The underestimated N-glycomes of lepidopteran species

Insects are significant to the environment, agriculture, health and biotechnology. Many of these aspects display some relationship to glycosylation, e.g., in case of pathogen binding or production of humanised antibodies; for a long time, it has been considered that insect N-glycosylation potentials...

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Published inBiochimica et biophysica acta Vol. 1861; no. 4; pp. 699 - 714
Main Authors Stanton, Rhiannon, Hykollari, Alba, Eckmair, Barbara, Malzl, Daniel, Dragosits, Martin, Palmberger, Dieter, Wang, Ping, Wilson, Iain B.H., Paschinger, Katharina
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.04.2017
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Online AccessGet full text
ISSN0304-4165
0006-3002
1872-8006
1878-2434
DOI10.1016/j.bbagen.2017.01.009

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Abstract Insects are significant to the environment, agriculture, health and biotechnology. Many of these aspects display some relationship to glycosylation, e.g., in case of pathogen binding or production of humanised antibodies; for a long time, it has been considered that insect N-glycosylation potentials are rather similar and simple, but as more species are glycomically analysed in depth, it is becoming obvious that there is indeed a large structural diversity and interspecies variability. Using an off-line LC-MALDI-TOF MS approach, we have analysed the N-glycomes of two lepidopteran species (the cabbage looper Trichoplusia ni and the gypsy moth Lymantria dispar) as well as of the commonly-used T. ni High Five cell line. We detected not only sulphated, glucuronylated, core difucosylated and Lewis-like antennal fucosylated structures, but also the zwitterion phosphorylcholine on antennal GlcNAc residues, a modification otherwise familiar from nematodes; in L. dispar, N-glycans with glycolipid-like antennae containing α-linked N-acetylgalactosamine were also revealed. The lepidopteran glycomes analysed not only display core α1,3-fucosylation, which is foreign to mammals, but also up to 5% anionic and/or zwitterionic glycans previously not found in these species. The occurrence of anionic and zwitterionic glycans in the Lepidoptera data is not only of glycoanalytical and evolutionary interest, but is of biotechnological relevance as lepidopteran cell lines are potential factories for recombinant glycoprotein production. [Display omitted] •Release, HPLC and MS of over 100 different N-glycans from lepidopteran species.•MS/MS and digestions demonstrate a number of novel N-glycan structures.•Modifications include phosphorylcholine, sulphate and glucuronic acid.
AbstractList Insects are significant to the environment, agriculture, health and biotechnology. Many of these aspects display some relationship to glycosylation, e.g., in case of pathogen binding or production of humanised antibodies; for a long time, it has been considered that insect N-glycosylation potentials are rather similar and simple, but as more species are glycomically analysed in depth, it is becoming obvious that there is indeed a large structural diversity and interspecies variability.Using an off-line LC-MALDI-TOF MS approach, we have analysed the N-glycomes of two lepidopteran species (the cabbage looper Trichoplusia ni and the gypsy moth Lymantria dispar) as well as of the commonly-used T. ni High Five cell line.We detected not only sulphated, glucuronylated, core difucosylated and Lewis-like antennal fucosylated structures, but also the zwitterion phosphorylcholine on antennal GlcNAc residues, a modification otherwise familiar from nematodes; in L. dispar, N-glycans with glycolipid-like antennae containing α-linked N-acetylgalactosamine were also revealed.The lepidopteran glycomes analysed not only display core α1,3-fucosylation, which is foreign to mammals, but also up to 5% anionic and/or zwitterionic glycans previously not found in these species.The occurrence of anionic and zwitterionic glycans in the Lepidoptera data is not only of glycoanalytical and evolutionary interest, but is of biotechnological relevance as lepidopteran cell lines are potential factories for recombinant glycoprotein production.
Insects are significant to the environment, agriculture, health and biotechnology. Many of these aspects display some relationship to glycosylation, e.g., in case of pathogen binding or production of humanised antibodies; for a long time, it has been considered that insect N-glycosylation potentials are rather similar and simple, but as more species are glycomically analysed in depth, it is becoming obvious that there is indeed a large structural diversity and interspecies variability. Using an off-line LC-MALDI-TOF MS approach, we have analysed the N-glycomes of two lepidopteran species (the cabbage looper Trichoplusia ni and the gypsy moth Lymantria dispar) as well as of the commonly-used T. ni High Five cell line. We detected not only sulphated, glucuronylated, core difucosylated and Lewis-like antennal fucosylated structures, but also the zwitterion phosphorylcholine on antennal GlcNAc residues, a modification otherwise familiar from nematodes; in L. dispar, N-glycans with glycolipid-like antennae containing α-linked N-acetylgalactosamine were also revealed. The lepidopteran glycomes analysed not only display core α1,3-fucosylation, which is foreign to mammals, but also up to 5% anionic and/or zwitterionic glycans previously not found in these species. The occurrence of anionic and zwitterionic glycans in the Lepidoptera data is not only of glycoanalytical and evolutionary interest, but is of biotechnological relevance as lepidopteran cell lines are potential factories for recombinant glycoprotein production. [Display omitted] •Release, HPLC and MS of over 100 different N-glycans from lepidopteran species.•MS/MS and digestions demonstrate a number of novel N-glycan structures.•Modifications include phosphorylcholine, sulphate and glucuronic acid.
