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Volumn 70, Issue 1, 2008, Pages 43-51

Rationale for diagnosing deficiency of ChEs and for applying exogenous HuChEs to the treatment of diseases

(1)  Shen, Zheng Xuan a  

a NONE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINESTERASE; CHOLINESTERASE;

EID: 36348929834     PISSN: 03069877     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mehy.2007.04.035     Document Type: Article
Times cited : (8)

References (72)
  • 1
    • 30444461377 scopus 로고    scopus 로고
    • The receptor concept: pharmacology's big idea
    • Rang H.P. The receptor concept: pharmacology's big idea. Br J Pharmacol 147 Suppl 1 (2006) S9-S16
    • (2006) Br J Pharmacol , vol.147 , Issue.SUPPL. 1
    • Rang, H.P.1
  • 2
    • 30444442330 scopus 로고    scopus 로고
    • Acetylcholine
    • Brown D.A. Acetylcholine. Br J Pharmacol 147 Suppl 1 (2006) S120-S126
    • (2006) Br J Pharmacol , vol.147 , Issue.SUPPL. 1
    • Brown, D.A.1
  • 3
    • 0034009408 scopus 로고    scopus 로고
    • Pesticides and susceptible populations: people with butyrylcholinesterase genetic variants may be at risk
    • Lockridge O., and Masson P. Pesticides and susceptible populations: people with butyrylcholinesterase genetic variants may be at risk. Neurotoxicology 21 1-2 (2000) 113-126
    • (2000) Neurotoxicology , vol.21 , Issue.1-2 , pp. 113-126
    • Lockridge, O.1    Masson, P.2
  • 4
    • 3242752041 scopus 로고    scopus 로고
    • Brain cholinesterases: I. The clinico-histopathological and biochemical basis of Alzheimer's disease
    • Shen Z.X. Brain cholinesterases: I. The clinico-histopathological and biochemical basis of Alzheimer's disease. Med Hyp 63 2 (2004) 285-297
    • (2004) Med Hyp , vol.63 , Issue.2 , pp. 285-297
    • Shen, Z.X.1
  • 5
    • 3242782586 scopus 로고    scopus 로고
    • Brain cholinesterases: II. The molecular and cellular basis of Alzheimer's disease
    • Shen Z.X. Brain cholinesterases: II. The molecular and cellular basis of Alzheimer's disease. Med Hyp 63 2 (2004) 308-321
    • (2004) Med Hyp , vol.63 , Issue.2 , pp. 308-321
    • Shen, Z.X.1
  • 6
    • 3242769206 scopus 로고    scopus 로고
    • Brain cholinesterases: III. Future perspectives of AD research and clinical practice
    • Shen Z.X. Brain cholinesterases: III. Future perspectives of AD research and clinical practice. Med Hyp 63 2 (2004) 298-307
    • (2004) Med Hyp , vol.63 , Issue.2 , pp. 298-307
    • Shen, Z.X.1
  • 7
    • 33646795325 scopus 로고    scopus 로고
    • Henry Dale and the discovery of acetylcholine
    • Tansey E.M. Henry Dale and the discovery of acetylcholine. C R Biol 329 5-6 (2006) 419-425
    • (2006) C R Biol , vol.329 , Issue.5-6 , pp. 419-425
    • Tansey, E.M.1
  • 8
    • 0031964633 scopus 로고    scopus 로고
    • Non-neuronal acetylcholine, a locally acting molecule, widely distributed in biological systems: expression and function in humans
    • Wessler I., Kirkpatrick C.J., and Racke K. Non-neuronal acetylcholine, a locally acting molecule, widely distributed in biological systems: expression and function in humans. Pharmacol Ther 77 1 (1998) 59-79
    • (1998) Pharmacol Ther , vol.77 , Issue.1 , pp. 59-79
    • Wessler, I.1    Kirkpatrick, C.J.2    Racke, K.3
  • 9
    • 0037470640 scopus 로고    scopus 로고
    • The non-neuronal cholinergic system in: expression, function and pathophysiology
    • Wessler I., Kilbinger H., Bittinger F., et al. The non-neuronal cholinergic system in: expression, function and pathophysiology. Life Sci 72 18-19 (2003) 2055-2061
    • (2003) Life Sci , vol.72 , Issue.18-19 , pp. 2055-2061
    • Wessler, I.1    Kilbinger, H.2    Bittinger, F.3
  • 10
    • 0141723971 scopus 로고    scopus 로고
    • High acetylcholine levels set circuit dynamics for attention and encoding and low acetylcholine levels set dynamics for consolidation
