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Volumn 138, Issue 3, 2011, Pages 553-563

Sugar-free frosting, a homolog of SAD kinase, drives neural-specific glycan expression in the Drosophila embryo

Author keywords

Drosophila; Glycosylation; Golgi; Nervous system

Indexed keywords

GLYCAN; PHOSPHOTRANSFERASE; SUGAR FREE FROSTING KINASE; UNCLASSIFIED DRUG;

EID: 78751490457     PISSN: 09501991     EISSN: 14779129     Source Type: Journal    
DOI: 10.1242/dev.055376     Document Type: Article
Times cited : (21)

References (77)
  • 1
    • 0025941824 scopus 로고
    • NCAM Polysialic acid can regulate both cell-cell and cell-substrate interactions
    • Acheson, A., Sunshine, J. L. and Rutishauser, U. (1991). NCAM Polysialic acid can regulate both cell-cell and cell-substrate interactions. J. Cell Biol. 114, 143-153.
    • (1991) J. Cell Biol. , vol.114 , pp. 143-153
    • Acheson, A.1    Sunshine, J.L.2    Rutishauser, U.3
  • 2
    • 0033566159 scopus 로고    scopus 로고
    • Morphological domains of Lewis-X/FORSE-1 immunolabeling in the embryonic neural tube are due to developmental regulation of cell surface carbohydrate expression
    • Allendoerfer, K. L., Durairaj, A., Matthews, G. A. and Patterson, P. H. (1999). Morphological domains of Lewis-X/FORSE-1 immunolabeling in the embryonic neural tube are due to developmental regulation of cell surface carbohydrate expression. Dev. Biol. 211, 208-219.
    • (1999) Dev. Biol. , vol.211 , pp. 208-219
    • Allendoerfer, K.L.1    Durairaj, A.2    Matthews, G.A.3    Patterson, P.A.4
  • 3
    • 34247849493 scopus 로고    scopus 로고
    • Dynamic developmental elaboration of N-linked glycan complexity in the Drosophila melanogaster embryo
    • Aoki, K., Perlman, M., Lim, J., Cantu, R., Wells, L. and Tiemeyer, M. (2007). Dynamic developmental elaboration of N-linked glycan complexity in the Drosophila melanogaster embryo. J. Biol. Chem. 282, 9127-9142.
    • (2007) J. Biol. Chem. , vol.282 , pp. 9127-9142
    • Aoki, K.1    Perlman, M.2    Lim, J.3    Cantu, R.4    Wells, L.5    Tiemeyer, M.6
  • 5
    • 0031871233 scopus 로고    scopus 로고
    • Regulation of ganglioside metabolism by phosphorylation and dephosphorylation
    • Bieberich, E., Freischutz, B., Liour, S. S. and Yu, R. K. (1998). Regulation of ganglioside metabolism by phosphorylation and dephosphorylation. J. Neurochem. 71, 972-979.
    • (1998) J. Neurochem. , vol.71 , pp. 972-979
    • Bieberich, E.1    Freischutz, B.2    Liour, S.S.3    Yu, R.A.4
  • 7
    • 0042235216 scopus 로고    scopus 로고
    • The role of protein phosphorylation in alpha2,6(N)-sialyltransferase activity
    • Breen, K. C. and Georgopoulou, N. (2003). The role of protein phosphorylation in alpha2,6(N)-sialyltransferase activity. Biochem. Biophys. Res. Commun. 309, 32-35.
    • (2003) Biochem. Biophys. Res. Commun. , vol.309 , pp. 32-35
    • Breen, K.C.1    Georgopoulou, N.2
  • 8
    • 0028310837 scopus 로고
    • Mammalian AMPactivated protein kinase is homologous to yeast and plant protein kinases involved in the regulation of carbon metabolism
    • Carling, D., Aguan, K., Woods, A., Verhoeven, A. J., Beri, R. K., Brennan, C. H., Sidebottom, C., Davison, M. D. and Scott, J. (1994). Mammalian AMPactivated protein kinase is homologous to yeast and plant protein kinases involved in the regulation of carbon metabolism. J. Biol. Chem. 269, 11442-11448.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11442-11448
    • Carling, D.1    Aguan, K.2    Woods, A.3    Verhoeven, A.J.4    Beri, R.K.5    Brennan, C.H.6    Sidebottom, C.7    Davison, M.D.8    Scott, J.9
  • 9
    • 0022967045 scopus 로고
    • A cell surface molecule distributed in a dorso-ventral gradient in the perinatal rat retina
    • Constantine-Paton, M., Blum, A. S., Mendez-Otero, R. and Barnstable, C. J. (1986). A cell surface molecule distributed in a dorso-ventral gradient in the perinatal rat retina. Nature 324, 459-462.
