메뉴 건너뛰기




Volumn 7, Issue 1, 2014, Pages

Interaction of Acetylcholinesterase with Neurexin-1β Regulates Glutamatergic Synaptic stability in Hippocampal neurons

Author keywords

Glycosylation; Neurodegeneration; Protein interaction; Synaptic apoptosis

Indexed keywords

ACETYLCHOLINESTERASE; GLUTAMIC ACID; NEUREXIN; NEUREXIN 1BETA; NEUROLIGIN; UNCLASSIFIED DRUG;

EID: 84898047235     PISSN: None     EISSN: 17566606     Source Type: Journal    
DOI: 10.1186/1756-6606-7-15     Document Type: Article
Times cited : (10)

References (78)
  • 1
    • 0035320772 scopus 로고    scopus 로고
    • Acetylcholinesterase - New roles for an old actor
    • 10.1038/35067589 11283752
    • Acetylcholinesterase-new roles for an old actor. Soreq H, Seidman S, Nat Rev Neurosci 2001 2 294 302 10.1038/35067589 11283752
    • (2001) Nat Rev Neurosci , vol.2 , pp. 294-302
    • Soreq, H.1    Seidman, S.2
  • 2
    • 0037122918 scopus 로고    scopus 로고
    • PRiMA: The membrane anchor of acetylcholinesterase in the brain
    • 10.1016/S0896-6273(01)00584-0 11804574
    • PRiMA: the membrane anchor of acetylcholinesterase in the brain. Perrier AL, Massoulie J, Krejci E, Neuron 2002 33 275 285 10.1016/S0896-6273(01)00584-0 11804574
    • (2002) Neuron , vol.33 , pp. 275-285
    • Perrier, A.L.1    Massoulie, J.2    Krejci, E.3
  • 3
    • 79851507143 scopus 로고    scopus 로고
    • Membrane targeting, shedding and protein interactions of brain acetylcholinesterase
    • 10.1111/j.1471-4159.2010.07032.x 21214569
    • Membrane targeting, shedding and protein interactions of brain acetylcholinesterase. Hicks D, John D, Makova NZ, Henderson Z, Nalivaeva NN, Turner AJ, J Neurochem 2011 116 742 746 10.1111/j.1471-4159.2010.07032.x 21214569
    • (2011) J Neurochem , vol.116 , pp. 742-746
    • Hicks, D.1    John, D.2    Makova, N.Z.3    Henderson, Z.4    Nalivaeva, N.N.5    Turner, A.J.6
  • 4
    • 0004745686 scopus 로고
    • Evidence for a cholinergic projection to neocortex from neurons in basal forebrain
    • 10.1073/pnas.76.10.5392 388436
    • Evidence for a cholinergic projection to neocortex from neurons in basal forebrain. Johnston MV, McKinney M, Coyle JT, Proc Natl Acad Sci USA 1979 76 5392 5396 10.1073/pnas.76.10.5392 388436
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 5392-5396
    • Johnston, M.V.1    McKinney, M.2    Coyle, J.T.3
  • 5
    • 0028324174 scopus 로고
    • Multiple cholinergic markers are unexpectedly not altered in the rat dentate gyrus following entorhinal cortex lesions
    • 8182423
    • Multiple cholinergic markers are unexpectedly not altered in the rat dentate gyrus following entorhinal cortex lesions. Aubert I, Poirier J, Gauthier S, Quirion R, J Neurosci 1994 14 2476 2484 8182423
    • (1994) J Neurosci , vol.14 , pp. 2476-2484
    • Aubert, I.1    Poirier, J.2    Gauthier, S.3    Quirion, R.4
  • 6
    • 0037424301 scopus 로고    scopus 로고
    • Acetylcholinesterase is increased in mouse neuronal and astrocyte cultures after treatment with beta-amyloid peptides
    • 10.1016/S0006-8993(02)04159-8 12591148
    • Acetylcholinesterase is increased in mouse neuronal and astrocyte cultures after treatment with beta-amyloid peptides. Saez-Valero J, Fodero LR, White AR, Barrow CJ, Small DH, Brain Res 2003 965 283 286 10.1016/S0006-8993(02) 04159-8 12591148
    • (2003) Brain Res , vol.965 , pp. 283-286
    • Saez-Valero, J.1    Fodero, L.R.2    White, A.R.3    Barrow, C.J.4    Small, D.H.5
  • 7
    • 0020686674 scopus 로고
    • Alzheimer's disease: A disorder of cortical cholinergic innervation
    • 10.1126/science.6338589 6338589
    • Alzheimer's disease: a disorder of cortical cholinergic innervation. Coyle JT, Price DL, DeLong MR, Science 1983 219 1184 1190 10.1126/science. 6338589 6338589
    • (1983) Science , vol.219 , pp. 1184-1190
    • Coyle, J.T.1    Price, D.L.2    Delong, M.R.3
  • 8
    • 0022475304 scopus 로고
    • Molecular forms of acetylcholinesterase and butyrylcholinesterase in the aged human central nervous system
    • 3711902
    • Molecular forms of acetylcholinesterase and butyrylcholinesterase in the aged human central nervous system. Atack JR, Perry EK, Bonham JR, Candy JM, Perry RH, J Neurochem 1986 47 263 277 3711902
    • (1986) J Neurochem , vol.47 , pp. 263-277
    • Atack, J.R.1    Perry, E.K.2    Bonham, J.R.3    Candy, J.M.4    Perry, R.H.5
  • 9
    • 0022616905 scopus 로고
    • Distribution of the molecular forms of acetylcholinesterase in human brain: Alterations in dementia of the Alzheimer type
    • 10.1002/ana.410190305 3963769
