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Volumn 144, Issue 6, 1999, Pages 1349-1360

Genetic analysis of collagen Q: Roles in acetylcholinesterase and butyrylcholinesterase assembly and in synaptic structure and function

Author keywords

Acetylcholine; Acetylcholinesterase; Butyrylcholinesterase; Collagen; Neuromuscul ar junction

Indexed keywords

ACETYLCHOLINESTERASE; CHOLINESTERASE; COLLAGEN; COLLAGEN Q; UNCLASSIFIED DRUG;

EID: 0033594106     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.144.6.1349     Document Type: Article
Times cited : (154)

References (66)
  • 1
    • 0030873431 scopus 로고    scopus 로고
    • Acetylcholinesterase-transgenic mice display embryonic modulations in spinal cord choline acelyltransferase and neurexin I beta gene expression followed by late-onset neuromotor deterioration
    • Andres, C., R. Beeri, A. Friedman, E. Lev-Lehman, S. Henis, R. Timberg, M. Shani, and H. Soreq. 1997. Acetylcholinesterase-transgenic mice display embryonic modulations in spinal cord choline acelyltransferase and neurexin I beta gene expression followed by late-onset neuromotor deterioration. Proc. Natl. Acad. Sci. USA. 94:8173-8178.
    • (1997) Proc. Natl. Acad. Sci. USA , 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
  • 2
    • 0028346522 scopus 로고
    • Globular and asymmetric acetylcholinesterase in the synaptic basal lamina of skeletal muscle
    • Anglister, L., B. Haesaert, and U.J. McMahan. 1994. Globular and asymmetric acetylcholinesterase in the synaptic basal lamina of skeletal muscle. J. Cell Biol. 125:183-196.
    • (1994) J. Cell Biol. , vol.125 , pp. 183-196
    • Anglister, L.1    Haesaert, B.2    McMahan, U.J.3
  • 3
    • 0001537321 scopus 로고
    • Two selective inhibitors of cholinesterase
    • Austin, L., and W.K. Berry. 1953. Two selective inhibitors of cholinesterase. Biochem. J. 54:695-700.
    • (1953) Biochem. J. , vol.54 , pp. 695-700
    • Austin, L.1    Berry, W.K.2
  • 4
    • 0031017538 scopus 로고    scopus 로고
    • Quaternary association of acetylcholinesterase. I. Oligomeric associations of T subunits with and without the amino-terminal domain of the collagen tail
    • Bon, S., and J. Massoulié. 1997. Quaternary association of acetylcholinesterase. I. Oligomeric associations of T subunits with and without the amino-terminal domain of the collagen tail. J. Biol. Chem. 272:3007-3015.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3007-3015
    • Bon, S.1    Massoulié, J.2
  • 5
    • 0031016694 scopus 로고    scopus 로고
    • Quaternary associations of acetylcholinesterase. II. The polyproline attachment domain of the collagen tail
    • Bon, S., F. Coussen, and J. Massoulié. 1997. Quaternary associations of acetylcholinesterase. II. The polyproline attachment domain of the collagen tail. J. Biol. Chem. 272:3016-3021.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3016-3021
    • Bon, S.1    Coussen, F.2    Massoulié, J.3
  • 6
    • 0022240874 scopus 로고
    • Anchorage of collagen-tailed acetylcholinesterase to the extracellular matrix is mediated by heparan sulfate proteoglycans
    • Brandan, E., M. Maldonado, J. Garrido, and N.C. Inestrosa. 1985. Anchorage of collagen-tailed acetylcholinesterase to the extracellular matrix is mediated by heparan sulfate proteoglycans. J. Cell Biol. 101:985-992.
    • (1985) J. Cell Biol. , vol.101 , pp. 985-992
    • Brandan, E.1    Maldonado, M.2    Garrido, J.3    Inestrosa, N.C.4
  • 7
    • 0018344840 scopus 로고
    • Distribution of acetylcholinesterase molecular forms in neural and non-neural sections of human muscle
    • Carson, S., S. Bon, M. Vigny, J. Massoulie, and M. Fardeau. 1979. Distribution of acetylcholinesterase molecular forms in neural and non-neural sections of human muscle. FEBS Lett. 97:348-352.
