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Volumn 20, Issue 1-3, 1996, Pages 139-144

Post-translational modifications in insect cells

Author keywords

insect cells; post translational modification; proteins

Indexed keywords


EID: 0029805551     PISSN: 09209069     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00350394     Document Type: Review
Times cited : (10)

References (43)
  • 1
    • 0027772780 scopus 로고
    • Processing of asparagine-linked oligosaccharides in insect cells. N-Acetylglucosaminyltransferase I and II activities in cultured lepidopteran cells
    • Altmann F, Kornfeld G, Dalik T, Staudacher E & Glössl I (1993) Processing of asparagine-linked oligosaccharides in insect cells. N-Acetylglucosaminyltransferase I and II activities in cultured lepidopteran cells. Glycobiology 3, 619-625.
    • (1993) Glycobiology , vol.3 , pp. 619-625
    • Altmann, F.1    Kornfeld, G.2    Dalik, T.3    Staudacher, E.4    Glössl, I.5
  • 2
    • 0019470313 scopus 로고
    • Steps in the biosynthesis of mosquito cell membrane glycoproteins and the effects of tunicamycin
    • Butters TD, Hughes, RC & Vischer P (1981) Steps in the biosynthesis of mosquito cell membrane glycoproteins and the effects of tunicamycin. Biochim. Biophys. Acta 640, 672-686.
    • (1981) Biochim. Biophys. Acta , vol.640 , pp. 672-686
    • Butters, T.D.1    Hughes, R.C.2    Vischer, P.3
  • 3
    • 84920298626 scopus 로고
    • The effect of glycosidase inhibition on the N-glycans of HIV gp 120 expressed in lepidopteran cells
    • Butters TD, Jones I, Clarke VA & Jacob GS (1991) The effect of glycosidase inhibition on the N-glycans of HIV gp 120 expressed in lepidopteran cells. Glycoconj. J. 8 240.
    • (1991) Glycoconj. J. , vol.8 , pp. 240
    • Butters, T.D.1    Jones, I.2    Clarke, V.A.3    Jacob, G.S.4
  • 4
    • 0025773714 scopus 로고
    • Asparagine-linked oligosaccharide processing in lepidopteran insect cells. Temporal dependence of the nature of the oligosaccharides assembled on asparagine-289 of recombinant human plasminogen produced in baculovirus vector infected Spodoptera frugiperda (IPLB-SF-21AE) cells
    • Davidson DJ & Castellino FJ (1991a) Asparagine-linked oligosaccharide processing in lepidopteran insect cells. Temporal dependence of the nature of the oligosaccharides assembled on asparagine-289 of recombinant human plasminogen produced in baculovirus vector infected Spodoptera frugiperda (IPLB-SF-21AE) cells. Biochemistry 30, 6167-6174.
    • (1991) Biochemistry , vol.30 , pp. 6167-6174
    • Davidson, D.J.1    Castellino, F.J.2
  • 5
    • 0025741695 scopus 로고
    • Structures of the asparagine-289-linked oligosaccharide assembled on recombinant human plasminogen expressed in a Mammestra brassicae cell line (IZD-MBO 503)
    • Davidson DJ & Castellino FJ (1991b) Structures of the asparagine-289-linked oligosaccharide assembled on recombinant human plasminogen expressed in a Mammestra brassicae cell line (IZD-MBO 503). Biochemistry 30, 6689-6696.
    • (1991) Biochemistry , vol.30 , pp. 6689-6696
    • Davidson, D.J.1    Castellino, F.J.2
  • 6
    • 0025996759 scopus 로고
    • α-Mannosidase-catalized trimming of high-mannosidase glycans in noninfected and baculovirus-infected Spodoptera frugiperda cells (IPBL-SF-21AE). A possible contributing regulatory mechanism for assembly of complextype oligosaccharides in infected cells
    • Davidson DJ, Bretthauer RK & Castellino FJ (1991) α-Mannosidase-catalized trimming of high-mannosidase glycans in noninfected and baculovirus-infected Spodoptera frugiperda cells (IPBL-SF-21AE). A possible contributing regulatory mechanism for assembly of complextype oligosaccharides in infected cells, Biochemistry 30, 9811-9815.
