메뉴 건너뛰기




Volumn 9, Issue 5, 2016, Pages 513-527

Synaptic roles for phosphomannomutase type 2 in a new Drosophila congenital disorder of glycosylation disease model

Author keywords

Matrix metalloproteinase; Neuromuscular junction; Neurotransmission; Synapse; Synaptomatrix; Trans synaptic signaling; Wnt

Indexed keywords

GELATINASE A; MATRIX METALLOPROTEINASE; PHOSPHOMANNOMUTASE; PHOSPHOMANNOMUTASE TYPE 2; PROTEOHEPARAN SULFATE; UNCLASSIFIED DRUG; WNT PROTEIN; DROSOPHILA PROTEIN; GLYCOPROTEIN; MUTASE; OLIGOSACCHARIDE; PMM2 PROTEIN, DROSOPHILA; POLYSACCHARIDE;

EID: 84966460670     PISSN: 17548403     EISSN: 17548411     Source Type: Journal    
DOI: 10.1242/dmm.022939     Document Type: Article
Times cited : (28)

References (88)
  • 2
    • 0034838433 scopus 로고    scopus 로고
    • Genetic model organisms in the study of N-glycans
    • Altmann, F., Fabini, G., Ahorn, H. and Wilson, I. B. H. (2001). Genetic model organisms in the study of N-glycans. Biochimie 83, 703-712.
    • (2001) Biochimie , vol.83 , pp. 703-712
    • Altmann, F.1    Fabini, G.2    Ahorn, H.3    Wilson, I.B.H.4
  • 3
    • 84918564491 scopus 로고    scopus 로고
    • Conformational response to ligand binding in phosphomannomutase2: Insights into inborn glycosylation disorder
    • Andreotti, G., Cabeza de Vaca, I., Poziello, A., Monti, M. C., Guallar, V. and Cubellis, M. V. (2014). Conformational response to ligand binding in phosphomannomutase2: insights into inborn glycosylation disorder. J. Biol. Chem. 289, 34900-34910.
    • (2014) J. Biol. Chem. , vol.289 , pp. 34900-34910
    • Andreotti, G.1    Cabeza-De-Vaca, I.2    Poziello, A.3    Monti, M.C.4    Guallar, V.5    Cubellis, M.V.6
  • 4
    • 34247849493 scopus 로고    scopus 로고
    • Dynamic developmental elaboration of N-linked glycan complexity in the Drosophila melanogaster embryo
    • Aoki, K., Perlman, M., Lim, J.-M., 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.-M.3    Cantu, R.4    Wells, L.5    Tiemeyer, M.6
  • 6
    • 40249094509 scopus 로고    scopus 로고
    • Rapid activity-dependent modifications in synaptic structure and function require bidirectional Wnt signaling
    • Ataman, B., Ashley, J., Gorczyca, M., Ramachandran, P., Fouquet, W., Sigrist, S. J. and Budnik, V. (2008). Rapid activity-dependent modifications in synaptic structure and function require bidirectional Wnt signaling. Neuron 57, 705-718.
    • (2008) Neuron , vol.57 , pp. 705-718
    • Ataman, B.1    Ashley, J.2    Gorczyca, M.3    Ramachandran, P.4    Fouquet, W.5    Sigrist, S.J.6    Budnik, V.7
  • 7
    • 84926616856 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation with emphasis on cerebellar involvement
    • Barone, R., Fiumara, A. and Jaeken, J. (2014). Congenital disorders of glycosylation with emphasis on cerebellar involvement. Semin. Neurol. 34, 357-366.
    • (2014) Semin. Neurol. , vol.34 , pp. 357-366
    • Barone, R.1    Fiumara, A.2    Jaeken, J.3
  • 8
    • 84926685520 scopus 로고    scopus 로고
    • A nationwide survey of PMM2-CDG in Italy: High frequency of a mild neurological variant associated with the L32R mutation
    • Barone, R., Carrozzi, M., Parini, R., Battini, R., Martinelli, D., Elia, M., Spada, M., Lilliu, F., Ciana, G., Burlina, A. et al. (2015). A nationwide survey of PMM2-CDG in Italy: high frequency of a mild neurological variant associated with the L32R mutation. J. Neurol. 262, 154-164.
    • (2015) J. Neurol. , vol.262 , pp. 154-164
    • Barone, R.1    Carrozzi, M.2    Parini, R.3    Battini, R.4    Martinelli, D.5    Elia, M.6    Spada, M.7    Lilliu, F.8    Ciana, G.9    Burlina, A.10
  • 9
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand, A. H. and Perrimon, N. (1993). Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 118, 401-415.
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 10
    • 84868248946 scopus 로고    scopus 로고
    • A zebrafish model of PMM2-CDG reveals altered neurogenesis and a substrate-accumulation mechanism for N-linked glycosylation deficiency
    • Cline, A., Gao, N., Flanagan-Steet, H., Sharma, V., Rosa, S., Sonon, R., Azadi, P., Sadler, K. C., Freeze, H. H., Lehrman, M. A. et al. (2012). A zebrafish model of PMM2-CDG reveals altered neurogenesis and a substrate-accumulation mechanism for N-linked glycosylation deficiency. Mol. Biol. Cell. 23, 4175-4187.