Insects are significant to the environment, agriculture, health and biotechnology. Many of these aspects display some relationship to glycosylation, e.g., in case of pathogen binding or production of humanised antibodies; for a long time, it has been considered that insect N-glycosylation potentials are rather similar and simple, but as more species are glycomically analysed in depth, it is becoming obvious that there is indeed a large structural diversity and interspecies variability.BACKGROUNDInsects are significant to the environment, agriculture, health and biotechnology. Many of these aspects display some relationship to glycosylation, e.g., in case of pathogen binding or production of humanised antibodies; for a long time, it has been considered that insect N-glycosylation potentials are rather similar and simple, but as more species are glycomically analysed in depth, it is becoming obvious that there is indeed a large structural diversity and interspecies variability.Using an off-line LC-MALDI-TOF MS approach, we have analysed the N-glycomes of two lepidopteran species (the cabbage looper Trichoplusia ni and the gypsy moth Lymantria dispar) as well as of the commonly-used T. ni High Five cell line.METHODSUsing an off-line LC-MALDI-TOF MS approach, we have analysed the N-glycomes of two lepidopteran species (the cabbage looper Trichoplusia ni and the gypsy moth Lymantria dispar) as well as of the commonly-used T. ni High Five cell line.We detected not only sulphated, glucuronylated, core difucosylated and Lewis-like antennal fucosylated structures, but also the zwitterion phosphorylcholine on antennal GlcNAc residues, a modification otherwise familiar from nematodes; in L. dispar, N-glycans with glycolipid-like antennae containing α-linked N-acetylgalactosamine were also revealed.RESULTSWe detected not only sulphated, glucuronylated, core difucosylated and Lewis-like antennal fucosylated structures, but also the zwitterion phosphorylcholine on antennal GlcNAc residues, a modification otherwise familiar from nematodes; in L. dispar, N-glycans with glycolipid-like antennae containing α-linked N-acetylgalactosamine were also revealed.The lepidopteran glycomes analysed not only display core α1,3-fucosylation, which is foreign to mammals, but also up to 5% anionic and/or zwitterionic glycans previously not found in these species.CONCLUSIONThe lepidopteran glycomes analysed not only display core α1,3-fucosylation, which is foreign to mammals, but also up to 5% anionic and/or zwitterionic glycans previously not found in these species.The occurrence of anionic and zwitterionic glycans in the Lepidoptera data is not only of glycoanalytical and evolutionary interest, but is of biotechnological relevance as lepidopteran cell lines are potential factories for recombinant glycoprotein production.SIGNIFICANCEThe occurrence of anionic and zwitterionic glycans in the Lepidoptera data is not only of glycoanalytical and evolutionary interest, but is of biotechnological relevance as lepidopteran cell lines are potential factories for recombinant glycoprotein production.
Insects are significant to the environment, agriculture, health and biotechnology. Many of these aspects display some relationship to glycosylation, e.g., in case of pathogen binding or production of humanised antibodies; for a long time, it has been considered that insect N-glycosylation potentials are rather similar and simple, but as more species are glycomically analysed in depth, it is becoming obvious that there is indeed a large structural diversity and interspecies variability. Using an off-line LC-MALDI-TOF MS approach, we have analysed the N-glycomes of two lepidopteran species (the cabbage looper Trichoplusia ni and the gypsy moth Lymantria dispar) as well as of the commonly-used T. ni High Five cell line. We detected not only sulphated, glucuronylated, core difucosylated and Lewis-like antennal fucosylated structures, but also the zwitterion phosphorylcholine on antennal GlcNAc residues, a modification otherwise familiar from nematodes; in L. dispar, N-glycans with glycolipid-like antennae containing α-linked N-acetylgalactosamine were also revealed. The lepidopteran glycomes analysed not only display core α1,3-fucosylation, which is foreign to mammals, but also up to 5% anionic and/or zwitterionic glycans previously not found in these species. The occurrence of anionic and zwitterionic glycans in the Lepidoptera data is not only of glycoanalytical and evolutionary interest, but is of biotechnological relevance as lepidopteran cell lines are potential factories for recombinant glycoprotein production.
Author Dragosits, Martin
Hykollari, Alba
Eckmair, Barbara
Wilson, Iain B.H.
