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Volumn 88, Issue 1, 2010, Pages 155-166

Cholinesterase activity in brain of senescence-accelerated-resistant mouse SAMR1 and its variation in brain of senescence-accelerated-prone mouse SAMP8

Author keywords

Acetylcholinesterase; Butyrylcholinesterase; Cholinergic neurotransmission; Cognitive impairment; Gliosis

Indexed keywords

ACETYLCHOLINESTERASE; AMYLOID BETA PROTEIN; CHOLINESTERASE; DETERGENT; DIMER; GLIAL FIBRILLARY ACIDIC PROTEIN; LECTIN; MARKER; MESSENGER RNA; MONOMER; TETRAMER;

EID: 73949131047     PISSN: 03604012     EISSN: 10974547     Source Type: Journal    
DOI: 10.1002/jnr.22177     Document Type: Article
Times cited : (18)

References (65)
  • 1
    • 0026794041 scopus 로고
    • Changes in acetylcholinesterase and butyrylcholinesterase in Alzheimer's disease resemble embryonic development. A study of molecular forms
    • Arendt T, Brückner MK, Lange M, Bigl V. 1992. Changes in acetylcholinesterase and butyrylcholinesterase in Alzheimer's disease resemble embryonic development. A study of molecular forms. Neurochem Int 21:381-396.
    • (1992) Neurochem Int , vol.21 , pp. 381-396
    • Arendt, T.1    Brückner, M.K.2    Lange, M.3    Bigl, V.4
  • 2
    • 0141867783 scopus 로고    scopus 로고
    • Efflux of human and mouse amyloid β proteins 1-40 and 1-42 from brain: Impairment in a mouse model of Alzheimer's disease
    • Banks WA, Robinson SM, Verma S, Morley JE. 2003. Efflux of human and mouse amyloid β proteins 1-40 and 1-42 from brain: impairment in a mouse model of Alzheimer's disease. Neuroscience 121:487-492.
    • (2003) Neuroscience , vol.121 , pp. 487-492
    • Banks, W.A.1    Robinson, S.M.2    Verma, S.3    Morley, J.E.4
  • 4
    • 26244456297 scopus 로고    scopus 로고
    • The senescence-accelerated prone mouse (SAMP8): A model of age-related cognitive decline with relevance to alterations of the gene expression and protein abnormalities in Alzheimer's disease
    • Butterfield DA, Poon HF. 2005. The senescence-accelerated prone mouse (SAMP8): a model of age-related cognitive decline with relevance to alterations of the gene expression and protein abnormalities in Alzheimer's disease. Exp Gerontol 40:774-783.
    • (2005) Exp Gerontol , vol.40 , pp. 774-783
    • Butterfield, D.A.1    Poon, H.F.2
  • 5
    • 0030833450 scopus 로고    scopus 로고
    • Glycosylation of acetylcholinesterase forms in microsomal membranes from normal and dystrophic Lama2dy mouse muscle
    • Cabezas-Herrera J, Moral-Naranjo MT, Campoy FJ, Vidal CJ. 1997. Glycosylation of acetylcholinesterase forms in microsomal membranes from normal and dystrophic Lama2dy mouse muscle. J Neurochem 69:1964-1974.
    • (1997) J Neurochem , vol.69 , pp. 1964-1974
    • Cabezas-Herrera, J.1    Moral-Naranjo, M.T.2    Campoy, F.J.3    Vidal, C.J.4
  • 6
    • 0027932932 scopus 로고
    • Two-site immunoradiometric assay of chicken acetylcholinesterase: Active and inactive molecular forms in brain and muscle
    • Chatel JM, Eichler J, Vallette FM, Bon S, Massolié J, Grassi J. 1994. Two-site immunoradiometric assay of chicken acetylcholinesterase: active and inactive molecular forms in brain and muscle. J Neurochem 63:1111-1118.
    • (1994) J Neurochem , vol.63 , pp. 1111-1118
    • Chatel, J.M.1    Eichler, J.2    Vallette, F.M.3    Bon, S.4    Massolié, J.5    Grassi, J.6
  • 7
    • 33847168242 scopus 로고    scopus 로고
    • Differential gene expression profiles in the hippocampus of senescence- accelerated mouse
    • Cheng XR, Zhou WX, Zhang YX, Zhou DS, Yang RF, Chen LF. 2007. Differential gene expression profiles in the hippocampus of senescence- accelerated mouse. Neurobiol Aging 28:497-506.