    • (1979) FEBS Lett. , vol.97 , pp. 348-352
    • Carson, S.1    Bon, S.2    Vigny, M.3    Massoulie, J.4    Fardeau, M.5
  • 8
    • 0031040595 scopus 로고    scopus 로고
    • Schwann cells modify expression of acetylcholinesterase and butyrylcholinesterase at rat neuromuscular junctions
    • Chapron, J., S. De La Porte, L. Delepine, and J. Koenig. 1997. Schwann cells modify expression of acetylcholinesterase and butyrylcholinesterase at rat neuromuscular junctions. Eur. J. Neurosci. 9:260-270.
    • (1997) Eur. J. Neurosci. , vol.9 , pp. 260-270
    • Chapron, J.1    De La Porte, S.2    Delepine, L.3    Koenig, J.4
  • 9
    • 0024352019 scopus 로고
    • Comparison of butyrylcholinesterase and acetylcholinesterase
    • Chatonnet, A., and O. Lockridge. 1989. Comparison of butyrylcholinesterase and acetylcholinesterase. Biochem. J. 260:625-634.
    • (1989) Biochem. J. , vol.260 , pp. 625-634
    • Chatonnet, A.1    Lockridge, O.2
  • 10
    • 0028990147 scopus 로고
    • Two heparin-binding domains are present on the collagenic tail of asymmetric acetylcholinesterase
    • Deprez, P.N., and N.C. Inestrosa. 1995. Two heparin-binding domains are present on the collagenic tail of asymmetric acetylcholinesterase. J. Biol. Chem. 270:11043-11046.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11043-11046
    • Deprez, P.N.1    Inestrosa, N.C.2
  • 11
    • 0032231665 scopus 로고    scopus 로고
    • Mutation in the human acetylcholinesterase-associated collagen gene, COLQ, is responsible for congenital myasthenic syndrome with endplate acetylcholinesterase deficiency (type Ic)
    • Donger, C., E. Krejci, A.P. Serradell, B. Eymard, S. Bon, S. Nicole, D. Chateau, F. Gary, M. Fardeau, J. Massoulié, and P. Guicheney. 1998. Mutation in the human acetylcholinesterase-associated collagen gene, COLQ, is responsible for congenital myasthenic syndrome with endplate acetylcholinesterase deficiency (type Ic). Am. J. Hum. Genet. 63:967-975.
    • (1998) Am. J. Hum. Genet. , vol.63 , pp. 967-975
    • Donger, C.1    Krejci, E.2    Serradell, A.P.3    Eymard, B.4    Bon, S.5    Nicole, S.6    Chateau, D.7    Gary, F.8    Fardeau, M.9    Massoulié, J.10    Guicheney, P.11
  • 12
    • 0016366697 scopus 로고
    • Changes in motor endplates resulting from muscle fibre necrosis and regeneration. A light and electron microscopic study of the effects of the depolarizing fraction (cardiotoxin) of Dendroaspis jamesoni venom
    • Duchen, L.W., B.J. Excell, R. Patel, and B. Smith. 1974. Changes in motor endplates resulting from muscle fibre necrosis and regeneration. A light and electron microscopic study of the effects of the depolarizing fraction (cardiotoxin) of Dendroaspis jamesoni venom. J. Neurol. Sci. 21:391-417.
    • (1974) J. Neurol. Sci. , vol.21 , pp. 391-417
    • Duchen, L.W.1    Excell, B.J.2    Patel, R.3    Smith, B.4
  • 13
    • 0026639596 scopus 로고
    • H and T subunits of acetylcholinesterase from Torpedo, expressed in COS cells, generate all types of globular forms
    • Duval, N., J. Massoulié, and S. Bon. 1992. H and T subunits of acetylcholinesterase from Torpedo, expressed in COS cells, generate all types of globular forms. J. Cell Biol. 118:641-653.
    • (1992) J. Cell Biol. , vol.118 , pp. 641-653
    • Duval, N.1    Massoulié, J.2    Bon, S.3
  • 15
    • 0001173816 scopus 로고
    • Acquired autoimmune myasthenia gravis
    • A.G. Engel and C. Franzini-Armstrong, editors. McGraw Hill, New York
    • Engel, A.C. 1994a. Acquired autoimmune myasthenia gravis. In Myology. A.G. Engel and C. Franzini-Armstrong, editors. McGraw Hill, New York. 1769-1798.