    • Distribution of the molecular forms of acetylcholinesterase in human brain: alterations in dementia of the Alzheimer type. Fishman EB, Siek GC, MacCallum RD, Bird ED, Volicer L, Marquis JK, Ann Neurol 1986 19 246 252 10.1002/ana.410190305 3963769
    • (1986) Ann Neurol , vol.19 , pp. 246-252
    • Fishman, E.B.1    Siek, G.C.2    Maccallum, R.D.3    Bird, E.D.4    Volicer, L.5    Marquis, J.K.6
  • 10
    • 0026031094 scopus 로고
    • Anomalous molecular form of acetylcholinesterase in cerebrospinal fluid in histologically diagnosed Alzheimer's disease
    • 10.1016/0140-6736(91)93391-L 1671469
    • Anomalous molecular form of acetylcholinesterase in cerebrospinal fluid in histologically diagnosed Alzheimer's disease. Navaratnam DS, Priddle JD, McDonald B, Esiri MM, Robinson JR, Smith AD, Lancet 1991 337 447 450 10.1016/0140-6736(91)93391-L 1671469
    • (1991) Lancet , vol.337 , pp. 447-450
    • Navaratnam, D.S.1    Priddle, J.D.2    McDonald, B.3    Esiri, M.M.4    Robinson, J.R.5    Smith, A.D.6
  • 11
    • 0034806090 scopus 로고    scopus 로고
    • Acetylcholinesterase in Alzheimer's disease
    • 10.1016/S0047-6374(01)00309-8 11589914
    • Acetylcholinesterase in Alzheimer's disease. Talesa VN, Mech Ageing Dev 2001 122 1961 1969 10.1016/S0047-6374(01)00309-8 11589914
    • (2001) Mech Ageing Dev , vol.122 , pp. 1961-1969
    • Talesa, V.N.1
  • 12
    • 34547392200 scopus 로고    scopus 로고
    • Glycosylation of acetylcholinesterase as diagnostic marker for Alzheimer's disease
    • 10.1016/S0140-6736(97)24039-0 9314873
    • Glycosylation of acetylcholinesterase as diagnostic marker for Alzheimer's disease. Saez-Valero J, Sberna G, McLean CA, Masters CL, Small DH, Lancet 1997 350 929 10.1016/S0140-6736(97)24039-0 9314873
    • (1997) Lancet , vol.350 , pp. 929
    • Saez-Valero, J.1    Sberna, G.2    McLean, C.A.3    Masters, C.L.4    Small, D.H.5
  • 13
    • 0031587286 scopus 로고    scopus 로고
    • Acetylcholinesterase promotes the aggregation of amyloid-beta-peptide fragments by forming a complex with the growing fibrils
    • 10.1006/jmbi.1997.1245 9325095
    • Acetylcholinesterase promotes the aggregation of amyloid-beta-peptide fragments by forming a complex with the growing fibrils. Alvarez A, Opazo C, Alarcon R, Garrido J, Inestrosa NC, J Mol Biol 1997 272 348 361 10.1006/jmbi.1997.1245 9325095
    • (1997) J Mol Biol , vol.272 , pp. 348-361
    • Alvarez, A.1    Opazo, C.2    Alarcon, R.3    Garrido, J.4    Inestrosa, N.C.5
  • 14
    • 0344417185 scopus 로고    scopus 로고
    • Neurotoxicity of acetylcholinesterase amyloid beta-peptide aggregates is dependent on the type of Abeta peptide and the AChE concentration present in the complexes
    • 10.1016/S0014-5793(99)00468-8 10359075
    • Neurotoxicity of acetylcholinesterase amyloid beta-peptide aggregates is dependent on the type of Abeta peptide and the AChE concentration present in the complexes. Munoz FJ, Inestrosa NC, FEBS Lett 1999 450 205 209 10.1016/S0014-5793(99)00468-8 10359075
    • (1999) FEBS Lett , vol.450 , pp. 205-209
    • Munoz, F.J.1    Inestrosa, N.C.2
  • 15
    • 0038618612 scopus 로고    scopus 로고
    • Acetylcholinesterase promotes beta-amyloid plaques in cerebral cortex
    • 10.1016/S0197-4580(02)00230-0 12927760
    • Acetylcholinesterase promotes beta-amyloid plaques in cerebral cortex. Rees T, Hammond PI, Soreq H, Younkin S, Brimijoin S, Neurobiol Aging 2003 24 777 787 10.1016/S0197-4580(02)00230-0 12927760
    • (2003) Neurobiol Aging , vol.24 , pp. 777-787
    • Rees, T.1    Hammond, P.I.2    Soreq, H.3    Younkin, S.4    Brimijoin, S.5
  • 16
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • 10.1126/science.1074069 12399581
    • Alzheimer's disease is a synaptic failure. Selkoe DJ, Science 2002 298 789 791 10.1126/science.1074069 12399581
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 17
    • 0029036374 scopus 로고
    • Neuroligin 1: A splice site-specific ligand for beta-neurexins
    • 10.1016/0092-8674(95)90396-8 7736595
    • Neuroligin 1: a splice site-specific ligand for beta-neurexins. Ichtchenko K, Hata Y, Nguyen T, Ullrich B, Missler M, Moomaw C, Sudhof TC, Cell 1995 81 435 443 10.1016/0092-8674(95)90396-8 7736595
    • (1995) Cell , vol.81 , pp. 435-443
    • Ichtchenko, K.1    Hata, Y.2    Nguyen, T.3    Ullrich, B.4    Missler, M.5    Moomaw, C.6    Sudhof, T.C.7
  • 18
    • 0033514448 scopus 로고    scopus 로고
    • Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses
    • 10.1073/pnas.96.3.1100 9927700
    • Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses. Song JY, Ichtchenko K, Sudhof TC, Brose N, Proc Natl Acad Sci USA 1999 96 1100 1105 10.1073/pnas.96.3.1100 9927700
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1100-1105
