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Volumn 7, Issue 5, 2012, Pages

Mouse acetylcholinesterase enhances neurite outgrowth of rat R28 cells through interaction with laminin-1

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINESTERASE; LAMININ 1;

EID: 84860520931     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0036683     Document Type: Article
Times cited : (28)

References (67)
  • 1
    • 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
    • Sternfeld M, Ming G, Song H, Sela K, Timberg R, et al. (1998) Acetylcholinesterase enhances neurite growth and synapse development through alternative contributions of its hydrolytic capacity, core protein, and variable C termini. J Neurosci 18: 1240-1249.
    • (1998) J Neurosci , vol.18 , pp. 1240-1249
    • Sternfeld, M.1    Ming, G.2    Song, H.3    Sela, K.4    Timberg, R.5
  • 2
    • 0035320772 scopus 로고    scopus 로고
    • Acetylcholinesterase-new roles for an old actor
    • Soreq H, Seidman S, (2001) Acetylcholinesterase-new roles for an old actor. Nat Rev Neurosci 2: 294-302.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 294-302
    • Soreq, H.1    Seidman, S.2
  • 3
    • 84858832322 scopus 로고    scopus 로고
    • Co-opting Functions of Cholinesterases in Neural, Limb and Stem Cell Development
    • Vogel-Hopker A, Sperling LE, Layer PG, (2011) Co-opting Functions of Cholinesterases in Neural, Limb and Stem Cell Development. Protein Pept Lett.
    • (2011) Protein Pept Lett
    • Vogel-Hopker, A.1    Sperling, L.E.2    Layer, P.G.3
  • 4
    • 38549176068 scopus 로고    scopus 로고
    • Acetylcholinesterase in cell adhesion, neurite growth and network formation
    • Paraoanu LE, Layer PG, (2008) Acetylcholinesterase in cell adhesion, neurite growth and network formation. FEBS J 275: 618-624.
    • (2008) FEBS J , vol.275 , pp. 618-624
    • Paraoanu, L.E.1    Layer, P.G.2
  • 5
    • 0027198071 scopus 로고
    • Cholinesterases regulate neurite growth of chick nerve cells in vitro by means of a non-enzymatic mechanism
    • Layer PG, Weikert T, Alber R, (1993) Cholinesterases regulate neurite growth of chick nerve cells in vitro by means of a non-enzymatic mechanism. Cell Tissue Res 273: 219-226.
    • (1993) Cell Tissue Res , vol.273 , pp. 219-226
    • Layer, P.G.1    Weikert, T.2    Alber, R.3
  • 6
    • 0036789955 scopus 로고    scopus 로고
    • The stress-associated acetylcholinesterase variant AChE-R is expressed in human CD34(+) hematopoietic progenitors and its C-terminal peptide ARP promotes their proliferation
    • Deutsch VR, Pick M, Perry C, Grisaru D, Hemo Y, et al. (2002) The stress-associated acetylcholinesterase variant AChE-R is expressed in human CD34(+) hematopoietic progenitors and its C-terminal peptide ARP promotes their proliferation. Exp Hematol 30: 1153-1161.
    • (2002) Exp Hematol , vol.30 , pp. 1153-1161
    • Deutsch, V.R.1    Pick, M.2    Perry, C.3    Grisaru, D.4    Hemo, Y.5
  • 7
    • 0031009676 scopus 로고    scopus 로고
    • Immature human megakaryocytes produce nuclear-associated acetylcholinesterase
    • Lev-Lehman E, Deutsch V, Eldor A, Soreq H, (1997) Immature human megakaryocytes produce nuclear-associated acetylcholinesterase. Blood 89: 3644-3653.
    • (1997) Blood , vol.89 , pp. 3644-3653
    • Lev-Lehman, E.1    Deutsch, V.2    Eldor, A.3    Soreq, H.4
  • 8
    • 0035260244 scopus 로고    scopus 로고
    • ARP, a peptide derived from the stress-associated acetylcholinesterase variant, has hematopoietic growth promoting activities
    • Grisaru D, Deutsch V, Shapira M, Pick M, Sternfeld M, et al. (2001) ARP, a peptide derived from the stress-associated acetylcholinesterase variant, has hematopoietic growth promoting activities. Mol Med 7: 93-105.
