메뉴 건너뛰기




Volumn 15, Issue 18, 1996, Pages 4835-4843

The structure-function relationships in Drosophila neurotactin show that cholinesterasic domains may have adhesive properties

Author keywords

Cholinesterases; Drosophila; Heterophilic cell adhesion; Neurotactin; Three dimensional model

Indexed keywords

ACETYLCHOLINESTERASE; CHOLINESTERASE; MEMBRANE PROTEIN; NEUROTACTIN; UNCLASSIFIED DRUG;

EID: 0029816374     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00864.x     Document Type: Article
Times cited : (69)

References (34)
  • 1
    • 0029055716 scopus 로고
    • Gliotactin, a novel transmembrane protein on peripheral glia, is required to form the blood-nerve barrier in Drosophila
    • Auld, V.J., Fetter, R.D., Broadie, K. and Goodman, C.S. (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
  • 2
    • 0028230038 scopus 로고
    • Structure and dynamics of the active site gorge of acetylcholinesterase: Synergistic use of molecular dynamics simulation and X-ray crystallography
    • Axelsen, P.H., Harel, M., Silman, I. and Sussman, J.L. (1944) Structure and dynamics of the active site gorge of acetylcholinesterase: synergistic use of molecular dynamics simulation and X-ray crystallography. Protein Sci., 3, 188-197.
    • (1944) Protein Sci. , vol.3 , pp. 188-197
    • Axelsen, P.H.1    Harel, M.2    Silman, I.3    Sussman, J.L.4
  • 4
    • 0028818897 scopus 로고
    • Acetylcholinesterase inhibition by fasciculin: Crystal structure of the complex
    • Bourne, Y., Taylor, P. and Marchot, P. (1995) Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex. Cell, 83, 503-512.
    • (1995) Cell , vol.83 , pp. 503-512
    • Bourne, Y.1    Taylor, P.2    Marchot, P.3
  • 5
    • 0023140814 scopus 로고
    • Crystallographic R-factor refinement by molecular dynamics
    • Brünger, A.T., Kuriyan, J. and Karplus, M. (1987) Crystallographic R-factor refinement by molecular dynamics. Science, 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 6
    • 3042861298 scopus 로고    scopus 로고
    • A cholinesterase genes server (ESTHER): A database of cholinesterase-related sequences for multiple alignments, phylogenetic relationships, mutations and structural data retrieval
    • Cousin, X., Hotelier, T., Liévin, P., Toutant, J.-P. and Chatonnet, A. (1996) A cholinesterase genes server (ESTHER): a database of cholinesterase-related sequences for multiple alignments, phylogenetic relationships, mutations and structural data retrieval. Nucleic Acids Res., 24, 132-136.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 132-136
    • Cousin, X.1    Hotelier, T.2    Liévin, P.3    Toutant, J.-P.4    Chatonnet, A.5
  • 7
    • 0027535179 scopus 로고
    • Relationship between sequence conservation and tri-dimensional structure in a large family of esterases, lipases and related proteins
    • Cygler, M., Schrag, J.D., Sussman, J.L., Harel, M., Silman, I., Gentry, M.K. and Doctor, B.P. (1993) Relationship between sequence conservation and tri-dimensional structure in a large family of esterases, lipases and related proteins. Protein Sci., 2, 366-382.
    • (1993) Protein Sci. , vol.2 , pp. 366-382
    • Cygler, M.1    Schrag, J.D.2    Sussman, J.L.3    Harel, M.4    Silman, I.5    Gentry, M.K.6    Doctor, B.P.7
  • 8
    • 0025187057 scopus 로고
    • Characterization and gene cloning of neurotactin, a Drosophila transmembrane protein related to cholinesterases
    • De la Escalera, S., Bockamp, E.O., Moya, F., Piovant, M. and 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
  • 9
    • 0021867705 scopus 로고
    • The sequence of 967 amino acids at the carboxyl-end of rat thyroglobulin. Location and surroundings of two thyroxine-forming sites
    • Di Lauro, R., Obici, S., Condliffe, D., Ursini, V.M., Musti, A., Moscatelli, C. and Avvedimento, V.E. (1985) The sequence of 967 amino acids at the carboxyl-end of rat thyroglobulin. Location and surroundings of two thyroxine-forming sites. Eur. J. Biochem., 148, 7-11.
    • (1985) Eur. J. Biochem. , vol.148 , pp. 7-11
    • Di Lauro, R.1    Obici, S.2    Condliffe, D.3    Ursini, V.M.4    Musti, A.5    Moscatelli, C.6    Avvedimento, V.E.7
  • 12
    • 0010989660 scopus 로고
    • The Ace locus of Drosophila melanogaster, structural gene for acetylcholinesterase with an unusual 5′-leader