    • Song, J.Y.1    Ichtchenko, K.2    Sudhof, T.C.3    Brose, N.4
  • 19
    • 30344454380 scopus 로고    scopus 로고
    • Neuroligins and neurexins: Linking cell adhesion, synapse formation and cognitive function
    • 16337696
    • Neuroligins and neurexins: linking cell adhesion, synapse formation and cognitive function. Dean C, Dresbach T, Trends Neurosci 2006 29 21 29 16337696
    • (2006) Trends Neurosci , vol.29 , pp. 21-29
    • Dean, C.1    Dresbach, T.2
  • 20
    • 0242317361 scopus 로고    scopus 로고
    • Making connections: Cholinesterase-domain proteins in the CNS
    • 10.1016/j.tins.2003.09.004 14585602
    • Making connections: cholinesterase-domain proteins in the CNS. Scholl FG, Scheiffele P, Trends Neurosci 2003 26 618 624 10.1016/j.tins.2003.09.004 14585602
    • (2003) Trends Neurosci , vol.26 , pp. 618-624
    • Scholl, F.G.1    Scheiffele, P.2
  • 22
    • 0023105119 scopus 로고
    • Neurons segregate clusters of membrane-bound acetylcholinesterase along their neurites
    • 10.1073/pnas.84.7.2063 3470777
    • Neurons segregate clusters of membrane-bound acetylcholinesterase along their neurites. Rotundo RL, Carbonetto ST, Proc Natl Acad Sci USA 1987 84 2063 2067 10.1073/pnas.84.7.2063 3470777
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 2063-2067
    • Rotundo, R.L.1    Carbonetto, S.T.2
  • 24
    • 0029850424 scopus 로고    scopus 로고
    • Pyridostigmine brain penetration under stress enhances neuronal excitability and induces early immediate transcriptional response
    • 10.1038/nm1296-1382 8946841
    • Pyridostigmine brain penetration under stress enhances neuronal excitability and induces early immediate transcriptional response. Friedman A, Kaufer D, Shemer J, Hendler I, Soreq H, Tur-Kaspa I, Nat Med 1996 2 1382 1385 10.1038/nm1296-1382 8946841
    • (1996) Nat Med , vol.2 , pp. 1382-1385
    • Friedman, A.1    Kaufer, D.2    Shemer, J.3    Hendler, I.4    Soreq, H.5    Tur-Kaspa, I.6
  • 25
    • 33645988822 scopus 로고    scopus 로고
    • Virtues and woes of AChE alternative splicing in stress-related neuropathologies
    • 10.1016/j.tins.2006.02.005 16516310
    • Virtues and woes of AChE alternative splicing in stress-related neuropathologies. Meshorer E, Soreq H, Trends Neurosci 2006 29 216 224 10.1016/j.tins.2006.02.005 16516310
    • (2006) Trends Neurosci , vol.29 , pp. 216-224
    • Meshorer, E.1    Soreq, H.2
  • 26
    • 0032534987 scopus 로고    scopus 로고
    • Modulation of circulatory residence of recombinant acetylcholinesterase through biochemical or genetic manipulation of sialylation levels
    • 9841877
    • Modulation of circulatory residence of recombinant acetylcholinesterase through biochemical or genetic manipulation of sialylation levels. Chitlaru T, Kronman C, Zeevi M, Kam M, Harel A, Ordentlich A, Velan B, Shafferman A, Biochem J 1998 336 Pt 3 647 658 9841877
    • (1998) Biochem J , vol.336 , Issue.PART 3 , pp. 647-658
    • Chitlaru, T.1    Kronman, C.2    Zeevi, M.3    Kam, M.4    Harel, A.5    Ordentlich, A.6    Velan, B.7    Shafferman, A.8
  • 27
    • 0026333511 scopus 로고
    • The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys-580 - Ala mutant
    • 1748670
    • The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys-580 - Ala mutant. Velan B, Grosfeld H, Kronman C, Leitner M, Gozes Y, Lazar A, Flashner Y, Marcus D, Cohen S, Shafferman A, J Biol Chem 1991 266 23977 23984 1748670
    • (1991) J Biol Chem , vol.266 , pp. 23977-23984
    • Velan, B.1    Grosfeld, H.2    Kronman, C.3    Leitner, M.4    Gozes, Y.5    Lazar, A.6    Flashner, Y.7    Marcus, D.8    Cohen, S.9    Shafferman, A.10
  • 28
    • 0028241566 scopus 로고
    • Cellular expression of a cloned, hydrophilic, murine acetylcholinesterase. Evidence of palmitoylated membrane-bound forms
    • 7512968
    • Cellular expression of a cloned, hydrophilic, murine acetylcholinesterase. Evidence of palmitoylated membrane-bound forms. Randall WR, J Biol Chem 1994 269 12367 12374 7512968
    • (1994) J Biol Chem , vol.269 , pp. 12367-12374
    • Randall, W.R.1
  • 29
    • 0032528919 scopus 로고    scopus 로고
    • Bovine acetylcholinesterase: Cloning, expression and characterization
    • 9693127
    • Bovine acetylcholinesterase: cloning, expression and characterization. Mendelson I, Kronman C, Ariel N, Shafferman A, Velan B, Biochem J 1998 334 Pt 1 251 259 9693127
    • (1998) Biochem J , vol.334 , Issue.PART 1 , pp. 251-259
    • Mendelson, I.1    Kronman, C.2    Ariel, N.3    Shafferman, A.4    Velan, B.5
  • 30
    • 0036565780 scopus 로고    scopus 로고