    • (2001) Mol Med , vol.7 , pp. 93-105
    • Grisaru, D.1    Deutsch, V.2    Shapira, M.3    Pick, M.4    Sternfeld, M.5
  • 9
    • 0023106461 scopus 로고
    • Spatiotemporal relationship of embryonic cholinesterases with cell proliferation in chicken brain and eye
    • Layer PG, Sporns O, (1987) Spatiotemporal relationship of embryonic cholinesterases with cell proliferation in chicken brain and eye. Proc Natl Acad Sci U S A 84: 284-288.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 284-288
    • Layer, P.G.1    Sporns, O.2
  • 10
    • 0029163984 scopus 로고
    • Novel functions of cholinesterases in development, physiology and disease
    • Layer PG, 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
  • 11
    • 0034647050 scopus 로고    scopus 로고
    • Evidence for the direct role of acetylcholinesterase in neurite outgrowth in primary dorsal root ganglion neurons
    • Bigbee JW, Sharma KV, Chan EL, Bogler O, (2000) Evidence for the direct role of acetylcholinesterase in neurite outgrowth in primary dorsal root ganglion neurons. Brain Res 861: 354-362.
    • (2000) Brain Res , vol.861 , pp. 354-362
    • Bigbee, J.W.1    Sharma, K.V.2    Chan, E.L.3    Bogler, O.4
  • 12
    • 0037114681 scopus 로고    scopus 로고
    • Alternative acetylcholinesterase molecular forms exhibit similar ability to induce neurite outgrowth
    • De Jaco A, Augusti-Tocco G, Biagioni S, (2002) Alternative acetylcholinesterase molecular forms exhibit similar ability to induce neurite outgrowth. J Neurosci Res 70: 756-765.
    • (2002) J Neurosci Res , vol.70 , pp. 756-765
    • de Jaco, A.1    Augusti-Tocco, G.2    Biagioni, S.3
  • 13
    • 0033568704 scopus 로고    scopus 로고
    • Structural roles of acetylcholinesterase variants in biology and pathology
    • Grisaru D, Sternfeld M, Eldor A, Glick D, Soreq H, (1999) Structural roles of acetylcholinesterase variants in biology and pathology. Eur J Biochem 264: 672-686.
    • (1999) Eur J Biochem , vol.264 , pp. 672-686
    • Grisaru, D.1    Sternfeld, M.2    Eldor, A.3    Glick, D.4    Soreq, H.5
  • 14
    • 0032506149 scopus 로고    scopus 로고
    • Functional redundancy of acetylcholinesterase and neuroligin in mammalian neuritogenesis
    • Grifman M, Galyam N, Seidman S, Soreq H, (1998) Functional redundancy of acetylcholinesterase and neuroligin in mammalian neuritogenesis. Proc Natl Acad Sci U S A 95: 13935-13940.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 13935-13940
    • Grifman, M.1    Galyam, N.2    Seidman, S.3    Soreq, H.4
  • 15
    • 0030985407 scopus 로고    scopus 로고
    • Neurite differentiation is modulated in neuroblastoma cells engineered for altered acetylcholinesterase expression
    • Koenigsberger C, Chiappa S, Brimijoin S, (1997) Neurite differentiation is modulated in neuroblastoma cells engineered for altered acetylcholinesterase expression. J Neurochem 69: 1389-1397.
    • (1997) J Neurochem , vol.69 , pp. 1389-1397
    • Koenigsberger, C.1    Chiappa, S.2    Brimijoin, S.3
  • 16
    • 0031903979 scopus 로고    scopus 로고
    • Acetylcholinesterase antibody treatment results in neurite detachment and reduced outgrowth from cultured neurons: further evidence for a cell adhesive role for neuronal acetylcholinesterase
    • Sharma KV, Bigbee JW, (1998) Acetylcholinesterase antibody treatment results in neurite detachment and reduced outgrowth from cultured neurons: further evidence for a cell adhesive role for neuronal acetylcholinesterase. J Neurosci Res 53: 454-464.