Stanton, Rhiannon
Paschinger, Katharina
Malzl, Daniel
Palmberger, Dieter
Wang, Ping
AuthorAffiliation b Department für Biotechnologie, Universität für Bodenkultur, 1190 Wien, Austria
a Department für Chemie, Universität für Bodenkultur, 1190 Wien, Austria
c Department of Entomology, Cornell University, Geneva, NY 14456, USA
AuthorAffiliation_xml – name: c Department of Entomology, Cornell University, Geneva, NY 14456, USA
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Cites_doi 10.1093/glycob/10.8.837
10.1021/acs.jproteome.5b00746
10.1093/glycob/cwu132
10.1074/jbc.M606711200
10.1021/bi00054a005
10.1074/jbc.M100119200
10.1016/0003-2697(87)90253-3
10.1016/j.jbiosc.2010.04.008
10.1093/glycob/cwg071
10.1016/j.carres.2005.05.008
10.1074/jbc.M710279200
10.1007/BF02615077
10.1074/mcp.M115.051573
10.1002/elps.201400528
10.1016/j.carres.2007.12.018
10.1016/S0021-9258(17)43362-X
10.1111/j.1432-1033.1993.tb17870.x
10.1093/glycob/cwt015
10.1074/jbc.M113.478933
10.1074/jbc.M511023200
10.1242/jcs.112.19.3319
10.1074/jbc.M404925200
10.1016/j.jip.2013.05.010
10.1016/0005-2736(81)90096-1
10.1007/s13238-016-0260-y
10.1074/jbc.M309912200
10.1016/j.jprot.2015.05.030
10.1093/aesa/55.5.591
10.1021/acschembio.5b00340
10.1021/bp000057p
10.1074/jbc.M100573200
10.1093/glycob/6.2.157
10.1007/s10719-015-9585-7
10.1007/s00216-015-9154-8
10.1021/bp00017a003
10.1002/btpr.298
10.1016/j.jim.2007.08.002
10.1021/pr300806b
10.1371/annotation/bd906c17-a44b-443d-9051-7d31d8e47afa
10.1016/j.jbiotec.2011.02.009
10.1007/s40265-013-0103-6
10.1074/jbc.M508334200
10.1023/A:1007029017400
10.1016/0003-2697(88)90126-1
10.1128/JVI.02243-14
10.1016/S0076-6879(10)80014-X
10.1371/journal.pone.0110422
10.1016/j.cellsig.2004.05.014
10.1093/glycob/cwv060
10.1006/abbi.1994.1021
10.1074/jbc.M111.296814
10.1271/bbb.67.2055
10.1016/0005-2760(95)00168-9
10.1006/mpev.2000.0799
10.1074/jbc.M408978200
10.1002/arch.21099
10.1093/jisesa/iev088
10.1042/BJ20040535
10.1016/S0021-9258(19)81354-6
10.1016/S0021-9258(19)38733-2
10.1042/BJ20060964
10.1021/pr8006528
10.1007/BF00731872
10.1007/978-1-4939-6493-2_13
10.1093/glycob/cwr149
10.1016/j.bbrc.2014.06.087
10.1016/0304-4165(91)90245-C
10.1046/j.1432-1327.2000.01383.x
10.1093/glycob/cwv091
10.1074/mcp.M115.055061
10.1074/jbc.273.1.466
10.1007/s00284-009-9362-6
10.1074/jbc.M116.720789
10.1016/j.ijpara.2012.01.002
10.1016/0003-2697(91)90047-W
10.1515/BC.2001.028
10.1074/jbc.M209344200
10.1021/pr5003005
10.1016/j.ibmb.2015.11.001
10.1016/S0006-291X(76)80218-5
10.1074/jbc.272.14.9062
10.1093/glycob/8.7.741
10.1093/glycob/cwi028
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Keywords N-linked oligosaccharides
Sulphate
Glucuronic acid
Phosphorylcholine
Insect
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References Sarkar, Hess, Mondal, Banerjee, Sharma, Das (bb0430) 2009; 8
Tomiya, Lee, Yoshida, Wada, Awaya, Kurono, Takahashi (bb0160) 1991; 193
Green, Adelt, Baenziger, Wilson, Van Halbeek (bb0185) 1988; 263
Pogue, Schaefer (bb0080) 2007
Wickham, Davis, Granados, Shuler, Wood (bb0085) 1992; 8
Eckmair, Jin, Abed-Navandi, Paschinger (bb0100) 2016; 15
Geisler, Jarvis (bb0060) 2009
Hamouda, Kaup, Ullah, Berger, Sandig, Tauber, Blanchard (bb0400) 2014; 13
Kawar, Karaveg, Moremen, Jarvis (bb0365) 2001; 276
van Die, van Tetering, Bakker, van den Eijnden, Joziasse (bb0370) 1996; 6
Vadaie, Jarvis (bb0375) 2004; 279