    • (1994) Myology , pp. 1769-1798
    • Engel, A.C.1
  • 16
    • 0001509765 scopus 로고
    • Myasthenic syndromes
    • A.G. Engel and C. Franzini-Armstrong, editors. McGraw Hill, New York
    • Engel, A.G. 1994b. Myasthenic syndromes. In Myology. A.G. Engel and C. Franzini-Armstrong, editors. McGraw Hill, New York. 1798-1835.
    • (1994) Myology , pp. 1798-1835
    • Engel, A.G.1
  • 17
    • 0017474455 scopus 로고
    • A new myasthenic syndrome with endplate acetylcholinesterase deficiency, small nerve terminals, and reduced acetylcholine release
    • Engel, A.G., E.H. Lambert, and M.R. Gomez, 1977. A new myasthenic syndrome with endplate acetylcholinesterase deficiency, small nerve terminals, and reduced acetylcholine release. Ann. Neurol. 1:315-330.
    • (1977) Ann. Neurol. , vol.1 , pp. 315-330
    • Engel, A.G.1    Lambert, E.H.2    Gomez, M.R.3
  • 18
    • 0015890033 scopus 로고
    • Multiple forms of acetylcholinesterase and their distribution in endplate and non-endplate regions of rat diaphragm muscle
    • Hall, Z.W. 1973. Multiple forms of acetylcholinesterase and their distribution in endplate and non-endplate regions of rat diaphragm muscle. J. Neurobiol. 4:343-361.
    • (1973) J. Neurobiol. , vol.4 , pp. 343-361
    • Hall, Z.W.1
  • 19
    • 0015223161 scopus 로고
    • Enzymatic detachment of endplate acetylcholinesterase from muscle
    • Hall, Z.W., and R.B. Kelly. 1971. Enzymatic detachment of endplate acetylcholinesterase from muscle. Nat. New Biol. 232:62-63.
    • (1971) Nat. New Biol. , vol.232 , pp. 62-63
    • Hall, Z.W.1    Kelly, R.B.2
  • 20
    • 0016614506 scopus 로고
    • Ultrastructure of motor endplates during pharmacologically-induced degeneration and subsequent regeneration of skeletal muscle
    • Jirmanová, I. 1975. Ultrastructure of motor endplates during pharmacologically-induced degeneration and subsequent regeneration of skeletal muscle. J. Neurocytol. 4:141-155.
    • (1975) J. Neurocytol. , vol.4 , pp. 141-155
    • Jirmanová, I.1
  • 21
    • 78651153462 scopus 로고
    • A "direct-coloring" thiocholine method for cholinesterases
    • Karnovsky, M.J., and L. Roots. 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
  • 22
    • 0025735608 scopus 로고
    • Primary structure of a collagenic tail peptide of Torpedo acetylcholinesterase: Co-expression with catalytic subunit induces the production of collagen-tailed forms in transfected cells
    • Krejci, E., F. Coussen, N. Duval, J.M. Chatel, C. Legay, M. Puype, J. Vandekerckhove, J. Cartaud, S. Bon, and J. Massoulié. 1991. Primary structure of a collagenic tail peptide of Torpedo acetylcholinesterase: co-expression with catalytic subunit induces the production of collagen-tailed forms in transfected cells. EMBO (Eur. Mol. Biol. Organ.) J. 10:1285-1293.
    • (1991) EMBO (Eur. Mol. Biol. Organ.) J. , vol.10 , pp. 1285-1293
    • Krejci, E.1    Coussen, F.2    Duval, N.3    Chatel, J.M.4    Legay, C.5    Puype, M.6    Vandekerckhove, J.7    Cartaud, J.8    Bon, S.9    Massoulié, J.10
  • 24
    • 13144251123 scopus 로고    scopus 로고
    • Synaptic plasticity: Keeping synapses under control
    • Landmesser, L.T. 1998. Synaptic plasticity: keeping synapses under control. Curr. Biol. 8:R564-R567.
