Acetylcholinesterase inhibitors as Alzheimer therapy: From nerve toxins to neuroprotection

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

Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein

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

Acetylcholinesterase Accelerates Assembly of Amyloid-β-Peptides into Alzheimer's Fibrils: Possible Role of the Peripheral Site of the Enzyme

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

The Toxins of Cyanobacteria

Carmichael, W. W. (1994) · Scientific American · doi:10.1038/scientificamerican0194-78 · Cited by 1,100

Acetylcholinesterase: Enzyme structure, reaction dynamics, and virtual transition states

Quinn, D. M. (1987) · Chemical Reviews · doi:10.1021/cr00081a005 · Cited by 1,072

Autoimmune Response to Acetylcholine Receptor

Patrick, J., & Lindstrom, J. M. (1973) · Science · doi:10.1126/science.180.4088.871 · Cited by 1,049

Mechanism of Action of Organophosphorus and Carbamate Insecticides

Fukuto, T. R. (1990) · Environmental Health Perspectives · doi:10.1289/ehp.9087245 · Cited by 1,043

Tau pathology in Alzheimer disease and other tauopathies

Iqbal, K., del C. Alonso, A., Chen, S., Chohan, M. O., El-Akkad, E., Gong, C.-X., Khatoon, S., Li, B., Liu, F., Rahman, A., et al. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.09.008 · Cited by 1,037

Review Article: Genetics of Alzheimer Disease

Bekris, L. M., Yu, C.-E., Bird, T. D., & Tsuang, D. W. (2010) · Journal of Geriatric Psychiatry and Neurology · doi:10.1177/0891988710383571 · Cited by 1,029

Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase.

Harel, M., Schalk, I. J., Ehret‐Sabatier, L., Bouet, F., Goeldner, M. P., HIRTH, C. G., Axelsen, P. H., Silman, I., & Sussman, J. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.19.9031 · Cited by 902

Alzheimer's Disease: Molecular Understanding Predicts Amyloid-Based Therapeutics

Selkoe, D. J., & Schenk, D. (2003) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.43.100901.140248 · Cited by 829

The Molecular Forms of Cholinesterase and Acetylcholinesterase in Vertebrates

Massoulié, J., & Bon, S. (1982) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.05.030182.000421 · Cited by 818

Organophosphates⧸Nerve Agent Poisoning: Mechanism of Action, Diagnosis, Prophylaxis, And Treatment

Bajgar, J. (2004) · Advances in clinical chemistry · doi:10.1016/s0065-2423(04)38006-6 · Cited by 701

Targeting acetylcholinesterase and butyrylcholinesterase in dementia

Lane, R. M., Potkin, S. G., & Enz, A. (2005) · The International Journal of Neuropsychopharmacology · doi:10.1017/s1461145705005833 · Cited by 654

ULTRASTRUCTURAL STUDIES IN ALZHEIMER'S PRESENILE DEMENTIA.

Terry, R. D., Gonatas, N. K., & WEISS, M. (1964) · PubMed Central · Cited by 644

The Prevalence and Malignancy of Alzheimer Disease

Katzman, R. (1976) · Archives of Neurology · doi:10.1001/archneur.1976.00500040001001 · Cited by 623

Poisoning due to organophosphate insecticides

Namba, T., Nolte, C. T., Jackrel, J., & Grob, D. (1971) · The American Journal of Medicine · doi:10.1016/0002-9343(71)90337-8 · Cited by 586

Medical Aspects of Chemical and Biological Warfare

Wilde, H. D. (1998) · JAMA · doi:10.1001/jama.280.13.1199 · Cited by 578

Organophosphorus pesticides; organic and biological chemistry

Etō, M. (1974) · Cited by 547

A review on coumarins as acetylcholinesterase inhibitors for Alzheimer’s disease

Anand, P., Singh, B., & Singh, N. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.12.042 · Cited by 530

Prevalence and Malignancy of Alzheimer Disease

Lijtmaer, H., Fuld, P. A., & Katzman, R. (1976) · Archives of Neurology · doi:10.1001/archneur.1976.00500040088017 · Cited by 517

Organophosphorus pesticides: Organic and biological chemistry

Hart, G. J. (1975) · Pesticide Biochemistry and Physiology · doi:10.1016/0048-3575(75)90061-9 · Cited by 501

Functional network disruption in the degenerative dementias

Pievani, M., de Haan, W., Wu, T., Seeley, W. W., & Frisoni, G. B. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(11)70158-2 · Cited by 481

A Structural Motif of Acetylcholinesterase That Promotes Amyloid β-Peptide Fibril Formation

Ferrari, G. V. D., Canales, M. A., Shin, I., Weiner, L. M., Silman, I., & Inestrosa, N. C. (2001) · Biochemistry · doi:10.1021/bi0101392 · Cited by 415

Organophosphorus Ester-Induced Delayed Neurotoxicity

Abou-Donia, M. B. (1981) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.21.040181.002455 · Cited by 404

THE FINE STRUCTURE OF NEUROFIBRILLARY TANGLES IN ALZHEIMERʼS DISEASE

Terry, R. D. (1963) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-196310000-00005 · Cited by 403 · cited 2×

Calcium hypothesis of Alzheimer’s disease

Berridge, M. J. (2009) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-009-0736-1 · Cited by 394

Review of Oximes in the Antidotal Treatment of Poisoning by Organophosphorus Nerve Agents

Kassa, J. (2002) · Journal of Toxicology Clinical Toxicology · doi:10.1081/clt-120015840 · Cited by 391

Occupational exposure to pesticides increases the risk of incident AD

Hayden, K. M., Norton, M. C., Darcey, D. J., Østbye, T., Zandi, P. P., Breitner, J. C. S., & Welsh-Bohmer, K. A. (2010) · Neurology · doi:10.1212/wnl.0b013e3181dd4423 · Cited by 387

CHOLINESTERASES, A TARGET OF PHARMACOLOGY AND TOXICOLOGY

Pohanka, M. (2011) · Biomedical Papers · doi:10.5507/bp.2011.036 · Cited by 377

Neurofibrillary tangles of paired helical filaments

Wı́sniewski, H. M., Narang, H. K., & Terry, R. D. (1976) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(76)90059-9 · Cited by 372