Palmberger, Rendic, Tauber, Krammer, Wilson, Grabherr (bb0415) 2011; 153
Nomura, Ikeda, Ishiyama, Mita, Tamura, Okada, Fujiyama, Usami (bb0350) 2010; 110
Minagawa, Sekiguchi, Nakaso, Tomita, Takahisa, Yasuda (bb0315) 2015; 15
Geisler, Jarvis (bb0330) 2012; 287
Hsieh, Robbins (bb0010) 1984; 259
Sarkar, Schachter (bb0325) 2001; 382
Varki, Cummings, Aebi, Packer, Seeberger, Esko, Stanley, Hart, Darvill, Kinoshita, Prestegard, Schnaar, Freeze, Marth, Bertozzi, Etzler, Frank, Vliegenthart, Lutteke, Perez, Bolton, Rudd, Paulson, Kanehisa, Toukach, Aoki-Kinoshita, Dell, Narimatsu, York, Taniguchi, Kornfeld (bb0125) 2015; 25
Bell, Owens, Shapiro, Tardif (bb0095) 1981
Paschinger, Gonzalez-Sapienza, Wilson (bb0145) 2012; 42
Tomiya, Awaya, Kurono, Endo, Arata, Takahashi (bb0275) 1988; 171
Hykollari, Balog, Rendić, Braulke, Wilson, Paschinger (bb0115) 2013; 12
Hård, Van Doorn, Thomas-Oates, Kamerling, Van der Horst (bb0235) 1993; 32
Geisler, Jarvis (bb0345) 2010; 26
Cabrera, Salazar, Montesino, Tambara, Struwe, Lugo, Harvey, Antoine, Rincon, Domon, Mendez Martinez, Portela, Gonzalez-Hernandez, Triguero, Duran, Lundberg, Vonasek, Gonzalez (bb0070) 2015; 26
Kurz, Aoki, Jin, Karlsson, Tiemeyer, Wilson, Paschinger (bb0065) 2015; 126
Seppo, Moreland, Schweingruber, Tiemeyer (bb0225) 2000; 267
Chen, Zhong, Fei, Gao, Zhang, Li, Wang, Blissard (bb0150) 2014; 88
Ailor, Takahashi, Tsukamoto, Masuda, Rahman, Jarvis, Lee, Betenbaugh (bb0250) 2000; 10
Kulakosky, Hughes, Wood (bb0260) 1998; 8
Yang (bb0435) 2013; 73
Hancock, Narang, Pattabhi, Yushak, Khan, Lin, Plemons, Betenbaugh, Tsang (bb0440) 2008; 330
Gagneux, Varki (bb0445) 2001; 18
Fabini, Freilinger, Altmann, Wilson (bb0040) 2001; 276
Rendić, Linder, Paschinger, Borth, Wilson, Fabini (bb0175) 2006; 281
Mucha, Domlatil, Lochnit, Rendić, Paschinger, Hinterkörner, Hofinger, Kosma, Wilson (bb0385) 2004; 382
Yang, Wang (bb0410) 2016; 291
Aoki, Tiemeyer (bb0055) 2010; 480
Goodridge, Deehan, Harnett, Harnett (bb0420) 2005; 17
van Frankenhuyzen (bb0425) 2013; 114
Yan, Jin, Wilson, Paschinger (bb0280) 2015; 14
Paschinger, Gutternigg, Rendić, Wilson (bb0210) 2008; 343
Sugita, Fujii, Dulaney, Inagaki, Suzuki, Suzuki, Ohta (bb0215) 1995; 1259
Williams, Wormald, Dwek, Rademacher, Parker, Roberts (bb0015) 1991; 1075
Ishida, Irikura, Matsuda, Sato, Sone, Tanaka, Asano (bb0395) 2009; 58
Kubelka, Altmann, Staudacher, Tretter, März, Hård, Kamerling, Vliegenthart (bb0025) 1993; 213
Palmberger, Wilson, Berger, Grabherr, Rendic (bb0255) 2012; 7
Zhang, Tiewsiri, Kain, Huang, Wang (bb0090) 2012; 7
Tomiya, Kurono, Ishihara, Tejima, Endo, Arata, Takahashi (bb0200) 1987; 163
Rabouille, Kuntz, Lockyer, Watson, Signorelli, Rose, van den Heuvel, Roberts (bb0360) 1999; 112
Joshi, Davis, Mattu, Rudd, Dwek, Shuler, Wood (bb0245) 2000; 16
Wilson, Williams, Schachter (bb0405) 1976; 72
Maes, Garenaux, Strecker, Leroy, Wieruszeski, Brassart, Guerardel (bb0230) 2005; 340
Rendić, Klaudiny, Stemmer, Schmidt, Paschinger, Wilson (bb0300) 2007; 402
Léonard, Rendić, Rabouille, Wilson, Préat, Altmann (bb0335) 2006; 281
Mabashi-Asazuma, Kuo, Khoo, Jarvis (bb0190) 2015; 10
Kajiura, Hamaguchi, Mizushima, Misaki, Fujiyama (bb0270) 2015; 25
Koles, Irvine, Panin (bb0045) 2004; 279
Butters, Hughes (bb0005) 1981; 640
Dragosits, Yan, Razzazi-Fazeli, Wilson, Rendić (bb0130) 2015; 25
Choi, Tomiya, Kim, Slavicek, Betenbaugh, Lee (bb0265) 2003; 13