    • (2012) Mol. Biol. Cell. , vol.23 , pp. 4175-4187
    • Cline, A.1    Gao, N.2    Flanagan-Steet, H.3    Sharma, V.4    Rosa, S.5    Sonon, R.6    Azadi, P.7    Sadler, K.C.8    Freeze, H.H.9    Lehrman, M.A.10
  • 11
    • 84884299773 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation. Part I. Defects of protein N-glycosylation
    • Cylwik, B., Naklicki, M., Chrostek, L. and Gruszewska, E. (2013). Congenital disorders of glycosylation. Part I. Defects of protein N-glycosylation. Acta Biochim. Pol. 60, 151-161.
    • (2013) Acta Biochim. Pol. , vol.60 , pp. 151-161
    • Cylwik, B.1    Naklicki, M.2    Chrostek, L.3    Gruszewska, E.4
  • 12
    • 83455236106 scopus 로고    scopus 로고
    • Glycosylated synaptomatrix regulation of transsynaptic signaling
    • Dani, N. and Broadie, K. (2012). Glycosylated synaptomatrix regulation of transsynaptic signaling. Dev. Neurobiol. 72, 2-21.
    • (2012) Dev. Neurobiol. , vol.72 , pp. 2-21
    • Dani, N.1    Broadie, K.2
  • 13
    • 84870690924 scopus 로고    scopus 로고
    • A targeted glycan-related gene screen reveals heparan sulfate proteoglycan sulfation regulates WNT and BMP trans-synaptic signaling
    • Dani, N., Nahm, M., Lee, S. and Broadie, K. (2012). A targeted glycan-related gene screen reveals heparan sulfate proteoglycan sulfation regulates WNT and BMP trans-synaptic signaling. PLoS Genet. 8, e1003031.
    • (2012) PLoS Genet , vol.8 , pp. e1003031
    • Dani, N.1    Nahm, M.2    Lee, S.3    Broadie, K.4
  • 14
    • 84907298254 scopus 로고    scopus 로고
    • Two protein N-acetylgalactosaminyl transferases regulate synaptic plasticity by activity-dependent regulation of integrin signaling
    • Dani, N., Zhu, H. and Broadie, K. (2014). Two protein N-acetylgalactosaminyl transferases regulate synaptic plasticity by activity-dependent regulation of integrin signaling. J. Neurosci. 34, 13047-13065.
    • (2014) J. Neurosci. , vol.34 , pp. 13047-13065
    • Dani, N.1    Zhu, H.2    Broadie, K.3
  • 17
    • 84953431930 scopus 로고    scopus 로고
    • Two classes of matrix metalloproteinases reciprocally regulate synaptogenesis
    • Dear, M. L., Dani, N., Parkinson, W., Zhou, S. and Broadie, K. (2016). Two classes of matrix metalloproteinases reciprocally regulate synaptogenesis. Development 143, 75-87.
    • (2016) Development , vol.143 , pp. 75-87
    • Dear, M.L.1    Dani, N.2    Parkinson, W.3    Zhou, S.4    Broadie, K.5
  • 18
    • 84893734160 scopus 로고    scopus 로고
    • Solving glycosylation disorders: Fundamental approaches reveal complicated pathways
    • Freeze, H. H., Chong, J. X., Bamshad, M. J. and Ng, B. G. (2014). Solving glycosylation disorders: fundamental approaches reveal complicated pathways. Am. J. Hum. Genet. 94, 161-175.
    • (2014) Am. J. Hum. Genet , vol.94 , pp. 161-175
    • Freeze, H.H.1    Chong, J.X.2    Bamshad, M.J.3    Ng, B.G.4
  • 20
    • 84888878289 scopus 로고    scopus 로고
    • Fragile X mental retardation protein regulates trans-synaptic signaling in Drosophila
    • Friedman, S. H., Dani, N., Rushton, E. and Broadie, K. (2013). Fragile X mental retardation protein regulates trans-synaptic signaling in Drosophila. Dis. Model. Mech. 6, 1400-1413.
    • (2013) Dis. Model. Mech. , vol.6 , pp. 1400-1413
    • Friedman, S.H.1    Dani, N.2    Rushton, E.3    Broadie, K.4
  • 22
    • 84855512490 scopus 로고    scopus 로고
    • Drosophila modeling of heritable neurodevelopmental disorders
    • Gatto, C. L. and Broadie, K. (2011). Drosophila modeling of heritable neurodevelopmental disorders. Curr. Opin. Neurobiol. 21, 834-841.
    • (2011) Curr. Opin. Neurobiol. , vol.21 , pp. 834-841
    • Gatto, C.L.1    Broadie, K.2
  • 23
    • 84875352766 scopus 로고    scopus 로고
    • Neural circuits for peristaltic wave propagation in crawling Drosophila larvae: Analysis and modeling
    • Gjorgjieva, J., Berni, J., Evers, J. F. and Eglen, S. J. (2013). Neural circuits for peristaltic wave propagation in crawling Drosophila larvae: analysis and modeling. Front. Comput. Neurol. 7, 24.
