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Volumn 116, Issue 6, 2011, Pages 1088-1096

Dramatic increase in readthrough acetylcholinesterase in a cellular model of oxidative stress

Author keywords

acetylcholinesterase; Bcl 2; caspase; neurodegeneration; splicing; stress

Indexed keywords

ACETYLCHOLINESTERASE; CASPASE 3; LACTATE DEHYDROGENASE; MESSENGER RNA; PROTEIN BCL 2;

EID: 79952450722     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2010.07164.x     Document Type: Article
Times cited : (53)

References (55)
  • 1
    • 0037093691 scopus 로고    scopus 로고
    • 2+-dependent caspase-2 activation induced by oxidative stress leads to SH-SY5Y human neuroblastoma cell apoptosis
    • DOI 10.1002/jnr.10199
    • Amoroso S., D'Alessio A., Sirabella R., Di Renzo G., and, Annunziato L., (2002) Ca(2+)-independent caspase-3 but not Ca(2+)-dependent caspase-2 activation induced by oxidative stress leads to SH-SY5Y human neuroblastoma cell apoptosis. J. Neurosci. Res. 68, 454-462. (Pubitemid 34461576)
    • (2002) Journal of Neuroscience Research , vol.68 , Issue.4 , pp. 454-462
    • Amoroso, S.1    D'Alessio, A.2    Sirabella, R.3    Di Renzo, G.4    Annunziato, L.5
  • 2
    • 0026794041 scopus 로고
    • Changes in acetylcholinesterase and butyrylcholinesterase in Alzheimer's disease resemble embryonic development - A study of molecular forms
    • Arendt T., Bruckner M. K., Lange M., and, 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    Bruckner, M.K.2    Lange, M.3    Bigl, V.4
  • 3
    • 37549022563 scopus 로고    scopus 로고
    • Changes in readthrough acetylcholinesterase expression modulate amyloid-beta pathology
    • et al.
    • Berson A., Knobloch M., Hanan M., et al. (2008) Changes in readthrough acetylcholinesterase expression modulate amyloid-beta pathology. Brain 131, 109-119.
    • (2008) Brain , vol.131 , pp. 109-119
    • Berson, A.1    Knobloch, M.2    Hanan, M.3
  • 4
    • 34548260315 scopus 로고    scopus 로고
    • Multiple cascade effects of oxidative stress on astroglia
    • DOI 10.1002/glia.20547
    • Bond C. E., and, Greenfield S. A., (2007) Multiple cascade effects of oxidative stress on astroglia. Glia 55, 1348-1361. (Pubitemid 47328938)
    • (2007) GLIA , vol.55 , Issue.13 , pp. 1348-1361
    • Bond, C.E.1    Greenfield, S.A.2
  • 5
    • 33746215796 scopus 로고    scopus 로고
    • Astroglia up-regulate transcription and secretion of 'readthrough' acetylcholinesterase following oxidative stress
    • DOI 10.1111/j.1460-9568.2006.04898.x
    • Bond C. E., Patel P., Crouch L., Tetlow N., Day T., Abu-Hayyeh S., Williamson C., and, Greenfield S. A., (2006) Astroglia up-regulate transcription and secretion of 'readthrough' acetylcholinesterase following oxidative stress. Eur. J. Neurosci. 24, 381-386. (Pubitemid 44100330)
    • (2006) European Journal of Neuroscience , vol.24 , Issue.2 , pp. 381-386
    • Bond, C.E.1    Patel, P.2    Crouch, L.3    Tetlow, N.4    Day, T.5    Abu-Hayyeh, S.6    Williamson, C.7    Greenfield, S.A.8
  • 6
    • 62849094251 scopus 로고    scopus 로고
    • Upregulation of alpha7 nicotinic receptors by acetylcholinesterase C-terminal peptides
    • e4846.
    • Bond C. E., Zimmermann M., and, Greenfield S. A., (2009) Upregulation of alpha7 nicotinic receptors by acetylcholinesterase C-terminal peptides. PLoS ONE 4, e4846.
    • (2009) PLoS ONE , vol.4
    • Bond, C.E.1    Zimmermann, M.2    Greenfield, S.A.3
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M., (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0036386343 scopus 로고    scopus 로고
    • Neuronal overexpression of "readthrough" acetylcholinesterase is associated with antisense-suppressible behavioral impairments
    • Cohen O., Erb C., Ginzberg D., Pollak Y., Seidman S., Shoham S., Yirmiya R., and, Soreq H., (2002) Neuronal overexpression of "readthrough" acetylcholinesterase is associated with antisense-suppressible behavioral impairments. Mol. Psychiatry 7, 874-885.