    • (1998) J Neurosci Res , vol.53 , pp. 454-464
    • Sharma, K.V.1    Bigbee, J.W.2
  • 17
    • 10844222503 scopus 로고    scopus 로고
    • 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, et al. (2004) Impaired formation of the inner retina in an AChE knockout mouse results in degeneration of all photoreceptors. Eur J Neurosci 20: 2953-2962.
    • (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
  • 18
    • 0030657499 scopus 로고    scopus 로고
    • Enhanced hemicholinium binding and attenuated dendrite branching in cognitively impaired acetylcholinesterase-transgenic mice
    • Beeri R, Le Novere N, Mervis R, Huberman T, Grauer E, et al. (1997) Enhanced hemicholinium binding and attenuated dendrite branching in cognitively impaired acetylcholinesterase-transgenic mice. J Neurochem 69: 2441-2451.
    • (1997) J Neurochem , vol.69 , pp. 2441-2451
    • Beeri, R.1    Le Novere, N.2    Mervis, R.3    Huberman, T.4    Grauer, E.5
  • 19
    • 0025187057 scopus 로고
    • Characterization and gene cloning of neurotactin, a Drosophila transmembrane protein related to cholinesterases
    • de la Escalera S, Bockamp EO, Moya F, Piovant M, Jimenez F, (1990) Characterization and gene cloning of neurotactin, a Drosophila transmembrane protein related to cholinesterases. EMBO J 9: 3593-3601.
    • (1990) EMBO J , vol.9 , pp. 3593-3601
    • de la Escalera, S.1    Bockamp, E.O.2    Moya, F.3    Piovant, M.4    Jimenez, F.5
  • 20
    • 0029055716 scopus 로고
    • Gliotactin, a novel transmembrane protein on peripheral glia, is required to form the blood-nerve barrier in Drosophila
    • Auld VJ, Fetter RD, Broadie K, Goodman CS, (1995) Gliotactin, a novel transmembrane protein on peripheral glia, is required to form the blood-nerve barrier in Drosophila. Cell 81: 757-767.
    • (1995) Cell , vol.81 , pp. 757-767
    • Auld, V.J.1    Fetter, R.D.2    Broadie, K.3    Goodman, C.S.4
  • 21
    • 0032080309 scopus 로고    scopus 로고
    • Stable complexes involving acetylcholinesterase and amyloid-beta peptide change the biochemical properties of the enzyme and increase the neurotoxicity of Alzheimer's fibrils
    • Alvarez A, Alarcon R, Opazo C, Campos EO, Munoz FJ, et al. (1998) Stable complexes involving acetylcholinesterase and amyloid-beta peptide change the biochemical properties of the enzyme and increase the neurotoxicity of Alzheimer's fibrils. J Neurosci 18: 3213-3223.
    • (1998) J Neurosci , vol.18 , pp. 3213-3223
    • Alvarez, A.1    Alarcon, R.2    Opazo, C.3    Campos, E.O.4    Munoz, F.J.5
  • 22
    • 0037422539 scopus 로고    scopus 로고
    • Interaction of "readthrough" acetylcholinesterase with RACK1 and PKCbeta II correlates with intensified fear-induced conflict behavior
    • Birikh KR, Sklan EH, Shoham S, Soreq H, (2003) Interaction of "readthrough" acetylcholinesterase with RACK1 and PKCbeta II correlates with intensified fear-induced conflict behavior. Proc Natl Acad Sci U S A 100: 283-288.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 283-288
    • Birikh, K.R.1    Sklan, E.H.2    Shoham, S.3    Soreq, H.4
  • 23
    • 4944253492 scopus 로고    scopus 로고
    • Mouse acetylcholinesterase interacts in yeast with the extracellular matrix component laminin-1beta
    • Paraoanu LE, Layer PG, (2004) Mouse acetylcholinesterase interacts in yeast with the extracellular matrix component laminin-1beta. FEBS Lett 576: 161-164.