    • (2013) Front. Comput. Neurol. , vol.7 , pp. 24
    • Gjorgjieva, J.1    Berni, J.2    Evers, J.F.3    Eglen, S.J.4
  • 24
    • 62449085119 scopus 로고    scopus 로고
    • Distinct functions for the catalytic and hemopexin domains of a Drosophila matrix metalloproteinase
    • Glasheen, B. M., Kabra, A. T. and Page-McCaw, A. (2009). Distinct functions for the catalytic and hemopexin domains of a Drosophila matrix metalloproteinase. Proc. Natl. Acad. Sci. USA 106, 2659-2664.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 2659-2664
    • Glasheen, B.M.1    Kabra, A.T.2    Page-McCaw, A.3
  • 25
    • 77955272997 scopus 로고    scopus 로고
    • A matrix metalloproteinase mediates airway remodeling in Drosophila
    • Glasheen, B. M., Robbins, R. M., Piette, C., Beitel, G. J. and Page-McCaw, A. (2010). A matrix metalloproteinase mediates airway remodeling in Drosophila. Dev. Biol. 344, 772-783.
    • (2010) Dev. Biol. , vol.344 , pp. 772-783
    • Glasheen, B.M.1    Robbins, R.M.2    Piette, C.3    Beitel, G.J.4    Page-McCaw, A.5
  • 26
    • 0033861140 scopus 로고    scopus 로고
    • Inflated wings, tissue autolysis and early death in tissue inhibitor of metalloproteinases mutants of Drosophila
    • Godenschwege, T. A., Pohar, N., Buchner, S. and Buchner, E. (2000). Inflated wings, tissue autolysis and early death in tissue inhibitor of metalloproteinases mutants of Drosophila. Eur. J. Cell Biol. 79, 495-501.
    • (2000) Eur. J. Cell Biol. , vol.79 , pp. 495-501
    • Godenschwege, T.A.1    Pohar, N.2    Buchner, S.3    Buchner, E.4
  • 28
    • 70349089028 scopus 로고    scopus 로고
    • The clinical spectrum of phosphomannomutase 2 deficiency (CDG-Ia)
    • Grünewald, S. (2009). The clinical spectrum of phosphomannomutase 2 deficiency (CDG-Ia). Biochim. Biophys. Acta. 1792, 827-834.
    • (2009) Biochim. Biophys. Acta. , vol.1792 , pp. 827-834
    • Grünewald, S.1
  • 29
    • 71749102704 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: An update on defects affecting the biosynthesis of dolichol-linked oligosaccharides
    • Haeuptle, M. A. and Hennet, T. (2009). Congenital disorders of glycosylation: an update on defects affecting the biosynthesis of dolichol-linked oligosaccharides. Hum. Mutat. 30, 1628-1641.
    • (2009) Hum. Mutat. , vol.30 , pp. 1628-1641
    • Haeuptle, M.A.1    Hennet, T.2
  • 30
    • 84945351446 scopus 로고    scopus 로고
    • Lack of phosphomannomutase 2 affects Xenopus laevis morphogenesis and the non-canonical Wnt5a/Ror2 signalling
    • Himmelreich, N., Kaufmann, L. T., Steinbeisser, H., Körner, C. and Thiel, C. (2015). Lack of phosphomannomutase 2 affects Xenopus laevis morphogenesis and the non-canonical Wnt5a/Ror2 signalling. Inherit. Metab. Dis. 38, 1137-1146.
    • (2015) Inherit. Metab. Dis. , vol.38 , pp. 1137-1146
    • Himmelreich, N.1    Kaufmann, L.T.2    Steinbeisser, H.3    Körner, C.4    Thiel, C.5
  • 31
    • 78650401291 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation
    • Jaeken, J. (2010). Congenital disorders of glycosylation. Ann. N. Y. Acad. Sci. 1214, 190-198.
    • (2010) Ann. N. Y. Acad. Sci. , vol.1214 , pp. 190-198
    • Jaeken, J.1
  • 32
    • 84876835227 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation
    • Jaeken, J. (2013). Congenital disorders of glycosylation. Handb. Clin. Neurol. 113, 1737-1743.
    • (2013) Handb. Clin. Neurol. , vol.113 , pp. 1737-1743
    • Jaeken, J.1
  • 33
    • 0000249979 scopus 로고
    • Familial psychomotor retardation with markedly fluctuating serum prolactin, FSH and GH levels, partial TBG-deficiency, increased serum arylsulphatase A and increased CSF protein: A new syndrome?
    • Jaeken, J., Vanderschueren-Lodeweyckx, M., Casaer, P., Snoeck, L., Corbeel, L., Eggermont, E. and Eeckels, R. (1980). Familial psychomotor retardation with markedly fluctuating serum prolactin, FSH and GH levels, partial TBG-deficiency, increased serum arylsulphatase A and increased CSF protein: a new syndrome? Pediatr. Res. 14, 179.
    • (1980) Pediatr. Res. , vol.14 , pp. 179
    • Jaeken, J.1    Vanderschueren-Lodeweyckx, M.2    Casaer, P.3    Snoeck, L.4    Corbeel, L.5    Eggermont, E.6    Eeckels, R.7
  • 34
    • 84947982717 scopus 로고    scopus 로고
    • Mmp1 and Mmp2 cooperatively induce Drosophila fat body cell dissociation with distinct roles
    • Jia, Q., Liu, Y., Liu, H. and Li, S. (2014). Mmp1 and Mmp2 cooperatively induce Drosophila fat body cell dissociation with distinct roles. Sci. Rep. 4, 7535.