    • (2002) Mol. Psychiatry , vol.7 , pp. 874-885
    • Cohen, O.1    Erb, C.2    Ginzberg, D.3    Pollak, Y.4    Seidman, S.5    Shoham, S.6    Yirmiya, R.7    Soreq, H.8
  • 11
    • 0344441446 scopus 로고    scopus 로고
    • A peptide derived from acetylcholinesterase induces neuronal cell death: Characterisation of possible mechanisms
    • DOI 10.1007/s00221-003-1567-5
    • Day T., and, Greenfield S. A., (2003) A peptide derived from acetylcholinesterase induces neuronal cell death: characterisation of possible mechanisms. Exp. Brain Res. 153, 334-342. (Pubitemid 37463975)
    • (2003) Experimental Brain Research , vol.153 , Issue.3 , pp. 334-342
    • Day, T.1    Greenfield, S.A.2
  • 12
    • 33646894444 scopus 로고    scopus 로고
    • ARP, the cleavable C-terminal peptide of "readthrough" acetylcholinesterase, promotes neuronal development and plasticity
    • DOI 10.1385/JMN:28:3:247
    • Dori A., and, Soreq H., (2006) ARP, the cleavable C-terminal peptide of "readthrough" acetylcholinesterase, promotes neuronal development and plasticity. J. Mol. Neurosci. 28, 247-255. (Pubitemid 43780317)
    • (2006) Journal of Molecular Neuroscience , vol.28 , Issue.3 , pp. 247-255
    • Dori, A.1    Soreq, H.2
  • 13
    • 33747880669 scopus 로고    scopus 로고
    • Regional acetylcholinesterase activity and its correlation with behavioral performances in 15-month old transgenic mice expressing the human C99 fragment of APP
    • DOI 10.1007/s00702-005-0373-6
    • Dumont M., Lalonde R., Ghersi-Egea J. F., Fukuchi K., and, Strazielle C., (2006) Regional acetylcholinesterase activity and its correlation with behavioral performances in 15-month old transgenic mice expressing the human C99 fragment of APP. J. Neural Transm. 113, 1225-1241. (Pubitemid 44291017)
    • (2006) Journal of Neural Transmission , vol.113 , Issue.9 , pp. 1225-1241
    • Dumont, M.1    Lalonde, R.2    Ghersi-Egea, J.-F.3    Fukuchi, K.4    Strazielle, C.5
  • 16
    • 12244311203 scopus 로고    scopus 로고
    • Chronic acetylcholinesterase overexpression induces multilevelled aberrations in mouse neuromuscular physiology
    • Farchi N., Soreq H., and, Hochner B., (2003) Chronic acetylcholinesterase overexpression induces multilevelled aberrations in mouse neuromuscular physiology. J. Physiol. 546, 165-173.
    • (2003) J. Physiol. , vol.546 , pp. 165-173
    • Farchi, N.1    Soreq, H.2    Hochner, B.3
  • 17
  • 18
    • 38549159882 scopus 로고    scopus 로고
    • Non-hydrolytic functions of acetylcholinesterase: The significance of C-terminal peptides
    • DOI 10.1111/j.1742-4658.2007.06235.x
    • Greenfield S. A., Zimmermann M., and, Bond C. E., (2008) Non-hydrolytic functions of acetylcholinesterase. The significance of C-terminal peptides. FEBS J. 275, 604-611. (Pubitemid 351160966)
    • (2008) FEBS Journal , vol.275 , Issue.4 , pp. 604-611
    • Greenfield, S.A.1    Zimmermann, M.2    Bond, C.E.3
  • 20
    • 77953916706 scopus 로고    scopus 로고
    • Co-localization of PRiMA with acetylcholinesterase in cholinergic neurons of rat brain: An immunocytochemical study
    • Henderson Z., Matto N., John D., Nalivaeva N. N., and, Turner A. J., (2010) Co-localization of PRiMA with acetylcholinesterase in cholinergic neurons of rat brain: an immunocytochemical study. Brain Res. 1344, 34-42.