Interaction of fluorescence probes with acetylcholinesterase. Site and specificity of propidium binding

Taylor, P., & Lappi, S. (1975) · Biochemistry · doi:10.1021/bi00680a029 · Cited by 367

Acetylcholinesterase inhibitory activity of some Amaryllidaceae alkaloids and Narcissus extracts

López, S., Bastida, J., Viladomat, F., & Codina, C. J. (2002) · Life Sciences · doi:10.1016/s0024-3205(02)02034-9 · Cited by 359

Highly Potent, Selective, and Low Cost Bis-tetrahydroaminacrine Inhibitors of Acetylcholinesterase

Pang, Y., Quiram, P. A., Jelacic, T. M., Hong, F., & Brimijoin, S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.39.23646 · Cited by 344

Linking Calcium to Aβ and Alzheimer's Disease

Green, K. N., & LaFerla, F. M. (2008) · Neuron · doi:10.1016/j.neuron.2008.07.013 · Cited by 332

The Peripheral Anionic Site of Acetylcholinesterase: Structure, Functions and Potential Role in Rational Drug Design

Johnson, G., & Moore, S. W. (2005) · Current Pharmaceutical Design · doi:10.2174/138161206775193127 · Cited by 322

Stable Complexes Involving Acetylcholinesterase and Amyloid-β Peptide Change the Biochemical Properties of the Enzyme and Increase the Neurotoxicity of Alzheimer’s Fibrils

Alvarez, A. R., Alarcón, R., Opazo, C., Campos, E. O., Muñoz, F. J., Calderón, F. H., Dajas, F., Gentry, M. K., Doctor, B. P., Mello, F. G. D., et al. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-09-03213.1998 · Cited by 320

Galantamine — a Novel Cholinergic Drug with a Unique Dual Mode of Action for the Treatment of Patients with Alzheimer's Disease

Lilienfeld, S. (2002) · CNS Drug Reviews · doi:10.1111/j.1527-3458.2002.tb00221.x · Cited by 309

Acetylcholinesterase promotes the aggregation of amyloid-beta-peptide fragments by forming a complex with the growing fibrils.

Álvarez, A., Opazo, C., Alarcón, R., Garrido, J., & Inestrosa, N. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1245 · Cited by 308

Chemical warfare agents: II. nerve agents

Sidell, F. R., & Borak, J. (1992) · Annals of Emergency Medicine · doi:10.1016/s0196-0644(05)81036-4 · Cited by 288

Organophosphorus compounds as chemical warfare agents: a review

Delfino, R. T., Ribeiro, T. S., & Figueroa‐Villar, J. D. (2009) · Journal of the Brazilian Chemical Society · doi:10.1590/s0103-50532009000300003 · Cited by 283

Developing β‐secretase inhibitors for treatment of Alzheimer’s disease

Ghosh, A. K., Brindisi, M., & Tang, J. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07476.x · Cited by 282

New Tacrine–4-Oxo-4H-chromene Hybrids as Multifunctional Agents for the Treatment of Alzheimer’s Disease, with Cholinergic, Antioxidant, and β-Amyloid-Reducing Properties

Fernández‐Bachiller, M. I., Pérez, C., Monjas, L., Rademann, J., & Rodrı́guez-Franco, M. I. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm201460y · Cited by 271

Multi-Target-Directed Drug Design Strategy: From a Dual Binding Site Acetylcholinesterase Inhibitor to a Trifunctional Compound against Alzheimer’s Disease

Bolognesi, M. L., Cavalli, A., Valgimigli, L., Bartolini, M., Rosini, M., Andrisano, V., Recanatini, M., & Melchiorre, C. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm701225u · Cited by 266

Amyloid–cholinesterase interactions

Inestrosa, N. C., Dinamarca, M. C., & Alvarez, A. R. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2007.06238.x · Cited by 261

Post‐synaptic potentiation: interaction between quanta of acetylcholine at the skeletal neuromuscular synapse.

Hartzell, H. C., Kuffler, S. W., & Yoshikami, D. (1975) · The Journal of Physiology · doi:10.1113/jphysiol.1975.sp011102 · Cited by 258

Novel Tacrine−Melatonin Hybrids as Dual-Acting Drugs for Alzheimer Disease, with Improved Acetylcholinesterase Inhibitory and Antioxidant Properties

Rodrı́guez-Franco, M. I., Fernández‐Bachiller, M. I., Pérez, C., Hernández‐Ledesma, B., & Bartolomé, B. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm050746d · Cited by 250

Acetylcholinesterase

Rosenberry, T. L. (1975) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122884.ch3 · Cited by 249

Calcium Ionophore Increases Amyloid .beta. Peptide Production by Cultured Cells

Querfurth, H. W., & Selkoe, D. J. (1994) · Biochemistry · doi:10.1021/bi00181a016 · Cited by 247

Hydrogen Peroxide Is Generated during the Very Early Stages of Aggregation of the Amyloid Peptides Implicated in Alzheimer Disease and Familial British Dementia

Tabner, B. J., El‐Agnaf, O. M. A., Turnbull, S., German, M. J., Paleologou, K. E., Hayashi, Y., Cooper, L. J., Fullwood, N. J., & Allsop, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500238200 · Cited by 243

Crystal structure of an acetylcholinesterase–fasciculin complex: interaction of a three-fingered toxin from snake venom with its target

Harel, M., Kleywegt, G. J., Ravelli, R. B. G., Silman, I., & Sussman, J. L. (1995) · Structure · doi:10.1016/s0969-2126(01)00273-8 · Cited by 242

Anatoxin-a(s), a potent anticholinesterase from Anabaena flos-aquae

Matsunaga, S., Moore, R. E., Niemczura, W. P., & Carmichael, W. W. (1989) · Journal of the American Chemical Society · doi:10.1021/ja00202a057 · Cited by 240

Introduction to insect biology and diversity

Daly, H. V., Doyen, J. T., & Ehrlich, P. R. (1978) · Cited by 230

Rational Approach To Discover Multipotent Anti-Alzheimer Drugs

Rosini, M., Andrisano, V., Bartolini, M., Bolognesi, M. L., Hrelia, P., Minarini, A., Tarozzi, A., & Melchiorre, C. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm049112h · Cited by 228

Introduction to Insect Biology and Diversity

Zenger, J. T., Daly, H. V., Doyen, J. T., & Purcell, A. H. (1999) · Florida Entomologist · doi:10.2307/3495844 · Cited by 217

Calcium dysregulation in Alzheimer's disease

Bojarski, Ł., Herms, J. W., & Kuźnicki, J. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.10.002 · Cited by 207

Mitochondrial Dysfunction: The First Domino in Brain Aging and Alzheimer's Disease?