    • (1991) Biochemistry , vol.30 , pp. 9811-9815
    • Davidson, D.J.1    Bretthauer, R.K.2    Castellino, F.J.3
  • 7
    • 0025336176 scopus 로고
    • Oligosaccharide processing in the expression of human plasminogen cDNA by lepidopteran insect (Spodoptera frugiperda) cells
    • Davidson DJ, Fraser MJ & and Castellino FJ (1990) Oligosaccharide processing in the expression of human plasminogen cDNA by lepidopteran insect (Spodoptera frugiperda) cells. Biochemistry 29, 5584-5590.
    • (1990) Biochemistry , vol.29 , pp. 5584-5590
    • Davidson, D.J.1    Fraser, M.J.2    Castellino, F.J.3
  • 8
    • 0027428354 scopus 로고
    • Expression of the glycosylphosphatidylinositol-linked complement-inhibiting protein CD59 antigen in insect cells using a baculovirus vector
    • Davies A & Morgan BP (1993) Expression of the glycosylphosphatidylinositol-linked complement-inhibiting protein CD59 antigen in insect cells using a baculovirus vector. Biochem. J. 295, 889-896.
    • (1993) Biochem. J. , vol.295 , pp. 889-896
    • Davies, A.1    Morgan, B.P.2
  • 9
    • 0022515730 scopus 로고
    • Host cell mediated selection of a mutant influenza A virus that has lost a complex oligosaccharide from the tip of the hemagglutinin
    • Deom CM, Caton AJ & Schulze IT (1986) Host cell mediated selection of a mutant influenza A virus that has lost a complex oligosaccharide from the tip of the hemagglutinin. Proc. Natl. Acad. Sci. USA 83 3771-3775.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3771-3775
    • Deom, C.M.1    Caton, A.J.2    Schulze, I.T.3
  • 10
    • 0023159808 scopus 로고
    • Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains
    • Elbein AD (1987) Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains. Annu. Rev. Biochemistry 56, 497-534.
    • (1987) Annu. Rev. Biochemistry , vol.56 , pp. 497-534
    • Elbein, A.D.1
  • 12
    • 0021770329 scopus 로고
    • Regulation of asparagine-linked oligosaccharide processing. Oligosaccharide processing in Aedes albopictus mosquito cells
    • Hsieh P & Robbins PW (1984) Regulation of asparagine-linked oligosaccharide processing. Oligosaccharide processing in Aedes albopictus mosquito cells. J. Biol. Chem. 259, 2375-2382.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2375-2382
    • Hsieh, P.1    Robbins, P.W.2
  • 13
    • 0023226676 scopus 로고
    • Expression of envelope glycoproteins of human immunodeficiency virus by an insect virus vector
    • Hu S-L, Kosowski SG & Schaaf KF (1987) Expression of envelope glycoproteins of human immunodeficiency virus by an insect virus vector. J. Virol. 61, 3617-3620.
    • (1987) J. Virol. , vol.61 , pp. 3617-3620
    • Hu, S.-L.1    Kosowski, S.G.2    Schaaf, K.F.3
  • 15
    • 0001561789 scopus 로고
    • Activation cleavage in viral spike proteins by host proteases
    • (Winner E, ed.) Cold Spring Harbor Laboratory Press
    • Klenk H-D & Garten W (1995) Activation cleavage in viral spike proteins by host proteases. In: Cellular Receptors for Animal Viruses (Winner E, ed.) pp. 241-279. Cold Spring Harbor Laboratory Press.