    • (2010) Brain Res. , vol.1344 , pp. 34-42
    • Henderson, Z.1    Matto, N.2    John, D.3    Nalivaeva, N.N.4    Turner, A.J.5
  • 21
    • 38549098085 scopus 로고    scopus 로고
    • Amyloid-cholinesterase interactions: Implications for Alzheimer's disease
    • DOI 10.1111/j.1742-4658.2007.06238.x
    • Inestrosa N. C., Dinamarca M. C., and, Alvarez A., (2008) Amyloid-cholinesterase interactions. Implications for Alzheimer's disease. FEBS J. 275, 625-632. (Pubitemid 351160969)
    • (2008) FEBS Journal , vol.275 , Issue.4 , pp. 625-632
    • Inestrosa, N.C.1    Dinamarca, M.C.2    Alvarez, A.3
  • 22
    • 37349067811 scopus 로고    scopus 로고
    • GSK3β mediates the induced expression of synaptic acetylcholinesterase during apoptosis
    • DOI 10.1111/j.1471-4159.2007.04975.x
    • Jing P., Jin Q., Wu J., and, Zhang X. J., (2008) GSK3beta mediates the induced expression of synaptic acetylcholinesterase during apoptosis. J. Neurochem. 104, 409-419. (Pubitemid 350293871)
    • (2008) Journal of Neurochemistry , vol.104 , Issue.2 , pp. 409-419
    • Jing, P.1    Jin, Q.2    Wu, J.3    Zhang, X.-J.4
  • 23
    • 0032574973 scopus 로고    scopus 로고
    • Acute stress facilitates long-lasting changes in cholinergic gene expression
    • DOI 10.1038/30741
    • Kaufer D., Friedman A., Seidman S., and, Soreq H., (1998) Acute stress facilitates long-lasting changes in cholinergic gene expression. Nature 393, 373-377. (Pubitemid 28269711)
    • (1998) Nature , vol.393 , Issue.6683 , pp. 373-377
    • Kaufer, D.1    Friedman, A.2    Seidman, S.3    Soreq, H.4
  • 24
    • 0029163984 scopus 로고
    • Novel functions of cholinesterases in development, physiology and disease
    • Layer P. G., and, Willbold E., (1995) Novel functions of cholinesterases in development, physiology and disease. Prog. Histochem. Cytochem. 29, 1-94.
    • (1995) Prog. Histochem. Cytochem. , vol.29 , pp. 1-94
    • Layer, P.G.1    Willbold, E.2
  • 26
    • 77949567203 scopus 로고    scopus 로고
    • Strain and regional dependence of alternate splicing of acetylcholinesterase in the murine brain following stress or treatment with diisopropylfluorophosphate
    • Livneh U., Dori A., Katzav A., and, Kofman O., (2010) Strain and regional dependence of alternate splicing of acetylcholinesterase in the murine brain following stress or treatment with diisopropylfluorophosphate. Behav. Brain Res. 210, 107-115.
    • (2010) Behav. Brain Res. , vol.210 , pp. 107-115
    • Livneh, U.1    Dori, A.2    Katzav, A.3    Kofman, O.4
  • 27
    • 0037146896 scopus 로고    scopus 로고
    • Cabergoline prevents necrotic neuronal death in an in vitro model of oxidative stress
    • DOI 10.1016/S0014-2999(02)02683-3, PII S0014299902026833
    • Lombardi G., Varsaldi F., Miglio G., Papini M. G., Battaglia A., and, Canonico P. L., (2002) Cabergoline prevents necrotic neuronal death in an in vitro model of oxidative stress. Eur. J. Pharmacol. 457, 95-98. (Pubitemid 35447651)
    • (2002) European Journal of Pharmacology , vol.457 , Issue.2-3 , pp. 95-98
    • Lombardi, G.1    Varsaldi, F.2    Miglio, G.3    Papini, M.G.4    Battaglia, A.5    Canonico, P.L.6
  • 28
    • 0032105344 scopus 로고    scopus 로고
    • Acetylcholinesterase: C-terminal domains, molecular forms and functional localization
    • DOI 10.1016/S0928-4257(98)80007-7
    • Massoulie J., Anselmet A., Bon S., Krejci E., Legay C., Morel N., and, Simon S., (1998) Acetylcholinesterase: C-terminal domains, molecular forms and functional localization. J. Physiol. Paris 92, 183-190. (Pubitemid 29050931)
    • (1998) Journal of Physiology Paris , vol.92 , Issue.3-4 , pp. 183-190
    • Massoulie, J.1    Anselmet, A.2    Bon, S.3    Krejci, E.4    Legay, C.5    Morel, N.6    Simon, S.7
  • 29
    • 28744432658 scopus 로고    scopus 로고
    • The C-terminal peptides of acetylcholinesterase: Cellular trafficking, oligomerization and functional anchoring
    • DOI 10.1016/j.cbi.2005.10.002, PII S0009279705002425