    • Hasselmo M.E., and McGaughy J. High acetylcholine levels set circuit dynamics for attention and encoding and low acetylcholine levels set dynamics for consolidation. Prog Brain Res 145 (2004) 207-231
    • (2004) Prog Brain Res , vol.145 , pp. 207-231
    • Hasselmo, M.E.1    McGaughy, J.2
  • 11
    • 34047234320 scopus 로고    scopus 로고
    • The non-neuronal cholinergic system of human skin
    • Kurzen H., Wessler I., Kirkpatrick C.J., et al. The non-neuronal cholinergic system of human skin. Horm Metab Res 39 2 (2007) 125-135
    • (2007) Horm Metab Res , vol.39 , Issue.2 , pp. 125-135
    • Kurzen, H.1    Wessler, I.2    Kirkpatrick, C.J.3
  • 12
    • 0037309371 scopus 로고    scopus 로고
    • Muscarinic and nicotinic cholinergic mechanisms in the mesostriatal dopamine systems
    • Zhou F.M., Wilson C., and Dani J.A. Muscarinic and nicotinic cholinergic mechanisms in the mesostriatal dopamine systems. Neuroscientist 9 1 (2003) 23-36
    • (2003) Neuroscientist , vol.9 , Issue.1 , pp. 23-36
    • Zhou, F.M.1    Wilson, C.2    Dani, J.A.3
  • 13
    • 33748932546 scopus 로고    scopus 로고
    • Termination and beyond: acetylcholinesterase as a modulator of synaptic transmission
    • Zimmerman G., and Soreq H. Termination and beyond: acetylcholinesterase as a modulator of synaptic transmission. Cell Tissue Res 326 2 (2006) 655-669
    • (2006) Cell Tissue Res , vol.326 , Issue.2 , pp. 655-669
    • Zimmerman, G.1    Soreq, H.2
  • 14
    • 0031846012 scopus 로고    scopus 로고
    • Cholinesterase affects dynamic transduction properties from vagal stimulation to heart rate
    • Nakahara T., Kawada T., Sugimachi M., et al. Cholinesterase affects dynamic transduction properties from vagal stimulation to heart rate. Am J Physiol 275 2 Pt 2 (1998) R541-R547
    • (1998) Am J Physiol , vol.275 , Issue.2 PART 2
    • Nakahara, T.1    Kawada, T.2    Sugimachi, M.3
  • 15
    • 23744450102 scopus 로고    scopus 로고
    • Acetylcholine modulates cortical synaptic transmission via different muscarinic receptors, as studied with receptor knockout mice
    • Kczewski N., Aztiria E., Gautam D., et al. Acetylcholine modulates cortical synaptic transmission via different muscarinic receptors, as studied with receptor knockout mice. J Physiol 566 Pt 3 (2005) 907-919
    • (2005) J Physiol , vol.566 , Issue.PART 3 , pp. 907-919
    • Kczewski, N.1    Aztiria, E.2    Gautam, D.3
  • 16
    • 0021989064 scopus 로고
    • Acetylcholinesterase: inhibition by tetranitromethane and arsenite. Binding of arsenite by tyrosine residues
    • Page J.D., and Wilson I.B. Acetylcholinesterase: inhibition by tetranitromethane and arsenite. Binding of arsenite by tyrosine residues. J Biol Chem 260 3 (1985) 1475-1478
    • (1985) J Biol Chem , vol.260 , Issue.3 , pp. 1475-1478
    • Page, J.D.1    Wilson, I.B.2
  • 17
    • 0021952040 scopus 로고
    • Butyrylcholinesterase: inhibition by arsenite, fluoride, and other ligands, cooperativity in binding
    • Page J.D., Wilson I.B., and Silman I. Butyrylcholinesterase: inhibition by arsenite, fluoride, and other ligands, cooperativity in binding. Mol Pharmacol 27 4 (1985) 437-443
    • (1985) Mol Pharmacol , vol.27 , Issue.4 , pp. 437-443
    • Page, J.D.1    Wilson, I.B.2    Silman, I.3
  • 18
    • 0023086090 scopus 로고
    • Acetylcholinesterase and monoamine oxidase in various brain structures in chronic alcoholic intoxication
    • Mel'nikova T.N., and Murav'eva L.I. Acetylcholinesterase and monoamine oxidase in various brain structures in chronic alcoholic intoxication. Zh Nevropatol Psikhiatr Im S S Korsakova 87 2 (1987) 235-237
    • (1987) Zh Nevropatol Psikhiatr Im S S Korsakova , vol.87 , Issue.2 , pp. 235-237
    • Mel'nikova, T.N.1    Murav'eva, L.I.2
  • 19
    • 0031044792 scopus 로고    scopus 로고
    • Cholinesterase. Its significance in anaesthetic practice