    • (1995) Cellular Receptors for Animal Viruses , pp. 241-279
    • Klenk, H.-D.1    Garten, W.2
  • 16
    • 0023803844 scopus 로고
    • The molecular biology of influenza virus pathogenicity
    • Klenk HD & Rott R (1988) The molecular biology of influenza virus pathogenicity. Adv. Virus Res. 34, 247-281.
    • (1988) Adv. Virus Res. , vol.34 , pp. 247-281
    • Klenk, H.D.1    Rott, R.2
  • 17
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld R & Kornfeld S (1985) Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54, 631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 18
    • 0028078123 scopus 로고
    • Baculovirus infection does not alter N-glycosylation in Spodoptera frugiperda cells
    • Kretzschmar E, Geyer R & Klenk H-D (1994) Baculovirus infection does not alter N-glycosylation in Spodoptera frugiperda cells. Biol. Chem. Hoppe-Seyler. 375, 323-327.
    • (1994) Biol. Chem. Hoppe-Seyler. , vol.375 , pp. 323-327
    • Kretzschmar, E.1    Geyer, R.2    Klenk, H.-D.3
  • 19
    • 0025193736 scopus 로고
    • The oligosaccharides of influenza virus hemagglutinin expressed in insect cells by a baculovirus vector
    • Kuroda K, Geyer H, Geyer R, Doerfler W & Klenk H-D (1990) The oligosaccharides of influenza virus hemagglutinin expressed in insect cells by a baculovirus vector. Virology 174, 418-429.
    • (1990) Virology , vol.174 , pp. 418-429
    • Kuroda, K.1    Geyer, H.2    Geyer, R.3    Doerfler, W.4    Klenk, H.-D.5
  • 21
    • 0022729887 scopus 로고
    • Expression of the influenza virus haemagglutinin in insect cells by a baculovirus vector
    • Kuroda K, Hauser C, Rott R, Klenk H-D & Doerfler W (1986) Expression of the influenza virus haemagglutinin in insect cells by a baculovirus vector. EMBO J. 5, 1359-1365.
    • (1986) EMBO J. , vol.5 , pp. 1359-1365
    • Kuroda, K.1    Hauser, C.2    Rott, R.3    Klenk, H.-D.4    Doerfler, W.5
  • 22
    • 0025956827 scopus 로고
    • Retarded processing of influenza virus hemagglutinin in insect cells
    • Kuroda K, Veit M & Klenk H-D (1991) Retarded processing of influenza virus hemagglutinin in insect cells. Virology 180, 159-165.
    • (1991) Virology , vol.180 , pp. 159-165
    • Kuroda, K.1    Veit, M.2    Klenk, H.-D.3
  • 24
    • 0021744087 scopus 로고
    • Spatial conformation of glycans and glycoproteins
    • Montreuil J (1984) Spatial conformation of glycans and glycoproteins. Biol. Cell 51, 115-132.
    • (1984) Biol. Cell , vol.51 , pp. 115-132
    • Montreuil, J.1
  • 25
    • 0026642422 scopus 로고
    • Carbohydrate masking of an antigenic epitope of influenza virus haemagglutinin independent of oligosaccharide size
    • Munk K, Pritzer E, Kretzschmar E, Gutte B, Garten W & Klenk H-D (1992) Carbohydrate masking of an antigenic epitope of influenza virus haemagglutinin independent of oligosaccharide size. Glycobiology 2, 233-240.
    • (1992) Glycobiology , vol.2 , pp. 233-240
    • Munk, K.1    Pritzer, E.2    Kretzschmar, E.3    Gutte, B.4    Garten, W.5    Klenk, H.-D.6
  • 26
    • 0024452967 scopus 로고
    • Structural domains and organizational conformation involved in the sorting and transport of influenza virus transmembrane proteins
    • Nayak DP & Jabbar MA (1989) Structural domains and organizational conformation involved in the sorting and transport of influenza virus transmembrane proteins. Annu. Rev. Microbiol. 43, 465-501.