    • Massoulie J., Bon S., Perrier N., and, Falasca C., (2005) The C-terminal peptides of acetylcholinesterase: cellular trafficking, oligomerization and functional anchoring. Chem. Biol. Interact. 157-158, 3-14. (Pubitemid 41757627)
    • (2005) Chemico-Biological Interactions , vol.157-158 , pp. 3-14
    • Massoulie, J.1    Bon, S.2    Perrier, N.3    Falasca, C.4
  • 30
    • 0037219182 scopus 로고    scopus 로고
    • Involvement of oxidative stress in the enhancement of acetylcholinesterase activity induced by amyloid beta-peptide
    • DOI 10.1016/S0168-0102(02)00201-8, PII S0168010202002018
    • Melo J. B., Agostinho P., and, Oliveira C. R., (2003) Involvement of oxidative stress in the enhancement of acetylcholinesterase activity induced by amyloid beta-peptide. Neurosci. Res. 45, 117-127. (Pubitemid 36044475)
    • (2003) Neuroscience Research , vol.45 , Issue.1 , pp. 117-127
    • Melo, J.B.1    Agostinho, P.2    Oliveira, C.R.3
  • 31
    • 33645988822 scopus 로고    scopus 로고
    • Virtues and woes of AChE alternative splicing in stress-related neuropathologies
    • Meshorer E., and, 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
  • 32
    • 0035377458 scopus 로고    scopus 로고
    • Post-translational modifications of proteins: Acetylcholinesterase as a model system
    • Nalivaeva N. N., and, Turner A. J., (2001) Post-translational modifications of proteins: acetylcholinesterase as a model system. Proteomics 1, 735-747. (Pubitemid 33696516)
    • (2001) Proteomics , vol.1 , Issue.6 , pp. 735-747
    • Nalivaeva, N.N.1    Turner, A.J.2
  • 33
    • 0016666182 scopus 로고
    • Disordered cholinergic neurotransmission and dysautoregulation after acute cerebral infarction
    • Ott E. O., Abraham J., Meyer J. S., Achari A. N., Chee A. N., and, Mathew N. T., (1975) Disordered cholinergic neurotransmission and dysautoregulation after acute cerebral infarction. Stroke 6, 172-180.
    • (1975) Stroke , vol.6 , pp. 172-180
    • Ott, E.O.1    Abraham, J.2    Meyer, J.S.3    Achari, A.N.4    Chee, A.N.5    Mathew, N.T.6
  • 34
    • 10844253547 scopus 로고    scopus 로고
    • Acetylcholinesterase Plays a Pivotal Role in Apoptosome Formation
    • DOI 10.1158/0008-5472.CAN-04-0649
    • Park S. E., Kim N. D., and, Yoo Y. H., (2004) Acetylcholinesterase plays a pivotal role in apoptosome formation. Cancer Res. 64, 2652-2655. (Pubitemid 38500595)
    • (2004) Cancer Research , vol.64 , Issue.8 , pp. 2652-2655
    • Park, S.E.1    Kim, N.D.2    Yoo, Y.H.3
  • 36
    • 0037122918 scopus 로고    scopus 로고
    • PRiMA: The membrane anchor of acetylcholinesterase in the brain
    • DOI 10.1016/S0896-6273(01)00584-0
    • Perrier A. L., Massoulie J., and, Krejci E., (2002) PRiMA: the membrane anchor of acetylcholinesterase in the brain. Neuron 33, 275-285. (Pubitemid 34127759)
    • (2002) Neuron , vol.33 , Issue.2 , pp. 275-285
    • Perrier, A.L.1    Massoulie, J.2    Krejci, E.3
  • 37
    • 23244463063 scopus 로고    scopus 로고
    • The readthrough variant of acetylcholinesterase remains very minor after heat shock, organophosphate inhibition and stress, in cell culture and in vivo
    • DOI 10.1111/j.1471-4159.2005.03140.x
    • Perrier N. A., Salani M., Falasca C., Bon S., Augusti-Tocco G., and, Massoulie J., (2005) The readthrough variant of acetylcholinesterase remains very minor after heat shock, organophosphate inhibition and stress, in cell culture and in vivo. J. Neurochem. 94, 629-638. (Pubitemid 41098495)
    • (2005) Journal of Neurochemistry , vol.94 , Issue.3 , pp. 629-638
    • Perrier, N.A.1    Salani, M.2    Falasca, C.3    Bon, S.4    Augusti-Tocco, G.5    Massoulie, J.6
  • 38
    • 0031663777 scopus 로고    scopus 로고
    • Butyrylcholinesterase antisense transfection increases apoptosis in differentiating retinal reaggregates of the chick embryo
    • Robitzki A., Mack A., Hoppe U., Chatonnet A., and, Layer P. G., (1998) Butyrylcholinesterase antisense transfection increases apoptosis in differentiating retinal reaggregates of the chick embryo. J. Neurochem. 71, 413-420.