    • (2004) FEBS Lett , vol.576 , pp. 161-164
    • Paraoanu, L.E.1    Layer, P.G.2
  • 25
    • 0025865325 scopus 로고
    • Laminin receptors in the retina: sequence analysis of the chick integrin alpha 6 subunit. Evidence for transcriptional and posttranslational regulation
    • de Curtis I, Quaranta V, Tamura RN, Reichardt LF, (1991) Laminin receptors in the retina: sequence analysis of the chick integrin alpha 6 subunit. Evidence for transcriptional and posttranslational regulation. J Cell Biol 113: 405-416.
    • (1991) J Cell Biol , vol.113 , pp. 405-416
    • de Curtis, I.1    Quaranta, V.2    Tamura, R.N.3    Reichardt, L.F.4
  • 26
    • 0026020097 scopus 로고
    • Extracellular matrix molecules and their receptors: functions in neural development
    • Reichardt LF, Tomaselli KJ, (1991) Extracellular matrix molecules and their receptors: functions in neural development. Annu Rev Neurosci 14: 531-570.
    • (1991) Annu Rev Neurosci , vol.14 , pp. 531-570
    • Reichardt, L.F.1    Tomaselli, K.J.2
  • 27
    • 0030957735 scopus 로고    scopus 로고
    • Neuronal laminins and their cellular receptors
    • Powell SK, Kleinman HK, (1997) Neuronal laminins and their cellular receptors. Int J Biochem Cell Biol 29: 401-414.
    • (1997) Int J Biochem Cell Biol , vol.29 , pp. 401-414
    • Powell, S.K.1    Kleinman, H.K.2
  • 29
    • 64149117286 scopus 로고    scopus 로고
    • Protein CutA undergoes an unusual transfer into the secretory pathway and affects the folding, oligomerization, and secretion of acetylcholinesterase
    • Liang D, Nunes-Tavares N, Xie HQ, Carvalho S, Bon S, et al. (2009) Protein CutA undergoes an unusual transfer into the secretory pathway and affects the folding, oligomerization, and secretion of acetylcholinesterase. J Biol Chem 284: 5195-5207.
    • (2009) J Biol Chem , vol.284 , pp. 5195-5207
    • Liang, D.1    Nunes-Tavares, N.2    Xie, H.Q.3    Carvalho, S.4    Bon, S.5
  • 30
    • 2642554616 scopus 로고    scopus 로고
    • Identification of a structural site on acetylcholinesterase that promotes neurite outgrowth and binds laminin-1 and collagen IV
    • Johnson G, Moore SW, (2004) Identification of a structural site on acetylcholinesterase that promotes neurite outgrowth and binds laminin-1 and collagen IV. Biochem Biophys Res Commun 319: 448-455.
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 448-455
    • Johnson, G.1    Moore, S.W.2
  • 31
    • 16644392579 scopus 로고    scopus 로고
    • Functional idiotypic mimicry of an adhesion- and differentiation-promoting site on acetylcholinesterase
    • Johnson G, Moore SW, (2004) Functional idiotypic mimicry of an adhesion- and differentiation-promoting site on acetylcholinesterase. J Cell Biochem 91: 999-1009.
    • (2004) J Cell Biochem , vol.91 , pp. 999-1009
    • Johnson, G.1    Moore, S.W.2
  • 32
    • 0033583819 scopus 로고    scopus 로고
    • The adhesion function on acetylcholinesterase is located at the peripheral anionic site
    • Johnson G, Moore SW, (1999) The adhesion function on acetylcholinesterase is located at the peripheral anionic site. Biochem Biophys Res Commun 258: 758-762.
    • (1999) Biochem Biophys Res Commun , vol.258 , pp. 758-762
    • Johnson, G.1    Moore, S.W.2
  • 34
    • 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
    • Johnson G, Moore SW, (2003) Human acetylcholinesterase binds to mouse laminin-1 and human collagen IV by an electrostatic mechanism at the peripheral anionic site. Neurosci Lett 337: 37-40.