Leuner, K., Hauptmann, S., Abdel-Kader, R. M., Scherping, I., Keil, U., Strosznajder, J. B., Eckert, A., & Müller, W. E. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1763 · Cited by 195

Novel donepezil-based inhibitors of acetyl- and butyrylcholinesterase and acetylcholinesterase-induced beta-amyloid aggregation.

Camps, P., Formosa, X., Galdeano, C., Gómez, T., Muñoz-Torrero, D., Scarpellini, M., Viayna, E., Badía, A., Clos, M. V., Camins, A., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm8001313 · Cited by 194

Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding.

Avigdor Shafferman, C., Kronman, C., Flashner, Y., Leitner, M., Grosfeld, H., Ordentlich, A., Gozes, Y., Cohen, S., Ariel, N., & Barak, D. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)37091-7 · Cited by 192

Inhibition of Acetylcholinesterase, β-Amyloid Aggregation, and NMDA Receptors in Alzheimer’s Disease: A Promising Direction for the Multi-target-Directed Ligands Gold Rush

Rosini, M., Simoni, E., Bartolini, M., Cavalli, A., Ceccarini, L., Pascu, N., McClymont, D. W., Tarozzi, A., Bolognesi, M. L., Minarini, A., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800577j · Cited by 186

Tau Proteins and Neurofibrillary Degeneration

Goedert, M., Spillantini, M. G., & Crowther, R. A. (1991) · Brain Pathology · doi:10.1111/j.1750-3639.1991.tb00671.x · Cited by 178

Termination and beyond: acetylcholinesterase as a modulator of synaptic transmission

Zimmerman, G., & Soreq, H. (2006) · Cell and Tissue Research · doi:10.1007/s00441-006-0239-8 · Cited by 171

Anesthesia and myasthenia gravis

Blichfeldt‐Lauridsen, L., & HANSEN, B. D. (2011) · Acta Anaesthesiologica Scandinavica · doi:10.1111/j.1399-6576.2011.02558.x · Cited by 170

CHEMICAL WARFARE

Holstege, C. P., Kirk, M., & Sidell, F. R. (1997) · Critical Care Clinics · doi:10.1016/s0749-0704(05)70374-2 · Cited by 169

The Nicotinic Allosteric Potentiating Ligand Galantamine Facilitates Synaptic Transmission in the Mammalian Central Nervous System

Santos, M. D., Alkondon, M., Pereira, E. F. R., Aracava, Y., Eisenberg, H. M., Maelicke, A., & Albuquerque, E. X. (2002) · Molecular Pharmacology · doi:10.1124/mol.61.5.1222 · Cited by 169

Risk factors for Alzheimer's disease and dementia

Prince, M. J., FRANZCP, M. C., & MANN, A. H. (1994) · Neurology · doi:10.1212/wnl.44.1.97 · Cited by 163

Chemical warfare agents: Toxicology and treatment

Watson, K. D. (1997) · General Pharmacology The Vascular System · doi:10.1016/s0306-3623(97)89718-2 · Cited by 163

Peripheral and Dual Binding Site Acetylcholinesterase Inhibitors: Implications in treatment of Alzheimers Disease

Castro, A., & Martı́nez, A. (2001) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557013406864 · Cited by 160

Donepezil–tacrine hybrid related derivatives as new dual binding site inhibitors of AChE

Alonso, D. A., Dorronsoro, I., Rubio, L., Muñoz, P., García‐Palomero, E., del Monte, M., Bidon‐Chanal, A., Orozco, M., Luque, F. J., Castro, A., et al. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.09.029 · Cited by 158

The Pharmacology of Physostigmine

Triggle, D. J., Mitchell, J. M., & Filler, R. (1998) · CNS Drug Reviews · doi:10.1111/j.1527-3458.1998.tb00059.x · Cited by 156

A Textbook of Clinical Neurology.

(1947) · Archives of Internal Medicine · doi:10.1001/archinte.1947.00220170127009 · Cited by 155

Design, Synthesis, and Biological Evaluation of Conformationally Restricted Rivastigmine Analogues

Bolognesi, M. L., Bartolini, M., Cavalli, A., Andrisano, V., Rosini, M., Minarini, A., & Melchiorre, C. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm049782n · Cited by 150

The role of tau phosphorylation and cleavage in neuronal cell death

Chun, W. (2006) · Frontiers in bioscience · doi:10.2741/2097 · Cited by 144

The role of excitotoxicity in organophosphorous nerve agents central poisoning

Solberg, Y., & Belkin, M. (1997) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(97)89540-5 · Cited by 140

Common structural features determine the effectiveness of carvedilol, daunomycin and rolitetracycline as inhibitors of Alzheimer β-amyloid fibril formation

Howlett, D. R., George, A. R., OWEN, D. E., Ward, R. V., & Markwell, R. E. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3430419 · Cited by 132

The role of excitotoxicity in organophosphorous nerve agents central poisoning

Solber, Y., & Belkin, M. (1997) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(97)90617-9 · Cited by 131

Primary structures of the catalytic subunits from two molecular forms of acetylcholinesterase. A comparison of NH2-terminal and active center sequences.