Kubelka, Altmann, März (bb0020) 1995; 12
Yan, Wilson, Paschinger (bb0120) 2015; 36
Paschinger, Hykollari, Razzazi-Fazeli, Greenwell, Leitsch, Walochnik, Wilson (bb0105) 2012; 22
Yu, Yu, Tang, Chen, Xiao, Su (bb0290) 2016; 7
Hykollari, Eckmair, Voglmeir, Jin, Yan, Vanbeselaere, Razzazi-Fazeli, Wilson, Paschinger (bb0165) 2016; 15
Huo, Chen, Qu, Chen, Yang (bb0355) 2013; 83
Kurz, King, Dinglasan, Paschinger, Wilson (bb0320) 2016; 68
Aoki, Perlman, Lim, Cantu, Wells, Tiemeyer (bb0050) 2007; 282
Kubelka, Altmann, Kornfeld, März (bb0030) 1994; 308
Paschinger, Staudacher, Stemmer, Fabini, Wilson (bb0295) 2005; 15
Ihara, Okada, Ikeda (bb0310) 2014; 450
Ichimiya, Maeda, Sakamura, Kanazawa, Nishihara, Kimura (bb0380) 2015; 32
Hsu, Takahashi, Tsukamoto, Kato, Shimada, Masuda, Whiteley, Fan, Lee, Betenbaugh (bb0035) 1997; 272
Rendić, Wilson, Paschinger (bb0170) 2008; 8
Kimura, Kimura, Tsumura, Okihara, Sugimoto, Yamada, Yonekura (bb0205) 2003; 67
Wilson, Paschinger (bb0135) 2016; 408
Juliant, Harduin-Lepers, Monjaret, Catieau, Violet, Cerutti, Ozil, Duonor-Cerutti (bb0305) 2014; 9
Shorey, Andres, Hale (bb0075) 1962; 55
Kim, Tsuchida, Lincecum, Kitagawa, Bernfield, Sugahara (bb0390) 2003; 278
Hykollari, Paschinger, Eckmair, Wilson (bb0110) 2017; 1503
Vaughn, Goodwin, Tompkins, McCawley (bb0155) 1977; 13
Lochnit, Dennis, Ulmer, Geyer (bb0180) 1998; 273
Paschinger, Rendić, Lochnit, Jantsch, Wilson (bb0140) 2004; 279
Dabrowski, Dabrowski, Helling, Wiegandt (bb0195) 1990; 265
Geisler, Aumiller, Jarvis (bb0340) 2008; 283
Park, Wood, Lee (bb0240) 1999; 16
Gaunitz, Jin, Nilsson, Liu, Karlsson, Holgersson (bb0220) 2013; 23
Kurz, Jin, Hykollari, Gregorich, Giomarelli, Vasta, Wilson, Paschinger (bb0285) 2013; 288
Hykollari (10.1016/j.bbagen.2017.01.009_bb0110) 2017; 1503
Paschinger (10.1016/j.bbagen.2017.01.009_bb0295) 2005; 15
Paschinger (10.1016/j.bbagen.2017.01.009_bb0210) 2008; 343
Dabrowski (10.1016/j.bbagen.2017.01.009_bb0195) 1990; 265
Rendić (10.1016/j.bbagen.2017.01.009_bb0170) 2008; 8
Mabashi-Asazuma (10.1016/j.bbagen.2017.01.009_bb0190) 2015; 10
Palmberger (10.1016/j.bbagen.2017.01.009_bb0415) 2011; 153
Geisler (10.1016/j.bbagen.2017.01.009_bb0060) 2009
Koles (10.1016/j.bbagen.2017.01.009_bb0045) 2004; 279
Kubelka (10.1016/j.bbagen.2017.01.009_bb0020) 1995; 12
Yu (10.1016/j.bbagen.2017.01.009_bb0290) 2016; 7
Green (10.1016/j.bbagen.2017.01.009_bb0185) 1988; 263
Kurz (10.1016/j.bbagen.2017.01.009_bb0065) 2015; 126
Nomura (10.1016/j.bbagen.2017.01.009_bb0350) 2010; 110
Kimura (10.1016/j.bbagen.2017.01.009_bb0205) 2003; 67
Sugita (10.1016/j.bbagen.2017.01.009_bb0215) 1995; 1259
Butters (10.1016/j.bbagen.2017.01.009_bb0005) 1981; 640
Geisler (10.1016/j.bbagen.2017.01.009_bb0330) 2012; 287
Geisler (10.1016/j.bbagen.2017.01.009_bb0340) 2008; 283
Ichimiya (10.1016/j.bbagen.2017.01.009_bb0380) 2015; 32
Yan (10.1016/j.bbagen.2017.01.009_bb0120) 2015; 36
Kajiura (10.1016/j.bbagen.2017.01.009_bb0270) 2015; 25
Paschinger (10.1016/j.bbagen.2017.01.009_bb0105) 2012; 22
Hsu (10.1016/j.bbagen.2017.01.009_bb0035) 1997; 272
Paschinger (10.1016/j.bbagen.2017.01.009_bb0145) 2012; 42
Dragosits (10.1016/j.bbagen.2017.01.009_bb0130) 2015; 25
Mucha (10.1016/j.bbagen.2017.01.009_bb0385) 2004; 382
Shorey (10.1016/j.bbagen.2017.01.009_bb0075) 1962; 55
Kurz (10.1016/j.bbagen.2017.01.009_bb0320) 2016; 68
Zhang (10.1016/j.bbagen.2017.01.009_bb0090) 2012; 7