    • (2007) Neurobiol Aging , vol.28 , pp. 497-506
    • Cheng, X.R.1    Zhou, W.X.2    Zhang, Y.X.3    Zhou, D.S.4    Yang, R.F.5    Chen, L.F.6
  • 10
    • 33750005095 scopus 로고    scopus 로고
    • Differential CSF butyrylcholinesterase levels in Alzheimer's disease with the ApoE-ε4 allele, in relation to cognitive function and cerebral glucose metabolism
    • Darreh-Shori T, Brimijoin S, Kadir A, Almkvist O, Nordberg A. 2006. Differential CSF butyrylcholinesterase levels in Alzheimer's disease with the ApoE-ε4 allele, in relation to cognitive function and cerebral glucose metabolism. Neurobiol Dis 24:326-333.
    • (2006) Neurobiol Dis , vol.24 , pp. 326-333
    • Darreh-Shori, T.1    Brimijoin, S.2    Kadir, A.3    Almkvist, O.4    Nordberg, A.5
  • 11
  • 14
    • 33747880669 scopus 로고    scopus 로고
    • Regional acetylcholinesterase activity and its correlation with behavioral performance in 15-month old transgenic mice expressing the human C99 fragment of APP
    • Dumont M, Lalonde R, Ghersi-Egea JF, Fukuchi K, Strazielle C. 2006. Regional acetylcholinesterase activity and its correlation with behavioral performance in 15-month old transgenic mice expressing the human C99 fragment of APP. J Neural Transm 113:1225-1241.
    • (2006) J Neural Transm , vol.113 , pp. 1225-1241
    • Dumont, M.1    Lalonde, R.2    Ghersi-Egea, J.F.3    Fukuchi, K.4    Strazielle, C.5
  • 15
    • 0038198881 scopus 로고    scopus 로고
    • Neurons, glia, and plasticity in normal brain aging
    • Finch CE. 2003. Neurons, glia, and plasticity in normal brain aging. Neurobiol Aging 24:S123-S127.
    • (2003) Neurobiol Aging , vol.24
    • Finch, C.E.1
  • 17
    • 29044448249 scopus 로고    scopus 로고
    • Antisense inhibition of acetylcholinesterase gene expression for treating cognition deficit in Alzheimer's disease model mice
    • Fu AL, Zhang XM, Sun MJ. 2005. Antisense inhibition of acetylcholinesterase gene expression for treating cognition deficit in Alzheimer's disease model mice. Brain Res 1066:10-15.
    • (2005) Brain Res , vol.1066 , pp. 10-15
    • Fu, A.L.1    Zhang, X.M.2    Sun, M.J.3
  • 18
    • 18544397726 scopus 로고    scopus 로고
    • Amphiphilic properties of acetylcholinesterase monomers in mouse plasma
    • García-Ayllón MS, Gómez JL, Vidal CJ. 1999. Amphiphilic properties of acetylcholinesterase monomers in mouse plasma. Neurosci Lett 265:211-214.
    • (1999) Neurosci Lett , vol.265 , pp. 211-214
    • García-Ayllón, M.S.1    Gómez, J.L.2    Vidal, C.J.3
  • 19
    • 0035900625 scopus 로고    scopus 로고
    • Identification of hybrid cholinesterase forms consisting of acetyl- and butyrylcholinesterase subunits in human glioma
    • García-Ayllón MS, Sáez-Valero J, Muñoz-Delgado E, Vidal CJ. 2001. Identification of hybrid cholinesterase forms consisting of acetyl- and butyrylcholinesterase subunits in human glioma. Neuroscience 107:199-208.
    • (2001) Neuroscience , vol.107 , pp. 199-208
    • García-Ayllón, M.S.1    Sáez-Valero, J.2    Muñoz-Delgado, E.3    Vidal, C.J.4
  • 20
    • 33947659446 scopus 로고    scopus 로고
    • Butyrylcholinesterase activity in the rat forebrain and upper brainstem: Postnatal development and adult distribution
    • Geula C, Nagykery N. 2007. Butyrylcholinesterase activity in the rat forebrain and upper brainstem: postnatal development and adult distribution. Exp Neurol 204:640-657.
    • (2007) Exp Neurol , vol.204 , pp. 640-657
    • Geula, C.1    Nagykery, N.2
  • 21
    • 4043074138 scopus 로고    scopus 로고
    • Cholinesterase inhibitors: New roles and therapeutic alternatives
    • Giacobini E. 2004. Cholinesterase inhibitors: new roles and therapeutic alternatives. Pharmacol Res 50:433-440.