    • Hall, L.M.C. and Spierer, P. (1986) The Ace locus of Drosophila melanogaster, structural gene for acetylcholinesterase with an unusual 5′-leader. EMBO J., 5, 2949-2954.
    • (1986) EMBO J. , vol.5 , pp. 2949-2954
    • Hall, L.M.C.1    Spierer, P.2
  • 13
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton, R.M., Hunt, H.D., Ho, S.N., Pullen, J.K. and Pease, L.R. (1989) Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene, 77, 61-68.
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 14
    • 0025606148 scopus 로고
    • Drosophila neurotactin, a surface glycoprotein with homology to serine esterases, is dynamically expressed during embryogenesis
    • Hortsch, M., Patel, N.H., Bieber, A.J., Traquina, Z.R. and Goodman, C.S. (1990) Drosophila neurotactin, a surface glycoprotein with homology to serine esterases, is dynamically expressed during embryogenesis. Development, 110, 1327-1340.
    • (1990) Development , vol.110 , pp. 1327-1340
    • Hortsch, M.1    Patel, N.H.2    Bieber, A.J.3    Traquina, Z.R.4    Goodman, C.S.5
  • 15
    • 0024844513 scopus 로고
    • Primary sequence of a motor neuron-selective adhesive site in the synaptic basal lamina protein S-laminin
    • Hunter, D.D., Porter, B.E., Bulock, J.W., Adams, S.P., Merlie, J.P. and Sanes, J.R. (1989) Primary sequence of a motor neuron-selective adhesive site in the synaptic basal lamina protein S-laminin. Cell, 59, 905-913.
    • (1989) Cell , vol.59 , pp. 905-913
    • Hunter, D.D.1    Porter, B.E.2    Bulock, J.W.3    Adams, S.P.4    Merlie, J.P.5    Sanes, J.R.6
  • 17
    • 0024436650 scopus 로고
    • The Notch gene product is a glycoprotein expressed on the cell surface of both epidermal and neuronal precursor cells during Drosophila development
    • Johansen, K.M., Fehon, R.G. and Artavanis-Tsakonas, S. (1989) The Notch gene product is a glycoprotein expressed on the cell surface of both epidermal and neuronal precursor cells during Drosophila development. J. Cell. Biol., 109, 2427-2440.
    • (1989) J. Cell. Biol. , vol.109 , pp. 2427-2440
    • Johansen, K.M.1    Fehon, R.G.2    Artavanis-Tsakonas, S.3
  • 18
    • 0024557468 scopus 로고
    • Analysis of the gene encoding the largest subunit of RNA polymerase II in Drosophila
    • Jokerst, R.S., Weeks, J.R., Zehring, W.A. and Greenleaf, A.L. (1989) Analysis of the gene encoding the largest subunit of RNA polymerase II in Drosophila. Mol. Gen. Genet., 215, 266-275.
    • (1989) Mol. Gen. Genet. , vol.215 , pp. 266-275
    • Jokerst, R.S.1    Weeks, J.R.2    Zehring, W.A.3    Greenleaf, A.L.4
  • 19
    • 0025369197 scopus 로고
    • Drosophila chaoptin, a member of the leucine-rich repeat family, is a photoreceptor cell-specific adhesion molecule
    • Krantz, D.E. and Zipursky, S.L. (1990) Drosophila chaoptin, a member of the leucine-rich repeat family, is a photoreceptor cell-specific adhesion molecule. EMBO J., 9, 1969-1977.
    • (1990) EMBO J. , vol.9 , pp. 1969-1977
    • Krantz, D.E.1    Zipursky, S.L.2
  • 20
    • 0025991577 scopus 로고
    • Cholinesterase-like domains in enzymes and structural proteins: Functional and evolutionary relationships and identification of a catalytically essential aspartic acid
    • Krejci, E., Duval, N., Chatonnet, A., Vincens, P. and Massoulié, J. (1991) Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid. Proc. Natl Acad. Sci. USA, 88, 6647-6651.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 6647-6651
    • Krejci, E.1    Duval, N.2    Chatonnet, A.3    Vincens, P.4    Massoulié, J.5
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0025270460 scopus 로고
    • Glutactin, a novel Drosophila basement membrane-related glycoprotein with sequence similarity to serine esterases
    • Olson, P.F., Fessler, L.I., Nelson, R.E., Sterne, R.E., Campbell, A.G. and Fessler, J.H. (1990) Glutactin, a novel Drosophila basement membrane-related glycoprotein with sequence similarity to serine esterases. EMBO J., 9, 1219-1227.
    • (1990) EMBO J. , vol.9 , pp. 1219-1227
    • Olson, P.F.1    Fessler, L.I.2    Nelson, R.E.3    Sterne, R.E.4    Campbell, A.G.5    Fessler, J.H.6
  • 23
    • 0023886888 scopus 로고