    • Davis L., Britten J.J., and Morgan M. Cholinesterase. Its significance in anaesthetic practice. Anaesthesia 52 3 (1997) 244-260
    • (1997) Anaesthesia , vol.52 , Issue.3 , pp. 244-260
    • Davis, L.1    Britten, J.J.2    Morgan, M.3
  • 20
    • 12944269052 scopus 로고    scopus 로고
    • Specific chemical and structural damage to proteins produced by synchrotron radiation
    • Weik M., Ravelli R.B., Kryger G., et al. Specific chemical and structural damage to proteins produced by synchrotron radiation. Proc Natl Acad Sci USA 97 2 (2000) 623-628
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.2 , pp. 623-628
    • Weik, M.1    Ravelli, R.B.2    Kryger, G.3
  • 21
    • 0042344717 scopus 로고    scopus 로고
    • 3,4-Methylenedioxymethamphetamine (MDMA) abuse markedly inhibits acetylcholinesterase activity and induces severe oxidative damage and liperoxidative damage
    • Zhou J.F., Zhou Y.H., Zhang L., et al. 3,4-Methylenedioxymethamphetamine (MDMA) abuse markedly inhibits acetylcholinesterase activity and induces severe oxidative damage and liperoxidative damage. Biomed Environ Sci 16 1 (2003) 53-61
    • (2003) Biomed Environ Sci , vol.16 , Issue.1 , pp. 53-61
    • Zhou, J.F.1    Zhou, Y.H.2    Zhang, L.3
  • 22
    • 11144250257 scopus 로고    scopus 로고
    • Diet-induced changes in AChE activity after long-term exposure
    • Kaizer R.R., da Silva A.C., Morsch V.M., et al. Diet-induced changes in AChE activity after long-term exposure. Neurochem Res 29 12 (2004) 2251-2255
    • (2004) Neurochem Res , vol.29 , Issue.12 , pp. 2251-2255
    • Kaizer, R.R.1    da Silva, A.C.2    Morsch, V.M.3
  • 23
    • 28744432034 scopus 로고    scopus 로고
    • Inhibition of acetylcholinesterase by the anticancer prodrug CPT-11
    • Hyatt J.L., Tsurkan L., Morton C.L., et al. Inhibition of acetylcholinesterase by the anticancer prodrug CPT-11. Chem Biol Interact 157-158 (2005) 247-252
    • (2005) Chem Biol Interact , vol.157-158 , pp. 247-252
    • Hyatt, J.L.1    Tsurkan, L.2    Morton, C.L.3
  • 24
    • 23744437423 scopus 로고    scopus 로고
    • Inhibition of human plasma cholinesterase by malachite green and related triarylmethane dyes: mechanistic implications
    • Kucukkilinc T., and Ozer I. Inhibition of human plasma cholinesterase by malachite green and related triarylmethane dyes: mechanistic implications. Arch Biochem Biophys 440 2 (2005) 118-122
    • (2005) Arch Biochem Biophys , vol.440 , Issue.2 , pp. 118-122
    • Kucukkilinc, T.1    Ozer, I.2
  • 25
    • 28244482330 scopus 로고    scopus 로고
    • Do metals inhibit acetylcholinesterase (AChE)? Implementation of assay conditions for the use of AChE activity as a biomarker of metal toxicity
    • Frasco M.F., Fournier D., Carvalho F., and Guilhermino L. Do metals inhibit acetylcholinesterase (AChE)? Implementation of assay conditions for the use of AChE activity as a biomarker of metal toxicity. Biomarkers 10 5 (2005) 360-375
    • (2005) Biomarkers , vol.10 , Issue.5 , pp. 360-375
    • Frasco, M.F.1    Fournier, D.2    Carvalho, F.3    Guilhermino, L.4
  • 26
    • 28444465103 scopus 로고    scopus 로고
    • Effects of widely used pharmaceuticals and a detergent on oxidative stress biomarkers of the crustacean Artemia parthenogenetica
    • Nunes B., Carvalho F., and Guilhermino L. Effects of widely used pharmaceuticals and a detergent on oxidative stress biomarkers of the crustacean Artemia parthenogenetica. Chemosphere 62 4 (2006) 581-594
    • (2006) Chemosphere , vol.62 , Issue.4 , pp. 581-594
    • Nunes, B.1    Carvalho, F.2    Guilhermino, L.3
  • 27
    • 27544478172 scopus 로고    scopus 로고
    • Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma
    • Li B., Sedlacek M., Manoharan I., et al. Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma. Biochem Pharmacol 70 11 (2005) 1673-1684
    • (2005) Biochem Pharmacol , vol.70 , Issue.11 , pp. 1673-1684
    • Li, B.1    Sedlacek, M.2    Manoharan, I.3