    • Overloading and removal of N-glycosylation targets on human acetylcholinesterase: Effects on glycan composition and circulatory residence time
    • 10.1042/0264-6021:3630619 11964163
    • Overloading and removal of N-glycosylation targets on human acetylcholinesterase: effects on glycan composition and circulatory residence time. Chitlaru T, Kronman C, Velan B, Shafferman A, Biochem J 2002 363 619 631 10.1042/0264-6021:3630619 11964163
    • (2002) Biochem J , vol.363 , pp. 619-631
    • Chitlaru, T.1    Kronman, C.2    Velan, B.3    Shafferman, A.4
  • 31
    • 0027762066 scopus 로고
    • N-glycosylation of human acetylcholinesterase: Effects on activity, stability and biosynthesis
    • 8280063
    • N-glycosylation of human acetylcholinesterase: effects on activity, stability and biosynthesis. Velan B, Kronman C, Ordentlich A, Flashner Y, Leitner M, Cohen S, Shafferman A, Biochem J 1993 296 Pt 3 649 656 8280063
    • (1993) Biochem J , vol.296 , Issue.PART 3 , pp. 649-656
    • Velan, B.1    Kronman, C.2    Ordentlich, A.3    Flashner, Y.4    Leitner, M.5    Cohen, S.6    Shafferman, A.7
  • 32
    • 0030873431 scopus 로고    scopus 로고
    • Acetylcholinesterase-transgenic mice display embryonic modulations in spinal cord choline acetyltransferase and neurexin Ibeta gene expression followed by late-onset neuromotor deterioration
    • 10.1073/pnas.94.15.8173 9223334
    • Acetylcholinesterase-transgenic mice display embryonic modulations in spinal cord choline acetyltransferase and neurexin Ibeta gene expression followed by late-onset neuromotor deterioration. Andres C, Beeri R, Friedman A, Lev-Lehman E, Henis S, Timberg R, Shani M, Soreq H, Proc Natl Acad Sci U S A 1997 94 8173 8178 10.1073/pnas.94.15.8173 9223334
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 8173-8178
    • Andres, C.1    Beeri, R.2    Friedman, A.3    Lev-Lehman, E.4    Henis, S.5    Timberg, R.6    Shani, M.7    Soreq, H.8
  • 33
    • 0028241554 scopus 로고
    • Conserved domain structure of beta-neurexins. Unusual cleaved signal sequences in receptor-like neuronal cell-surface proteins
    • 8163501
    • Conserved domain structure of beta-neurexins. Unusual cleaved signal sequences in receptor-like neuronal cell-surface proteins. Ushkaryov YA, Hata Y, Ichtchenko K, Moomaw C, Afendis S, Slaughter CA, Sudhof TC, J Biol Chem 1994 269 11987 11992 8163501
    • (1994) J Biol Chem , vol.269 , pp. 11987-11992
    • Ushkaryov, Y.A.1    Hata, Y.2    Ichtchenko, K.3    Moomaw, C.4    Afendis, S.5    Slaughter, C.A.6    Sudhof, T.C.7
  • 34
    • 33646464124 scopus 로고    scopus 로고
    • Structure function and splice site analysis of the synaptogenic activity of the neurexin-1 beta LNS domain
    • 10.1523/JNEUROSCI.1253-05.2006 16624946
    • Structure function and splice site analysis of the synaptogenic activity of the neurexin-1 beta LNS domain. Graf ER, Kang Y, Hauner AM, Craig AM, J Neurosci 2006 26 4256 4265 10.1523/JNEUROSCI.1253-05.2006 16624946
    • (2006) J Neurosci , vol.26 , pp. 4256-4265
    • Graf, E.R.1    Kang, Y.2    Hauner, A.M.3    Craig, A.M.4
  • 35
    • 0027934296 scopus 로고
    • Electrostatic attraction by surface charge does not contribute to the catalytic efficiency of acetylcholinesterase
    • 8062821
    • Electrostatic attraction by surface charge does not contribute to the catalytic efficiency of acetylcholinesterase. Shafferman A, Ordentlich A, Barak D, Kronman C, Ber R, Bino T, Ariel N, Osman R, Velan B, EMBO J 1994 13 3448 3455 8062821
    • (1994) EMBO J , vol.13 , pp. 3448-3455
    • Shafferman, A.1    Ordentlich, A.2    Barak, D.3    Kronman, C.4    Ber, R.5    Bino, T.6    Ariel, N.7    Osman, R.8    Velan, B.9
  • 36
    • 0030828982 scopus 로고    scopus 로고
    • Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. Distinctions between active center ligands and fasciculin
    • 10.1074/jbc.272.37.23265 9287336
    • Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. Distinctions between active center ligands and fasciculin. Radic Z, Kirchhoff PD, Quinn DM, McCammon JA, Taylor P, J Biol Chem 1997 272 23265 23277 10.1074/jbc.272.37.23265 9287336
    • (1997) J Biol Chem , vol.272 , pp. 23265-23277
    • Radic, Z.1    Kirchhoff, P.D.2    Quinn, D.M.3    McCammon, J.A.4    Taylor, P.5
  • 37
    • 4944253492 scopus 로고    scopus 로고
    • Mouse acetylcholinesterase interacts in yeast with the extracellular matrix component laminin-1beta
    • 10.1016/j.febslet.2004.08.078 15474030
    • Mouse acetylcholinesterase interacts in yeast with the extracellular matrix component laminin-1beta. Paraoanu LE, Layer PG, FEBS Lett 2004 576 161 164 10.1016/j.febslet.2004.08.078 15474030
    • (2004) FEBS Lett , vol.576 , pp. 161-164