    • (1989) Annu. Rev. Microbiol. , vol.43 , pp. 465-501
    • Nayak, D.P.1    Jabbar, M.A.2
  • 27
    • 0024447392 scopus 로고
    • Baculovirus polyhedrin promotor directed expression of Rubella virus envelope glycoproteins, E1 and E2, in Spodoptera frugiperda cells
    • Oker-Blom C, Pettersson RF & Summers MD (1989) Baculovirus polyhedrin promotor directed expression of Rubella virus envelope glycoproteins, E1 and E2, in Spodoptera frugiperda cells. Virology 172, 82-91.
    • (1989) Virology , vol.172 , pp. 82-91
    • Oker-Blom, C.1    Pettersson, R.F.2    Summers, M.D.3
  • 28
    • 0024844959 scopus 로고
    • Expression and characterization of the Haras p21 protein produced at high levels in the insect/baculovirus system
    • Page MJ, Hall A, Rhodes S, Skinner RH, Murphy V, Sydenham M & Lowe PN (1989) Expression and characterization of the Haras p21 protein produced at high levels in the insect/baculovirus system. J. Biol. Chem. 264, 19147-19154.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19147-19154
    • Page, M.J.1    Hall, A.2    Rhodes, S.3    Skinner, R.H.4    Murphy, V.5    Sydenham, M.6    Lowe, P.N.7
  • 29
    • 0024355330 scopus 로고
    • Glycoproteins: What are the sugar chains for?
    • Paulson JC (1989) Glycoproteins: what are the sugar chains for? TIBS 14, 272-276.
    • (1989) TIBS , vol.14 , pp. 272-276
    • Paulson, J.C.1
  • 31
    • 0024522732 scopus 로고
    • Expression of the fusion glycoprotein of human parainfluenza type 3 virus in insect cells by a recombinant beculovirus and analysis of its immunogenic property
    • Ray R, Galinski MS & Compans RW (1989) Expression of the fusion glycoprotein of human parainfluenza type 3 virus in insect cells by a recombinant beculovirus and analysis of its immunogenic property. Virus Res. 12, 169-180.
    • (1989) Virus Res. , vol.12 , pp. 169-180
    • Ray, R.1    Galinski, M.S.2    Compans, R.W.3
  • 32
    • 0024433220 scopus 로고
    • Fatty acid acylation of the 67K envelope glycoprotein of a baculovirus: Autographa caltfornica nuclear polyhedrosis virus
    • Roberts TE & Faulkner P (1989) Fatty acid acylation of the 67K envelope glycoprotein of a baculovirus: Autographa caltfornica nuclear polyhedrosis virus. Virology 172, 377-381.
    • (1989) Virology , vol.172 , pp. 377-381
    • Roberts, T.E.1    Faulkner, P.2
  • 33
    • 0021911623 scopus 로고
    • Alterations in the hemagglutinin associated with adaptation of influenza B virus to growth in eggs
    • Robertson JS, Naeve CW, Webster RG, Bootman JS, Newman R & Schild GC (1985) Alterations in the hemagglutinin associated with adaptation of influenza B virus to growth in eggs. Virology 143, 166-174.
    • (1985) Virology , vol.143 , pp. 166-174
    • Robertson, J.S.1    Naeve, C.W.2    Webster, R.G.3    Bootman, J.S.4    Newman, R.5    Schild, G.C.6
  • 34
    • 0027158077 scopus 로고
    • Generation of structural and functional diversity in furin-like proteins in Drosophila melanogaster by alternative splicing of the DFUR1 gene
    • Roebroek AJM, Creemers JWM, Pauli IGL, Bogaert T & Van de Ven WJM (1993) Generation of structural and functional diversity in furin-like proteins in Drosophila melanogaster by alternative splicing of the DFUR1 gene. EMBO J. 12, 1853-1870.