    • (2004) Pharmacol Res , vol.50 , pp. 433-440
    • Giacobini, E.1
  • 22
    • 33748750251 scopus 로고    scopus 로고
    • Anti-inflammatory drugs in the treatment of neurodegenerative diseases: Current state
    • Gilgun-Sherki Y, Melamed E, Offen D. 2006. Anti-inflammatory drugs in the treatment of neurodegenerative diseases: current state. Curr Pharm Des 12:3509-3519.
    • (2006) Curr Pharm Des , vol.12 , pp. 3509-3519
    • Gilgun-Sherki, Y.1    Melamed, E.2    Offen, D.3
  • 24
    • 0029000138 scopus 로고
    • Neurochemical changes related to ageing in the senescence-accelerated mouse brain and the effect of chronic administration of nimodipine
    • Kabuto H, Yokoi I, Mori A, Murakami M, Sawada S. 1995. Neurochemical changes related to ageing in the senescence-accelerated mouse brain and the effect of chronic administration of nimodipine. Mech Ageing Dev 80:1-9.
    • (1995) Mech Ageing Dev , vol.80 , pp. 1-9
    • Kabuto, H.1    Yokoi, I.2    Mori, A.3    Murakami, M.4    Sawada, S.5
  • 25
    • 25444495866 scopus 로고    scopus 로고
    • Microglia in health and disease
    • Kim SU, de Vellis J. 2005. Microglia in health and disease. J Neurosci Res 81:302-323.
    • (2005) J Neurosci Res , vol.81 , pp. 302-323
    • Kim, S.U.1    de Vellis, J.2
  • 30
    • 0033956134 scopus 로고    scopus 로고
    • The key role of butyrylcholinesterase during neurogenesis and neural disorders: An antisense-5′-butyrylcholinesterase- DNA study
    • Mack A, Robitzki A. 2000. The key role of butyrylcholinesterase during neurogenesis and neural disorders: an antisense-5′-butyrylcholinesterase- DNA study. Prog Neurobiol 60:607-628.
    • (2000) Prog Neurobiol , vol.60 , pp. 607-628
    • Mack, A.1    Robitzki, A.2
  • 31
    • 28744432658 scopus 로고    scopus 로고
    • The C-terminal peptides of acetylcholinesterase: Cellular trafficking, oligomerization and functional anchoring
    • Massoulié J, Bon S, Perrier N, Falasca C. 2005. The C-terminal peptides of acetylcholinesterase: cellular trafficking, oligomerization and functional anchoring. Chem-Biol Interact 157-158:3-14.
    • (2005) Chem-Biol Interact , vol.157-158 , pp. 3-14
    • Massoulié, J.1    Bon, S.2    Perrier, N.3    Falasca, C.4
  • 32
    • 33645988822 scopus 로고    scopus 로고
    • Virtues and woes of AChE alternative splicing in stress-related neuropathologies
    • Meshorer E, Soreq H. 2006. Virtues and woes of AChE alternative splicing in stress-related neuropathologies. Trends Neurosci 29:216-224.
    • (2006) Trends Neurosci , vol.29 , pp. 216-224
    • Meshorer, E.1    Soreq, H.2
  • 35
    • 0028061167 scopus 로고
    • Nitric oxide as a potential pathological mechanism in demyelination: Its differential effects on primary glial cells in vitro
    • Mitrovic B, Ignarro LJ, Montestruque S, Smoll A, Merril JE. 1994. Nitric oxide as a potential pathological mechanism in demyelination: its differential effects on primary glial cells in vitro. Neuroscience 61:575-585.
    • (1994) Neuroscience , vol.61 , pp. 575-585
    • Mitrovic, B.1    Ignarro, L.J.2    Montestruque, S.3    Smoll, A.4    Merril, J.E.5
  • 36
    • 0022970786 scopus 로고
    • Age-related changes in learning and memory in the senescence-accelerated mouse (SAM)
    • Miyamoto M, Kiyota Y, Nagaoka A, Matsuo Y, Takeda T. 1986. Age-related changes in learning and memory in the senescence-accelerated mouse (SAM). Physiol Behav 38:406.
    • (1986) Physiol Behav , vol.38 , pp. 406
    • Miyamoto, M.1    Kiyota, Y.2    Nagaoka, A.3    Matsuo, Y.4    Takeda, T.5
  • 39
    • 0030043539 scopus 로고    scopus 로고
    • Molecular forms of acetyl- and butyrylcholinesterase in normal and dystrophic mouse brain
    • Moral-Naranjo MT, Cabezas-Herrera J, Vidal CJ. 1996. Molecular forms of acetyl- and butyrylcholinesterase in normal and dystrophic mouse brain. J Neurosci Res 43:224-234.