    • (1986) Nature , vol.324 , pp. 459-462
    • Constantine-Paton, M.1    Blum, A.S.2    Mendez-Otero, R.3    Barnstable, C.J.4
  • 10
    • 0035137995 scopus 로고    scopus 로고
    • The SAD-1 kinase regulates presynaptic vesicle clustering and axon termination
    • Crump, J., Zhen, M., Yishi, J. and Bargmann, C. (2001). The SAD-1 kinase regulates presynaptic vesicle clustering and axon termination. Neuron 29, 115-129.
    • (2001) Neuron , vol.29 , pp. 115-129
    • Crump, J.1    Zhen, M.2    Yishi, J.3    Bargmann, C.4
  • 11
    • 72249094196 scopus 로고    scopus 로고
    • Metabolism, cell surface organization, and disease
    • Dennis, J. W., Nabi, I. R. and Demetriou, M. (2009). Metabolism, cell surface organization, and disease. Cell 139, 1229-1241.
    • (2009) Cell , vol.139 , pp. 1229-1241
    • Dennis, J.W.1    Nabi, I.R.2    Demetriou, M.3
  • 12
    • 0027948932 scopus 로고
    • A Drosophila receptor tyrosine phosphatase expressed in the embryonic CNS and larval optic lobes is a member of the set of proteins bearing the 'HRP' carbohydrate epitope
    • Desai, C. J., Popova, E. and Zinn, K. (1994). A Drosophila receptor tyrosine phosphatase expressed in the embryonic CNS and larval optic lobes is a member of the set of proteins bearing the 'HRP' carbohydrate epitope. J. Neurosci. 14, 7272-7283.
    • (1994) J. Neurosci. , vol.14 , pp. 7272-7283
    • Desai, C.J.1    Popova, E.2    Zinn, K.3
  • 13
    • 0034618073 scopus 로고    scopus 로고
    • Phosphorylation of the vesicle-tethering protein p115 by a casein kinase II-like enzyme is required for Golgi reassembly from isolated mitotic fragments
    • Dirac-Svejstrup, A. B., Shorter, J., Waters, M. G. and Warren, G. (2000). Phosphorylation of the vesicle-tethering protein p115 by a casein kinase II-like enzyme is required for Golgi reassembly from isolated mitotic fragments. J. Cell Biol. 150, 475-488.
    • (2000) J. Cell Biol. , vol.150 , pp. 475-488
    • Dirac-Svejstrup, A.B.1    Shorter, J.2    Waters, M.G.3    Warren, G.4
  • 14
    • 0037031658 scopus 로고    scopus 로고
    • Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network
    • Doray, B., Ghosh, P., Griffith, J., Geuze, H. J. and Kornfeld, S. (2002). Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network. Science 297, 1700-1703.
    • (2002) Science , vol.297 , pp. 1700-1703
    • Doray, B.1    Ghosh, P.2    Griffith, J.3    Geuze, H.J.4    Kornfeld, S.5
  • 15
    • 0035958916 scopus 로고    scopus 로고
    • Identification of core alpha 1,3 fucosylated glycans and cloning of the requisite fucosyltransferase cDNA from Drosophila melanogaster. Potential basis of the neural anti-horseradish peroxidase epitope
    • Fabini, G., Freilinger, A., Altmann, F. and Wilson, I. B. (2001). Identification of core alpha 1,3 fucosylated glycans and cloning of the requisite fucosyltransferase cDNA from Drosophila melanogaster. Potential basis of the neural anti-horseradish peroxidase epitope. J. Biol. Chem. 276, 28058-28067.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28058-28067
    • Fabini, G.1    Freilinger, A.2    Altmann, F.3    Wilson, I.A.4
  • 16
    • 0037137478 scopus 로고    scopus 로고
    • Human disorders in N-glycosylation and animal models
    • Freeze, H. H. (2002). Human disorders in N-glycosylation and animal models. Biochim. Biophys. Acta 1573, 388-393.
    • (2002) Biochim. Biophys. Acta , vol.1573 , pp. 388-393
    • Freeze, H.H.1
  • 17
    • 0034666618 scopus 로고    scopus 로고
    • Regulation of neural cell adhesion molecule polysialylation state by cell-cell contact and protein kinase C delta
    • Gallagher, H. C., Odumeru, O. A. and Regan, C. M. (2000). Regulation of neural cell adhesion molecule polysialylation state by cell-cell contact and protein kinase C delta. J. Neurosci. Res. 61, 636-645.