    • (2014) Sci. Rep. , vol.4 , pp. 7535
    • Jia, Q.1    Liu, Y.2    Liu, H.3    Li, S.4
  • 35
    • 84919645000 scopus 로고    scopus 로고
    • Overelaborated synaptic architecture and reduced synaptomatrix glycosylation in a Drosophila classic galactosemia disease model
    • Jumbo-Lucioni, P., Parkinson, W. and Broadie, K. (2014). Overelaborated synaptic architecture and reduced synaptomatrix glycosylation in a Drosophila classic galactosemia disease model. Dis. Model. Mech. 7, 1365-1378.
    • (2014) Dis. Model. Mech. , vol.7 , pp. 1365-1378
    • Jumbo-Lucioni, P.1    Parkinson, W.2    Broadie, K.3
  • 36
    • 84872712215 scopus 로고    scopus 로고
    • The N's and O's of Drosophila glycoprotein glycobiology
    • Katoh, T. and Tiemeyer, M. (2013). The N's and O's of Drosophila glycoprotein glycobiology. Glycoconj. J. 30, 57-66.
    • (2013) Glycoconj. J. , vol.30 , pp. 57-66
    • Katoh, T.1    Tiemeyer, M.2
  • 37
    • 84887928744 scopus 로고    scopus 로고
    • Deficiency of α-glucosidase I alters glycoprotein glycosylation and lifespan in Caenorhabditis elegans
    • Katoh, T., Takase, J., Tani, Y., Amamoto, R., Aoshima, N., Tiemeyer, M., Yamamoto, K. and Ashida, H. (2013). Deficiency of α-glucosidase I alters glycoprotein glycosylation and lifespan in Caenorhabditis elegans. Glycobiology 23, 1142-1151.
    • (2013) Glycobiology , vol.23 , pp. 1142-1151
    • Katoh, T.1    Takase, J.2    Tani, Y.3    Amamoto, R.4    Aoshima, N.5    Tiemeyer, M.6    Yamamoto, K.7    Ashida, H.8
  • 39
    • 77950931419 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Regulators of the tumor microenvironment
    • Kessenbrock, K., Plaks, V. and Werb, Z. (2010). Matrix metalloproteinases: regulators of the tumor microenvironment. Cell 141, 52-67.
    • (2010) Cell , vol.141 , pp. 52-67
    • Kessenbrock, K.1    Plaks, V.2    Werb, Z.3
  • 41
    • 84923252813 scopus 로고    scopus 로고
    • A group of segmental premotor interneurons regulates the speed of axial locomotion in Drosophila larvae
    • Kohsaka, H., Takasu, E., Morimoto, T. and Nose, A. (2014). A group of segmental premotor interneurons regulates the speed of axial locomotion in Drosophila larvae. Curr. Biol. 24, 2632-2642.
    • (2014) Curr. Biol. , vol.24 , pp. 2632-2642
    • Kohsaka, H.1    Takasu, E.2    Morimoto, T.3    Nose, A.4
  • 42
    • 36248936100 scopus 로고    scopus 로고
    • Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster
    • Koles, K., Lim, J.-M., Aoki, K., Porterfield, M., Tiemeyer, M., Wells, L. and Panin, V. (2007). Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster. Glycobiology 17, 1388-1403.
    • (2007) Glycobiology , vol.17 , pp. 1388-1403
    • Koles, K.1    Lim, J.-M.2    Aoki, K.3    Porterfield, M.4    Tiemeyer, M.5    Wells, L.6    Panin, V.7
  • 43
    • 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
  • 44
    • 0028147879 scopus 로고
    • Ectopic and increased expression of Fasciclin II alters motoneuron growth cone guidance
    • Lin, D. M. and Goodman, C. S. (1994). Ectopic and increased expression of Fasciclin II alters motoneuron growth cone guidance. Neuron 13, 507-523.
    • (1994) Neuron , vol.13 , pp. 507-523
    • Lin, D.M.1    Goodman, C.S.2
  • 45
    • 0034680919 scopus 로고    scopus 로고
    • Dm1-MMP, a matrix metalloproteinase from Drosophila with a potential role in extracellular matrix remodeling during neural development
    • Llano, E., Pendás, A. M., Aza-Blanc, P., Kornberg, T. B. and López-Otín, C. (2000). Dm1-MMP, a matrix metalloproteinase from Drosophila with a potential role in extracellular matrix remodeling during neural development. J. Biol. Chem. 275, 35978-35985.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35978-35985
    • Llano, E.1    Pendás, A.M.2    Aza-Blanc, P.3    Kornberg, T.B.4    López-Otín, C.5
  • 46
    • 0037189532 scopus 로고    scopus 로고
    • Structural and enzymatic characterization of Drosophila Dm2-MMP, a membrane-bound matrix metalloproteinase with tissue-specific expression
    • Llano, E., Adam, G., Pendás, A. M., Quesada, V., Sánchez, L. M., Santamariá, I., Noselli, S. and López-Otín, C. (2002). Structural and enzymatic characterization of Drosophila Dm2-MMP, a membrane-bound matrix metalloproteinase with tissue-specific expression. J. Biol. Chem. 277, 23321-23329.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23321-23329
    • Llano, E.1    Adam, G.2    Pendás, A.M.3    Quesada, V.4    Sánchez, L.M.5    Santamariá, I.6    Noselli, S.7    López-Otín, C.8
  • 47
    • 22744434107 scopus 로고    scopus 로고
    • Calories do not explain extension of life span by dietary restriction in Drosophila
    • Mair, W., Piper, M. D. W. and Partridge, L. (2005). Calories do not explain extension of life span by dietary restriction in Drosophila. PLoS Biol. 3, e223.