    • Membrane glycoproteins immunologically related to the human insulin receptor are associated with presumptive neuronal territories and developing neurons
    • Piovant, M. and Léna, P. (1988) Membrane glycoproteins immunologically related to the human insulin receptor are associated with presumptive neuronal territories and developing neurons. Development, 103, 145-156.
    • (1988) Development , vol.103 , pp. 145-156
    • Piovant, M.1    Léna, P.2
  • 24
    • 0002908272 scopus 로고
    • TURBO-FRODO
    • Silicon Graphics Committee (eds), Silicon Graphics, Mountain View, CA
    • Roussel, A. and Cambillau, C. (1989) TURBO-FRODO. In Silicon Graphics Committee (eds), Silicon Graphics Geometry Partners Directory. Silicon Graphics, Mountain View, CA, pp. 77-78.
    • (1989) Silicon Graphics Geometry Partners Directory , pp. 77-78
    • Roussel, A.1    Cambillau, C.2
  • 25
    • 0015328565 scopus 로고
    • Cell lines derived from late embryonic stages of Drosophila melanogaster
    • Schneider, I. (1972) Cell lines derived from late embryonic stages of Drosophila melanogaster. J. Embryol. Exp. Morphol., 27, 353-365.
    • (1972) J. Embryol. Exp. Morphol. , vol.27 , pp. 353-365
    • Schneider, I.1
  • 26
    • 0023128247 scopus 로고
    • Redesigning the body plan of Drosophila by ectopic expression of the homoeotic gene Antennapedia
    • Schneuwly, S., Klemenz, R. and Gehring, W.J. (1987) Redesigning the body plan of Drosophila by ectopic expression of the homoeotic gene Antennapedia. Nature, 325, 816-818.
    • (1987) Nature , vol.325 , pp. 816-818
    • Schneuwly, S.1    Klemenz, R.2    Gehring, W.J.3
  • 27
    • 0024291344 scopus 로고
    • Characterization of Amalgam: A member of the immunoglobulin gene family from Drosophila
    • Seeger, M.A., Haffley, L. and Kaufman, T. (1988) Characterization of Amalgam: a member of the immunoglobulin gene family from Drosophila. Cell, 55, 589-600.
    • (1988) Cell , vol.55 , pp. 589-600
    • Seeger, M.A.1    Haffley, L.2    Kaufman, T.3
  • 28
    • 0023371687 scopus 로고
    • cDNA sequences of Torpedo marmorata acetylcholinesterase: Primary structure of the precursor of a catalytic subunit; existence of multiple 5́-untranslated regions
    • Sikorav, J.L., Krejci, E. and Massoulié, J. (1987) cDNA sequences of Torpedo marmorata acetylcholinesterase: primary structure of the precursor of a catalytic subunit; existence of multiple 5́-untranslated regions. EMBO J., 6, 1865-1873.
    • (1987) EMBO J. , vol.6 , pp. 1865-1873
    • Sikorav, J.L.1    Krejci, E.2    Massoulié, J.3
  • 29
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman, J.L., Harel, M., Frolow, F., Oefner, C., Goldman, A., Toker, L. and Silman, I. (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    Toker, L.6    Silman, I.7
  • 30
    • 0029160437 scopus 로고
    • Morphogenetic roles of classic cadherins
    • Takeichi, M. (1995) Morphogenetic roles of classic cadherins. Curr. Opin. Cell Biol., 7, 619-627.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 619-627
    • Takeichi, M.1
  • 31
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G. and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 32
    • 0024210345 scopus 로고
    • Vectors for Drosophila and tissue culture transfection
    • Thummel, C.S., Boulet, A.M. and Lipshitz, H.D. (1988) Vectors for Drosophila and tissue culture transfection. Gene, 74, 445-456.
    • (1988) Gene , vol.74 , pp. 445-456
    • Thummel, C.S.1    Boulet, A.M.2    Lipshitz, H.D.3
  • 33
    • 0023845219 scopus 로고
    • Native molecular forms of head acetylcholinesterase from adult Drosophila melanogaster: Quaternary structure and hydrophobic character
    • Toutant, J.P., Arpagaus, M. and Fournier, D. (1988) Native molecular forms of head acetylcholinesterase from adult Drosophila melanogaster: quaternary structure and hydrophobic character. J. Neurochem., 50, 209-218.
    • (1988) J. Neurochem. , vol.50 , pp. 209-218
    • Toutant, J.P.1    Arpagaus, M.2    Fournier, D.3
  • 34
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedures and some applications
    • Towbin, H., Staehelin, T. and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedures and some applications. Proc. Natl Acad. Sci. USA, 76, 4350-4354.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.