    • (2003) Neurosci Lett , vol.337 , pp. 37-40
    • Johnson, G.1    Moore, S.W.2
  • 35
    • 0034046591 scopus 로고    scopus 로고
    • Localization of a novel adhesion-promoting site on acetylcholinesterase using catalytic antiacetylcholinesterase antibodies displaying cholinesterase-like activity
    • Discussion 145-153
    • Johnson G, Moore SW, (2000) Localization of a novel adhesion-promoting site on acetylcholinesterase using catalytic antiacetylcholinesterase antibodies displaying cholinesterase-like activity. Appl Biochem Biotechnol 83: 131-144; discussion 145-153.
    • (2000) Appl Biochem Biotechnol , vol.83 , pp. 131-144
    • Johnson, G.1    Moore, S.W.2
  • 36
    • 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
    • Inestrosa NC, Alvarez A, Perez CA, Moreno RD, Vicente M, et al. (1996) Acetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron 16: 881-891.
    • (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
  • 37
    • 0035807054 scopus 로고    scopus 로고
    • A structural motif of acetylcholinesterase that promotes amyloid beta-peptide fibril formation
    • De Ferrari GV, Canales MA, Shin I, Weiner LM, Silman I, et al. (2001) A structural motif of acetylcholinesterase that promotes amyloid beta-peptide fibril formation. Biochemistry 40: 10447-10457.
    • (2001) Biochemistry , vol.40 , pp. 10447-10457
    • de Ferrari, G.V.1    Canales, M.A.2    Shin, I.3    Weiner, L.M.4    Silman, I.5
  • 38
    • 76749102435 scopus 로고    scopus 로고
    • Acetylcholinesterase variants in Alzheimer's disease: from neuroprotection to programmed cell death
    • Greenberg DS, Toiber D, Berson A, Soreq H, (2010) Acetylcholinesterase variants in Alzheimer's disease: from neuroprotection to programmed cell death. Neurodegener Dis 7: 60-63.
    • (2010) Neurodegener Dis , vol.7 , pp. 60-63
    • Greenberg, D.S.1    Toiber, D.2    Berson, A.3    Soreq, H.4
  • 39
    • 84860511958 scopus 로고    scopus 로고
    • Molecular Assembly and Biosynthesis of Acetylcholinesterase in Brain and Muscle: the Roles of t-peptide, FHB Domain, and N-linked Glycosylation
    • Chen VP, Luk WK, Chan WK, Leung KW, Guo AJ, et al. (2011) Molecular Assembly and Biosynthesis of Acetylcholinesterase in Brain and Muscle: the Roles of t-peptide, FHB Domain, and N-linked Glycosylation. Front Mol Neurosci 4: 36.
    • (2011) Front Mol Neurosci , vol.4 , pp. 36
    • Chen, V.P.1    Luk, W.K.2    Chan, W.K.3    Leung, K.W.4    Guo, A.J.5
  • 40
    • 33646894444 scopus 로고    scopus 로고
    • ARP, the cleavable C-terminal peptide of "readthrough" acetylcholinesterase, promotes neuronal development and plasticity
    • Dori A, Soreq H, (2006) ARP, the cleavable C-terminal peptide of "readthrough" acetylcholinesterase, promotes neuronal development and plasticity. J Mol Neurosci 28: 247-255.
    • (2006) J Mol Neurosci , vol.28 , pp. 247-255
    • Dori, A.1    Soreq, H.2
  • 41
    • 0029867463 scopus 로고    scopus 로고
    • Establishment of an E1A-immortalized retinal cell culture
    • Seigel GM, (1996) Establishment of an E1A-immortalized retinal cell culture. In Vitro Cell Dev Biol Anim 32: 66-68.