    • Paraoanu, L.E.1    Layer, P.G.2
  • 38
    • 84860520931 scopus 로고    scopus 로고
    • Mouse acetylcholinesterase enhances neurite outgrowth of rat R28 cells through interaction with laminin-1
    • 10.1371/journal.pone.0036683 22570738
    • Mouse acetylcholinesterase enhances neurite outgrowth of rat R28 cells through interaction with laminin-1. Sperling LE, Klaczinski J, Schutz C, Rudolph L, Layer PG, PLoS One 2012 7 36683 10.1371/journal.pone.0036683 22570738
    • (2012) PLoS One , vol.7 , pp. 536683
    • Sperling, L.E.1    Klaczinski, J.2    Schutz, C.3    Rudolph, L.4    Layer, P.G.5
  • 39
    • 0034625250 scopus 로고    scopus 로고
    • Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons
    • 10.1016/S0092-8674(00)80877-6 10892652
    • Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons. Scheiffele P, Fan J, Choih J, Fetter R, Serafini T, Cell 2000 101 657 669 10.1016/S0092-8674(00)80877-6 10892652
    • (2000) Cell , vol.101 , pp. 657-669
    • Scheiffele, P.1    Fan, J.2    Choih, J.3    Fetter, R.4    Serafini, T.5
  • 40
    • 18744414554 scopus 로고    scopus 로고
    • Acetylcholinesterase: 'Classical' and 'non-classical' functions and pharmacology
    • 10.1016/j.coph.2005.01.014 15907917
    • Acetylcholinesterase: 'classical' and 'non-classical' functions and pharmacology. Silman I, Sussman JL, Curr Opin Pharmacol 2005 5 293 302 10.1016/j.coph.2005.01.014 15907917
    • (2005) Curr Opin Pharmacol , vol.5 , pp. 293-302
    • Silman, I.1    Sussman, J.L.2
  • 41
    • 0027198071 scopus 로고
    • Cholinesterases regulate neurite growth of chick nerve cells in vitro by means of a non-enzymatic mechanism
    • 10.1007/BF00312823 8103422
    • Cholinesterases regulate neurite growth of chick nerve cells in vitro by means of a non-enzymatic mechanism. Layer PG, Weikert T, Alber R, Cell Tissue Res 1993 273 219 226 10.1007/BF00312823 8103422
    • (1993) Cell Tissue Res , vol.273 , pp. 219-226
    • Layer, P.G.1    Weikert, T.2    Alber, R.3
  • 42
    • 10844222503 scopus 로고    scopus 로고
    • Impaired formation of the inner retina in an AChE knockout mouse results in degeneration of all photoreceptors
    • 10.1111/j.1460-9568.2004.03753.x 15579149
    • Impaired formation of the inner retina in an AChE knockout mouse results in degeneration of all photoreceptors. Bytyqi AH, Lockridge O, Duysen E, Wang Y, Wolfrum U, Layer PG, Eur J Neurosci 2004 20 2953 2962 10.1111/j.1460-9568.2004. 03753.x 15579149
    • (2004) Eur J Neurosci , vol.20 , pp. 2953-2962
    • Bytyqi, A.H.1    Lockridge, O.2    Duysen, E.3    Wang, Y.4    Wolfrum, U.5    Layer, P.G.6
  • 43
    • 0030657499 scopus 로고    scopus 로고
    • Enhanced hemicholinium binding and attenuated dendrite branching in cognitively impaired acetylcholinesterase-transgenic mice
    • 9375677
    • Enhanced hemicholinium binding and attenuated dendrite branching in cognitively impaired acetylcholinesterase-transgenic mice. Beeri R, Le Novere N, Mervis R, Huberman T, Grauer E, Changeux JP, Soreq H, J Neurochem 1997 69 2441 2451 9375677
    • (1997) J Neurochem , vol.69 , pp. 2441-2451
    • Beeri, R.1    Le Novere, N.2    Mervis, R.3    Huberman, T.4    Grauer, E.5    Changeux, J.P.6    Soreq, H.7
  • 44
    • 0032077169 scopus 로고    scopus 로고
    • Transgenic acetylcholinesterase induces enlargement of murine neuromuscular junctions but leaves spinal cord synapses intact
    • 10.1016/S0197-0186(97)00121-6 9676744
    • Transgenic acetylcholinesterase induces enlargement of murine neuromuscular junctions but leaves spinal cord synapses intact. Andres C, Seidman S, Beeri R, Timberg R, Soreq H, Neurochem Int 1998 32 449 456 10.1016/S0197-0186(97)00121-6 9676744
    • (1998) Neurochem Int , vol.32 , pp. 449-456
    • Andres, C.1    Seidman, S.2    Beeri, R.3    Timberg, R.4    Soreq, H.5
  • 45
    • 0026517792 scopus 로고
    • Chicken retinospheroids as developmental and pharmacological in vitro models: Acetylcholinesterase is regulated by its own and by butyrylcholinesterase activity
    • 10.1007/BF00319147 1628298
    • Chicken retinospheroids as developmental and pharmacological in vitro models: acetylcholinesterase is regulated by its own and by butyrylcholinesterase activity. Layer PG, Weikert T, Willbold E, Cell Tissue Res 1992 268 409 418 10.1007/BF00319147 1628298
    • (1992) Cell Tissue Res , vol.268 , pp. 409-418
    • Layer, P.G.1    Weikert, T.2    Willbold, E.3
  • 46
    • 0346118881 scopus 로고    scopus 로고
    • Characterization of the interaction of a recombinant soluble neuroligin-1 with neurexin-1beta
    • 10.1074/jbc.M306803200 14522992