    • (1998) Curr. Biol. , vol.8
    • Landmesser, L.T.1
  • 25
    • 0017652935 scopus 로고
    • Initial ultrastructural abnormalities at the motor endplate produced by a cholinesterase inhibitor
    • Laskowski, M.B., W.H. Olson, and W.D. Dettharn. 1977. Initial ultrastructural abnormalities at the motor endplate produced by a cholinesterase inhibitor. Exp. Neurol. 57:13-33.
    • (1977) Exp. Neurol. , vol.57 , pp. 13-33
    • Laskowski, M.B.1    Olson, W.H.2    Dettharn, W.D.3
  • 26
    • 0029163984 scopus 로고
    • Novel functions of cholinesterases in development, physiology and disease
    • Layer, P.G., and E. Willbold. 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
  • 27
    • 0018731409 scopus 로고
    • Agonist-induced myopathy at the neuromuscular junction is mediated by calcium
    • Leonard, J.P., and M.M. Salpeter. 1979 Agonist-induced myopathy at the neuromuscular junction is mediated by calcium. J. Cell Biol. 82:811-819.
    • (1979) J. Cell Biol. , vol.82 , pp. 811-819
    • Leonard, J.P.1    Salpeter, M.M.2
  • 28
    • 0017274362 scopus 로고
    • Molecular forms of acetylcholinesterase from Torpedo californica: Their relationship to synaptic membranes
    • Lwebuga-Mukasa, J.S., S. Lappi, and P. Taylor. 1976. Molecular forms of acetylcholinesterase from Torpedo californica: their relationship to synaptic membranes. Biochemistry. 15:1425-1434.
    • (1976) Biochemistry , vol.15 , pp. 1425-1434
    • Lwebuga-Mukasa, J.S.1    Lappi, S.2    Taylor, P.3
  • 29
    • 0028935085 scopus 로고
    • Role for a synapse-specific carbohydrate in agrin-induced clustering of acetylcholine receptors
    • Martin, P.T., and J.R. Sanes. 1995. Role for a synapse-specific carbohydrate in agrin-induced clustering of acetylcholine receptors. Neuron. 14:743-754.
    • (1995) Neuron. , vol.14 , pp. 743-754
    • Martin, P.T.1    Sanes, J.R.2
  • 30
    • 0020021171 scopus 로고
    • The molecular forms of cholinesterase and acetylcholinesterase in vertebrates
    • Massoulié, J., and S. Bon. 1982. The molecular forms of cholinesterase and acetylcholinesterase in vertebrates. Ann. Rev. Neurosci. 5:57-106.
    • (1982) Ann. Rev. Neurosci. , vol.5 , pp. 57-106
    • Massoulié, J.1    Bon, S.2
  • 32
    • 0032105344 scopus 로고    scopus 로고
    • Acetylcholinesterase: C-terminal domains, molecular forms and functional localization
    • Massoulié, J., A. Anselmet, S. Bon, E. Krejci, C. Legay, N. Morel, and S. Simon. 1998. Acetylcholinesterase: C-terminal domains, molecular forms and functional localization. J. Physiol. 92:183-190.
    • (1998) J. Physiol. , vol.92 , pp. 183-190
    • Massoulié, J.1    Anselmet, A.2    Bon, S.3    Krejci, E.4    Legay, C.5    Morel, N.6    Simon, S.7
  • 33
    • 0017928049 scopus 로고
    • Cholinesterase is associated with the basal lamina at the neuromuscular junction
    • McMahan, U.J., J.R. Sanes, and L.M. Marshall. 1978. Cholinesterase is associated with the basal lamina at the neuromuscular junction. Nature. 271:172-174.
    • (1978) Nature , vol.271 , pp. 172-174
    • McMahan, U.J.1    Sanes, J.R.2    Marshall, L.M.3
  • 34
    • 0028171098 scopus 로고
    • Collagen IV α3, α4, and α5 chains in rodent basal laminae: Sequence, distribution, association with laminins, and developmental switches
    • Miner, J.H., and J.R. Sanes. 1994. Collagen IV α3, α4, and α5 chains in rodent basal laminae: sequence, distribution, association with laminins, and developmental switches. J. Cell Biol. 127:879-891.