    • (2000) J. Neurosci. Res. , vol.61 , pp. 636-645
    • Gallagher, H.C.1    Odumeru, O.A.2    Regan, C.A.3
  • 18
    • 0035050814 scopus 로고    scopus 로고
    • Protein kinase C delta regulates neural cell adhesion molecule polysialylation state in the rat brain
    • Gallagher, H. C., Murphy, K. J., Foley, A. G. and Regan, C. M. (2001). Protein kinase C delta regulates neural cell adhesion molecule polysialylation state in the rat brain. J. Neurochem. 77, 425-434.
    • (2001) J. Neurochem. , vol.77 , pp. 425-434
    • Gallagher, H.C.1    Murphy, K.J.2    Foley, A.G.3    Regan, C.A.4
  • 19
    • 0034851008 scopus 로고    scopus 로고
    • Nucleotide sugar transporters: Biological and functional aspects
    • Gerardy-Schahn, R., Oelmann, S. and Bakker, H. (2001). Nucleotide sugar transporters: biological and functional aspects. Biochimie 83, 775-782.
    • (2001) Biochimie , vol.83 , pp. 775-782
    • Gerardy-Schahn, R.1    Oelmann, S.2    Bakker, H.3
  • 20
    • 22444448589 scopus 로고    scopus 로고
    • Functional analysis of Drosophila beta1,4- Nacetylgalactosaminyltransferases
    • Haines, N. and Irvine, K. D. (2005). Functional analysis of Drosophila beta1,4-Nacetylgalactosaminyltransferases. Glycobiology 15, 335-346.
    • (2005) Glycobiology , vol.15 , pp. 335-346
    • Haines, N.1    Irvine, K.A.2
  • 21
    • 0029020282 scopus 로고
    • The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S. K. and Hunter, T. (1995). The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9, 576-596.
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 22
    • 0242720096 scopus 로고    scopus 로고
    • Mutational analysis of the cytoplasmic domain of beta1,4- galactosyltransferase I: Influence of phosphorylation on cell surface expression
    • Hathaway, H. J., Evans, S. C., Dubois, D. H., Foote, C. I., Elder, B. H. and Shur, B. D. (2003). Mutational analysis of the cytoplasmic domain of beta1,4-galactosyltransferase I: influence of phosphorylation on cell surface expression. J. Cell Sci. 116, 4319-4330.
    • (2003) J. Cell Sci. , vol.116 , pp. 4319-4330
    • Hathaway, H.J.1    Evans, S.C.2    Dubois, D.H.3    Foote, C.I.4    Elder, B.H.5    Shur, B.A.6
  • 24
  • 25
    • 0020121682 scopus 로고
    • Antibodies to horseradish peroxidase as specific neuronal markers in Drosophila and grasshopper embryos
    • Jan, L. Y. and Jan, Y. N. (1982). Antibodies to horseradish peroxidase as specific neuronal markers in Drosophila and grasshopper embryos. Proc. Natl. Acad. Sci. USA 79, 2700-2704.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2700-2704
    • Jan, L.Y.1    Jan, Y.A.2
  • 26
    • 0037187643 scopus 로고    scopus 로고
    • Drosophila liprin-alpha and the receptor phosphatase Dlar control synapse morphogenesis
    • Kaufmann, N., DeProto, J., Ranjan, R., Wan, H. and Van Vactor, D. (2002). Drosophila liprin-alpha and the receptor phosphatase Dlar control synapse morphogenesis. Neuron 28, 27-38.
    • (2002) Neuron , vol.28 , pp. 27-38
    • Kaufmann, N.1    Deproto, J.2    Ranjan, R.3    Wan, H.4    Van Vactor, D.5
  • 27
    • 13644267037 scopus 로고    scopus 로고
    • Mammalian SAD kinases are required for neuronal polarization
    • Kishi, M., Pan, Y. A., Crump, J. G. and Sanes, J. R. (2005). Mammalian SAD kinases are required for neuronal polarization. Science 307, 929-932.