    • Characterization of the interaction of a recombinant soluble neuroligin-1 with neurexin-1beta. Comoletti D, Flynn R, Jennings LL, Chubykin A, Matsumura T, Hasegawa H, Sudhof TC, Taylor P, J Biol Chem 2003 278 50497 50505 10.1074/jbc.M306803200 14522992
    • (2003) J Biol Chem , vol.278 , pp. 50497-50505
    • Comoletti, D.1    Flynn, R.2    Jennings, L.L.3    Chubykin, A.4    Matsumura, T.5    Hasegawa, H.6    Sudhof, T.C.7    Taylor, P.8
  • 47
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: Possible role of the peripheral site of the enzyme
    • 10.1016/S0896-6273(00)80108-7 8608006
    • Acetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Inestrosa NC, Alvarez A, Perez CA, Moreno RD, Vicente M, Linker C, Casanueva OI, Soto C, Garrido J, Neuron 1996 16 881 891 10.1016/S0896-6273(00)80108-7 8608006
    • (1996) Neuron , vol.16 , pp. 881-891
    • Inestrosa, N.C.1    Alvarez, A.2    Perez, C.A.3    Moreno, R.D.4    Vicente, M.5    Linker, C.6    Casanueva, O.I.7    Soto, C.8    Garrido, J.9
  • 49
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • 10.1126/science.1678899 1678899
    • Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silman I, Science 1991 253 872 879 10.1126/science. 1678899 1678899
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 50
    • 0037472358 scopus 로고    scopus 로고
    • Human acetylcholinesterase binds to mouse laminin-1 and human collagen IV by an electrostatic mechanism at the peripheral anionic site
    • 10.1016/S0304-3940(02)01298-3 12524166
    • Human acetylcholinesterase binds to mouse laminin-1 and human collagen IV by an electrostatic mechanism at the peripheral anionic site. Johnson G, Moore SW, Neurosci Lett 2003 337 37 40 10.1016/S0304-3940(02)01298-3 12524166
    • (2003) Neurosci Lett , vol.337 , pp. 37-40
    • Johnson, G.1    Moore, S.W.2
  • 52
    • 37049027105 scopus 로고    scopus 로고
    • Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ interactions
    • 10.1016/j.neuron.2007.12.002 18093522
    • Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ interactions. Arac D, Boucard AA, Ozkan E, Strop P, Newell E, Sudhof TC, Brunger AT, Neuron 2007 56 992 1003 10.1016/j.neuron.2007.12.002 18093522
    • (2007) Neuron , vol.56 , pp. 992-1003
    • Arac, D.1    Boucard, A.A.2    Ozkan, E.3    Strop, P.4    Newell, E.5    Sudhof, T.C.6    Brunger, A.T.7
  • 53
    • 0032931885 scopus 로고    scopus 로고
    • Cholinesterase inhibitors: A therapeutic strategy for Alzheimer disease
    • 10.1345/aph.18211 10332536
    • Cholinesterase inhibitors: a therapeutic strategy for Alzheimer disease. Krall WJ, Sramek JJ, Cutler NR, Ann Pharmacother 1999 33 441 450 10.1345/aph.18211 10332536
    • (1999) Ann Pharmacother , vol.33 , pp. 441-450
    • Krall, W.J.1    Sramek, J.J.2    Cutler, N.R.3
  • 54
    • 0025490658 scopus 로고
    • Cholinesterases preceding major tracts in vertebrate neurogenesis
    • 10.1002/bies.950120904 2256905
    • Cholinesterases preceding major tracts in vertebrate neurogenesis. Layer PG, Bioessays 1990 12 415 420 10.1002/bies.950120904 2256905
    • (1990) Bioessays , vol.12 , pp. 415-420
    • Layer, P.G.1
  • 55
    • 0028858086 scopus 로고
    • Postnatal development of cortical acetylcholinesterase-rich neurons in the rat brain: Permanent and transient patterns
    • 10.1006/exnr.1995.1046 7556536
    • Postnatal development of cortical acetylcholinesterase-rich neurons in the rat brain: permanent and transient patterns. Geula C, Mesulam MM, Kuo CC, Tokuno H, Exp Neurol 1995 134 157 178 10.1006/exnr.1995.1046 7556536
    • (1995) Exp Neurol , vol.134 , pp. 157-178
    • Geula, C.1    Mesulam, M.M.2    Kuo, C.C.3    Tokuno, H.4
  • 56
    • 0024340538 scopus 로고
    • The postnatal expression of acetylcholinesterase in somatostatin-positive cells of mouse hippocampus
    • 10.1016/0165-3806(89)90094-1 2752576
    • The postnatal expression of acetylcholinesterase in somatostatin-positive cells of mouse hippocampus. Forloni G, Blake K, Hohmann CH, Coyle JT, Brain Res Dev Brain Res 1989 48 73 85 10.1016/0165-3806(89)90094-1 2752576
    • (1989) Brain Res Dev Brain Res , vol.48 , pp. 73-85
    • Forloni, G.1    Blake, K.2    Hohmann, C.H.3    Coyle, J.T.4
  • 57
    • 79954420691 scopus 로고    scopus 로고
    • Chronic variable stress alters inflammatory and cholinergic parameters in hippocampus of rats
    • 10.1007/s11064-010-0367-0 21184279
    • Chronic variable stress alters inflammatory and cholinergic parameters in hippocampus of rats. Tagliari B, Tagliari AP, Schmitz F, da Cunha AA, Dalmaz C, Wyse AT, Neurochem Res 2011 36 487 493 10.1007/s11064-010-0367-0 21184279
    • (2011) Neurochem Res , vol.36 , pp. 487-493