    • (1996) J Neurosci Res , vol.43 , pp. 224-234
    • Moral-Naranjo, M.T.1    Cabezas-Herrera, J.2    Vidal, C.J.3
  • 40
    • 0037131559 scopus 로고    scopus 로고
    • Muscular dystrophy with laminin deficiency decreases the content of butyrylcholinesterase tetramers in sciatic nerves of Lama2dy mice
    • Moral-Naranjo MT, Cabezas-Herrera J, Vidal CJ, Campoy FJ. 2002. Muscular dystrophy with laminin deficiency decreases the content of butyrylcholinesterase tetramers in sciatic nerves of Lama2dy mice. Neurosci Lett 331:155-158.
    • (2002) Neurosci Lett , vol.331 , pp. 155-158
    • Moral-Naranjo, M.T.1    Cabezas-Herrera, J.2    Vidal, C.J.3    Campoy, F.J.4
  • 41
    • 0036169030 scopus 로고    scopus 로고
    • Morley JE, Farr SA, Kumar VB, Banks WA. 2002. Alzheimer's disease through the eye of a mouse: acceptance lecture for the 2001 Gayle A. Olson and Richard D. Olson prize. Peptides 23:589-599.
    • Morley JE, Farr SA, Kumar VB, Banks WA. 2002. Alzheimer's disease through the eye of a mouse: acceptance lecture for the 2001 Gayle A. Olson and Richard D. Olson prize. Peptides 23:589-599.
  • 42
    • 28244492010 scopus 로고    scopus 로고
    • Muscular dystrophy by merosin deficiency decreases acetylcholinesterase activity in thymus of Lama2dy mice
    • Nieto-Cerón S, Sánchez del Campo LF, Muñoz-Delgado E, Vidal CJ, Campoy FJ. 2005. Muscular dystrophy by merosin deficiency decreases acetylcholinesterase activity in thymus of Lama2dy mice. J Neurochem 95:1035-1046.
    • (2005) J Neurochem , vol.95 , pp. 1035-1046
    • Nieto-Cerón, S.1    Sánchez del Campo, L.F.2    Muñoz-Delgado, E.3    Vidal, C.J.4    Campoy, F.J.5
  • 43
    • 0036948167 scopus 로고    scopus 로고
    • Regional differences in PACAP transport across the blood-brain barrier in mice: A possible influence of strain, amyloid β-protein, and age
    • Nonaka N, Banks WA, Mizushima H, Shioda S, Morley JE. 2002. Regional differences in PACAP transport across the blood-brain barrier in mice: a possible influence of strain, amyloid β-protein, and age. Peptides 23:2197-2202.
    • (2002) Peptides , vol.23 , pp. 2197-2202
    • Nonaka, N.1    Banks, W.A.2    Mizushima, H.3    Shioda, S.4    Morley, J.E.5
  • 44
    • 0032421523 scopus 로고    scopus 로고
    • Senescence-accelerated mouse (SAM) as an animal model of senile dementia: Pharmacological, neurochemical and molecular biology approach
    • Okuma Y, Nomura Y. 1998. Senescence-accelerated mouse (SAM) as an animal model of senile dementia: pharmacological, neurochemical and molecular biology approach. Jpn J Pharmacol 78:399-404.
    • (1998) Jpn J Pharmacol , vol.78 , pp. 399-404
    • Okuma, Y.1    Nomura, Y.2
  • 45
    • 0242708697 scopus 로고    scopus 로고
    • Expression of PRiMA in the mouse brain: Membrane anchoring and accumulation of "tailed" acetylcholinesterase
    • Perrier NA, Kherif S, Perrier AL, Dumas S, Mallet J, Massoulie J. 2003. Expression of PRiMA in the mouse brain: membrane anchoring and accumulation of "tailed" acetylcholinesterase. Eur J Neurosci 18:1837-1847.