    • (1996) In Vitro Cell Dev Biol Anim , vol.32 , pp. 66-68
    • Seigel, G.M.1
  • 42
    • 33646913370 scopus 로고    scopus 로고
    • A mutation linked with autism reveals a common mechanism of endoplasmic reticulum retention for the alpha,beta-hydrolase fold protein family
    • De Jaco A, Comoletti D, Kovarik Z, Gaietta G, Radic Z, et al. (2006) A mutation linked with autism reveals a common mechanism of endoplasmic reticulum retention for the alpha,beta-hydrolase fold protein family. J Biol Chem 281: 9667-9676.
    • (2006) J Biol Chem , vol.281 , pp. 9667-9676
    • de Jaco, A.1    Comoletti, D.2    Kovarik, Z.3    Gaietta, G.4    Radic, Z.5
  • 43
    • 0031842365 scopus 로고    scopus 로고
    • Influence of acetylcholinesterase on embryonic spinal rat motoneurones growth in culture: a quantitative morphometric study
    • Bataille S, Portalier P, Coulon P, Ternaux JP, (1998) Influence of acetylcholinesterase on embryonic spinal rat motoneurones growth in culture: a quantitative morphometric study. Eur J Neurosci 10: 560-572.
    • (1998) Eur J Neurosci , vol.10 , pp. 560-572
    • Bataille, S.1    Portalier, P.2    Coulon, P.3    Ternaux, J.P.4
  • 44
    • 0030045560 scopus 로고    scopus 로고
    • Overexpression of alternative human acetylcholinesterase forms modulates process extensions in cultured glioma cells
    • Karpel R, Sternfeld M, Ginzberg D, Guhl E, Graessmann A, et al. (1996) Overexpression of alternative human acetylcholinesterase forms modulates process extensions in cultured glioma cells. J Neurochem 66: 114-123.
    • (1996) J Neurochem , vol.66 , pp. 114-123
    • Karpel, R.1    Sternfeld, M.2    Ginzberg, D.3    Guhl, E.4    Graessmann, A.5
  • 45
    • 0037498151 scopus 로고    scopus 로고
    • Acetylcholinesterase promotes neurite elongation, synapse formation, and surface expression of AMPA receptors in hippocampal neurones
    • Olivera S, Rodriguez-Ithurralde D, Henley JM, (2003) Acetylcholinesterase promotes neurite elongation, synapse formation, and surface expression of AMPA receptors in hippocampal neurones. Mol Cell Neurosci 23: 96-106.
    • (2003) Mol Cell Neurosci , vol.23 , pp. 96-106
    • Olivera, S.1    Rodriguez-Ithurralde, D.2    Henley, J.M.3
  • 46
    • 1842855294 scopus 로고    scopus 로고
    • Neuronal gene expression and function in the growth-stimulated R28 retinal precursor cell line
    • Seigel GM, Sun W, Wang J, Hershberger DH, Campbell LM, et al. (2004) Neuronal gene expression and function in the growth-stimulated R28 retinal precursor cell line. Curr Eye Res 28: 257-269.
    • (2004) Curr Eye Res , vol.28 , pp. 257-269
    • Seigel, G.M.1    Sun, W.2    Wang, J.3    Hershberger, D.H.4    Campbell, L.M.5
  • 47
    • 77952928699 scopus 로고    scopus 로고
    • Integrin signaling switches the cytoskeletal and exocytic machinery that drives neuritogenesis
    • Gupton SL, Gertler FB, (2010) Integrin signaling switches the cytoskeletal and exocytic machinery that drives neuritogenesis. Dev Cell 18: 725-736.
    • (2010) Dev Cell , vol.18 , pp. 725-736
    • Gupton, S.L.1    Gertler, F.B.2
  • 48
    • 0031308121 scopus 로고    scopus 로고
    • A possible role for cholinergic neurons of the basal forebrain and pontomesencephalon in consciousness
    • Woolf NJ, (1997) A possible role for cholinergic neurons of the basal forebrain and pontomesencephalon in consciousness. Conscious Cogn 6: 574-596.