    • Tagliari, B.1    Tagliari, A.P.2    Schmitz, F.3    Da Cunha, A.A.4    Dalmaz, C.5    Wyse, A.T.6
  • 58
    • 0037072536 scopus 로고    scopus 로고
    • Clomipramine treatment in neonatal rats alters the brain acetylcholinesterase activity in adulthood
    • 10.1016/S0304-3940(02)00725-5 12213647
    • Clomipramine treatment in neonatal rats alters the brain acetylcholinesterase activity in adulthood. Mavanji V, Datta S, Neurosci Lett 2002 330 119 121 10.1016/S0304-3940(02)00725-5 12213647
    • (2002) Neurosci Lett , vol.330 , pp. 119-121
    • Mavanji, V.1    Datta, S.2
  • 59
    • 40849140689 scopus 로고    scopus 로고
    • The role of the read through variant of acetylcholinesterase in anxiogenic effects of predator stress in mice
    • 10.1016/j.bbr.2007.12.023 18243359
    • The role of the read through variant of acetylcholinesterase in anxiogenic effects of predator stress in mice. Adamec R, Head D, Soreq H, Blundell J, Behav Brain Res 2008 189 180 190 10.1016/j.bbr.2007.12.023 18243359
    • (2008) Behav Brain Res , vol.189 , pp. 180-190
    • Adamec, R.1    Head, D.2    Soreq, H.3    Blundell, J.4
  • 60
    • 0029360450 scopus 로고
    • Transgenic expression of human acetylcholinesterase induces progressive cognitive deterioration in mice
    • 10.1016/S0960-9822(95)00211-9 8542283
    • Transgenic expression of human acetylcholinesterase induces progressive cognitive deterioration in mice. Beeri R, Andres C, Lev-Lehman E, Timberg R, Huberman T, Shani M, Soreq H, Curr Biol 1995 5 1063 1071 10.1016/S0960-9822(95) 00211-9 8542283
    • (1995) Curr Biol , vol.5 , pp. 1063-1071
    • Beeri, R.1    Andres, C.2    Lev-Lehman, E.3    Timberg, R.4    Huberman, T.5    Shani, M.6    Soreq, H.7
  • 61
    • 13544269142 scopus 로고    scopus 로고
    • Control of excitatory and inhibitory synapse formation by neuroligins
    • 10.1126/science.1107470 15681343
    • Control of excitatory and inhibitory synapse formation by neuroligins. Chih B, Engelman H, Scheiffele P, Science 2005 307 1324 1328 10.1126/science.1107470 15681343
    • (2005) Science , vol.307 , pp. 1324-1328
    • Chih, B.1    Engelman, H.2    Scheiffele, P.3
  • 62
    • 11144352245 scopus 로고    scopus 로고
    • Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins
    • 10.1016/j.cell.2004.11.035 15620359
    • Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins. Graf ER, Zhang X, Jin SX, Linhoff MW, Craig AM, Cell 2004 119 1013 1026 10.1016/j.cell.2004.11.035 15620359
    • (2004) Cell , vol.119 , pp. 1013-1026
    • Graf, E.R.1    Zhang, X.2    Jin, S.X.3    Linhoff, M.W.4    Craig, A.M.5
  • 63
    • 0038071095 scopus 로고    scopus 로고
    • Cell-cell signaling during synapse formation in the CNS
    • 10.1146/annurev.neuro.26.043002.094940 12626697
    • Cell-cell signaling during synapse formation in the CNS. Scheiffele P, Ann Rev Neurosci 2003 26 485 508 10.1146/annurev.neuro.26.043002.094940 12626697
    • (2003) Ann Rev Neurosci , vol.26 , pp. 485-508
    • Scheiffele, P.1
  • 64
    • 54049091941 scopus 로고    scopus 로고
    • Neuroligins and neurexins link synaptic function to cognitive disease
    • 10.1038/nature07456 18923512
    • Neuroligins and neurexins link synaptic function to cognitive disease. Sudhof TC, Nature 2008 455 903 911 10.1038/nature07456 18923512
    • (2008) Nature , vol.455 , pp. 903-911
    • Sudhof, T.C.1
  • 65
    • 71749084011 scopus 로고    scopus 로고
    • MicroRNA-132 potentiates cholinergic anti-inflammatory signaling by targeting acetylcholinesterase
    • 10.1016/j.immuni.2009.09.019 20005135
    • MicroRNA-132 potentiates cholinergic anti-inflammatory signaling by targeting acetylcholinesterase. Shaked I, Meerson A, Wolf Y, Avni R, Greenberg D, Gilboa-Geffen A, Soreq H, Immunity 2009 31 965 973 10.1016/j.immuni.2009.09. 019 20005135
    • (2009) Immunity , vol.31 , pp. 965-973
    • Shaked, I.1    Meerson, A.2    Wolf, Y.3    Avni, R.4    Greenberg, D.5    Gilboa-Geffen, A.6    Soreq, H.7
  • 68
    • 0032520131 scopus 로고    scopus 로고
    • Acetylcholinesterase enhances neurite growth and synapse development through alternative contributions of its hydrolytic capacity, core protein, and variable C termini
    • 9454834
    • Acetylcholinesterase enhances neurite growth and synapse development through alternative contributions of its hydrolytic capacity, core protein, and variable C termini. Sternfeld M, Ming G, Song H, Sela K, Timberg R, Poo M, Soreq H, J Neurosci 1998 18 1240 1249 9454834
    • (1998) J Neurosci , vol.18 , pp. 1240-1249
    • Sternfeld, M.1    Ming, G.2    Song, H.3    Sela, K.4    Timberg, R.5    Poo, M.6    Soreq, H.7
  • 69