    • (2005) Science , vol.307 , pp. 929-932
    • Kishi, M.1    Pan, Y.A.2    Crump, J.G.3    Sanes, J.A.4
  • 29
    • 1042289780 scopus 로고    scopus 로고
    • Functional characterization of Drosophila sialyltransferase
    • Koles, K., Irvine, K. D. and Panin, V. M. (2004). Functional characterization of Drosophila sialyltransferase. J. Biol. Chem. 279, 4346-4357.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4346-4357
    • Koles, K.1    Irvine, K.D.2    Panin, V.M.3
  • 30
    • 70450223327 scopus 로고    scopus 로고
    • The Golgi apparatus: Lessons from Drosophila
    • Kondylis, V. and Rabouille, C. (2009). The Golgi apparatus: lessons from Drosophila. FEBS Lett. 583, 3827-3838.
    • (2009) FEBS Lett. , vol.583 , pp. 3827-3838
    • Kondylis, V.1    Rabouille, C.2
  • 31
    • 0029988151 scopus 로고    scopus 로고
    • A neural tetraspanin, encoded by late bloomer, that facilitates synapse formation
    • Kopczynski, C. C., Davis, G. W. and Goodman, C. S. (1996). A neural tetraspanin, encoded by late bloomer, that facilitates synapse formation. Science 271, 1867-1870.
    • (1996) Science , vol.271 , pp. 1867-1870
    • Kopczynski, C.C.1    Davis, G.W.2    Goodman, C.S.3
  • 32
    • 0021251168 scopus 로고
    • Neural cell adhesion molecules and myelinassociated glycoprotein share a common carbohydrate moiety recognized by monoclonal antibodies L2 and HNK-1
    • Kruse, J., Mailhammer, R., Wernecke, H., Faissner, A., Sommer, I., Goridis, C. and Schachner, M. (1984). Neural cell adhesion molecules and myelinassociated glycoprotein share a common carbohydrate moiety recognized by monoclonal antibodies L2 and HNK-1. Nature 311, 153-155.
    • (1984) Nature , vol.311 , pp. 153-155
    • Kruse, J.1    Mailhammer, R.2    Wernecke, H.3    Faissner, A.4    Sommer, I.5    Goridis, C.6    Schachner, M.7
  • 33
    • 0025797046 scopus 로고
    • The structure of a neural specific carbohydrate epitope of horseradish peroxidase recognized by anti-horseradish peroxidase antiserum
    • Kurosaka, A., Yano, A., Itoh, N., Kuroda, Y., Nakagawa, T. and Kawasaki, T. (1991). The structure of a neural specific carbohydrate epitope of horseradish peroxidase recognized by anti-horseradish peroxidase antiserum. J. Biol. Chem. 266, 4168-4172.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4168-4172
    • Kurosaka, A.1    Yano, A.2    Itoh, N.3    Kuroda, Y.4    Nakagawa, T.5    Kawasaki, T.6
  • 35
    • 36348954543 scopus 로고    scopus 로고
    • N-glycan processing deficiency promotes spontaneous inflammatory demyelination and neurodegeneration
    • Lee, S. U., Grigorian, A., Pawling, J., Chen, I. J., Gao, G., Mozaffar, T., McKerlie, C. and Demetriou, M. (2007). N-glycan processing deficiency promotes spontaneous inflammatory demyelination and neurodegeneration. J. Biol. Chem. 282, 33725-33734.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33725-33734
    • Lee, S.U.1    Grigorian, A.2    Pawling, J.3    Chen, I.J.4    Gao, G.5    Mozaffar, T.6    McKerlie, C.7    Demetriou, M.8
  • 36
    • 33646178162 scopus 로고    scopus 로고
    • The Drosophila fused lobes gene encodes an N-acetylglucosaminidase involved in N-glycan processing
    • Leonard, R., Rendic, D., Rabouille, C., Wilson, I. B., Preat, T. and Altmann, F. (2006). The Drosophila fused lobes gene encodes an N-acetylglucosaminidase involved in N-glycan processing. J. Biol. Chem. 281, 4867-4875.
    • (2006) J. Biol. Chem. , vol.281 , pp. 4867-4875
    • Leonard, R.1    Rendic, D.2    Rabouille, C.3    Wilson, I.B.4    Preat, T.5    Altmann, F.6
  • 37
    • 44449169489 scopus 로고    scopus 로고
    • Defining the regulated secreted proteome of rodent adipocytes upon the induction of insulin resistance
    • Lim, J. M., Sherling, D., Teo, C. F., Hausman, D. B., Lin, D. and Wells, L. (2008). Defining the regulated secreted proteome of rodent adipocytes upon the induction of insulin resistance. J. Proteome Res. 7, 1251-1263.