  • 28
    • 8144226101 scopus 로고    scopus 로고
    • A paradigm for single nucleotide polymorphism analysis: the case of the acetylcholinesterase gene
    • Hasin Y., Avidan N., Bercovich D., et al. A paradigm for single nucleotide polymorphism analysis: the case of the acetylcholinesterase gene. Hum Mutat 24 5 (2004) 408-416
    • (2004) Hum Mutat , vol.24 , Issue.5 , pp. 408-416
    • Hasin, Y.1    Avidan, N.2    Bercovich, D.3
  • 29
    • 23444455800 scopus 로고    scopus 로고
    • Cholinesterases: anchored enzymes in membranes and basal laminae
    • Krejci E. Cholinesterases: anchored enzymes in membranes and basal laminae. J Soc Biol 199 1 (2005) 55-60
    • (2005) J Soc Biol , vol.199 , Issue.1 , pp. 55-60
    • Krejci, E.1
  • 30
    • 0037176796 scopus 로고    scopus 로고
    • Three novel COLQ mutations and variation of phenotypic expressivity due to G240X
    • Shapira Y.A., Sadeh M.E., Bergtraum M.P., et al. Three novel COLQ mutations and variation of phenotypic expressivity due to G240X. Neurology 8 4 (2002) 603-609
    • (2002) Neurology , vol.8 , Issue.4 , pp. 603-609
    • Shapira, Y.A.1    Sadeh, M.E.2    Bergtraum, M.P.3
  • 31
    • 2942536284 scopus 로고    scopus 로고
    • Increased proNGF levels in subjects with mild cognitive impairment and mild Alzheimer disease
    • Peng S., Wuu J., Mufson E.J., and Fahnestock M. Increased proNGF levels in subjects with mild cognitive impairment and mild Alzheimer disease. J Neuropathol Exp Neurol 63 6 (2004) 641-649
    • (2004) J Neuropathol Exp Neurol , vol.63 , Issue.6 , pp. 641-649
    • Peng, S.1    Wuu, J.2    Mufson, E.J.3    Fahnestock, M.4
  • 32
    • 16844377812 scopus 로고    scopus 로고
    • The role of nerve growth factor receptors in cholinergic basal forebrain degeneration in prodromal Alzheimer disease
    • Counts S.E., and Mufson E.J. The role of nerve growth factor receptors in cholinergic basal forebrain degeneration in prodromal Alzheimer disease. J Neuropathol Exp Neurol 64 4 (2005) 263-272
    • (2005) J Neuropathol Exp Neurol , vol.64 , Issue.4 , pp. 263-272
    • Counts, S.E.1    Mufson, E.J.2
  • 33
    • 0024409092 scopus 로고
    • Choline levels are increased in cerebrospinal fluid of Alzheimer patients
    • Elble R., Giacobini E., and Higgins C. Choline levels are increased in cerebrospinal fluid of Alzheimer patients. Neurobiol Aging 10 1 (1989) 45-50
    • (1989) Neurobiol Aging , vol.10 , Issue.1 , pp. 45-50
    • Elble, R.1    Giacobini, E.2    Higgins, C.3
  • 34
    • 0034705173 scopus 로고    scopus 로고
    • Increased CSF levels of nerve growth factor in patients with Alzheimer's disease
    • Hock C., Heese K., Muller-Spahn F., et al. Increased CSF levels of nerve growth factor in patients with Alzheimer's disease. Neurology 54 10 (2000) 2009-2011
    • (2000) Neurology , vol.54 , Issue.10 , pp. 2009-2011
    • Hock, C.1    Heese, K.2    Muller-Spahn, F.3
  • 35
    • 27744453518 scopus 로고    scopus 로고
    • Cerebral acetylcholine esterase activity in mild cognitive impairment
    • Herholz K., Weisenbach S., Kalbe E., et al. Cerebral acetylcholine esterase activity in mild cognitive impairment. Neuroreport 16 13 (2005) 1431-1434
    • (2005) Neuroreport , vol.16 , Issue.13 , pp. 1431-1434
    • Herholz, K.1    Weisenbach, S.2    Kalbe, E.3
  • 36
    • 17144364730 scopus 로고    scopus 로고
    • Blood cells cholinesterase activity in early stage Alzheimer's disease and vascular dementia
    • von Bernhardi R., Alarcon R., Mezzano D., et al. Blood cells cholinesterase activity in early stage Alzheimer's disease and vascular dementia. Dement Geriatr Cogn Disord 19 4 (2005) 204-212
    • (2005) Dement Geriatr Cogn Disord , vol.19 , Issue.4 , pp. 204-212
    • von Bernhardi, R.1    Alarcon, R.2    Mezzano, D.3
  • 37
    • 85069033117 scopus 로고    scopus 로고
    • http://www.medscape.com/viewarticle/530368.