    • 0030026657 scopus 로고    scopus 로고
    • Structures, alternative splicing, and neurexin binding of multiple neuroligins
    • 10.1074/jbc.271.5.2676 8576240
    • Structures, alternative splicing, and neurexin binding of multiple neuroligins. Ichtchenko K, Nguyen T, Sudhof TC, J Biol Chem 1996 271 2676 2682 10.1074/jbc.271.5.2676 8576240
    • (1996) J Biol Chem , vol.271 , pp. 2676-2682
    • Ichtchenko, K.1    Nguyen, T.2    Sudhof, T.C.3
  • 70
    • 0033103549 scopus 로고    scopus 로고
    • Neurexins are functional alpha-latrotoxin receptors
    • 10.1016/S0896-6273(00)80704-7 10197529
    • Neurexins are functional alpha-latrotoxin receptors. Sugita S, Khvochtev M, Sudhof TC, Neuron 1999 22 489 496 10.1016/S0896-6273(00)80704-7 10197529
    • (1999) Neuron , vol.22 , pp. 489-496
    • Sugita, S.1    Khvochtev, M.2    Sudhof, T.C.3
  • 71
    • 0034647495 scopus 로고    scopus 로고
    • Tandem repeats are involved in G1 domain inhibition of versican expression and secretion and the G3 domain enhances glycosaminoglycan modification and product secretion via the complement-binding protein-like motif
    • 10.1074/jbc.M001443200 10801813
    • Tandem repeats are involved in G1 domain inhibition of versican expression and secretion and the G3 domain enhances glycosaminoglycan modification and product secretion via the complement-binding protein-like motif. Yang BL, Cao L, Kiani C, Lee V, Zhang Y, Adams ME, Yang BB, J Biol Chem 2000 275 21255 21261 10.1074/jbc.M001443200 10801813
    • (2000) J Biol Chem , vol.275 , pp. 21255-21261
    • Yang, B.L.1    Cao, L.2    Kiani, C.3    Lee, V.4    Zhang, Y.5    Adams, M.E.6    Yang, B.B.7
  • 72
    • 0033571214 scopus 로고    scopus 로고
    • SUMO-1 modification activates the transcriptional response of p53
    • 10.1093/emboj/18.22.6455 10562557
    • SUMO-1 modification activates the transcriptional response of p53. Rodriguez MS, Desterro JM, Lain S, Midgley CA, Lane DP, Hay RT, EMBO J 1999 18 6455 6461 10.1093/emboj/18.22.6455 10562557
    • (1999) EMBO J , vol.18 , pp. 6455-6461
    • Rodriguez, M.S.1    Desterro, J.M.2    Lain, S.3    Midgley, C.A.4    Lane, D.P.5    Hay, R.T.6
  • 75
    • 0027226219 scopus 로고
    • Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination
    • 10.1002/jnr.490350513 8377226
    • Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination. Brewer GJ, Torricelli JR, Evege EK, Price PJ, J Neurosci Res 1993 35 567 576 10.1002/jnr.490350513 8377226
    • (1993) J Neurosci Res , vol.35 , pp. 567-576
    • Brewer, G.J.1    Torricelli, J.R.2    Evege, E.K.3    Price, P.J.4
  • 76
    • 33745863464 scopus 로고    scopus 로고
    • Versican G3 domain regulates neurite growth and synaptic transmission of hippocampal neurons by activation of epidermal growth factor receptor
    • 10.1074/jbc.M512980200 16648628
    • Versican G3 domain regulates neurite growth and synaptic transmission of hippocampal neurons by activation of epidermal growth factor receptor. Xiang YY, Dong H, Wan Y, Li J, Yee A, Yang BB, Lu WY, J Biol Chem 2006 281 19358 19368 10.1074/jbc.M512980200 16648628
    • (2006) J Biol Chem , vol.281 , pp. 19358-19368
    • Xiang, Y.Y.1    Dong, H.2    Wan, Y.3    Li, J.4    Yee, A.5    Yang, B.B.6    Lu, W.Y.7
  • 77
    • 77954724789 scopus 로고    scopus 로고
    • Variability of distribution of Ca(2+)/calmodulin-dependent kinase II at mixed synapses on the mauthner cell: Colocalization and association with connexin 35
    • 10.1523/JNEUROSCI.4466-09.2010 20631177
    • Variability of distribution of Ca(2+)/calmodulin-dependent kinase II at mixed synapses on the mauthner cell: colocalization and association with connexin 35. Flores CE, Cachope R, Nannapaneni S, Ene S, Nairn AC, Pereda AE, J Neurosci 2010 30 9488 9499 10.1523/JNEUROSCI.4466-09.2010 20631177
    • (2010) J Neurosci , vol.30 , pp. 9488-9499
    • Flores, C.E.1    Cachope, R.2    Nannapaneni, S.3    Ene, S.4    Nairn, A.C.5    Pereda, A.E.6
  • 78
    • 1442323992 scopus 로고    scopus 로고
    • Long-lasting acetylcholinesterase splice variations in anticholinesterase-treated Alzheimer's disease patients
    • 10.1046/j.1471-4159.2003.02230.x 15009666
    • Long-lasting acetylcholinesterase splice variations in anticholinesterase-treated Alzheimer's disease patients. Darreh-Shori T, Hellstrom-Lindahl E, Flores-Flores C, Guan ZZ, Soreq H, Nordberg A, J Neurochem 2004 88 1102 1113 10.1046/j.1471-4159.2003.02230.x 15009666
    • (2004) J Neurochem , vol.88 , pp. 1102-1113
    • Darreh-Shori, T.1    Hellstrom-Lindahl, E.2    Flores-Flores, C.3    Guan, Z.Z.4    Soreq, H.5    Nordberg, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.