Tomiya (10.1016/j.bbagen.2017.01.009_bb0160) 1991; 193
Fabini (10.1016/j.bbagen.2017.01.009_bb0040) 2001; 276
Eckmair (10.1016/j.bbagen.2017.01.009_bb0100) 2016; 15
Hamouda (10.1016/j.bbagen.2017.01.009_bb0400) 2014; 13
Hykollari (10.1016/j.bbagen.2017.01.009_bb0115) 2013; 12
Rendić (10.1016/j.bbagen.2017.01.009_bb0175) 2006; 281
Choi (10.1016/j.bbagen.2017.01.009_bb0265) 2003; 13
Yang (10.1016/j.bbagen.2017.01.009_bb0410) 2016; 291
Ailor (10.1016/j.bbagen.2017.01.009_bb0250) 2000; 10
Pogue (10.1016/j.bbagen.2017.01.009_bb0080) 2007
Léonard (10.1016/j.bbagen.2017.01.009_bb0335) 2006; 281
Ihara (10.1016/j.bbagen.2017.01.009_bb0310) 2014; 450
Ishida (10.1016/j.bbagen.2017.01.009_bb0395) 2009; 58
Varki (10.1016/j.bbagen.2017.01.009_bb0125) 2015; 25
Maes (10.1016/j.bbagen.2017.01.009_bb0230) 2005; 340
Vadaie (10.1016/j.bbagen.2017.01.009_bb0375) 2004; 279
Yang (10.1016/j.bbagen.2017.01.009_bb0435) 2013; 73
Juliant (10.1016/j.bbagen.2017.01.009_bb0305) 2014; 9
van Frankenhuyzen (10.1016/j.bbagen.2017.01.009_bb0425) 2013; 114
Minagawa (10.1016/j.bbagen.2017.01.009_bb0315) 2015; 15
Seppo (10.1016/j.bbagen.2017.01.009_bb0225) 2000; 267
Kulakosky (10.1016/j.bbagen.2017.01.009_bb0260) 1998; 8
Rendić (10.1016/j.bbagen.2017.01.009_bb0300) 2007; 402
Aoki (10.1016/j.bbagen.2017.01.009_bb0055) 2010; 480
Wilson (10.1016/j.bbagen.2017.01.009_bb0405) 1976; 72
Cabrera (10.1016/j.bbagen.2017.01.009_bb0070) 2015; 26
Wilson (10.1016/j.bbagen.2017.01.009_bb0135) 2016; 408
Palmberger (10.1016/j.bbagen.2017.01.009_bb0255) 2012; 7
Gagneux (10.1016/j.bbagen.2017.01.009_bb0445) 2001; 18
Hancock (10.1016/j.bbagen.2017.01.009_bb0440) 2008; 330
Paschinger (10.1016/j.bbagen.2017.01.009_bb0140) 2004; 279
Kurz (10.1016/j.bbagen.2017.01.009_bb0285) 2013; 288
Kawar (10.1016/j.bbagen.2017.01.009_bb0365) 2001; 276
Tomiya (10.1016/j.bbagen.2017.01.009_bb0200) 1987; 163
Joshi (10.1016/j.bbagen.2017.01.009_bb0245) 2000; 16
Sarkar (10.1016/j.bbagen.2017.01.009_bb0325) 2001; 382
Hykollari (10.1016/j.bbagen.2017.01.009_bb0165) 2016; 15
Kubelka (10.1016/j.bbagen.2017.01.009_bb0030) 1994; 308
Geisler (10.1016/j.bbagen.2017.01.009_bb0345) 2010; 26
Goodridge (10.1016/j.bbagen.2017.01.009_bb0420) 2005; 17
Wickham (10.1016/j.bbagen.2017.01.009_bb0085) 1992; 8
Kubelka (10.1016/j.bbagen.2017.01.009_bb0025) 1993; 213
Gaunitz (10.1016/j.bbagen.2017.01.009_bb0220) 2013; 23
Hård (10.1016/j.bbagen.2017.01.009_bb0235) 1993; 32
Kim (10.1016/j.bbagen.2017.01.009_bb0390) 2003; 278
van Die (10.1016/j.bbagen.2017.01.009_bb0370) 1996; 6
Park (10.1016/j.bbagen.2017.01.009_bb0240) 1999; 16
Yan (10.1016/j.bbagen.2017.01.009_bb0280) 2015; 14
Huo (10.1016/j.bbagen.2017.01.009_bb0355) 2013; 83
Lochnit (10.1016/j.bbagen.2017.01.009_bb0180) 1998; 273
Bell (10.1016/j.bbagen.2017.01.009_bb0095) 1981
Aoki (10.1016/j.bbagen.2017.01.009_bb0050) 2007; 282
Vaughn (10.1016/j.bbagen.2017.01.009_bb0155) 1977; 13
Rabouille (10.1016/j.bbagen.2017.01.009_bb0360) 1999; 112
Chen (10.1016/j.bbagen.2017.01.009_bb0150) 2014; 88
Hsieh (10.1016/j.bbagen.2017.01.009_bb0010) 1984; 259
Tomiya (10.1016/j.bbagen.2017.01.009_bb0275) 1988; 171
Williams (10.1016/j.bbagen.2017.01.009_bb0015) 1991; 1075
Sarkar (10.1016/j.bbagen.2017.01.009_bb0430) 2009; 8
References_xml – volume: 343
  start-page: 2041
  year: 2008
  end-page: 2049
  ident: bb0210
  article-title: The N-glycosylation pattern of
  publication-title: Carbohydr. Res.