MacPhee-Quigley, K., Taylor, P., & Taylor, S. S. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39005-1 · Cited by 129

Common structural features determine the effectiveness of carvedilol, daunomycin and rolitetracycline as inhibitors of Alzheimer beta-amyloid fibril formation.

Howlett, D. R., George, A. R., OWEN, D. E., Ward, R. V., & Markwell, R. E. (1999) · PubMed Central · Cited by 123

Calcium-mediated Transient Phosphorylation of Tau and Amyloid Precursor Protein Followed by Intraneuronal Amyloid-β Accumulation

Pierrot, N., Santos, S. F., Feyt, C., Morel, M., Brion, J., & Octave, J. N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606015200 · Cited by 121

Indole alkaloids from Tabernaemontana australis (Müell. Arg) Miers that inhibit acetylcholinesterase enzyme

Andrade, M. T., Lima, J. A., Pinto, A. C., Rezende, C. M., Carvalho, M. P., & Epifanio, R. D. A. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.03.045 · Cited by 117

Design, Synthesis, and Pharmacological Profile of Novel Fused Pyrazolo[4,3- d ]pyridine and Pyrazolo[3,4- b ][1,8]naphthyridine Isosteres: A New Class of Potent and Selective Acetylcholinesterase Inhibitors

Barreiro, E. J., Câmara, C. A., Verli, H., Brazil-Más, L., Castro, N. G., Cintra, W. M., Aracava, Y., Rodrigues, C. R., & Fraga, C. A. M. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm020391n · Cited by 113

Novel Benzisoxazole Derivatives as Potent and Selective Inhibitors of Acetylcholinesterase

Villalobos, A., Blake, J. F., Bíggers, C. K., Butler, T. W., Chapin, D. S., Chen, Y. L., Ives, J. L., Jones, S. B., & Liston, D. R. (1994) · Journal of Medicinal Chemistry · doi:10.1021/jm00043a012 · Cited by 112

Ligand binding properties of acetylcholinesterase determined with fluorescent probes

Mooser, G., & Sigman, D. S. (1974) · Biochemistry · doi:10.1021/bi00708a010 · Cited by 111

Further Bioactive Piperidine Alkaloids from the Flowers and Green Fruits of Cassia spectabilis

Viegas, C., Bolzani, V. D. S., Furlan, M., Barreiro, E. J., Young, M. C. M., Tomazela, D. M., & Eberlin, M. N. (2004) · Journal of Natural Products · doi:10.1021/np0303963 · Cited by 110

Neuroprotective and Cholinergic Properties of Multifunctional Glutamic Acid Derivatives for the Treatment of Alzheimer’s Disease

Arce, M. P., Rodrı́guez-Franco, M. I., González-Muñoz, G. C., Pérez, C., López, B., Villarroya, M., López, M. G., Garcı́a, A. G., & Conde, S. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900628z · Cited by 109

Synthesis of Tricyclic 1,3-Oxazin-4-ones and Kinetic Analysis of Cholesterol Esterase and Acetylcholinesterase Inhibition

Pietsch, M., & Gütschow, M. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm0508639 · Cited by 106

Progress in Clinical, Pharmacological, Chemical and Structural Biological Studies of Huperzine A: A Drug of Traditional Chinese Medicine Origin for the Treatment of Alzheimers Disease

Jiang, H., Luo, X., & Bai, D. (2003) · Current Medicinal Chemistry · doi:10.2174/0929867033456747 · Cited by 106

Galangin, a flavonol derived from Rhizoma Alpiniae Officinarum, inhibits acetylcholinesterase activity in vitro

Guo, A. J. Y., Xie, H. Q., Choi, R. C. Y., Zheng, Y., Bi, C. W. C., Xu, S. L., Dong, T. T.-X., & Tsim, K. W. K. (2010) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.05.002 · Cited by 104

Homobivalent Quinazolinimines as Novel Nanomolar Inhibitors of Cholinesterases with Dirigible Selectivity toward Butyrylcholinesterase

Decker, M. W. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm060682m · Cited by 101

Targeting Alzheimer’s disease: Novel indanone hybrids bearing a pharmacophoric fragment of AP2238

Rizzo, S., Bartolini, M., Ceccarini, L., Piazzi, L., Gobbi, S., Cavalli, A., Recanatini, M., Andrisano, V., & Rampa, A. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.01.071 · Cited by 99

Synthesis, biological evaluation, and molecular modeling of berberine derivatives as potent acetylcholinesterase inhibitors

Huang, L., Shi, A., He, F., & Li, X. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.12.035 · Cited by 94

A Higher Form of Killing: The Secret Story of Chemical and Biological Warfare

Harris, R., & Paxman, J. (1982) · Virtual Defense Library (Ministerio de Defensa) · Cited by 93

Synthesis, biological evaluation and molecular modelling of diversely functionalized heterocyclic derivatives as inhibitors of acetylcholinesterase/butyrylcholinesterase and modulators of Ca2+ channels and nicotinic receptors

Marco, J. L., Rı́os, C. D. L., Garcı́a, A. G., Villarroya, M., Carreiras, M. C., Martins, C., Eleutério, A., Morreale, A., Orozco, M., & Luque, F. J. (2004) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2004.02.017 · Cited by 91

Contemporary Anticholinesterase Pharmaceuticals of Natural Origin and Their Synthetic Analogues for the Treatment of Alzheimers Disease

Orhan, G., Orhan, I., Subutay-Oztekin, N., Ak, F., & Sener, B. (2009) · Recent Patents on CNS Drug Discovery · doi:10.2174/157488909787002582 · Cited by 90

Cholinesterase Inhibitors: Xanthostigmine Derivatives Blocking the Acetylcholinesterase-Induced β-Amyloid Aggregation

Belluti, F., Rampa, A., Piazzi, L., Bisi, A., Gobbi, S., Bartolini, M., Andrisano, V., Cavalli, A., Recanatini, M., & Valenti, P. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm049515h · Cited by 87

Fluorescence energy transfer on acetylcholinesterase: spatial relationship between peripheral site and active center

Berman, H. A., Yguerabide, J., & Taylor, P. (1980) · Biochemistry · doi:10.1021/bi00551a036 · Cited by 86

Novel tricyclic quinazolinimines and related tetracyclic nitrogen bridgehead compounds as cholinesterase inhibitors with selectivity towards butyrylcholinesterase

Decker, M. W., Krauth, F., & Lehmann, J. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.10.044 · Cited by 85

Histopathology and APOE genotype of the first Alzheimer disease patient, Auguste D.