    • (1994) J. Cell Biol. , vol.127 , pp. 879-891
    • Miner, J.H.1    Sanes, J.R.2
  • 35
    • 0030457613 scopus 로고    scopus 로고
    • Molecular and functional defects in kidneys of mice lacking collagen α3(IV): Implications for Alport syndrome
    • Miner, J.H., and J.R. Sanes. 1996. Molecular and functional defects in kidneys of mice lacking collagen α3(IV): implications for Alport syndrome. J. Cell Biol. 135:1403-1413.
    • (1996) J. Cell Biol. , vol.135 , pp. 1403-1413
    • Miner, J.H.1    Sanes, J.R.2
  • 36
    • 0027321548 scopus 로고
    • Derivation of completely cell culture-derived mice from early-passage embryonic stem cells
    • Nagy, A., J. Rossant, R. Nagy, W. Abramow-Newerly, and J.C. Roder. 1993. Derivation of completely cell culture-derived mice from early-passage embryonic stem cells. Proc. Natl. Acad. Sci. USA. 90:8424-8428.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8424-8428
    • Nagy, A.1    Rossant, J.2    Nagy, R.3    Abramow-Newerly, W.4    Roder, J.C.5
  • 37
    • 0028908326 scopus 로고
    • Aberrant differentiation of neuromuscular junctions in mice lacking s-laminin/laminin β2
    • Noakes, P.G., M. Gautam, J. Mudd, J.R. Sanes, and J.P. Merlie. 1995. Aberrant differentiation of neuromuscular junctions in mice lacking s-laminin/laminin β2. Nature. 374:258-262.
    • (1995) Nature , vol.374 , pp. 258-262
    • Noakes, P.G.1    Gautam, M.2    Mudd, J.3    Sanes, J.R.4    Merlie, J.P.5
  • 38
    • 0032483003 scopus 로고    scopus 로고
    • Human endplate acetylcholinesterase deficiency caused by mutations in the collagen-like tail subunit (COLO) of the asymmetric enzyme
    • Ohno, K., J. Brengman, A. Tsujino, and A.G. Engel. 1998. Human endplate acetylcholinesterase deficiency caused by mutations in the collagen-like tail subunit (COLO) of the asymmetric enzyme. Proc. Natl Acad. Sci. USA. 95: 9654-9659.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 9654-9659
    • Ohno, K.1    Brengman, J.2    Tsujino, A.3    Engel, A.G.4
  • 39
    • 0032543577 scopus 로고    scopus 로고
    • Synaptic laminin prevents glial entry into the synaptic cleft
    • Patton, B.L., A.Y. Chiu, and J.R. Sanes. 1998. Synaptic laminin prevents glial entry into the synaptic cleft. Nature. 393:698-701.
    • (1998) Nature , vol.393 , pp. 698-701
    • Patton, B.L.1    Chiu, A.Y.2    Sanes, J.R.3
  • 40
    • 0026317642 scopus 로고
    • Mutagenesis of the 43-kD postsynaplic protein defines domains involved in plasma membrane targeting and AChR clustering
    • Phillips, W.D., M.M. Maimone, and J.P. Merlie. 1991. Mutagenesis of the 43-kD postsynaplic protein defines domains involved in plasma membrane targeting and AChR clustering. J. Cell Biol. 115:1713-1723.
    • (1991) J. Cell Biol. , vol.115 , pp. 1713-1723
    • Phillips, W.D.1    Maimone, M.M.2    Merlie, J.P.3
  • 41
    • 0029907384 scopus 로고    scopus 로고
    • Extracellular and asymmetric forms of acetylcholinesterase are expressed on cholinergic and noncholinergic terminal neuropil of the developing chick retina
    • Reiss, Y., S. Kroger, J. Grassi, K.W.K. Tsim, E. Willbold, and P.G. Layer. 1996. Extracellular and asymmetric forms of acetylcholinesterase are expressed on cholinergic and noncholinergic terminal neuropil of the developing chick retina. Cell Tissue Res. 286:13-22.
    • (1996) Cell Tissue Res. , vol.286 , pp. 13-22
    • Reiss, Y.1    Kroger, S.2    Grassi, J.3    Tsim, K.W.K.4    Willbold, E.5    Layer, P.G.6
  • 42
    • 0020956527 scopus 로고
    • Fasciculin, a powerful anticholinesterase polypeptide from Dendroaspis angusticeps venom
    • Rodriguez-Ithurralde, D., R. Silveira, L. Barbieto, and F. Dajas. 1983. Fasciculin, a powerful anticholinesterase polypeptide from Dendroaspis angusticeps venom. Neurochem. Int. 5:267-274.