    • (1998) J. Neurochem. , vol.71 , pp. 413-420
    • Robitzki, A.1    MacK, A.2    Hoppe, U.3    Chatonnet, A.4    Layer, P.G.5
  • 39
    • 38949164347 scopus 로고    scopus 로고
    • Effect of donepezil and tacrine on oxidative stress in intracerebral streptozotocin-induced model of dementia in mice
    • Saxena G., Singh S. P., Agrawal R., and, Nath C., (2008) Effect of donepezil and tacrine on oxidative stress in intracerebral streptozotocin- induced model of dementia in mice. Eur. J. Pharmacol. 581, 283-289.
    • (2008) Eur. J. Pharmacol. , vol.581 , pp. 283-289
    • Saxena, G.1    Singh, S.P.2    Agrawal, R.3    Nath, C.4
  • 40
    • 0035320772 scopus 로고    scopus 로고
    • Acetylcholinesterase - New roles for an old actor
    • DOI 10.1038/35067589
    • Soreq H., and, Seidman S., (2001) Acetylcholinesterase-new roles for an old actor. Nat. Rev. Neurosci. 2, 294-302. (Pubitemid 33673070)
    • (2001) Nature Reviews Neuroscience , vol.2 , Issue.4 , pp. 294-302
    • Soreq, H.1    Seidman, S.2
  • 45
    • 77953808415 scopus 로고    scopus 로고
    • Effect of melatonin on neuroinflammation and acetylcholinesterase activity induced by LPS in rat brain
    • Tyagi E., Agrawal R., Nath C., and, Shukla R., (2010) Effect of melatonin on neuroinflammation and acetylcholinesterase activity induced by LPS in rat brain. Eur. J. Pharmacol. 640, 206-210.
    • (2010) Eur. J. Pharmacol. , vol.640 , pp. 206-210
    • Tyagi, E.1    Agrawal, R.2    Nath, C.3    Shukla, R.4
  • 46
    • 0035341089 scopus 로고    scopus 로고
    • Role of oxidative stress in the apoptotic cell death of cultured cerebellar granule neurons
    • DOI 10.1002/jnr.1077
    • Valencia A., and, Moran J., (2001) Role of oxidative stress in the apoptotic cell death of cultured cerebellar granule neurons. J. Neurosci. Res. 64, 284-297. (Pubitemid 32385697)
    • (2001) Journal of Neuroscience Research , vol.64 , Issue.3 , pp. 284-297
    • Valencia, A.1    Morn, J.2
  • 47
    • 0020072221 scopus 로고
    • Alzheimer's disease and senile dementia: Loss of neurons in the basal forebrain
    • Whitehouse P. J., Price D. L., Struble R. G., Clark A. W., Coyle J. T., and, Delon M. R., (1982) Alzheimer's disease and senile dementia: loss of neurons in the basal forebrain. Science 215, 1237-1239. (Pubitemid 12106486)
    • (1982) Science , vol.215 , Issue.4537 , pp. 1237-1239
    • Whitehouse, P.J.1    Price, D.L.2    Struble, R.G.3
  • 48
    • 57549099864 scopus 로고    scopus 로고
    • Role of oxidative stress and caspase 3 in CD47-mediated neuronal cell death
    • Xing C., Lee S., Kim W. J., Jin G., Yang Y. G., Ji X., Wang X., and, Lo E. H., (2009) Role of oxidative stress and caspase 3 in CD47-mediated neuronal cell death. J. Neurochem. 108, 430-436.