    • (2008) J. Proteome Res. , vol.7 , pp. 1251-1263
    • Lim, J.M.1    Sherling, D.2    Teo, C.F.3    Hausman, D.B.4    Lin, D.5    Wells, L.6
  • 38
    • 0027959402 scopus 로고
    • Genetic analysis of Fasciclin II in Drosophila: Defasciculation, refasciculation, and altered fasciculation
    • Lin, D. M., Fetter, R. D., Kopczynski, C., Grenningloh, G. and Goodman, C. S. (1994). Genetic analysis of Fasciclin II in Drosophila: defasciculation, refasciculation, and altered fasciculation. Neuron 13, 1055-1069.
    • (1994) Neuron , vol.13 , pp. 1055-1069
    • Lin, D.M.1    Fetter, R.D.2    Kopczynski, C.3    Grenningloh, G.4    Goodman, C.S.5
  • 39
    • 0033583193 scopus 로고    scopus 로고
    • Sialyltransferase isoforms are phosphorylated in the cis-medial Golgi on serine and threonine residues in their luminal sequences
    • Ma, J., Simonovic, M., Qian, R. and Colley, K. J. (1999). Sialyltransferase isoforms are phosphorylated in the cis-medial Golgi on serine and threonine residues in their luminal sequences. J. Biol. Chem. 274, 8046-8052.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8046-8052
    • Ma, J.1    Simonovic, M.2    Qian, R.3    Colley, K.J.4
  • 40
    • 42549165123 scopus 로고    scopus 로고
    • The L1-type cell adhesion molecule Neuroglian is necessary for maintenance of sensory axon advance in the Drosophila embryo
    • Martin, V., Mrkusich, E., Steinel, M. C., Rice, J., Merritt, D. J. and Whitington, P. M. (2008). The L1-type cell adhesion molecule Neuroglian is necessary for maintenance of sensory axon advance in the Drosophila embryo. Neural Dev. 3, 10.
    • (2008) Neural Dev. , vol.3 , pp. 10
    • Martin, V.1    Mrkusich, E.2    Steinel, M.C.3    Rice, J.4    Merritt, D.J.5    Whitington, P.A.6
  • 41
    • 34347224363 scopus 로고    scopus 로고
    • Ligand, modulatory, and coreceptor functions of neural glycans
    • Matani, P., Sharrow, M. and Tiemeyer, M. (2007). Ligand, modulatory, and coreceptor functions of neural glycans. Front. Biosci. 12, 3852-3879.
    • (2007) Front. Biosci. , vol.12 , pp. 3852-3879
    • Matani, P.1    Sharrow, M.2    Tiemeyer, M.3
  • 42
    • 77949316198 scopus 로고    scopus 로고
    • A small genomic region containing several loci required for gastrulation in Drosophila
    • Mathew, S. J., Kerridge, S. and Leptin, M. (2009). A small genomic region containing several loci required for gastrulation in Drosophila. PLoS ONE 4, e7437.
    • (2009) PLoS ONE , vol.4
    • Mathew, S.J.1    Kerridge, S.2    Leptin, M.3
  • 43
    • 0036758606 scopus 로고    scopus 로고
    • Aggrecan glycoforms contribute to the molecular heterogeneity of perineuronal nets
    • Matthews, R. T., Kelly, G. M., Zerillo, C. A., Tiemeyer, M. and Hockfield, S. (2002). Aggrecan glycoforms contribute to the molecular heterogeneity of perineuronal nets. J. Neurosci. 22, 7536-7547.
    • (2002) J. Neurosci. , vol.22 , pp. 7536-7547
    • Matthews, R.T.1    Kelly, G.M.2    Zerillo, C.A.3    Tiemeyer, M.4    Hockfield, S.5
  • 44
    • 0028922684 scopus 로고
    • Central projections of sensory neurons in the Drosophila embryo correlate with sensory modality, soma position, and proneural gene function
    • Merritt, D. J. and Whitington, P. M. (1995). Central projections of sensory neurons in the Drosophila embryo correlate with sensory modality, soma position, and proneural gene function. J. Neurosci. 15, 1755-1767.
    • (1995) J. Neurosci. , vol.15 , pp. 1755-1767
    • Merritt, D.J.1    Whitington, P.A.2
  • 45
    • 0038182574 scopus 로고    scopus 로고
    • Dystrophin-glycoprotein complex: Post-translational processing and dystroglycan function
    • Michele, D. E. and Campbell, K. P. (2003). Dystrophin-glycoprotein complex: Post-translational processing and dystroglycan function. J. Biol. Chem. 278, 15457-15460.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15457-15460
    • Michele, D.E.1    Campbell, K.P.2
  • 46
    • 0029168017 scopus 로고
    • Mitotic disassembly of the Golgi apparatus in vivo
    • Misteli, T. and Warren, G. (1995). Mitotic disassembly of the Golgi apparatus in vivo. J. Cell Sci. 108, 2715-2727.