    • (1997) Conscious Cogn , vol.6 , pp. 574-596
    • Woolf, N.J.1
  • 49
    • 0021052719 scopus 로고
    • Connectin: cell surface protein that binds both laminin and actin
    • Brown SS, Malinoff HL, Wicha MS, (1983) Connectin: cell surface protein that binds both laminin and actin. Proc Natl Acad Sci U S A 80: 5927-5930.
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 5927-5930
    • Brown, S.S.1    Malinoff, H.L.2    Wicha, M.S.3
  • 51
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein
    • Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, et al. (1991) Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 253: 872-879.
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5
  • 52
    • 33749402097 scopus 로고    scopus 로고
    • Substrate and product trafficking through the active center gorge of acetylcholinesterase analyzed by crystallography and equilibrium binding
    • Bourne Y, Radic Z, Sulzenbacher G, Kim E, Taylor P, et al. (2006) Substrate and product trafficking through the active center gorge of acetylcholinesterase analyzed by crystallography and equilibrium binding. J Biol Chem 281: 29256-29267.
    • (2006) J Biol Chem , vol.281 , pp. 29256-29267
    • Bourne, Y.1    Radic, Z.2    Sulzenbacher, G.3    Kim, E.4    Taylor, P.5
  • 53
    • 0030276257 scopus 로고    scopus 로고
    • Acetylcholinesterase is a senile plaque component that promotes assembly of amyloid beta-peptide into Alzheimer's filaments
    • Inestrosa NC, Alvarez A, Calderon F, (1996) Acetylcholinesterase is a senile plaque component that promotes assembly of amyloid beta-peptide into Alzheimer's filaments. Mol Psychiatry 1: 359-361.
    • (1996) Mol Psychiatry , vol.1 , pp. 359-361
    • Inestrosa, N.C.1    Alvarez, A.2    Calderon, F.3
  • 54
    • 0013945471 scopus 로고
    • Responses of acetylcholinesterase from Torpedo marmorata to salts and curarizing drugs
    • Changeux JP, (1966) Responses of acetylcholinesterase from Torpedo marmorata to salts and curarizing drugs. Mol Pharmacol 2: 369-392.
    • (1966) Mol Pharmacol , vol.2 , pp. 369-392
    • Changeux, J.P.1
  • 55
    • 0026070409 scopus 로고
    • Substrate-binding sites in acetylcholinesterase
    • Hucho F, Jarv J, Weise C, (1991) Substrate-binding sites in acetylcholinesterase. Trends Pharmacol Sci 12: 422-426.
    • (1991) Trends Pharmacol Sci , vol.12 , pp. 422-426
    • Hucho, F.1    Jarv, J.2    Weise, C.3
  • 56
    • 0037198403 scopus 로고    scopus 로고
    • A non-cholinergic, trophic action of acetylcholinesterase on hippocampal neurones in vitro: molecular mechanisms
    • Day T, Greenfield SA, (2002) A non-cholinergic, trophic action of acetylcholinesterase on hippocampal neurones in vitro: molecular mechanisms. Neuroscience 111: 649-656.
    • (2002) Neuroscience , vol.111 , pp. 649-656
    • Day, T.1    Greenfield, S.A.2
  • 57
    • 84858113728 scopus 로고    scopus 로고
    • Cholinesterase-Targeting microRNAs Identified in silico Affect Specific Biological Processes
    • Hanin G, Soreq H, (2011) Cholinesterase-Targeting microRNAs Identified in silico Affect Specific Biological Processes. Front Mol Neurosci 4: 28.
    • (2011) Front Mol Neurosci , vol.4 , pp. 28
    • Hanin, G.1    Soreq, H.2
  • 58
    • 78650560147 scopus 로고    scopus 로고
    • microRNA-132 regulates dendritic growth and arborization of newborn neurons in the adult hippocampus
    • Magill ST, Cambronne XA, Luikart BW, Lioy DT, Leighton BH, et al. (2010) microRNA-132 regulates dendritic growth and arborization of newborn neurons in the adult hippocampus. Proc Natl Acad Sci U S A 107: 20382-20387.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 20382-20387
    • Magill, S.T.1    Cambronne, X.A.2    Luikart, B.W.3    Lioy, D.T.4    Leighton, B.H.5
  • 59
    • 49549113138 scopus 로고    scopus 로고
    • Integrin-laminin interactions controlling neurite outgrowth from adult DRG neurons in vitro
    • Plantman S, Patarroyo M, Fried K, Domogatskaya A, Tryggvason K, et al. (2008) Integrin-laminin interactions controlling neurite outgrowth from adult DRG neurons in vitro. Mol Cell Neurosci 39: 50-62.