  • 38
    • 0037470614 scopus 로고    scopus 로고
    • Increased acetylcholine levels in skin biopsies of patients with atopic dermatitis
    • Wessler I., Reinheimer T., Kilbinger H., et al. Increased acetylcholine levels in skin biopsies of patients with atopic dermatitis. Life Sci 72 18-19 (2003) 2169-2172
    • (2003) Life Sci , vol.72 , Issue.18-19 , pp. 2169-2172
    • Wessler, I.1    Reinheimer, T.2    Kilbinger, H.3
  • 39
    • 23144441616 scopus 로고    scopus 로고
    • Expression of non-neuronal acetylcholine in lymphocytes and its contribution to the regulation of immune function
    • Kawashima K., and Fujii T. Expression of non-neuronal acetylcholine in lymphocytes and its contribution to the regulation of immune function. Front Biosci 9 (2004) 2063-2085
    • (2004) Front Biosci , vol.9 , pp. 2063-2085
    • Kawashima, K.1    Fujii, T.2
  • 40
    • 33646232738 scopus 로고    scopus 로고
    • Duration but not intensity of alcohol and tobacco exposure predicts p16INK4A homozygous deletion in head and neck squamous cell carcinoma
    • Kraunz K.S., McClean M.D., Nelson H.H., et al. Duration but not intensity of alcohol and tobacco exposure predicts p16INK4A homozygous deletion in head and neck squamous cell carcinoma. Cancer Res 66 8 (2006) 4512-4515
    • (2006) Cancer Res , vol.66 , Issue.8 , pp. 4512-4515
    • Kraunz, K.S.1    McClean, M.D.2    Nelson, H.H.3
  • 41
    • 22144452878 scopus 로고    scopus 로고
    • Risk of brain tumors in children and susceptibility to organophosphorus insecticides: the potential role of paraoxonase (PON1)
    • Searles Nielsen S., Mueller B.A., De Roos A.J., et al. Risk of brain tumors in children and susceptibility to organophosphorus insecticides: the potential role of paraoxonase (PON1). Environ Health Perspect 113 7 (2005) 909-913
    • (2005) Environ Health Perspect , vol.113 , Issue.7 , pp. 909-913
    • Searles Nielsen, S.1    Mueller, B.A.2    De Roos, A.J.3
  • 42
    • 33644813190 scopus 로고    scopus 로고
    • Epidemiologic and radiobiologic features of neoplasms in respiratory and gastrointestinal tracts among patients who had occupational contact with uranium
    • Shpagina L.A., Panacheva L.A., Potapenko A.T., et al. Epidemiologic and radiobiologic features of neoplasms in respiratory and gastrointestinal tracts among patients who had occupational contact with uranium. Med Tr Prom Ekol 11 (2005) 43-47
    • (2005) Med Tr Prom Ekol , Issue.11 , pp. 43-47
    • Shpagina, L.A.1    Panacheva, L.A.2    Potapenko, A.T.3
  • 43
    • 3242737375 scopus 로고    scopus 로고
    • Chromosomal aberrations in human lymphocytes exposed to the anticholinesterase pesticide isofenphos with mechanisms of leukemogenesis
    • Williams R.D., Boros L.G., Kolanko C.J., et al. Chromosomal aberrations in human lymphocytes exposed to the anticholinesterase pesticide isofenphos with mechanisms of leukemogenesis. Leukemia Res 28 (2004) 947-958
    • (2004) Leukemia Res , vol.28 , pp. 947-958
    • Williams, R.D.1    Boros, L.G.2    Kolanko, C.J.3
  • 44
    • 33845296073 scopus 로고    scopus 로고
    • Development of novel therapeutic strategies for lung cancer: targeting the cholinergic system
    • Russo P., Catassi A., Cesario A., and Servent D. Development of novel therapeutic strategies for lung cancer: targeting the cholinergic system. Curr Med Chem 13 29 (2006) 3493-3512
    • (2006) Curr Med Chem , vol.13 , Issue.29 , pp. 3493-3512
    • Russo, P.1    Catassi, A.2    Cesario, A.3    Servent, D.4
  • 46
    • 0029005015 scopus 로고
    • Clinical and analytical considerations in the utilization of cholinesterase measurements
    • McQueen M.J. Clinical and analytical considerations in the utilization of cholinesterase measurements. Clin Chim Acta 237 1-2 (1995) 91-105
    • (1995) Clin Chim Acta , vol.237 , Issue.1-2 , pp. 91-105
    • McQueen, M.J.1
  • 47