    • (1983) Neurochem. Int. , vol.5 , pp. 267-274
    • Rodriguez-Ithurralde, D.1    Silveira, R.2    Barbieto, L.3    Dajas, F.4
  • 43
    • 0017387580 scopus 로고
    • Structure of 18S and 14S acetylcholinesterase. Identification of collagen-like subunits that are linked by disulfide bonds to catalytic subunits
    • Rosenberry, T.L., and J.M. Richardson. 1977. Structure of 18S and 14S acetylcholinesterase. Identification of collagen-like subunits that are linked by disulfide bonds to catalytic subunits. Biochemistry. 16:3550-3558.
    • (1977) Biochemistry , vol.16 , pp. 3550-3558
    • Rosenberry, T.L.1    Richardson, J.M.2
  • 44
    • 0027181202 scopus 로고
    • Localization of "non-exlractable" acetylcholinesterase to the vertebrate neuromuscular junction
    • Rossi, S.G., and R.L. Rotundo. 1993. Localization of "non-exlractable" acetylcholinesterase to the vertebrate neuromuscular junction. J. Biol. Chem. 268: 19152-19159.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19152-19159
    • Rossi, S.G.1    Rotundo, R.L.2
  • 45
    • 0030027551 scopus 로고    scopus 로고
    • Transient interactions between collagen-tailed acetylcholinesterase and sulfated proteoglycans prior to immobilization on the extracellular matrix
    • Rossi, S.G., and R.L. Rotundo. 1996. Transient interactions between collagen-tailed acetylcholinesterase and sulfated proteoglycans prior to immobilization on the extracellular matrix. J. Biol. Chem. 271:1979-1987.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1979-1987
    • Rossi, S.G.1    Rotundo, R.L.2
  • 46
    • 0031047803 scopus 로고    scopus 로고
    • Transplantation of quail collagen-tailed acetylcholinesterase molecules onto the frog neuromuscular synapse
    • Rotundo, R.L., S.G. Rossi, and L. Anglister. 1997. Transplantation of quail collagen-tailed acetylcholinesterase molecules onto the frog neuromuscular synapse. J. Cell Biol. 136:367-374.
    • (1997) J. Cell Biol. , vol.136 , pp. 367-374
    • Rotundo, R.L.1    Rossi, S.G.2    Anglister, L.3
  • 47
    • 0018577243 scopus 로고
    • Antibodies that hind specifically to synaptic sites on muscle fiber basal lamina
    • Sanes, J.R., and Z.W. Hall. 1979. Antibodies that hind specifically to synaptic sites on muscle fiber basal lamina. J. Cell Biol. 83:357-370.
    • (1979) J. Cell Biol. , vol.83 , pp. 357-370
    • Sanes, J.R.1    Hall, Z.W.2
  • 48
    • 0032936983 scopus 로고    scopus 로고
    • Development of the vertebrate neuromuscular junction
    • Sanes, J.R., and J.W. Lichtman. 1999. Development of the vertebrate neuromuscular junction. Ann. Rev. Neurosci. 22:389-442.
    • (1999) Ann. Rev. Neurosci. , vol.22 , pp. 389-442
    • Sanes, J.R.1    Lichtman, J.W.2
  • 49
    • 0023836803 scopus 로고
    • A synapse-specific carbohydrate at the neuromuscular junction: Association with both acetylcholinesterase and a glycolipid
    • Scott, L.J., F. Bacou, and J.R. Sanes. 1988. A synapse-specific carbohydrate at the neuromuscular junction: association with both acetylcholinesterase and a glycolipid. J. Neurosci. 8:932-944.
