10.1016/s0742-8413(98)10102-0 · Cited by 30
Boudreau‐Larivière, C., Gisiger, V., Michel, R. N., Hubatsch, D. A., & Jasmin, B. J. (1997) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1997.272.1.c68 · Cited by 30
Colonisation of the developing human brain and spinal cord by microglia: a review
Rezaie, P., & Male, D. K. (1999) · Microscopy Research and Technique · doi:10.1002/(sici)1097-0029(19990615)45:6 · Cited by 205
Novel Messenger RNA and Alternative Promoter for Murine Acetylcholinesterase
Atanasova, E. A., CHIAPPA, S. A., Wieben, E. D., & Brimijoin, S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.30.21078 · Cited by 30
Dunant, Y., & Gisiger, V. (2017) · Molecules · doi:10.3390/molecules22081300 · Cited by 28
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Bentley, G. N., Jones, A. K., & AGNEW, A. M. (2003) · Gene · doi:10.1016/s0378-1119(03)00709-1 · Cited by 29
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Barak, R., Ordentlich, A., Barak, D., Fischer, M., Benschop, H. P., Jong, L. P. A. D., Segall, Y., Velan, B., & Avigdor Shafferman, C. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00375-x · Cited by 29
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Sanes, J. R. (1995) · Seminars in Developmental Biology · doi:10.1016/s1044-5781(06)80026-5 · Cited by 29
Fossati, S. M., Candiani, S., Nödl, M., Maragliano, L., Pennuto, M., Domíngues, P., Benfenati, F., Pestarino, M., & Zullo, L. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8842-2 · Cited by 28
Alves-Amaral, G., Pires-Oliveira, M., Andrade-Lopes, A. L., Chiavegatti, T., & Godinho, R. O. (2010) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.04.002 · Cited by 28
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Badiou, A., Brunet, J., & Belzunces, L. (2007) · Archives of Insect Biochemistry and Physiology · doi:10.1002/arch.20204 · Cited by 28
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Boyd, A. E., Marnett, A. B., Wong, L. M., & Taylor, P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000606200 · Cited by 28
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de Freitas, R. M. (2009) · Neurochemical Research · doi:10.1007/s11064-009-0041-6 · Cited by 27
Webster, R. G. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051326 · Cited by 27
da Costa, G. V., Ferreira, E. F. B., Ramos, R. D. S., Silva, L. B., de Sá, E. M. F., Silva, A. K. P. D., Lobato, C. M., Souto, R. N. P., da Silva, C. H. T. D. P., Federico, L. B., et al. (2019) · Pharmaceuticals · doi:10.3390/ph12020061 · Cited by 27
El‐Sayed, N. F., El‐Hussieny, M., Ewies, E. F., Fouad, M. A., & Boulos, L. S. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.103499 · Cited by 27
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Arshad, M. N., Ahmed, K., Bashir, M., Kosar, N., Kanwal, M., Ahmed, M., Khan, H. U., Khan, S., Rauf, A., Waseem, A., et al. (2021) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2021.131204 · Cited by 27
Xiang, K., He, Z., Fu, J., Wang, G., Li, H., Zhang, Y., Zhang, S., & Chen, L. (2022) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2022.129454 · Cited by 28
Kopańska, M., Lukáč, N., Kapusta, E., & Formicki, G. (2015) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.21717 · Cited by 27
Carrozzo, M. M., Cannazza, G., Pinetti, D., Viesti, V. D., Battisti, U. M., Braghiroli, D., Parenti, C., & Baraldi, M. (2010) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2010.09.016 · Cited by 27
Biochemical and molecular characterization of acetylcholinesterase from the hagfish Myxine glutinosa
Sanders, M., Mathews, B., Sutherland, D. J., Soong, W., Giles, H., & Pezzementi, L. (1996) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/0305-0491(96)00088-0 · Cited by 26