    • (1995) J. Cell Sci. , vol.108 , pp. 2715-2727
    • Misteli, T.1    Warren, G.2
  • 47
    • 0029843580 scopus 로고    scopus 로고
    • A regulatory role for cAMP-dependent protein kinase in protein traffic along the exocytic route
    • Muniz, M., Alonso, M., Hidalgo, J. and Velasco, A. (1996). A regulatory role for cAMP-dependent protein kinase in protein traffic along the exocytic route. J. Biol. Chem. 271, 30935-30941.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30935-30941
    • Muniz, M.1    Alonso, M.2    Hidalgo, J.3    Velasco, A.4
  • 48
    • 0031474609 scopus 로고    scopus 로고
    • Protein kinase A activity is required for the budding of constitutive transport vesicles from the trans-Golgi network
    • Muniz, M., Martin, M. E., Hidalgo, J. and Velasco, A. (1997). Protein kinase A activity is required for the budding of constitutive transport vesicles from the trans-Golgi network. Proc. Natl. Acad. Sci. USA 94, 14461-14466.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14461-14466
    • Muniz, M.1    Martin, M.E.2    Hidalgo, J.3    Velasco, A.4
  • 50
    • 0030953187 scopus 로고    scopus 로고
    • The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner
    • Nakamura, N., Lowe, M., Levine, T. P., Rabouille, C. and Warren, G. (1997). The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner. Cell 89, 445-455.
    • (1997) Cell , vol.89 , pp. 445-455
    • Nakamura, N.1    Lowe, M.2    Levine, T.P.3    Rabouille, C.4    Warren, G.5
  • 51
    • 70450223118 scopus 로고    scopus 로고
    • Sorting out glycosylation enzymes in the Golgi apparatus
    • Nilsson, T., Au, C. E. and Bergeron, J. J. (2009). Sorting out glycosylation enzymes in the Golgi apparatus. FEBS Lett. 583, 3764-3769.
    • (2009) FEBS Lett. , vol.583 , pp. 3764-3769
    • Nilsson, T.1    Au, C.E.2    Bergeron, J.J.3
  • 52
    • 0037074006 scopus 로고    scopus 로고
    • Regulation of notch signaling by o-linked fucose
    • Okajima, T. and Irvine, K. D. (2002). Regulation of notch signaling by o-linked fucose. Cell 111, 893-904.
    • (2002) Cell , vol.111 , pp. 893-904
    • Okajima, T.1    Irvine, K.A.2
  • 54
    • 0028722641 scopus 로고
    • Imaging neuronal subsets and other cell types in whole mount drosophila embryos and larvae using antibody probes
    • (ed. L. S. B. Goldstein and E. Fyrberg). San Diego: Academic Press
    • Patel, N. H. (1994). Imaging Neuronal Subsets and Other Cell Types in Whole Mount Drosophila Embryos and Larvae Using Antibody Probes. In Drosophila melanogaster: Practical Uses in Cell and Molecular Biology, vol. 44 (ed. L. S. B. Goldstein and E. Fyrberg), pp. 445-487. San Diego: Academic Press.
    • (1994) Drosophila Melanogaster: Practical Uses in Cell and Molecular Biology , vol.44 , pp. 445-487
    • Patel, N.H.1
  • 56
    • 15544382255 scopus 로고    scopus 로고
    • Kinases regulating Golgi apparatus structure and function
    • Preisinger, C. and Barr, F. A. (2005). Kinases regulating Golgi apparatus structure and function. Biochem. Soc. Symp. 72, 15-30.
    • (2005) Biochem. Soc. Symp. , vol.72 , pp. 15-30
    • Preisinger, C.1    Barr, F.A.2
  • 57
    • 71149117138 scopus 로고    scopus 로고
    • A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1
    • Ren, Y., Yip, C. K., Tripathi, A., Huie, D., Jeffrey, P. D., Walz, T. and Hughson, F. M. (2009). A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1. Cell 139, 1119-1129.