    • (2009) J. Neurochem. , vol.108 , pp. 430-436
    • Xing, C.1    Lee, S.2    Kim, W.J.3    Jin, G.4    Yang, Y.G.5    Ji, X.6    Wang, X.7    Lo, E.H.8
  • 49
    • 47149103346 scopus 로고    scopus 로고
    • Transfection of the anti-apoptotic gene bcl-2 inhibits oxidative stress-induced cell injuries through delaying of NF-χB activation
    • Yanada S., Misumi M., Saitoh Y., Kaneda Y., and, Miwa N., (2006) Transfection of the anti-apoptotic gene bcl-2 inhibits oxidative stress-induced cell injuries through delaying of NF-kB activation. Gene Ther. Mol. Biol. 10, 269-276. (Pubitemid 351976171)
    • (2006) Gene Therapy and Molecular Biology , vol.10 , Issue.2 , pp. 269-276
    • Yanada, S.1    Misumi, M.2    Saitoh, Y.3    Kaneda, Y.4    Miwa, N.5
  • 50
    • 0036237097 scopus 로고    scopus 로고
    • Increased expression of intranuclear AChE involved in apoptosis of SK-N-SH cells
    • DOI 10.1016/S0168-0102(02)00005-6, PII S0168010202000056
    • Yang L., He H. Y., and, Zhang X. J., (2002) Increased expression of intranuclear AChE involved in apoptosis of SK-N-SH cells. Neurosci. Res. 42, 261-268. (Pubitemid 34414986)
    • (2002) Neuroscience Research , vol.42 , Issue.4 , pp. 261-268
    • Yang, L.1    He, H.-Y.2    Zhang, X.-J.3
  • 52
    • 27744516094 scopus 로고    scopus 로고
    • Mitochondria-targeted peptide prevents mitochondrial depolarization and apoptosis induced by tert-butyl hydroperoxide in neuronal cell lines
    • DOI 10.1016/j.bcp.2005.08.022, PII S0006295205005666
    • Zhao K., Luo G., Giannelli S., and, Szeto H. H., (2005) Mitochondria-targeted peptide prevents mitochondrial depolarization and apoptosis induced by tert-butyl hydroperoxide in neuronal cell lines. Biochem. Pharmacol. 70, 1796-1806. (Pubitemid 41612010)
    • (2005) Biochemical Pharmacology , vol.70 , Issue.12 , pp. 1796-1806
    • Zhao, K.1    Luo, G.2    Giannelli, S.3    Szeto, H.H.4
  • 53
    • 4544239545 scopus 로고    scopus 로고
    • Acetylcholinesterase inhibitors increase ADAM10 activity by promoting its trafficking in neuroblastoma cell lines
    • DOI 10.1111/j.1471-4159.2004.02680.x
    • Zimmermann M., Gardoni F., Marcello E., Colciaghi F., Borroni B., Padovani A., Cattabeni F., and, Di Luca M., (2004) Acetylcholinesterase inhibitors increase ADAM10 activity by promoting its trafficking in neuroblastoma cell lines. J. Neurochem. 90, 1489-1499. (Pubitemid 39223651)
    • (2004) Journal of Neurochemistry , vol.90 , Issue.6 , pp. 1489-1499
    • Zimmermann, M.1    Gardoni, F.2    Marcello, E.3    Colciaghi, F.4    Borroni, B.5    Padovani, A.6    Cattabeni, F.7    Di Luca, M.8
  • 54
    • 37249093071 scopus 로고    scopus 로고
    • Selective enhancement of the activity of C-terminally truncated, but not intact, acetylcholinesterase
    • DOI 10.1111/j.1471-4159.2007.05045.x
    • Zimmermann M., Grosgen S., Westwell M. S., and, Greenfield S. A., (2008) Selective enhancement of the activity of C-terminally truncated, but not intact, acetylcholinesterase. J. Neurochem. 104, 221-232. (Pubitemid 350265074)
    • (2008) Journal of Neurochemistry , vol.104 , Issue.1 , pp. 221-232
    • Zimmermann, M.1    Grosgen, S.2    Westwell, M.S.3    Greenfield, S.A.4
  • 55
    • 58249099965 scopus 로고    scopus 로고
    • Impact of detergents on the activity of acetylcholinesterase and on the effectiveness of its inhibitors
    • Zimmermann M., Westwell M. S., and, Greenfield S. A., (2009) Impact of detergents on the activity of acetylcholinesterase and on the effectiveness of its inhibitors. Biol. Chem. 390, 19-26.
    • (2009) Biol. Chem. , vol.390 , pp. 19-26
    • Zimmermann, M.1    Westwell, M.S.2    Greenfield, S.A.3


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