    • (2005) PLoS Biol. , vol.3 , pp. e223
    • Mair, W.1    Piper, M.D.W.2    Partridge, L.3
  • 48
    • 0037605951 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: Review of their molecular bases, clinical presentations and specific therapies
    • Marquardt, T. and Denecke, J. (2003). Congenital disorders of glycosylation: review of their molecular bases, clinical presentations and specific therapies. Eur. J. Pediatr. 162, 359-379.
    • (2003) Eur. J. Pediatr. , vol.162 , pp. 359-379
    • Marquardt, T.1    Denecke, J.2
  • 49
    • 3042585525 scopus 로고    scopus 로고
    • Glycobiology of the neuromuscular junction
    • Martin, P. T. (2003). Glycobiology of the neuromuscular junction. J. Neurocyt. 32, 915-929.
    • (2003) J. Neurocyt. , vol.32 , pp. 915-929
    • Martin, P.T.1
  • 50
    • 28144441697 scopus 로고    scopus 로고
    • Wingless signaling at synapses is through cleavage and nuclear import of receptor DFrizzled2
    • Mathew, D., Ataman, B., Chen, J., Zhang, Y., Cumberledge, S. and Budnik, V. (2005). Wingless signaling at synapses is through cleavage and nuclear import of receptor DFrizzled2. Science 310, 1344-1347.
    • (2005) Science , vol.310 , pp. 1344-1347
    • Mathew, D.1    Ataman, B.2    Chen, J.3    Zhang, Y.4    Cumberledge, S.5    Budnik, V.6
  • 51
    • 0031981557 scopus 로고    scopus 로고
    • Lack of homozygotes for the most frequent disease allele in carbohydrate deficient glycoprotein syndrome type 1A
    • Matthijs, G., Schollen, E., Van Schaftingen, E., Cassiman, J.-J. and Jaeken, J. (1998). Lack of homozygotes for the most frequent disease allele in carbohydrate deficient glycoprotein syndrome type 1A. Am. J. Hum. Genet. 62, 542-550.
    • (1998) Am. J. Hum. Genet , vol.62 , pp. 542-550
    • Matthijs, G.1    Schollen, E.2    Van-Schaftingen, E.3    Cassiman, J.-J.4    Jaeken, J.5
  • 52
    • 0031836642 scopus 로고    scopus 로고
    • Mannose supplementation in carbohydrate-deficient glycoprotein syndrome type I and phosphomannomutase deficiency
    • Mayatepek, E. and Kohlmüller, D. (1998). Mannose supplementation in carbohydrate-deficient glycoprotein syndrome type I and phosphomannomutase deficiency. Eur. J. Pediatr. 157, 605-606.
    • (1998) Eur. J. Pediatr. , vol.157 , pp. 605-606
    • Mayatepek, E.1    Kohlmüller, D.2
  • 53
    • 33646748876 scopus 로고    scopus 로고
    • Restriction of amino acids extends lifespan in Drosophila melanogaster
    • Min, K.-J. and Tatar, M. (2006). Restriction of amino acids extends lifespan in Drosophila melanogaster. Mech. Ageing Dev. 127, 643-646.
    • (2006) Mech. Ageing Dev. , vol.127 , pp. 643-646
    • Min, K.-J.1    Tatar, M.2
  • 55
    • 78650748153 scopus 로고    scopus 로고
    • Regulation and functions of the lms homeobox gene during development of embryonic lateral transverse muscles and direct flight muscles in Drosophila
    • Müller, D., Jagla, T., Bodart, L. M., Jährling, N., Dodt, H.-U., Jagla, K. and Frasch, M. (2010). Regulation and functions of the lms homeobox gene during development of embryonic lateral transverse muscles and direct flight muscles in Drosophila. PLoS ONE 5, e14323.
    • (2010) PLoS ONE , vol.5 , pp. e14323
    • Müller, D.1    Jagla, T.2    Bodart, L.M.3    Jährling, N.4    Dodt, H.-U.5    Jagla, K.6    Frasch, M.7
  • 56
    • 84863746862 scopus 로고    scopus 로고
    • Methods to assay Drosophila behavior
    • Nichols, C. D., Becnel, J. and Pandey, U. B. (2012). Methods to assay Drosophila behavior. J. Vis. Exp. 61, e3795.
    • (2012) J. Vis. Exp. , vol.61 , pp. e3795
    • Nichols, C.D.1    Becnel, J.2    Pandey, U.B.3
  • 57
    • 0036848075 scopus 로고    scopus 로고
    • The Drosophila Wnt, wingless, provides an essential signal for pre- and postsynaptic differentiation
    • Packard, M., Koo, E. S., Gorczyca, M., Sharpe, J., Cumberledge, S. and Budnik, V. (2002). The Drosophila Wnt, wingless, provides an essential signal for pre- and postsynaptic differentiation. Cell 111, 319-330.