Graeber, M. B., Kösel, S., Grasbon-Frodl, E. M., Möller, H. ‐., & Mehraein, P. (1998) · Neurogenetics · doi:10.1007/s100480050033 · Cited by 82

Clinical effects of organophosphorus cholinesterase inhibitors

Sidell, F. R. (1994) · Journal of Applied Toxicology · doi:10.1002/jat.2550140212 · Cited by 80

Synthesis and evaluation of tacrine–Huperzine a hybrids as acetylcholinesterase inhibitors of potential interest for the treatment of alzheimer’s disease

Badı́a, A., Baños, J.-E., Camps, P., Contreras, J., GOERBIG, D. M., Muñoz‐Torrero, D., Simón, M., & Vivas, N. M. (1998) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(98)00015-7 · Cited by 80

N-Benzylpiperidine derivatives of 1,2,4-thiadiazolidinone as new acetylcholinesterase inhibitors

Martı́nez, A., Fernandez, E., Castro, A., Conde, S., Rodrı́guez-Franco, M. I., Baños, J.-E., & Badı́a, A. (2000) · European Journal of Medicinal Chemistry · doi:10.1016/s0223-5234(00)01166-1 · Cited by 79

Methyl Analogues of the Experimental Alzheimer Drug Phenserine: Synthesis and Structure/Activity Relationships for Acetyl- and Butyrylcholinesterase Inhibitory Action

Yu, Q., Holloway, H. W., Flippen-Anderson, J. L., Hoffman, B., Brossi, A. R., & Greig, N. H. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm010080x · Cited by 79

Synthesis, biological evaluation and molecular modeling of oxoisoaporphine and oxoaporphine derivatives as new dual inhibitors of acetylcholinesterase/butyrylcholinesterase

Tang, H., Wei, Y., Zhang, C., Ning, F.-X., Qiao, W., Huang, S., Ma, L., Huang, Z., & Gu, L. (2009) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2009.01.021 · Cited by 75

Acetylcholinesterase: C-terminal domains, molecular forms and functional localization

Massoulié, J., Anselmet, A., Bon, S., Krejci, É., Legay, C., Morel, N., & Simon, S. (1998) · Journal of Physiology-Paris · doi:10.1016/s0928-4257(98)80007-7 · Cited by 73

Metrifonate for Alzheimer's disease

López-Arrieta, J., & Schneider, L. S. S. (2006) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd003155.pub3 · Cited by 72

Design, synthesis and evaluation of galanthamine derivatives as acetylcholinesterase inhibitors

Jia, P. J., Sheng, R., Zhang, J., Fang, L., He, Q., Yang, B., & Hu, Y. (2008) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2008.04.018 · Cited by 70

Synthesis and Pharmacological Evaluation of Huprine−Tacrine Heterodimers: Subnanomolar Dual Binding Site Acetylcholinesterase Inhibitors

Camps, P., Formosa, X., Muñoz‐Torrero, D., Pétrignet, J., Badı́a, A., & Clos, M. V. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm0496741 · Cited by 70

Protein Tau: Prime Cause of Synaptic and Neuronal Degeneration in Alzheimer's Disease

Crespo‐Biel, N., Theunis, C., & LEUVEN, F. V. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/251426 · Cited by 69

Hybrids of oxoisoaporphine-tacrine congeners: Novel acetylcholinesterase and acetylcholinesterase-induced β-amyloid aggregation inhibitors

Tang, H., Zhao, L.-Z., Zhao, H., Huang, S., Zhong, S., Qin, J., Chen, Z., Huang, Z., & Liang, H. (2011) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2011.08.002 · Cited by 68

Cognitive Deficits in the Early Stages of Alzheimer's Disease

Storandt, M. (2008) · Current Directions in Psychological Science · doi:10.1111/j.1467-8721.2008.00574.x · Cited by 68

Cholinesterase inhibitors: SAR and enzyme inhibitory activity of 3-[ω-(benzylmethylamino)alkoxy]xanthen-9-ones

Piazzi, L., Belluti, F., Bisi, A., Gobbi, S., Rizzo, S., Bartolini, M., Andrisano, V., Recanatini, M., & Rampa, A. (2006) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2006.09.026 · Cited by 67

Bioactive and other piperidine alkaloids from Cassia leptophylla

Bolzani, V. D. S., Gunatilaka, A. A. L., & Kingston, D. G. I. (1995) · Tetrahedron · doi:10.1016/0040-4020(95)00254-6 · Cited by 67

Synthesis and Screening for Antiacetylcholinesterase Activity of (1-Benzyl-4-oxopiperidin-3-ylidene)methylindoles and -pyrroles Related to Donepezil

Andreani, A., Cavalli, A., Granaiola, M., Guardigli, M., Leoni, A., Locatelli, A., Morigi, R., Rambaldi, M., Recanatini, M., & Roda, A. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm0109356 · Cited by 66

Synthesis and in vitro evaluation of N-alkyl-7-methoxytacrine hydrochlorides as potential cholinesterase inhibitors in Alzheimer disease

Korábečný, J., Musílek, K., Holas, O., Binder, J., Zemek, F., Marek, J., Pohanka, M., Opletalová, V., Dohnal, V., & Kuča, K. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.08.044 · Cited by 65

New selective acetylcholinesterase inhibitors designed from natural piperidine alkaloids

Viegas, C., Bolzani, V. D. S., Pimentel, L. S. B., Castro, N. G., Cabral, R. F., da Costa, R. S., Floyd, C., Rocha, M. S., Young, M. C. M., Barreiro, E. J., et al. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.04.030 · Cited by 64

Synthesis and acetylcholinesterase/butyrylcholinesterase inhibition activity of new tacrine-like analogues