    • (2003) Eur J Neurosci , vol.18 , pp. 1837-1847
    • Perrier, N.A.1    Kherif, S.2    Perrier, A.L.3    Dumas, S.4    Mallet, J.5    Massoulie, J.6
  • 46
    • 40449118768 scopus 로고    scopus 로고
    • Human recombinant butyrylcholinesterase purified from the milk of transgenic goats interacts with beta-amyloid fibrils and suppresses their formation in vitro
    • Podoly E, Bruck T, Diamant S, Melamed-Book N, Weiss A, Huang Y, Livnah O, Langermann S, Wilgus H, Soreq H. 2008. Human recombinant butyrylcholinesterase purified from the milk of transgenic goats interacts with beta-amyloid fibrils and suppresses their formation in vitro. Neurodegen Dis 5:232-236.
    • (2008) Neurodegen Dis , vol.5 , pp. 232-236
    • Podoly, E.1    Bruck, T.2    Diamant, S.3    Melamed-Book, N.4    Weiss, A.5    Huang, Y.6    Livnah, O.7    Langermann, S.8    Wilgus, H.9    Soreq, H.10
  • 48
    • 0012017103 scopus 로고
    • Purification and properties of carbohydrate-binding proteins. Common lentil (Lens culinaris) phytohemagglutinin
    • Sage HJ, Green RW. 1972. Purification and properties of carbohydrate-binding proteins. Common lentil (Lens culinaris) phytohemagglutinin. Methods Enzymol 28:332-339.
    • (1972) Methods Enzymol , vol.28 , pp. 332-339
    • Sage, H.J.1    Green, R.W.2
  • 49
    • 0029867898 scopus 로고    scopus 로고
    • Molecular forms of acetyl- and butyrylcholinesterase in human glioma
    • Sáez-Valero J, Poza-Cisneros G, Vidal CJ. 1996. Molecular forms of acetyl- and butyrylcholinesterase in human glioma. Neurosci Lett 206:173-176.
    • (1996) Neurosci Lett , vol.206 , pp. 173-176
    • Sáez-Valero, J.1    Poza-Cisneros, G.2    Vidal, C.J.3
  • 50
    • 0345390947 scopus 로고    scopus 로고
    • Molecular isoform distribution and glycosylation of acetylcholinesterase are altered in brain and cerebrospinal fluid of patients with Alzheimer's disease
    • Sáez-Valero J, Sberna G, McLean CA, Small DH. 1999. Molecular isoform distribution and glycosylation of acetylcholinesterase are altered in brain and cerebrospinal fluid of patients with Alzheimer's disease. J Neurochem 72:1600-1608.
    • (1999) J Neurochem , vol.72 , pp. 1600-1608
    • Sáez-Valero, J.1    Sberna, G.2    McLean, C.A.3    Small, D.H.4
  • 52
    • 0031754362 scopus 로고    scopus 로고
    • Acetylcholinesterase is increased in the brains of transgenic mice expressing the C-terminal fragment (CT100) of the beta-amyloid precursor of Alzheimer's disease
    • Sberna G, Sáez-Valero J, Li QX, Czech C, Beyreuther K, Masters CL, McLean CA, Small DH. 1998. Acetylcholinesterase is increased in the brains of transgenic mice expressing the C-terminal fragment (CT100) of the beta-amyloid precursor of Alzheimer's disease. J Neurochem 71:723-731.
    • (1998) J Neurochem , vol.71 , pp. 723-731
    • Sberna, G.1    Sáez-Valero, J.2    Li, Q.X.3    Czech, C.4    Beyreuther, K.5    Masters, C.L.6    McLean, C.A.7    Small, D.H.8
  • 53
    • 3242752041 scopus 로고    scopus 로고
    • Brain cholinesterases: I. The clinico-histopathological basis of Alzheimer's disease
    • Shen ZX. 2004. Brain cholinesterases: I. The clinico-histopathological basis of Alzheimer's disease. Med Hypoth 63:285-297.
    • (2004) Med Hypoth , vol.63 , pp. 285-297
    • Shen, Z.X.1
  • 56
    • 0023200375 scopus 로고
    • Acetyl- and butyrylcholinesterase activity in the cerebrospinal fluid of patients with Parkinson's disease
    • Sirvio J, Soininen HS, Kutvonen R, Hyttinen JM, Helkala EL, Riekkinen PJ. 1987. Acetyl- and butyrylcholinesterase activity in the cerebrospinal fluid of patients with Parkinson's disease. J Neurol Sci 81:273-279.
    • (1987) J Neurol Sci , vol.81 , pp. 273-279
    • Sirvio, J.1    Soininen, H.S.2    Kutvonen, R.3    Hyttinen, J.M.4    Helkala, E.L.5    Riekkinen, P.J.6
  • 57
    • 0037436472 scopus 로고    scopus 로고
    • Cholinergic deficit in the septal-hippocampal pathway of the SAM-P/8 senescence accelerated mouse
    • Strong R, Reddy V, Morley JE. 2003. Cholinergic deficit in the septal-hippocampal pathway of the SAM-P/8 senescence accelerated mouse. Brain Res 966:150-156.