    • 23844437669 scopus 로고    scopus 로고
    • Alterations of serum cholinesterase in patients with gastric cancer
    • Gu S.Z., Zhao X.H., Quan P., et al. Alterations of serum cholinesterase in patients with gastric cancer. World J Gastroenterol 11 29 (2005) 4604-4606
    • (2005) World J Gastroenterol , vol.11 , Issue.29 , pp. 4604-4606
    • Gu, S.Z.1    Zhao, X.H.2    Quan, P.3
  • 48
    • 28744440838 scopus 로고    scopus 로고
    • Expression of cholinesterases in brain and non-brain tumours
    • Vidal C.J. Expression of cholinesterases in brain and non-brain tumours. Chem Biol Interact 157-158 (2005) 227-232
    • (2005) Chem Biol Interact , vol.157-158 , pp. 227-232
    • Vidal, C.J.1
  • 49
    • 33644863029 scopus 로고    scopus 로고
    • Cholinesterase activity of human lung tumours varies according to their histological classification
    • Martinez-Moreno P., Nieto-Ceron S., Torres-Lanzas J., et al. Cholinesterase activity of human lung tumours varies according to their histological classification. Carcinogenesis 27 3 (2006) 429-436
    • (2006) Carcinogenesis , vol.27 , Issue.3 , pp. 429-436
    • Martinez-Moreno, P.1    Nieto-Ceron, S.2    Torres-Lanzas, J.3
  • 50
    • 28744440975 scopus 로고    scopus 로고
    • Acetylcholinesterase: pivotal roles of its long omega loop (Cys69-Cys96) in regulating substrate binding
    • Bui J.M., and McCammon J.A. Acetylcholinesterase: pivotal roles of its long omega loop (Cys69-Cys96) in regulating substrate binding. Chem BiolInteract 157-158 (2005) 357-359
    • (2005) Chem BiolInteract , vol.157-158 , pp. 357-359
    • Bui, J.M.1    McCammon, J.A.2
  • 51
    • 33749076488 scopus 로고    scopus 로고
    • Cholinesterases are down-expressed in human colorectal carcinoma
    • Montenegro M.F., Ruiz-Espejo F., Campoy F.J., et al. Cholinesterases are down-expressed in human colorectal carcinoma. Cell Mol Life Sci 63 18 (2006) 2162-2175
    • (2006) Cell Mol Life Sci , vol.63 , Issue.18 , pp. 2162-2175
    • Montenegro, M.F.1    Ruiz-Espejo, F.2    Campoy, F.J.3
  • 52
    • 0020455652 scopus 로고
    • Acetylcholinesterase (AchE) activity of lymphocytes in chronic lymphoid leukemia (CLL)
    • Bartha E., Szelenyi J.G., and Hollan S.R. Acetylcholinesterase (AchE) activity of lymphocytes in chronic lymphoid leukemia (CLL). Leuk Res 6 6 (1982) 861-864
    • (1982) Leuk Res , vol.6 , Issue.6 , pp. 861-864
    • Bartha, E.1    Szelenyi, J.G.2    Hollan, S.R.3
  • 53
    • 7544233448 scopus 로고    scopus 로고
    • The lymphocytic cholinergic system and its modulation by organophosphorus pesticides
    • Tarkowski M., Lutz W., and Birindelli S. The lymphocytic cholinergic system and its modulation by organophosphorus pesticides. Int J Occup Med Environ Health 17 3 (2004) 325-337
    • (2004) Int J Occup Med Environ Health , vol.17 , Issue.3 , pp. 325-337
    • Tarkowski, M.1    Lutz, W.2    Birindelli, S.3
  • 54
    • 0029670364 scopus 로고    scopus 로고
    • Tetrameric (G4) acetylcholinesterase: structure, localization, and physiological regulation
    • Fernandez H.L., Moreno R.D., and Inestrosa N.C. Tetrameric (G4) acetylcholinesterase: structure, localization, and physiological regulation. J Neurochem 66 4 (1996) 1335-1346
    • (1996) J Neurochem , vol.66 , Issue.4 , pp. 1335-1346
    • Fernandez, H.L.1    Moreno, R.D.2    Inestrosa, N.C.3
  • 55
    • 27944448944 scopus 로고    scopus 로고
    • Early onset of puberty: tracking genetic and environmental factors
    • Parent A.S., Rasier G., Gerard A., et al. Early onset of puberty: tracking genetic and environmental factors. Horm Res 64 Suppl 2 (2005) 41-47
    • (2005) Horm Res , vol.64 , Issue.SUPPL. 2 , pp. 41-47
    • Parent, A.S.1    Rasier, G.2    Gerard, A.3
  • 56
    • 19744364810 scopus 로고    scopus 로고