Marco, J. L., Rı́os, C. D. L., Carreiras, M. C., Baños, J.-E., Badı́a, A., & Vivas, N. M. (2001) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(00)00284-4 · Cited by 63

Design, synthesis, and evaluation of 2-phenoxy-indan-1-one derivatives as acetylcholinesterase inhibitors

Sheng, R., Lin, X., Li, J., Jiang, Y., Shang, Z., & Hu, Y. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.05.132 · Cited by 63

Alzheimer's Disease

Wilkins, R. H., & Brody, I. A. (1969) · Archives of Neurology · doi:10.1001/archneur.1969.00480130123013 · Cited by 63

Further Studies on the Interaction of the 5-Hydroxytryptamine3(5-HT3) Receptor with Arylpiperazine Ligands. Development of a New 5-HT3Receptor Ligand Showing Potent Acetylcholinesterase Inhibitory Properties

Cappelli, A., Gallelli, A., Manini, M., Anzini, M., Mennuni, L., Makovec, F., Menziani, M. C., Alcaro, S., Ortuso, F., & Vomero, S. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm0493461 · Cited by 62

Differential effects of "peripheral" site ligands on Torpedo and chicken acetylcholinesterase.

Eichler, J., Anselment, A., Sussman, J. L., Massoulié, J., & Silman, I. (1994) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)09933-x · Cited by 62

Kinetics and structure–activity relationship studies on pregnane-type steroidal alkaloids that inhibit cholinesterases

Khalid, A., Ul‐Haq, Z., Anjum, S., Khan, M. R., Rahman, A., & Choudhary, M. I. (2004) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2004.03.002 · Cited by 59

Structure–activity relationships for inhibition of human cholinesterases by alkyl amide phenothiazine derivatives

Darvesh, S., McDonald, R. S., Penwell, A., Conrad, S., Darvesh, K. V., Mataija, D., Gomez, G., Caines, A., Walsh, R., & Martin, E. V. (2004) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2004.09.059 · Cited by 58

Onchidal: a naturally occurring irreversible inhibitor of acetylcholinesterase with a novel mechanism of action.

Abramson, S. N., Radić, Z., Manker, D. C., Faulkner, D. J., & Taylor, P. (1989) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)09328-9 · Cited by 58

Synthetic approaches to carnegine, a simple tetrahydroisoquinoline alkaloid

Bracca, A. B. J., & Kaufman, T. S. (2004) · Tetrahedron · doi:10.1016/j.tet.2004.08.033 · Cited by 58

Bivalent Ligands Derived from Huperzine A as Acetylcholinesterase Inhibitors

Haviv, H., Wong, D. M., Silman, I., & Sussman, J. L. (2007) · Current Topics in Medicinal Chemistry · doi:10.2174/156802607779941215 · Cited by 56

Anticholinesterase Agents

Koelle, G. B., Volle, R. L., Holmstedt, B. R., Karczmar, A. G., & O'Brien, R. D. (1963) · Science · doi:10.1126/science.141.3575.63 · Cited by 56

Novel Anticholinesterases Based on the Molecular Skeletons of Furobenzofuran and Methanobenzodioxepine

Luo, W., Yu, Q., Zhan, M., Parrish, D. A., Deschamps, J. R., Kulkarni, S. S., Holloway, H. W., Alley, G. M., Lahiri, D. K., Brossi, A. R., et al. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm049309+ · Cited by 55

A novel anti-Alzheimer's disease drug, ladostigil

Weinreb, O., Amit, T., Bar‐Am, O., & Youdim, M. B. H. (2011) · International review of neurobiology · doi:10.1016/b978-0-12-386467-3.00010-8 · Cited by 54

Selective Cholinesterase Inhibitory Activities of a New Monoterpene Diglycoside and Other Constituents from Nelumbo nucifera Stamens

Jung, H. A., Jung, Y. J., Hyun, S. K., Min, B.-S., Kim, D., Jung, J. H., & Choi, J. S. (2010) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.33.267 · Cited by 54

Search for dual function inhibitors for Alzheimer’s disease: Synthesis and biological activity of acetylcholinesterase inhibitors of pyridinium-type and their Aβ fibril formation inhibition capacity

Kapková, P., Alptüzün, V., Frey, P., Erciyas, E., & Holzgrabe, U. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.08.034 · Cited by 54

New potential AChE inhibitor candidates

de Paula, A. A. N., Martins, J. B. L., dos Santos, M. L., Nascente, L. D. C., Romeiro, L. A. S., Areas, T. F. M. A., Vieira, K. S. T., Gambôa, N. F., Castro, N. G., & Gargano, R. (2009) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2009.03.045 · Cited by 52

Novel γ-secretase modulators for the treatment of Alzheimer's disease: a review focusing on patents from 2010 to 2012

Pettersson, M., Stepan, A. F., Kauffman, G. W., & Johnson, D. S. (2013) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2013.821465 · Cited by 51

Behring's discovery of diphtheria and tetanus antitoxins

Fj, G. (1992) · Immunology Today · doi:10.1016/0167-5699(92)90125-q · Cited by 49

Synthesis and efficacy of 1-[bis(4-fluorophenyl)-methyl]piperazine derivatives for acetylcholinesterase inhibition, as a stimulant of central cholinergic neurotransmission in Alzheimer’s disease

Sadashiva, C. T., Chandra, J. N. N. S., Ponnappa, K. C., Gowda, T. V., & Rangappa, K. S. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.05.030 · Cited by 49

Spectroscopic studies on acetylcholinesterase: influence of peripheral-site occupation on active-center conformation

Berman, H. A., Becktel, W. J., & Taylor, P. (1981) · Biochemistry · doi:10.1021/bi00519a043 · Cited by 48

Structural Determinants of Torpedo c alifornica Acetylcholinesterase Inhibition by the Novel and Orally Active Carbamate Based Anti-Alzheimer Drug Ganstigmine (CHF-2819)

Bartolucci, C., Siotto, M., Ghidini, E., Amari, G., Bolzoni, P. T., Racchi, M., Villetti, G., Delcanale, M., & Lamba, D. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm060293s · Cited by 47