    • (2008) Mol Cell Neurosci , vol.39 , pp. 50-62
    • Plantman, S.1    Patarroyo, M.2    Fried, K.3    Domogatskaya, A.4    Tryggvason, K.5
  • 60
    • 52449122884 scopus 로고    scopus 로고
    • Non-enzymatic developmental functions of acetylcholinesterase-the question of redundancy
    • Johnson G, Swart C, Moore SW, (2008) Non-enzymatic developmental functions of acetylcholinesterase-the question of redundancy. FEBS J 275: 5129-5138.
    • (2008) FEBS J , vol.275 , pp. 5129-5138
    • Johnson, G.1    Swart, C.2    Moore, S.W.3
  • 61
    • 42449164646 scopus 로고    scopus 로고
    • Interaction of acetylcholinesterase with the G4 domain of the laminin alpha1-chain
    • Johnson G, Swart C, Moore SW, (2008) Interaction of acetylcholinesterase with the G4 domain of the laminin alpha1-chain. Biochem J 411: 507-514.
    • (2008) Biochem J , vol.411 , pp. 507-514
    • Johnson, G.1    Swart, C.2    Moore, S.W.3
  • 62
    • 12144286984 scopus 로고    scopus 로고
    • Molecular dissection of the alpha-dystroglycan- and integrin-binding sites within the globular domain of human laminin-10
    • Ido H, Harada K, Futaki S, Hayashi Y, Nishiuchi R, et al. (2004) Molecular dissection of the alpha-dystroglycan- and integrin-binding sites within the globular domain of human laminin-10. J Biol Chem 279: 10946-10954.
    • (2004) J Biol Chem , vol.279 , pp. 10946-10954
    • Ido, H.1    Harada, K.2    Futaki, S.3    Hayashi, Y.4    Nishiuchi, R.5
  • 63
    • 57649121587 scopus 로고    scopus 로고
    • Laminin isoforms containing the gamma3 chain are unable to bind to integrins due to the absence of the glutamic acid residue conserved in the C-terminal regions of the gamma1 and gamma2 chains
    • Ido H, Ito S, Taniguchi Y, Hayashi M, Sato-Nishiuchi R, et al. (2008) Laminin isoforms containing the gamma3 chain are unable to bind to integrins due to the absence of the glutamic acid residue conserved in the C-terminal regions of the gamma1 and gamma2 chains. J Biol Chem 283: 28149-28157.
    • (2008) J Biol Chem , vol.283 , pp. 28149-28157
    • Ido, H.1    Ito, S.2    Taniguchi, Y.3    Hayashi, M.4    Sato-Nishiuchi, R.5
  • 64
    • 0037122918 scopus 로고    scopus 로고
    • PRiMA: the membrane anchor of acetylcholinesterase in the brain
    • Perrier AL, Massoulie J, Krejci E, (2002) PRiMA: the membrane anchor of acetylcholinesterase in the brain. Neuron 33: 275-285.
    • (2002) Neuron , vol.33 , pp. 275-285
    • Perrier, A.L.1    Massoulie, J.2    Krejci, E.3
  • 66
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, (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
  • 67
    • 78651153462 scopus 로고
    • A "Direct-Coloring" Thiocholine Method for Cholinesterases
    • Karnovsky MJ, Roots L, (1964) A "Direct-Coloring" Thiocholine Method for Cholinesterases. J Histochem Cytochem 12: 219-221.
    • (1964) J Histochem Cytochem , vol.12 , pp. 219-221
    • Karnovsky, M.J.1    Roots, L.2


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