    • Pharmacokinetics and pharmacodynamics of mivacurium in patients phenotypically homozygous for the atypical plasma cholinesterase variant: effect of injection of human cholinesterase
    • Østergaard D., Viby-Mogensen J., Rasmussen S.N., Gätke M.R., and Varin F. Pharmacokinetics and pharmacodynamics of mivacurium in patients phenotypically homozygous for the atypical plasma cholinesterase variant: effect of injection of human cholinesterase. Anesthesiology 102 6 (2005) 1124-1132
    • (2005) Anesthesiology , vol.102 , Issue.6 , pp. 1124-1132
    • Østergaard, D.1    Viby-Mogensen, J.2    Rasmussen, S.N.3    Gätke, M.R.4    Varin, F.5
  • 57
    • 13444270325 scopus 로고    scopus 로고
    • Novel pharmacological approaches for the antagonism of neuromuscular blockade
    • Pic L.C. Novel pharmacological approaches for the antagonism of neuromuscular blockade. AANA J 73 1 (2005) 37-40
    • (2005) AANA J , vol.73 , Issue.1 , pp. 37-40
    • Pic, L.C.1
  • 58
    • 85069021327 scopus 로고    scopus 로고
    • Lockridge O, Schopfer LM, Winger G, Woods JH. Large scale purification of butyrylcholinesterase from human plasma suitable for injection into monkeys; a potential new therapeutic for protection against cocaine and nerve agent toxicity. J Med Chem Biol Radiol Def. 3:nihms5095.
  • 59
    • 28744449011 scopus 로고    scopus 로고
    • Bioscavengers for the protection of humans against organophosphate toxicity
    • Doctor B.P., and Saxena A. Bioscavengers for the protection of humans against organophosphate toxicity. Chem Biol Interact 157-158 (2005) 167-171
    • (2005) Chem Biol Interact , vol.157-158 , pp. 167-171
    • Doctor, B.P.1    Saxena, A.2
  • 60
    • 28744458362 scopus 로고    scopus 로고
    • In vitro and in vivo characterization of recombinant human butyrylcholinesterase (Protexia) as a potential nerve agent bioscavenger
    • Cerasoli D.M., Griffiths E.M., Doctor B.P., et al. In vitro and in vivo characterization of recombinant human butyrylcholinesterase (Protexia) as a potential nerve agent bioscavenger. Chem Biol Interact 157-158 (2005) 363-365
    • (2005) Chem Biol Interact , vol.157-158 , pp. 363-365
    • Cerasoli, D.M.1    Griffiths, E.M.2    Doctor, B.P.3
  • 61
    • 33747617345 scopus 로고    scopus 로고
    • Comparison of polyethylene glycol-conjugated recombinant human acetylcholinesterase and serum human butyrylcholinesterase as bioscavengers of organophosphate compounds
    • Cohen O., Kronman C., Raveh L., et al. Comparison of polyethylene glycol-conjugated recombinant human acetylcholinesterase and serum human butyrylcholinesterase as bioscavengers of organophosphate compounds. Mol Pharmacol 70 3 (2006) 1121-1131
    • (2006) Mol Pharmacol , vol.70 , Issue.3 , pp. 1121-1131
    • Cohen, O.1    Kronman, C.2    Raveh, L.3
  • 62
    • 11144270154 scopus 로고    scopus 로고
    • Lipsome-formulated enzymes for organophosphate scavenging: butyrylcholinesterase and Demeton-S
    • Fischer S., Arad A., and Margalit R. Lipsome-formulated enzymes for organophosphate scavenging: butyrylcholinesterase and Demeton-S. Arch Biochem Biophys 434 1 (2005) 108-115
    • (2005) Arch Biochem Biophys , vol.434 , Issue.1 , pp. 108-115
    • Fischer, S.1    Arad, A.2    Margalit, R.3
  • 63
    • 28744447563 scopus 로고    scopus 로고
    • Characterizing pea acetylcholinesterase
    • Muralidharan M., Soreq H., and Mor T.S. Characterizing pea acetylcholinesterase. Chem Biol Inter 157-158 (2005) 406-407
    • (2005) Chem Biol Inter , vol.157-158 , pp. 406-407
    • Muralidharan, M.1    Soreq, H.2    Mor, T.S.3
  • 64
    • 28744449989 scopus 로고    scopus 로고
    • Delivery of human acetylcholinesterase by adeno-associated virus to the acetylcholinesterase knockout mouse
    • Hrabovska A., Duysen E.G., Sanders J.D., et al. Delivery of human acetylcholinesterase by adeno-associated virus to the acetylcholinesterase knockout mouse. Chem Biol Interact 157-158 (2005) 71-78