Acetylcholinesterase inhibitory potential of a carbazole alkaloid, mahanimbine, from Murraya koenigii

Satheeshkumar, N., Mukherjee, P. K., Bhadra, S., Saha, B. P., & Pal, B. C. (2009) · Phytotherapy Research · doi:10.1002/ptr.3023 · Cited by 47

Inhibition of histamine versus acetylcholine metabolism as a mechanism of tacrine activity

Morisset‐Lopez, S., Traiffort, É., & Schwartz, J. (1996) · European Journal of Pharmacology · doi:10.1016/s0014-2999(96)00738-8 · Cited by 46

Subacute Neurotoxicity Induced in Mice by Potent Organophosphorus Neuropathy Target Esterase Inhibitors

Wu, S., & Casida, J. E. (1996) · Toxicology and Applied Pharmacology · doi:10.1006/taap.1996.0158 · Cited by 46

Synthesis, anticholinesterase activity and structure–Activity relationships of m-Aminobenzoic acid derivatives

Trujillo-Ferrara, J. G., Cano, L. M., & Espinoza-Fonseca, M. (2003) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(03)00198-7 · Cited by 46

p–Aminobenzoic acid derivatives as acetylcholinesterase inhibitors

Correa‐Basurto, J., Alcántara, I. V., Espinoza-Fonseca, M., & Trujillo-Ferrara, J. G. (2005) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2005.03.011 · Cited by 44

Synthesis, Biological Activity, and Docking Studies of New Acetylcholinesterase Inhibitors of the Bispyridinium Type

Kapková, P., Stiefl, N., Sürig, U., Engels, B., Baumann, K., & Holzgrabe, U. (2003) · Archiv der Pharmazie · doi:10.1002/ardp.200300795 · Cited by 44

Molecular Docking Studies of Natural Cholinesterase-Inhibiting Steroidal Alkaloids from Sarcococca saligna

Ul‐Haq, Z., Wellenzohn, B., Liedl, K. R., & Rode, B. M. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm0309194 · Cited by 43

Fluorescent phosphonate label for serine hydrolases, pyrenebutyl methylphosphonofluoridate: reaction with acetylcholinesterase

Berman, H. A., & Taylor, P. (1978) · Biochemistry · doi:10.1021/bi00602a019 · Cited by 43

Acetylcholinesterase Inhibitory Activity of Uleine from Himatanthus lancifolius

Seidl, C., Correia, B. L., Stinghen, A. E. M., & Santos, C. A. D. M. (2010) · Zeitschrift für Naturforschung C · doi:10.1515/znc-2010-7-804 · Cited by 43

Characterisation of the anticholinesterase activity of two new tacrine–huperzine A hybrids

Alcalá, M. D. M., Vivas, N. M., Camps, P., Muñoz‐Torrero, D., & Badı́a, A. (2003) · Neuropharmacology · doi:10.1016/s0028-3908(03)00071-6 · Cited by 43

Molecular recognition by acetylcholinesterase at the peripheral anionic site: structure–activity relationships for inhibitions by aryl carbamates

Lin, G., Lai, C., & Liao, W. (1999) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(99)00213-8 · Cited by 41

Preparation of secolycorines against acetylcholinesterase

Lee, S., Venkatesham, U., Rao, C. P., Lam, S.-H., & Lin, J. (2006) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2006.10.026 · Cited by 40

Central Cholinergic Agents. 6. Synthesis and Evaluation of 3-[1-(Phenylmethyl)-4-piperidinyl]-1-(2,3,4,5-tetrahydro-1H-1-benzazepin-8-yl)- 1-propanones and Their Analogs as Central Selective Acetylcholinesterase Inhibitors

Ishihara, Y., Hirai, K., Miyamoto, M., & Goto, G. (1994) · Journal of Medicinal Chemistry · doi:10.1021/jm00041a007 · Cited by 40

Synthesis and cholinesterase activity of phenylcarbamates related to Rivastigmine, a therapeutic agent for Alzheimer's disease

Mustazza, C., Borioni, A., Giudice, M. R. D., GATTA, F., Ferretti, R., Meneguz, A., Volpe, M. T., & Lorenzini, P. (2002) · European Journal of Medicinal Chemistry · doi:10.1016/s0223-5234(01)01324-1 · Cited by 39

Inhibition of Butyrylcholinesterase Activity by Some Isoquinoline Alkaloids

Jitka Ulrichová, A., Walterová, D., Preininger, V., & Šimánek, V. (1983) · Planta Medica · doi:10.1055/s-2007-969916 · Cited by 39

Isoquinoline derivatives as potential acetylcholinesterase inhibitors

Markmee, S., Ruchirawat, S., Prachyawarakorn, V., Ingkaninan, K., & Khorana, N. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.01.067 · Cited by 39

A Study of the SORL1 Gene in Alzheimer's Disease and Cognitive Function

Liu, F., Ikram, M. A., Janssens, A. C. J. W., Schuur, M., de Koning, I., Isaacs, A. J., Struchalin, M. V., Uitterlinden, A. G., den Dunnen, J. T., Sleegers, K., et al. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1137 · Cited by 38

New potent human acetylcholinesterase inhibitors in the tetracyclic triterpene series with inhibitory potency on amyloid β aggregation

Rouleau, J., Iorga, B. I., & Guillou, C. (2011) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2011.02.073 · Cited by 38

Synthesis of physostigmine analogues and evaluation of their anticholinesterase activities

Zhan, Z., Bian, H.-L., Wang, J., & Shan, W. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.01.097 · Cited by 38

Isoprenoids in aging and neurodegeneration

Edlund, C., Söderberg, M. P., & Kristensson, K. (1994) · Neurochemistry International · doi:10.1016/0197-0186(94)90050-7 · Cited by 36

Synthesis and structure–activity relationships of open D-Ring galanthamine analogues

Herlem, D., Martin, M., Thal, C., & Guillou, C. (2003) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(03)00397-4 · Cited by 34

Biological Mass Spectrometry. Basic Information on Nerve Gas and the Use of Sarin by Aum Shinrikyo. Plenary Lecture at the Biological Mass Spectrometry Conference Seto, Aichi, Japan July 3-6, 1995.