Self-citationGülcan, H. O., Orhan, İ. E., & Şener, B. (2015) · Current Pharmaceutical Biotechnology · doi:10.2174/1389201015666141202105105 · Cited by 27
Bonacci, S., Corsi, I., & Focardi, S. E. (2009) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2009.01.002 · Cited by 27
Development of the motor nervous system in ascidians
Zaniolo, G., Lane, N. J., Burighel, P., & Manni, L. (2002) · The Journal of Comparative Neurology · doi:10.1002/cne.10097 · Cited by 27
Gambardella, C., Nichino, D., Iacometti, C., Ferrando, S., Falugi, C., & Faimali, M. (2018) · Aquatic Toxicology · doi:10.1016/j.aquatox.2018.01.006 · Cited by 27
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Campanari, M., García‐Ayllón, M., Blázquez‐Llorca, L., Luk, W. K. W., Tsim, K. W. K., & Sáez‐Valero, J. (2013) · Journal of Molecular Neuroscience · doi:10.1007/s12031-013-0183-5 · Cited by 28
Burighel, P., Sorrentino, M., Zaniolo, G., Thorndyke, M. C., & Manni, L. (2001) · Invertebrate Biology · doi:10.1111/j.1744-7410.2001.tb00123.x · Cited by 27
Arnon, R., Tarrab‐Hazdai, R., & Silman, I. (1999) · Protein Science · doi:10.1110/ps.8.12.2553 · Cited by 27
Yu, Q., Greig, N. H., Holloway, H. W., & Brossi, A. R. (1998) · Journal of Medicinal Chemistry · doi:10.1021/jm9800494 · Cited by 27
Cholinesterase activity in human pulmonary arteries and veins
Walch, L., de Taisne, C., Gascard, J., Nashashibi, N., Brink, C., & Norel, X. (1997) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0700158 · Cited by 27
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Coussen, F., Ayon, A., Goff, A. L., Leroy, J., Massoulié, J., & Bon, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010817200 · Cited by 30
Self-citationBucht, G., Wikström, P., & Hjalmarsson, K. (1999) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00079-5 · Cited by 27
Choi, R. C. Y. (1996) · Neuroscience Letters · doi:10.1016/s0304-3940(96)13102-5 · Cited by 27
Bernard, V., Legay, C., Massoulié, J., & Bloch, B. (1995) · Neuroscience · doi:10.1016/0306-4522(94)00497-s · Cited by 27
Self-citationPakravan, N., Shokrzadeh, M., Bari, M. K., & Shadboorestan, A. (2015) · Human & Experimental Toxicology · doi:10.1177/0960327115584990 · Cited by 26
Wu, Q., Fung, A. H. Y., Xu, M. L., Poon, K., Liu, E. Y. L., Kong, X. P., Yao, P., Xiong, Q. P., Dong, T. T.-X., & Tsim, K. W. K. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003729 · Cited by 26
Quintana, R. V., López-Durán, R. M., Milić, M., Bonassi, S., Ocaña, M. A. O., Urióstegui-Acosta, M., Pérez-Flores, G. A., Gómez‐Olivares, J. L., & Sánchez-Alarcón, J. (2021) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph18126269 · Cited by 26
Molecular and Biomechanical Adaptations to Mechanical Stretch in Cultured Myotubes
Ren, D., Song, J., Liu, R., Zeng, X., Xiao, Y., Zhang, Q., & Yuan, X. H. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.689492 · Cited by 26
Purification of Soluble Acetylcholinesterase from Sheep Liver by Affinity Chromatography
Askar, K. A., Kudi, A. C., & Moody, A. J. (2011) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-011-9254-7 · Cited by 26
Mor, F., & Özmen, Ö. (2009) · Pesticide Biochemistry and Physiology · doi:10.1016/j.pestbp.2009.10.004 · Cited by 26
Time-dependent kinetic complexities in cholinesterase-catalyzed reactions
Masson, P. (2012) · Biochemistry (Moscow) · doi:10.1134/s0006297912100070 · Cited by 26
Rodrigues, C., Guimarães, L., & Vieira, N. (2019) · Hydrobiologia · doi:10.1007/s10750-019-03991-7 · Cited by 27
Sakayanathan, P., Loganathan, C., Kandasamy, S., Valmiki, R. R., Kumaradhas, P., & Palvannan, T. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.08.168 · Cited by 27