    • (2009) Cell , vol.139 , pp. 1119-1129
    • Ren, Y.1    Yip, C.K.2    Tripathi, A.3    Huie, D.4    Jeffrey, P.D.5    Walz, T.6    Hughson, F.A.7
  • 58
    • 33645641542 scopus 로고    scopus 로고
    • Modulation of neural carbohydrate epitope expression in Drosophila melanogaster cells
    • Rendic, D., Linder, A., Paschinger, K., Borth, N., Wilson, I. B. and Fabini, G. (2006). Modulation of neural carbohydrate epitope expression in Drosophila melanogaster cells. J. Biol. Chem. 281, 3343-3353.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3343-3353
    • Rendic, D.1    Linder, A.2    Paschinger, K.3    Borth, N.4    Wilson, I.B.5    Fabini, G.6
  • 59
    • 77957850844 scopus 로고    scopus 로고
    • Neural-specific alpha3-fucosylation of N-linked glycans in the Drosophila embryo requires fucosyltransferase A and influences developmental signaling associated with Oglycosylation
    • Rendic, D., Sharrow, M., Katoh, T., Overcarsh, B., Nguyen, K., Kapurch, J., Aoki, K., Wilson, I. B. and Tiemeyer, M. (2010). Neural-specific alpha3-fucosylation of N-linked glycans in the Drosophila embryo requires fucosyltransferase A and influences developmental signaling associated with Oglycosylation. Glycobiology 20, 1353-1365.
    • (2010) Glycobiology , vol.20 , pp. 1353-1365
    • Rendic, D.1    Sharrow, M.2    Katoh, T.3    Overcarsh, B.4    Nguyen, K.5    Kapurch, J.6    Aoki, K.7    Wilson, I.B.8    Tiemeyer, M.9
  • 61
    • 0022616860 scopus 로고
    • Expression of several adhesive macromolecules (N-CAM, L1, J1, NILE, uvomorulin, laminin, fibronectin, and a heparan sulfate proteoglycan) in embryonic, adult, and denervated adult skeletal muscle
    • Sanes, J. R., Schachner, M. and Covault, J. (1986). Expression of several adhesive macromolecules (N-CAM, L1, J1, NILE, uvomorulin, laminin, fibronectin, and a heparan sulfate proteoglycan) in embryonic, adult, and denervated adult skeletal muscle. J. Cell Biol. 102, 420-431.
    • (1986) J. Cell Biol. , vol.102 , pp. 420-431
    • Sanes, J.R.1    Schachner, M.2    Covault, J.3
  • 62
    • 33744951303 scopus 로고    scopus 로고
    • Null mutations in Drosophila Nacetylglucosaminyltransferase i produce defects in locomotion and a reduced life span
    • Sarkar, M., Leventis, P. A., Silvescu, C. I., Reinhold, V. N., Schachter, H. and Boulianne, G. L. (2006). Null mutations in Drosophila Nacetylglucosaminyltransferase I produce defects in locomotion and a reduced life span. J. Biol. Chem. 281, 12776-12785.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12776-12785
    • Sarkar, M.1    Leventis, P.A.2    Silvescu, C.I.3    Reinhold, V.N.4    Schachter, H.5    Boulianne, G.A.6
  • 63
    • 0020328414 scopus 로고
    • Cell type specificity of a neural cell surface antigen recognized by the monoclonal antibody A2B5
    • Schnitzer, J. and Schachner, M. (1982). Cell type specificity of a neural cell surface antigen recognized by the monoclonal antibody A2B5. Cell Tissue Res. 224, 625-636.
    • (1982) Cell Tissue Res. , vol.224 , pp. 625-636
    • Schnitzer, J.1    Schachner, M.2
  • 65
    • 0037383779 scopus 로고    scopus 로고
    • Induction of neuron-specific glycosylation by Tollo/Toll-8, a Drosophila Toll-like receptor expressed in non-neural cells
    • Seppo, A., Matani, P., Sharrow, M. and Tiemeyer, M. (2003). Induction of neuron-specific glycosylation by Tollo/Toll-8, a Drosophila Toll-like receptor expressed in non-neural cells. Development 130, 1439-1448.
    • (2003) Development , vol.130 , pp. 1439-1448
    • Seppo, A.1    Matani, P.2    Sharrow, M.3    Tiemeyer, M.4
  • 66
    • 20544455617 scopus 로고    scopus 로고
    • Golgins and GTPases, giving identity and structure to the Golgi apparatus
    • Short, B., Haas, A. and Barr, F. A. (2005). Golgins and GTPases, giving identity and structure to the Golgi apparatus. Biochim. Biophys. Acta 1744, 383-395.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 383-395
    • Short, B.1    Haas, A.2    Barr, F.A.3
  • 67
    • 58149181656 scopus 로고    scopus 로고
    • Golgi coiledcoil proteins contain multiple binding sites for Rab family G proteins
    • Sinka, R., Gillingham, A. K., Kondylis, V. and Munro, S. (2008). Golgi coiledcoil proteins contain multiple binding sites for Rab family G proteins. J. Cell Biol. 183, 607-615.