    • (2002) Cell , vol.111 , pp. 319-330
    • Packard, M.1    Koo, E.S.2    Gorczyca, M.3    Sharpe, J.4    Cumberledge, S.5    Budnik, V.6
  • 58
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • Page-McCaw, A., Ewald, A. J. and Werb, Z. (2007). Matrix metalloproteinases and the regulation of tissue remodelling. Nat. Rev. Mol. Cell Biol. 8, 221-233.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 221-233
    • Page-McCaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 59
    • 84888878912 scopus 로고    scopus 로고
    • N-glycosylation requirements in neuromuscular synaptogenesis
    • Parkinson, W., Dear, M. L., Rushton, E. and Broadie, K. (2013). N-glycosylation requirements in neuromuscular synaptogenesis. Development 140, 4970-4981.
    • (2013) Development , vol.140 , pp. 4970-4981
    • Parkinson, W.1    Dear, M.L.2    Rushton, E.3    Broadie, K.4
  • 60
    • 0345465698 scopus 로고    scopus 로고
    • Invertebrate tissue inhibitor of metalloproteinase: Structure and nested gene organization within the synapsin locus is conserved from Drosophila to human
    • Pohar, N., Godenschwege, T. A. and Buchner, E. (1999). Invertebrate tissue inhibitor of metalloproteinase: structure and nested gene organization within the synapsin locus is conserved from Drosophila to human. Genomics 57, 293-296.
    • (1999) Genomics , vol.57 , pp. 293-296
    • Pohar, N.1    Godenschwege, T.A.2    Buchner, E.3
  • 61
    • 0034837386 scopus 로고    scopus 로고
    • A systematic analysis of human disease-associated gene sequences in Drosophila
    • Reiter, L. T., Potocki, L., Chien, S., Gribskov, M. and Bier, E. (2001). A systematic analysis of human disease-associated gene sequences in Drosophila. Genome Res. 11, 1114-1125.
    • (2001) Genome Res. , vol.11 , pp. 1114-1125
    • Reiter, L.T.1    Potocki, L.2    Chien, S.3    Gribskov, M.4    Bier, E.5
  • 62
    • 79959350253 scopus 로고    scopus 로고
    • Extending life span by increasing oxidative stress
    • Ristow, M. and Schmeisser, S. (2011). Extending life span by increasing oxidative stress. Free Radic. Biol. Med. 51, 327-336.
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 327-336
    • Ristow, M.1    Schmeisser, S.2
  • 63
    • 35348976628 scopus 로고    scopus 로고
    • Presynaptic establishment of the synaptic cleft extracellular matrix is required for post-synaptic differentiation
    • Rohrbough, J., Rushton, E., Woodruff, E., III, Fergestad, T., Vigneswaran, K. and Broadie, K. (2007). Presynaptic establishment of the synaptic cleft extracellular matrix is required for post-synaptic differentiation. Genes Dev. 21, 2607-2628.
    • (2007) Genes Dev. , vol.21 , pp. 2607-2628
    • Rohrbough, J.1    Rushton, E.2    Woodruff, E.3    Fergestad, T.4    Vigneswaran, K.5    Broadie, K.6
  • 64
    • 84863589158 scopus 로고    scopus 로고
    • Structurefunction analysis of endogenous lectin mind-the-gap in synaptogenesis
    • Rushton, E., Rohrbough, J., Deutsch, K. and Broadie, K. (2012). Structurefunction analysis of endogenous lectin mind-the-gap in synaptogenesis. Dev. Neurobiol. 72, 1161-1179.
    • (2012) Dev. Neurobiol. , vol.72 , pp. 1161-1179
    • Rushton, E.1    Rohrbough, J.2    Deutsch, K.3    Broadie, K.4
  • 65
    • 33744951303 scopus 로고    scopus 로고
    • Null mutations in Drosophila N-acetylglucosaminyltransferase 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 N-acetylglucosaminyltransferase 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.L.6
  • 67
    • 84905483274 scopus 로고    scopus 로고
    • Out with the old, in with the new: Reassessing morpholino knockdowns in light of genome editing technology
    • Schulte-Merker, S. and Stainier, D. Y. R. (2014). Out with the old, in with the new: reassessing morpholino knockdowns in light of genome editing technology. Development 141, 3103-3104.
    • (2014) Development , vol.141 , pp. 3103-3104
    • Schulte-Merker, S.1    Stainier, D.Y.R.2
  • 68
    • 84911880613 scopus 로고    scopus 로고
    • N-glycosylation in regulation of the nervous system
    • Scott, H. and Panin, V. M. (2014a). N-glycosylation in regulation of the nervous system. Adv. Neurobiol. 9, 367-394.
    • (2014) Adv. Neurobiol. , vol.9 , pp. 367-394
    • Scott, H.1    Panin, V.M.2
  • 69
    • 84898737767 scopus 로고    scopus 로고
    • The role of protein N-glycosylation in neural transmission
    • Scott, H. and Panin, V. M. (2014b). The role of protein N-glycosylation in neural transmission. Glycobiology 24, 407-417.
    • (2014) Glycobiology , vol.24 , pp. 407-417
    • Scott, H.1    Panin, V.M.2
  • 70
    • 0033887691 scopus 로고    scopus 로고
    • Function and structure of Drosophila glycans
    • Seppo, A. and Tiemeyer, M. (2000). Function and structure of Drosophila glycans. Glycobiology 10, 751-760.