    • (1988) J. Neurosci. , vol.8 , pp. 932-944
    • Scott, L.J.1    Bacou, F.2    Sanes, J.R.3
  • 51
    • 0032476586 scopus 로고    scopus 로고
    • A four-to-one association between peptide motifs: Four C-terminal domains from cholinesterase assemble with one proline-rich attachment domain (PRAD) in the secretory pathway
    • Simon, S., E. Krejci, and J. Massoulié. 1998. A four-to-one association between peptide motifs: four C-terminal domains from cholinesterase assemble with one proline-rich attachment domain (PRAD) in the secretory pathway. EMBO (Eur. Mol. Biol. Organ.) J. 17:6178-6187.
    • (1998) EMBO (Eur. Mol. Biol. Organ.) J. , vol.17 , pp. 6178-6187
    • Simon, S.1    Krejci, E.2    Massoulié, J.3
  • 52
    • 0021876241 scopus 로고
    • Asymmetric molecular forms of acetylcholinesterase in mammalian skeletal muscles
    • Sketelj, J., and M. Brzin. 1985. Asymmetric molecular forms of acetylcholinesterase in mammalian skeletal muscles. J. Neurosci. Res. 14:95-103.
    • (1985) J. Neurosci. Res. , vol.14 , pp. 95-103
    • Sketelj, J.1    Brzin, M.2
  • 53
    • 0028819272 scopus 로고
    • Cholinergic regulation of neunte outgrowth from isolated chick sympathetic neurons in culture
    • Small, D.H., G. Reed, B. Whitefield, and V. Nurcombe. 1995. Cholinergic regulation of neunte outgrowth from isolated chick sympathetic neurons in culture. J. Neurosci. 15:144-151.
    • (1995) J. Neurosci. , vol.15 , pp. 144-151
    • Small, D.H.1    Reed, G.2    Whitefield, B.3    Nurcombe, V.4
  • 54
    • 0019855776 scopus 로고
    • Developmental changes in acetylcholine receptor aggregates at rat skeletal neuromuscular junctions
    • Steinbach, J.H. 1981. Developmental changes in acetylcholine receptor aggregates at rat skeletal neuromuscular junctions. Dev. Biol. 84:267-276.
    • (1981) Dev. Biol. , vol.84 , pp. 267-276
    • Steinbach, J.H.1
  • 55
    • 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., G. Ming, H. Song, K. Sela, R. Timberg, M. Poo, and H. Soreq. 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    Poo, M.6    Soreq, H.7
  • 56
    • 0013594560 scopus 로고
    • Cholinesterases: Tissue and cellular distribution of molecular forms and their physiological regulation
    • V.P. Whittaker, editor. Springer-Verlag
    • Toutant, J.P., and J. Massoulié. 1988. Cholinesterases: tissue and cellular distribution of molecular forms and their physiological regulation. In Handbook of Experimental Pharmacology. Volume 86. V.P. Whittaker, editor. Springer-Verlag. 225-265.
    • (1988) Handbook of Experimental Pharmacology , vol.86 , pp. 225-265
    • Toutant, J.P.1    Massoulié, J.2
  • 57
    • 0022004427 scopus 로고
    • Polymorphism of pseudocholinesterase in Torpedo marmorata tissues: Comparative study of the catalytic and molecular properties of this enzyme with acetylcholinesterase
    • Toutant, J.P., J. Massoulié, and S. Bon. 1985. Polymorphism of pseudocholinesterase in Torpedo marmorata tissues: comparative study of the catalytic and molecular properties of this enzyme with acetylcholinesterase. J. Neurochem. 44:580-592.
    • (1985) J. Neurochem. , vol.44 , pp. 580-592
    • Toutant, J.P.1    Massoulié, J.2    Bon, S.3
  • 58
    • 0023857207 scopus 로고
    • An asymmetric form of muscle acetylcholinesterase contains three subunit types and two enzymic activities in one molecule
    • Tsim, K.W.K., W.R. Randall, and E.A. Barnard. 1988a. An asymmetric form of muscle acetylcholinesterase contains three subunit types and two enzymic activities in one molecule. Proc. Natl. Acad. Sci. USA. 85:1262-1266.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1262-1266
    • Tsim, K.W.K.1    Randall, W.R.2    Barnard, E.A.3
  • 59
    • 0024066711 scopus 로고
    • Synaptic acetylcholinesterase of chicken muscle changes during development from a hybrid to a homogeneous enzyme
    • Tsim, K.W., W.R. Randall, and E.A. Barnard. 1988b. Synaptic acetylcholinesterase of chicken muscle changes during development from a hybrid to a homogeneous enzyme. EMBO (Eur. Mol. Biol. Organ.) J. 7:2451-2456.