    • (2008) J. Cell Biol. , vol.183 , pp. 607-615
    • Sinka, R.1    Gillingham, A.K.2    Kondylis, V.3    Munro, S.4
  • 68
    • 0023475207 scopus 로고
    • Neuralspecific carbohydrate moiety shared by many surface glycoproteins in Drosophila and grasshopper embryos
    • Snow, P. M., Patel, N. H., Harrelson, A. L. and Goodman, C. S. (1987). Neuralspecific carbohydrate moiety shared by many surface glycoproteins in Drosophila and grasshopper embryos. J. Neurosci. 7, 4137-4144.
    • (1987) J. Neurosci. , vol.7 , pp. 4137-4144
    • Snow, P.M.1    Patel, N.H.2    Harrelson, A.L.3    Goodman, C.S.4
  • 69
    • 0031460148 scopus 로고    scopus 로고
    • The mechanism of Golgi segregation during mitosis is cell type-specific
    • Stanley, H., Botas, J. and Malhotra, V. (1997). The mechanism of Golgi segregation during mitosis is cell type-specific. Proc. Natl. Acad. Sci. USA 94, 14467-14470.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14467-14470
    • Stanley, H.1    Botas, J.2    Malhotra, V.3
  • 70
    • 70450223107 scopus 로고    scopus 로고
    • Role of vesicle tethering factors in the ER-Golgi membrane traffic
    • Sztul, E. and Lupashin, V. (2009). Role of vesicle tethering factors in the ER-Golgi membrane traffic. FEBS Lett. 583, 3770-3783.
    • (2009) FEBS Lett. , vol.583 , pp. 3770-3783
    • Sztul, E.1    Lupashin, V.2
  • 71
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides
    • Varki, A. (1993). Biological roles of oligosaccharides. Glycobiology 3, 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 73
    • 33644870049 scopus 로고    scopus 로고
    • Bruchpilot, a protein with homology to ELKS/CAST, is required for structural integrity and function of synaptic active zones in Drosophila
    • Wagh, D. A., Rasse, T. M., Asan, E., Hofbauer, A., Schwenkert, I., Dürrbeck, H., Buchner, S., Dabauvalle, M. C., Schmidt, M., Qin, G. et al. (2006). Bruchpilot, a protein with homology to ELKS/CAST, is required for structural integrity and function of synaptic active zones in Drosophila. Neuron 49, 833-844.
    • (2006) Neuron , vol.49 , pp. 833-844
    • Wagh, D.A.1    Rasse, T.M.2    Asan, E.3    Hofbauer, A.4    Schwenkert, I.5    Dürrbeck, H.6    Buchner, S.7    Dabauvalle, M.C.8    Schmidt, M.9    Qin, G.10
  • 74
    • 51949089167 scopus 로고    scopus 로고
    • The Tsc1-Tsc2 complex influences neuronal polarity by modulating TORC1 activity and SAD levels
    • Wildonger, J., Jan, L. Y. and Jan, Y. N. (2008). The Tsc1-Tsc2 complex influences neuronal polarity by modulating TORC1 activity and SAD levels. Genes Dev. 22, 2447-2453.
    • (2008) Genes Dev. , vol.22 , pp. 2447-2453
    • Wildonger, J.1    Jan, L.Y.2    Jan, Y.A.3
  • 76
    • 0035946992 scopus 로고    scopus 로고
    • Regulation of glycosyltransferases in ganglioside biosynthesis by phosphorylation and dephosphorylation
    • Yu, R. K. and Bieberich, E. (2001). Regulation of glycosyltransferases in ganglioside biosynthesis by phosphorylation and dephosphorylation. Mol. Cell. Endocrinol. 177, 19-24.
    • (2001) Mol. Cell. Endocrinol. , vol.177 , pp. 19-24
    • Yu, R.K.1    Bieberich, E.2
  • 77
    • 0037137494 scopus 로고    scopus 로고
    • Hereditary multiple exostoses and heparan sulfate polymerization
    • Zak, B. M., Crawford, B. E. and Esko, J. D. (2002). Hereditary multiple exostoses and heparan sulfate polymerization. Biochim. Biophys. Acta 1573, 346-355.
    • (2002) Biochim. Biophys. Acta , vol.1573 , pp. 346-355
    • Zak, B.M.1    Crawford, B.E.2    Esko, J.A.3


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