– volume: 640
  start-page: 655
  year: 1981
  end-page: 671
  ident: bb0005
  article-title: Isolation and characterisation of mosquito cell membrane glycoproteins
  publication-title: Biochim. Biophys. Acta
– volume: 273
  start-page: 466
  year: 1998
  end-page: 474
  ident: bb0180
  article-title: Structural elucidation and monokine-inducing activity of two biologically active zwitterionic glycosphingolipids derived from the porcine parasitic nematode
  publication-title: J. Biol. Chem.
– volume: 25
  start-page: 1441
  year: 2015
  end-page: 1453
  ident: bb0270
  article-title: Sialylation potentials of the silkworm,
  publication-title: Glycobiology
– volume: 13
  start-page: 6144
  year: 2014
  end-page: 6151
  ident: bb0400
  article-title: Rapid analysis of cell surface N-glycosylation from living cells using mass spectrometry
  publication-title: J. Proteome Res.
– volume: 12
  start-page: 77
  year: 1995
  end-page: 83
  ident: bb0020
  article-title: The asparagine-linked carbohydrate of honeybee venom hyaluronidase
  publication-title: Glycoconj. J.
– volume: 88
  start-page: 13781
  year: 2014
  end-page: 13797
  ident: bb0150
  article-title: Transcriptome responses of the host
  publication-title: J. Virol.
– volume: 1259
  start-page: 220
  year: 1995
  end-page: 226
  ident: bb0215
  article-title: Structural elucidation of two novel amphoteric glycosphingolipids from the earthworm,
  publication-title: Biochim. Biophys. Acta
– volume: 13
  start-page: 213
  year: 1977
  end-page: 217
  ident: bb0155
  article-title: The establishment of two cell lines from the insect
  publication-title: In Vitro
– volume: 32
  start-page: 141
  year: 2015
  end-page: 151
  ident: bb0380
  article-title: Identification of β1,3-galactosyltransferases responsible for biosynthesis of insect complex-type N-glycans containing a T-antigen unit in the honeybee
  publication-title: Glycoconj. J.
– start-page: 165
  year: 2009
  end-page: 191
  ident: bb0060
  article-title: Insect cell glycosylation patterns in the context of biopharmaceuticals
  publication-title: Post-translational Modification of Protein Biopharmaceuticals
– volume: 12
  start-page: 1173
  year: 2013
  end-page: 1187
  ident: bb0115
  article-title: Mass spectrometric analysis of neutral and anionic N-glycans from a
  publication-title: J. Proteome Res.
– volume: 8
  start-page: 7
  year: 2008
  end-page: 21
  ident: bb0170
  article-title: The glycosylation capacity of insect cells
  publication-title: Croat. Chem. Acta
– volume: 7
  year: 2012
  ident: bb0255
  article-title: SweetBac: a new approach for the production of mammalianised glycoproteins in insect cells
  publication-title: PLoS One
– volume: 382
  start-page: 67
  year: 2004
  end-page: 74
  ident: bb0385
  article-title: The
  publication-title: Biochem. J.
– volume: 58
  start-page: 535
  year: 2009
  end-page: 540
  ident: bb0395
  article-title: Molecular cloning and expression of a novel cholinephosphotransferase involved in glycoglycerophospholipid biosynthesis of mycoplasma fermentans
  publication-title: Curr. Microbiol.
– volume: 25
  start-page: 448
  year: 2015
  end-page: 464
  ident: bb0130
  article-title: Enzymatic properties and subtle differences in the substrate specificity of phylogenetically distinct invertebrate N-glycan processing hexosaminidases
  publication-title: Glycobiology
– volume: 83
  start-page: 115
  year: 2013
  end-page: 126
  ident: bb0355
  article-title: Biochemical characterization of a novel β-N-acetylhexosaminidase from the insect
  publication-title: Arch. Insect Biochem. Physiol.
– volume: 340
  start-page: 1852
  year: 2005
  end-page: 1858
  ident: bb0230
  article-title: Major O-glycans from the nest of
  publication-title: Carbohydr. Res.
– volume: 1075
  start-page: 146
  year: 1991
  end-page: 153
  ident: bb0015
  article-title: Characterisation of oligosaccharides from
  publication-title: Biochim. Biophys. Acta Gen. Subj.
– volume: 67
  start-page: 2055
  year: 2003
  end-page: 2058
  ident: bb0205
  article-title: 350-kDa royal jelly glycoprotein (apisin), which stimulates proliferation of human monocytes, bears the β1-3galactosylated N-glycan: analysis of the N-glycosylation site
  publication-title: Biosci. Biotechnol. Biochem.
– volume: 281
  start-page: 3343
  year: 2006
  end-page: 3353
  ident: bb0175
  article-title: Modulation of neural carbohydrate epitope expression in
  publication-title: J. Biol. Chem.
– volume: 114
  start-page: 76
  year: 2013
  end-page: 85
  ident: bb0425
  article-title: Cross-order and cross-phylum activity of
  publication-title: J. Invertebr. Pathol.