    • (2005) Chem Biol Interact , vol.157-158 , pp. 71-78
    • Hrabovska, A.1    Duysen, E.G.2    Sanders, J.D.3
  • 65
    • 0023239299 scopus 로고
    • Acetylcholinesterase and butyrylcholinesterase activity in the cerebrospinal fluid of patients with neurodegenerative diseases involving cholinergic systems
    • Ruberg M., Villageois A., Bonnet A.M., et al. Acetylcholinesterase and butyrylcholinesterase activity in the cerebrospinal fluid of patients with neurodegenerative diseases involving cholinergic systems. J Neurol Neurosurg Psychiatry 50 5 (1987) 538-543
    • (1987) J Neurol Neurosurg Psychiatry , vol.50 , Issue.5 , pp. 538-543
    • Ruberg, M.1    Villageois, A.2    Bonnet, A.M.3
  • 66
    • 0022631832 scopus 로고
    • Acetylcholinesterase and butyrylcholinesterase in frontal cortex and cerebrospinal fluid of demented and non-demented patients with Parkinson's disease
    • Ruberg M., Rieger F., Villageois A., et al. Acetylcholinesterase and butyrylcholinesterase in frontal cortex and cerebrospinal fluid of demented and non-demented patients with Parkinson's disease. Brain Res 362 1 (1986) 83-91
    • (1986) Brain Res , vol.362 , Issue.1 , pp. 83-91
    • Ruberg, M.1    Rieger, F.2    Villageois, A.3
  • 67
    • 4444347674 scopus 로고    scopus 로고
    • Pharmacotherapy of chronic fatigue syndrome: another gallant attempt
    • Straus S.E. Pharmacotherapy of chronic fatigue syndrome: another gallant attempt. JAMA 292 10 (2004) 1234-1235
    • (2004) JAMA , vol.292 , Issue.10 , pp. 1234-1235
    • Straus, S.E.1
  • 68
    • 32444441009 scopus 로고    scopus 로고
    • Using anticholinergics to treat overactive bladder: the issue of treatment tolerability
    • Staskin D.R., and MacDiarmid S.A. Using anticholinergics to treat overactive bladder: the issue of treatment tolerability. Am J Med 119 3 Suppl 1 (2006) 9-15
    • (2006) Am J Med , vol.119 , Issue.3 SUPPL. 1 , pp. 9-15
    • Staskin, D.R.1    MacDiarmid, S.A.2
  • 69
    • 23244452563 scopus 로고    scopus 로고
    • The role of urinary urgency and its measurement in the overactive bladder symptom syndrome: current concepts and future prospects
    • Brading A.F. The role of urinary urgency and its measurement in the overactive bladder symptom syndrome: current concepts and future prospects. BJU Int 96 3 (2005) 441-442
    • (2005) BJU Int , vol.96 , Issue.3 , pp. 441-442
    • Brading, A.F.1
  • 70
    • 34047106626 scopus 로고    scopus 로고
    • Duysen EG, Li B, Darvesh S, Lockridge O. Sensitivity of butyrylcholinesterase Tknockout mice to (-)-huperzine A and donepezil suggests humans with butyrylcholinesterase deficiency may not tolerate these Alzheimer's disease drugs and indicates butyrylcholinesterase function in neurotransmission. Toxicol doi10.1016/j.tox 2006.11.069.
  • 71
    • 10844222503 scopus 로고    scopus 로고
    • Impaired formation of the inner retina in an AChE knockout mouse results in degeneration of all photoreceptors
    • Bytyqi A.H., Lockridge O., Duysen E., et al. Impaired formation of the inner retina in an AChE knockout mouse results in degeneration of all photoreceptors. Eur J Neurosci 20 11 (2004) 2953-2962
    • (2004) Eur J Neurosci , vol.20 , Issue.11 , pp. 2953-2962
    • Bytyqi, A.H.1    Lockridge, O.2    Duysen, E.3
  • 72
    • 33646913370 scopus 로고    scopus 로고
    • A mutation liked with autism reveals a common mechanism of endoplasmic reticulum retention for the alpha, beta-hydrlase fold protein family
    • De Jaco A., Comoletti D., Kovarik Z., et al. A mutation liked with autism reveals a common mechanism of endoplasmic reticulum retention for the alpha, beta-hydrlase fold protein family. J Biol Chem 281 14 (2006) 9667-9676
    • (2006) J Biol Chem , vol.281 , Issue.14 , pp. 9667-9676
    • De Jaco, A.1    Comoletti, D.2    Kovarik, Z.3


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