    • (2003) Brain Res , vol.966 , pp. 150-156
    • Strong, R.1    Reddy, V.2    Morley, J.E.3
  • 58
    • 62349123068 scopus 로고    scopus 로고
    • Senescence-accelerated mouse (SAM) with special references to neurodegeneration models, SAMP8 and SAMP10 mice
    • Takeda T. 2009. Senescence-accelerated mouse (SAM) with special references to neurodegeneration models, SAMP8 and SAMP10 mice. Neurochem Res 34:639-659.
    • (2009) Neurochem Res , vol.34 , pp. 639-659
    • Takeda, T.1
  • 59
    • 0030896787 scopus 로고    scopus 로고
    • Senescence-accelerated mouse (SAM): A novel murine model of senescence
    • Takeda T, Hosokawa M, Higuchi K. 1997. Senescence-accelerated mouse (SAM): a novel murine model of senescence. Exp Gerontol 32:105-109.
    • (1997) Exp Gerontol , vol.32 , pp. 105-109
    • Takeda, T.1    Hosokawa, M.2    Higuchi, K.3
  • 60
    • 21144455520 scopus 로고    scopus 로고
    • The age-related degeneration of oligodendrocytes in the hippocampus of the senescence-accelerated mouse (SAM) P8. A quantitative immunohistochemical study
    • Tanaka J, Okuma Y, Tomobe K, Nomura Y. 2005. The age-related degeneration of oligodendrocytes in the hippocampus of the senescence-accelerated mouse (SAM) P8. A quantitative immunohistochemical study. Biol Pharm Bull 24:615-618.
    • (2005) Biol Pharm Bull , vol.24 , pp. 615-618
    • Tanaka, J.1    Okuma, Y.2    Tomobe, K.3    Nomura, Y.4
  • 61
    • 0034564998 scopus 로고    scopus 로고
    • Changes in expressions of proinflammatory cytokines IL-1β, TNF-α and IL-6 in the brain of senescence accelerated mouse (SAM) P8
    • Tha KK, Okuma Y, Miyazaki H, Murayama T, Uehara T, Hatakeyama R, Hayashi Y, Nomura Y. 2000. Changes in expressions of proinflammatory cytokines IL-1β, TNF-α and IL-6 in the brain of senescence accelerated mouse (SAM) P8. Brain Res 885:25-31.
    • (2000) Brain Res , vol.885 , pp. 25-31
    • Tha, K.K.1    Okuma, Y.2    Miyazaki, H.3    Murayama, T.4    Uehara, T.5    Hatakeyama, R.6    Hayashi, Y.7    Nomura, Y.8
  • 63
    • 0026768242 scopus 로고
    • Ricinus communis agglutinin I reacting and nonreacting butyrylcholinesterase in human cerebrospinal fluid
    • Tornel PL, Sáez-Valero J, Vidal CJ. 1992. Ricinus communis agglutinin I reacting and nonreacting butyrylcholinesterase in human cerebrospinal fluid. Neurosci Lett 145:59-62.
    • (1992) Neurosci Lett , vol.145 , pp. 59-62
    • Tornel, P.L.1    Sáez-Valero, J.2    Vidal, C.J.3
  • 64
    • 0027950874 scopus 로고
    • Novel inactive and distinctively glycosylated forms of butyrylcholinesterase from chicken serum
    • Weikert T, Ebert C, Rasched I, Layer PG. 1994. Novel inactive and distinctively glycosylated forms of butyrylcholinesterase from chicken serum. J Neurochem 63:318-325.
    • (1994) J Neurochem , vol.63 , pp. 318-325
    • Weikert, T.1    Ebert, C.2    Rasched, I.3    Layer, P.G.4
  • 65
    • 17444421921 scopus 로고    scopus 로고
    • Age related changes of various markers of astrocytes in senescence-accelerated mice hippocampus
    • Wu Y, Zhang AQ, Yew DT. 2005. Age related changes of various markers of astrocytes in senescence-accelerated mice hippocampus. Neurochem Int 46:565-574.
    • (2005) Neurochem Int , vol.46 , pp. 565-574
    • Wu, Y.1    Zhang, A.Q.2    Yew, D.T.3


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