    • (1988) EMBO (Eur. Mol. Biol. Organ.) J. , vol.7 , pp. 2451-2456
    • Tsim, K.W.1    Randall, W.R.2    Barnard, E.A.3
  • 60
    • 0025780879 scopus 로고
    • Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene
    • Tybulewicz, V.L., C.E. Crawford, P.K. Jackson, R.T. Bronson, and R.C. Multigan. 1991. Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene. Cell. 65:1153-1163.
    • (1991) Cell , vol.65 , pp. 1153-1163
    • Tybulewicz, V.L.1    Crawford, C.E.2    Jackson, P.K.3    Bronson, R.T.4    Multigan, R.C.5
  • 61
    • 0342333428 scopus 로고
    • "Nonspecific" cholinesterase and acetylcholinesterase in rat tissues: Molecular forms, structural and catalytic properties, and significance of the two enzyme systems
    • Vigny, M., V. Gisiger, and J. Massoulié. 1978. "Nonspecific" cholinesterase and acetylcholinesterase in rat tissues: molecular forms, structural and catalytic properties, and significance of the two enzyme systems. Proc. Natl. Acad. Sci. USA. 75:2588-2592.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 2588-2592
    • Vigny, M.1    Gisiger, V.2    Massoulié, J.3
  • 62
    • 0020576660 scopus 로고
    • Interactions of asymmetric forms of acetylcholinesterase with basement membrane components
    • Vigny, M., G.R. Martin, and G.R. Grotendorst. 1983. Interactions of asymmetric forms of acetylcholinesterase with basement membrane components. J. Biol. Chem. 258:8794-8798.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8794-8798
    • Vigny, M.1    Martin, G.R.2    Grotendorst, G.R.3
  • 63
    • 0022658404 scopus 로고
    • Evidence of necrosis in human intercostal muscle following inhalation of an organophosphate insecticide
    • Wecker, L., R.E. Mrak, and W.D. Dettbarn. 1986. Evidence of necrosis in human intercostal muscle following inhalation of an organophosphate insecticide. Fund. Appl. Toxicol. 6:172-174.
    • (1986) Fund. Appl. Toxicol. , vol.6 , pp. 172-174
    • Wecker, L.1    Mrak, R.E.2    Dettbarn, W.D.3
  • 64
    • 0018772249 scopus 로고
    • Numerical reconstruction of the quantal event at nicotinic synapses
    • Whathey, J.C., N.M. Nass, and H.A. Lester. 1979. Numerical reconstruction of the quantal event at nicotinic synapses. Biophys. J. 27:145-164.
    • (1979) Biophys. J. , vol.27 , pp. 145-164
    • Whathey, J.C.1    Nass, N.M.2    Lester, H.A.3
  • 65
    • 0025672645 scopus 로고
    • Homologous recombination at c-fyn locus of mouse embryonic stem cells with use of diphtheria toxin A-fragment gene in negative selection
    • Yagi, T., Y. Ikawa, K. Yoshida, Y. Shigetani, N. Takeda, I. Mabuchi, T. Yamamoto. and S. Aizawa. 1990. Homologous recombination at c-fyn locus of mouse embryonic stem cells with use of diphtheria toxin A-fragment gene in negative selection. Proc. Natl. Acad. Sci. USA. 87:9918-9922.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9918-9922
    • Yagi, T.1    Ikawa, Y.2    Yoshida, K.3    Shigetani, Y.4    Takeda, N.5    Mabuchi, I.6    Yamamoto, T.7    Aizawa, S.8
  • 66
    • 0020405090 scopus 로고
    • Cellular localization of the molecular forms of acetylcholinesterase in rat diaphragm
    • Younkin, S.G., C. Rosenstein, P.L. Collins, and T.L. Rosenberry. 1982. Cellular localization of the molecular forms of acetylcholinesterase in rat diaphragm. J. Biol. Chem. 257:13630-13637.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13630-13637
    • Younkin, S.G.1    Rosenstein, C.2    Collins, P.L.3    Rosenberry, T.L.4


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