    • (2000) Glycobiology , vol.10 , pp. 751-760
    • Seppo, A.1    Tiemeyer, M.2
  • 71
    • 80655144748 scopus 로고    scopus 로고
    • Phosphomannose isomerase inhibitors improve Nglycosylation in selected phosphomannomutase-deficient fibroblasts
    • Sharma, V., Ichikawa, M., He, P., Bravo, Y., Dahl, R., Ng, B. G., Cosford, N. D. P. and Freeze, H. H. (2011). Phosphomannose isomerase inhibitors improve Nglycosylation in selected phosphomannomutase-deficient fibroblasts. J. Biol. Chem. 286, 39431-39438.
    • (2011) J. Biol. Chem. , vol.286 , pp. 39431-39438
    • Sharma, V.1    Ichikawa, M.2    He, P.3    Bravo, Y.4    Dahl, R.5    Ng, B.G.6    Cosford, N.D.P.7    Freeze, H.H.8
  • 72
    • 33744955343 scopus 로고    scopus 로고
    • The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a
    • Silvaggi, N. R., Zhang, C., Lu, Z., Dai, J., Dunaway-Mariano, D. and Allen, K. N. (2006). The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a. J. Biol. Chem. 281, 14918-14926.
    • (2006) J. Biol. Chem. , vol.281 , pp. 14918-14926
    • Silvaggi, N.R.1    Zhang, C.2    Lu, Z.3    Dai, J.4    Dunaway-Mariano, D.5    Allen, K.N.6
  • 73
    • 0018968051 scopus 로고
    • Foraging strategies of Drosophila melanogaster: A chromosomal analysis
    • Sokolowski, M. B. (1980). Foraging strategies of Drosophila melanogaster: a chromosomal analysis. Behav. Genet. 10, 291-302.
    • (1980) Behav. Genet , vol.10 , pp. 291-302
    • Sokolowski, M.B.1
  • 75
    • 84860852545 scopus 로고    scopus 로고
    • Nuclear envelope budding enables large ribonucleoprotein particle export during synaptic Wnt signaling
    • Speese, S. D., Ashley, J., Jokhi, V., Nunnari, J., Barria, R., Li, Y., Ataman, B., Koon, A., Chang, Y.-T., Li, Q. et al. (2012). Nuclear envelope budding enables large ribonucleoprotein particle export during synaptic Wnt signaling. Cell 149, 832-846.
    • (2012) Cell , vol.149 , pp. 832-846
    • Speese, S.D.1    Ashley, J.2    Jokhi, V.3    Nunnari, J.4    Barria, R.5    Li, Y.6    Ataman, B.7    Koon, A.8    Chang, Y.-T.9    Li, Q.10
  • 76
    • 67649839223 scopus 로고    scopus 로고
    • N-Glycans
    • (ed. A. Varki, R. D. Cummings, J. D. Esko, H. H. Freeze, P. Stanley, C. R. Bertozzi, G.W. Hart and M. E. Etzler), Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Stanley, P., Schachter, H. and Taniguchi, N. (2009). N-Glycans. In Essentials of Glycobiology (ed. A. Varki, R. D. Cummings, J. D. Esko, H. H. Freeze, P. Stanley, C. R. Bertozzi, G.W. Hart and M. E. Etzler), pp. 101-114. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (2009) Essentials of Glycobiology , pp. 101-114
    • Stanley, P.1    Schachter, H.2    Taniguchi, N.3
  • 77
    • 84925550191 scopus 로고    scopus 로고
    • Initial diagnosis of the congenital disorder of glycosylation PMM2-CDG (CDG1a) in a 4-year-old girl after neurosurgical intervention for cerebral hemorrhage
    • Stefanits, H., Konstantopoulou, V., Kuess, M., Milenkovic, I. and Matula, C. (2014). Initial diagnosis of the congenital disorder of glycosylation PMM2-CDG (CDG1a) in a 4-year-old girl after neurosurgical intervention for cerebral hemorrhage. J. Neurosurg. Pediatr. 14, 546-549.
    • (2014) J. Neurosurg. Pediatr. , vol.14 , pp. 546-549
    • Stefanits, H.1    Konstantopoulou, V.2    Kuess, M.3    Milenkovic, I.4    Matula, C.5
  • 78
    • 0035188727 scopus 로고    scopus 로고
    • How Matrix metalloproteinases regulate cell behavior
    • Sternlicht, M. D. and Werb, Z. (2001). How Matrix metalloproteinases regulate cell behavior. Annu. Rev. Cell Biol. 17, 463-516.
    • (2001) Annu. Rev. Cell Biol. , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 79
    • 58149343579 scopus 로고    scopus 로고
    • Glycobiology on the fly: Developmental and mechanistic insights from Drosophila
    • ten Hagen, K. G., Zhang, L., Tian, E. and Zhang, Y. (2009). Glycobiology on the fly: developmental and mechanistic insights from Drosophila. Glycobiology 2, 102-111.
    • (2009) Glycobiology , vol.2 , pp. 102-111
    • Ten Hagen, K.G.1    Zhang, L.2    Tian, E.3    Zhang, Y.4
  • 80
    • 84872688257 scopus 로고    scopus 로고
    • Therapies and therapeutic approaches in Congenital Disorders of Glycosylation
    • Thiel, C. and Körner, C. (2013). Therapies and therapeutic approaches in Congenital Disorders of Glycosylation. Glycoconj J. 30, 77-84.