    • (1993) EMBO J. , vol.12 , pp. 1853-1870
    • Roebroek, A.J.M.1    Creemers, J.W.M.2    Pauli, I.G.L.3    Bogaert, T.4    Van De Ven, W.J.M.5
  • 36
    • 0022817054 scopus 로고
    • Mutations blocking the transport of the influenza virus hemagglutinin between the rough endoplasmic reticulum and the Golgi apparatus
    • Schuy W, Will C, Kuroda K, Scholtissek C, Garten W & Klenk H-D (1986) Mutations blocking the transport of the influenza virus hemagglutinin between the rough endoplasmic reticulum and the Golgi apparatus EMBO J. 5, 2831-2836.
    • (1986) EMBO J. , vol.5 , pp. 2831-2836
    • Schuy, W.1    Will, C.2    Kuroda, K.3    Scholtissek, C.4    Garten, W.5    Klenk, H.-D.6
  • 38
    • 0026643396 scopus 로고
    • Influenza virus gemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease
    • Stieneke-Gröber A, Vey M, Angliker H, Shaw E, Thomas G, Roberts C, Klenk H-D & Garten W (1992) Influenza virus gemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease. EMBO J. 11, 2407-2414.
    • (1992) EMBO J. , vol.11 , pp. 2407-2414
    • Stieneke-Gröber, A.1    Vey, M.2    Angliker, H.3    Shaw, E.4    Thomas, G.5    Roberts, C.6    Klenk, H.-D.7    Garten, W.8
  • 39
    • 0025191329 scopus 로고
    • Synthesis of the membrane fusion and hemagglutinin proteins of measles virus, using a novel baculovirus vector containing the β-galactosidase gene
    • Vialard J, Lalumière M, Vernet T, Briedis D, Alkhatib G, Henning D, Levin D & Richardson C (1990) Synthesis of the membrane fusion and hemagglutinin proteins of measles virus, using a novel baculovirus vector containing the β-galactosidase gene. J. Virol. 64, 37-50.
    • (1990) J. Virol. , vol.64 , pp. 37-50
    • Vialard, J.1    Lalumière, M.2    Vernet, T.3    Briedis, D.4    Alkhatib, G.5    Henning, D.6    Levin, D.7    Richardson, C.8
  • 40
    • 0025726262 scopus 로고
    • Characterization of oligosaccharide structures on a chimeric respiratory syncytial virus protein expressed in insect cell line Sf9
    • Wathen MW, Aeed PA & Elhammer AP (1991) Characterization of oligosaccharide structures on a chimeric respiratory syncytial virus protein expressed in insect cell line Sf9. Biochemistry 30, 2863-2868.
    • (1991) Biochemistry , vol.30 , pp. 2863-2868
    • Wathen, M.W.1    Aeed, P.A.2    Elhammer, A.P.3
  • 41
    • 0000377997 scopus 로고
    • Antigene variation among type A influenza viruses
    • P & Kingsbury W (Eds) Springer Verlag, Wien
    • Webster RG, Laver WG & Air GM (1983) Antigene variation among type A influenza viruses. In: Genetics of Influenza Viruses Palese P & Kingsbury W (Eds) pp. 127-168, Springer Verlag, Wien.
    • (1983) Genetics of Influenza Viruses Palese , pp. 127-168
    • Webster, R.G.1    Laver, W.G.2    Air, G.M.3
  • 42
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley DC & Skehel JJ (1987) The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Ann. Rev. Biochem. 56, 365-394.
    • (1987) Ann. Rev. Biochem. , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 43
    • 0019890491 scopus 로고
    • Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3A resolution
    • Wilson JA, Skehel JJ & Wiley DC (1981) Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3A resolution. Nature (London) 289, 366-373.
    • (1981) Nature (London) , vol.289 , pp. 366-373
    • Wilson, J.A.1    Skehel, J.J.2    Wiley, D.C.3


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