Lan, T. T., Anh, D. T., Pham‐The, H., Dung, D. T. M., Hương, L. T. T., Park, E. J., Jeon, H. W., Kang, J. S., Thuần, N. T. D., Han, S., et al. (2019) · Medicinal Chemistry Research · doi:10.1007/s00044-019-02488-1 · Cited by 26
Hypermethioninemia Increases Cerebral Acetylcholinesterase Activity and Impairs Memory in Rats
Stefanello, F. M., Monteiro, S. C., Matté, C., Scherer, E. B. S., Netto, C. A., & Wyse, Â. T. D. S. (2007) · Neurochemical Research · doi:10.1007/s11064-007-9464-0 · Cited by 26
García‐Ayllón, M., Silveyra, M. X., Andreasen, N., Brimijoin, S., Blennow, K., & Sáez‐Valero, J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04461.x · Cited by 28
Marchot, P., Bourne, Y., Prowse, C. N., Bougis, P. E., & Taylor, P. (1998) · Toxicon · doi:10.1016/s0041-0101(98)00154-8 · Cited by 26
Hysteresis of butyrylcholinesterase in the approach to steady-state kinetics
Masson, P., Schopfer, L. M., Froment, M.-T., Debouzy, J. C., Nachon, F., Gillon, É., Lockridge, O., Hrabovská, A., & Goldstein, B. N. (2005) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2005.10.019 · Cited by 26
Rochu, D., Pernet, T., Renault, F., Bon, C., & Masson, P. (2001) · Journal of Chromatography A · doi:10.1016/s0021-9673(00)01211-5 · Cited by 26
Masson, P., Bec, N., Froment, M.-T., Nachon, F., Balny, C., Lockridge, O., & Schopfer, L. M. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04110.x · Cited by 26
Calcitonin gene‐related peptide decreases expression of acetylcholinesterase in mammalian myotubes
Boudreau‐Larivière, C., & Jasmin, B. J. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00015-0 · Cited by 26
Bourne, Y., Renault, L. L. R., & Marchot, P. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.603902 · Cited by 25
Akyüz, M., Yabo-Dambagi, L., Kılıç, T., & Çakır, A. (2022) · South African Journal of Botany · doi:10.1016/j.sajb.2022.01.040 · Cited by 25
Yücel, Y. Y., Tacal, Ö., & Özer, İ. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.07.006 · Cited by 25
Sigoillot, S. M., Bourgeois, F., Karmouch, J. L., Molgó, J., Dobbertin, A., Chevalier, C., Houlgatte, R., Leger, J. J., & Legay, C. (2016) · The FASEB Journal · doi:10.1096/fj.201500162 · Cited by 25
Metadata
- Authors
- Massoulié, J., Pezzementi, L., Bon, S., Krejci, E., & Vallette, F.-M.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Birmingham–Southern College (US)
- Institut de Biologie Physico-Chimique (FR)
- Venue
- Progress in Neurobiology
- Publisher
- Elsevier BV
- Published
- 1993-07
- Volume
- 41
- Issue
- 1
- Pages
- 31-91
- ISSN
- 0301-0082 (ISSN-L)
- OpenAlex
- W1971878065
- Cited by
- 1,214
- References
- 549
- Citations by year
- 2026: 15 · 2025: 24 · 2024: 34 · 2023: 35 · 2022: 40 · 2021: 30 · 2020: 33 · 2019: 28 · 2018: 29 · 2017: 31 · 2016: 35 · 2015: 29 · 2014: 25 · 2013: 27 · 2012: 30
- FWCI
- 10.08
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Progress in Neurobiology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Pharmacology (medical) › Cholinesterase and Neurodegenerative Diseases
- Physical Sciences › Chemistry › Organic Chemistry › Heterocyclic Compound Synthesis and Bioactivity
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme function and inhibition
- Keywords
- cholinesterase, acetylcholinesterase, butyrylcholinesterase, thiocarbohydrazones, enzyme inhibitors, structure-activity relationship, molecular docking, hydrogen bonding, donepezil comparison
- MeSH terms
- Animals, Cholinesterases, Humans, Muscles, Nervous System, Nervous System Physiological Phenomena
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