    • (2013) Glycoconj J. , vol.30 , pp. 77-84
    • Thiel, C.1    Körner, C.2
  • 81
    • 33746578432 scopus 로고    scopus 로고
    • Targeted disruption of the mouse phosphomannomutase 2 gene causes early embryonic lethality
    • Thiel, C., Lübke, T., Matthijs, G., von Figura, K. and Körner, C. (2006). Targeted disruption of the mouse phosphomannomutase 2 gene causes early embryonic lethality. Mol. Cell. Biol. 26, 5615-5620.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5615-5620
    • Thiel, C.1    Lübke, T.2    Matthijs, G.3    Von Figura, K.4    Körner, C.5
  • 82
    • 0035853268 scopus 로고    scopus 로고
    • Increased alpha3-fucosylation of alpha(1)-acid glycoprotein in patients with congenital disorder of glycosylation type IA (CDG-Ia)
    • Van Dijk, W., Koeleman, C., Van het Hof, B., Poland, D., Jakobs, C. and Jaeken, J. (2001). Increased alpha3-fucosylation of alpha(1)-acid glycoprotein in patients with congenital disorder of glycosylation type IA (CDG-Ia). FEBS Lett. 494, 232-235.
    • (2001) FEBS Lett. , vol.494 , pp. 232-235
    • Van Dijk, W.1    Koeleman, C.2    Van-Het-Hof, B.3    Poland, D.4    Jakobs, C.5    Jaeken, J.6
  • 83
    • 0002495856 scopus 로고    scopus 로고
    • Historical background and overview
    • (ed. A. Varki, R. D. Cummings, J. D. Esko, H. H. Freeze, P. Stanley, C. R. Bertozzi, G.W. Hart and M. E. Etzler), Cold Spring Harbor, NY: Cold Spring Harbor Lab Press
    • Varki, A. and Sharon, N. (2009). Historical background and overview. In Essentials of Glycobiology (ed. A. Varki, R. D. Cummings, J. D. Esko, H. H. Freeze, P. Stanley, C. R. Bertozzi, G.W. Hart and M. E. Etzler), pp. 1-22. Cold Spring Harbor, NY: Cold Spring Harbor Lab Press.
    • (2009) Essentials of Glycobiology , pp. 1-22
    • Varki, A.1    Sharon, N.2
  • 84
    • 79953879681 scopus 로고    scopus 로고
    • Identification of phosphorylated oligosaccharides in cells of patients with a congenital disorders of glycosylation (CDG-I)
    • Vleugels, W., Duvet, S., Peanne, R., Mir, A.-M., Cacan, R., Michalski, J.-C., Matthijs, G. and Foulquier, F. (2011). Identification of phosphorylated oligosaccharides in cells of patients with a congenital disorders of glycosylation (CDG-I). Biochimie 93, 823-833.
    • (2011) Biochimie , vol.93 , pp. 823-833
    • Vleugels, W.1    Duvet, S.2    Peanne, R.3    Mir, A.-M.4    Cacan, R.5    Michalski, J.-C.6    Matthijs, G.7    Foulquier, F.8
  • 85
    • 84907752234 scopus 로고    scopus 로고
    • A matrix metalloproteinase mediates longdistance attenuation of stem cell proliferation
    • Wang, X. and Page-McCaw, A. (2014). A matrix metalloproteinase mediates longdistance attenuation of stem cell proliferation. J. Cell Biol. 206, 923-936.
    • (2014) J. Cell Biol. , vol.206 , pp. 923-936
    • Wang, X.1    Page-McCaw, A.2
  • 86
    • 84938973394 scopus 로고    scopus 로고
    • The effects of PMM2-CDG-causing mutations on the folding, activity, and stability of the PMM2 protein
    • Yuste-Checa, P., Gámez, A., Brasil, S., Desviat, L. R., Ugarte, M., Pérez-Cerdá, C. and Pérez, B. (2015). The effects of PMM2-CDG-causing mutations on the folding, activity, and stability of the PMM2 protein. Hum. Mutat. 36, 851-860.
    • (2015) Hum. Mutat. , vol.36 , pp. 851-860
    • Yuste-Checa, P.1    Gámez, A.2    Brasil, S.3    Desviat, L.R.4    Ugarte, M.5    Pérez-Cerdá, C.6    Pérez, B.7
  • 87
    • 0030959948 scopus 로고    scopus 로고
    • The held out wings (how) Drosophila gene encodes a putative RNA-binding protein involved in the control of muscular and cardiac activity
    • Zaffran, S., Astier, M., Gratecos, D. and Sémériva, M. (1997). The held out wings (how) Drosophila gene encodes a putative RNA-binding protein involved in the control of muscular and cardiac activity. Development 124, 2087-2098.
    • (1997) Development , vol.124 , pp. 2087-2098
    • Zaffran, S.1    Astier, M.2    Gratecos, D.3    Sémériva, M.4
  • 88
    • 70449523098 scopus 로고    scopus 로고
    • Uninflatable encodes a novel ectodermal apical surface protein required for tracheal inflation in Drosophila
    • Zhang, L. and Ward, R. E. (2009). uninflatable encodes a novel ectodermal apical surface protein required for tracheal inflation in Drosophila. Dev. Biol. 336, 201-212.
    • (2009) Dev. Biol. , vol.336 , pp. 201-212
    • Zhang, L.1    Ward, R.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.