Tu, A. T. (1996) · Journal of the Mass Spectrometry Society of Japan · doi:10.5702/massspec.44.293 · Cited by 34

[13] Acetylcholinesterase

Rosenberry, T. L., Barnett, P., & Mays, C. (1982) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(82)82070-3 · Cited by 34

Prelude to the Discovery of Penicillin

Landsberg, H. (1949) · Isis · doi:10.1086/349043 · Cited by 32

Design, synthesis, and evaluation of benzophenone derivatives as novel acetylcholinesterase inhibitors

Belluti, F., Piazzi, L., Bisi, A., Gobbi, S., Bartolini, M., Cavalli, A., Valenti, P., & Rampa, A. (2008) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2008.02.035 · Cited by 32

Phenserine: a physostigmine derivative that is a long-acting inhibitor of cholinesterase and demonstrates a wide dose range for attenuating a scopolamine-induced learning impairment of rats in a 14-unit T-maze

Iijima, S., Greig, N. H., Garofalo, P., Spangler, E. L., Heller, B., Brossi, A. R., & Ingram, D. K. (1993) · Psychopharmacology · doi:10.1007/bf02244888 · Cited by 32

Terreulactone A, a novel meroterpenoid with anti-acetylcholinesterase activity from Aspergillus terreus

Kim, W., Cho, K., Lee, C., & Yoo, I. D. (2002) · Tetrahedron Letters · doi:10.1016/s0040-4039(02)00465-3 · Cited by 32

Amino acid sequence in the region of the reactive serine residue of eel acetylcholinesterase

Schaffer, N. K., Michel, H. O., & Bridges, A. F. (1973) · Biochemistry · doi:10.1021/bi00739a027 · Cited by 31

Latanoprost and Physostigmine Have Mostly Additive Ocular Hypotensive Effects in Human Eyes

Lindén, C. (1997) · Archives of Ophthalmology · doi:10.1001/archopht.1997.01100160027004 · Cited by 31

Antinociceptive Profile of (-)-Spectaline: A Piperidine Alkaloid fromCassia leptophylla

Alexandre‐Moreira, M. S., Viegas, C., Miranda, A. L. P., Bolzani, V. D. S., & Barreiro, E. J. (2003) · Planta Medica · doi:10.1055/s-2003-43201 · Cited by 29

Active site directed docking studies: Synthesis and pharmacological evaluation of cis-2,6-dimethyl piperidine sulfonamides as inhibitors of acetylcholinesterase

Girisha, H. R., Chandra, J. N. N. S., Boppana, S., Malviya, M., Sadashiva, C. T., & Rangappa, K. S. (2009) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2009.04.042 · Cited by 29

Oroxylin A analogs exhibited strong inhibitory activities against iNOS-mediated nitric oxide (NO) production

Pham, T.-A. N., Che, H., Phan, P.-T. T., Lee, J., Kim, S., & Park, H. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.01.135 · Cited by 29

Contemporary opinions about Mary Walker

Keesey, J. (1998) · Neurology · doi:10.1212/wnl.51.5.1433 · Cited by 29

The Crystal Structure of a Complex of Acetylcholinesterase with a Bis-(−)-nor-meptazinol Derivative Reveals Disruption of the Catalytic Triad

Paz, A., Xie, Q., Greenblatt, H. M., Fu, W., Tang, Y., Silman, I., Qiu, Z., & Sussman, J. L. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm801657v · Cited by 28

Synthesis and Acetylcholinesterase/Butyrylcholinesterase Inhibition Activity of 4-Amino-2, 3-diaryl-5, 6, 7, 8-tetrahydrofuro(and thieno)[2, 3-b]-quinolines, and 4-Amino-5, 6, 7, 8, 9-pentahydro-2, 3-diphenylcyclohepta[e]furo(and thieno)-[2, 3-b]pyridines

Marco, J. L., Rı́os, C. D. L., Carreiras, M. C., Baños, J.-E., Badı́a, A., & Vivas, N. M. (2002) · Archiv der Pharmazie · doi:10.1002/1521-4184(200209)335:7 · Cited by 28

Stephaoxocanine, a Novel Dihydroisoquinoline Alkaloid from Stephania cepharantha

Kashiwaba, N., Morooka, S., Kimura, M., Ono, M., Toda, J., Suzuki, H., & Sano, T. (1996) · Journal of Natural Products · doi:10.1021/np960381n · Cited by 27

Reversible and irreversible inhibitory activity of succinic and maleic acid derivatives on acetylcholinesterase

Trujillo-Ferrara, J. G., Vázquez, I., Espinosa, J., Santillan, R. L., Farfán, N., & Herbert Höpfl, B. (2003) · European Journal of Pharmaceutical Sciences · doi:10.1016/s0928-0987(03)00023-x · Cited by 27

Eletefine, a Stephaoxocane Alkaloid from Cissampelos glaberrima

da Cunha, E. V. L., Cornélio, M. L., Barbosa‐Filho, J. M., Braz‐Filho, R., & Gray, A. I. (1998) · Journal of Natural Products · doi:10.1021/np980018b · Cited by 26

Isoterreulactone A, a novel meroterpenoid with anti-acetylcholinesterase activity produced by Aspergillus terreus

Yoo, I., Cho, K., Lee, C., & Kim, W. (2004) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2004.10.067 · Cited by 26

2-N-Methylexcentricine, a New Alkaloid from Roots of Stephania excentrica

Deng, J., & Zhao, S. (1997) · Journal of Natural Products · doi:10.1021/np960371m · Cited by 25

Multiple enzyme inhibitions by histamine H3 receptor antagonists as potential procognitive agents.

Petroianu, G. A., Arafat, K., Sasse, B. C., & Stark, H. (2006) · PubMed · Cited by 25

Chemical terrorism: a primer for 2002.

Goozner, B., Lutwick, L. I., & Bourke, E. (2002) · PubMed · Cited by 25

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