– volume: 7
  start-page: 373
  year: 2016
  end-page: 382
  ident: bb0290
  article-title: Transcriptome analyses of insect cells to facilitate baculovirus-insect expression
  publication-title: Protein Cell
– volume: 382
  start-page: 209
  year: 2001
  end-page: 217
  ident: bb0325
  article-title: Cloning and expression of
  publication-title: Biol. Chem.
– volume: 112
  start-page: 3319
  year: 1999
  end-page: 3330
  ident: bb0360
  article-title: The
  publication-title: J. Cell Sci.
– volume: 8
  start-page: 741
  year: 1998
  end-page: 745
  ident: bb0260
  article-title: N-linked glycosylation of a baculovirus-expressed recombinant glycoprotein in insect larvae and tissue culture cells
  publication-title: Glycobiology
– volume: 279
  start-page: 33501
  year: 2004
  end-page: 33508
  ident: bb0375
  article-title: Molecular cloning and functional characterization of a Lepidopteran insect β4-
  publication-title: J. Biol. Chem.
– volume: 72
  start-page: 909
  year: 1976
  end-page: 916
  ident: bb0405
  article-title: The control of glycoprotein synthesis.
  publication-title: Biochem. Biophys. Res. Commun.
– volume: 265
  start-page: 9737
  year: 1990
  end-page: 9743
  ident: bb0195
  article-title: Novel phosphorus-containing glycosphingolipids from the blowfly
  publication-title: J. Biol. Chem.
– volume: 68
  start-page: 52
  year: 2016
  end-page: 63
  ident: bb0320
  article-title: The fucomic potential of mosquitoes: fucosylated N-glycan epitopes and their cognate fucosyltransferases
  publication-title: Insect Biochem. Mol. Biol.
– volume: 16
  start-page: 629
  year: 1999
  end-page: 638
  ident: bb0240
  article-title: Monosaccharide compositions of
  publication-title: Glycoconj. J.
– volume: 288
  start-page: 24410
  year: 2013
  end-page: 24428
  ident: bb0285
  article-title: Haemocytes and plasma of the eastern oyster (
  publication-title: J. Biol. Chem.
– volume: 267
  start-page: 3549
  year: 2000
  end-page: 3558
  ident: bb0225
  article-title: Zwitterionic and acidic glycosphingolipids of the
  publication-title: Eur. J. Biochem.
– year: 2007
  ident: bb0080
  article-title: A Review of Selected Species of Lymantria Hübner (1819) (Lepidoptera: Noctuidae: Lymantriinae) From Subtropical and Temperate Regions of Asia, Including the Descriptions of Three new Species, Some Potentially Invasive to North America
– volume: 287
  start-page: 7084
  year: 2012
  end-page: 7097
  ident: bb0330
  article-title: Substrate specificities and intracellular distributions of three N-glycan processing enzymes functioning at a key branch point in the insect N-glycosylation pathway
  publication-title: J. Biol. Chem.
– volume: 10
  start-page: 2199
  year: 2015
  end-page: 2208
  ident: bb0190
  article-title: Modifying an insect cell N-glycan processing pathway using CRISPR-Cas technology
  publication-title: ACS Chem. Biol.
– volume: 73
  start-page: 1357
  year: 2013
  end-page: 1366
  ident: bb0435
  article-title: Recombinant trivalent influenza vaccine (FluBlok®): a review of its use in the prevention of seasonal influenza in adults
  publication-title: Drugs
– volume: 213
  start-page: 1193
  year: 1993
  end-page: 1204
  ident: bb0025
  article-title: Primary structures of the N-linked carbohydrate chains from honeybee venom phospholipase A
  publication-title: Eur. J. Biochem.
– volume: 25
  start-page: 1323
  year: 2015
  end-page: 1324
  ident: bb0125
  article-title: Symbol nomenclature for graphical representations of glycans
  publication-title: Glycobiology
– volume: 10
  start-page: 837
  year: 2000
  end-page: 847
  ident: bb0250
  article-title: N-glycan patterns of human transferrin produced in
  publication-title: Glycobiology
– volume: 153
  start-page: 160
  year: 2011
  end-page: 166
  ident: bb0415
  article-title: Insect cells for antibody production: evaluation of an efficient alternative
  publication-title: J. Biotechnol.
– volume: 279
  start-page: 4346
  year: 2004
  end-page: 4357
  ident: bb0045
  article-title: Functional characterization of
  publication-title: J. Biol. Chem.
– start-page: 599
  year: 1981
  end-page: 633
  ident: bb0095
  article-title: Development of mass-rearing technology
  publication-title: The Gypsy Moth: Research Toward Integrated Pest Management
– volume: 193
  start-page: 90
  year: 1991
  end-page: 100
  ident: bb0160
  article-title: Calculated two-dimensional sugar map of pyridylaminated oligosaccharides: elucidation of the jack bean α-mannosidase digestion pathway of Man
  publication-title: Anal. Biochem.
– volume: 32
  start-page: 766
  year: 1993
  end-page: 775
  ident: bb0235
  article-title: Structure of the Asn-linked oligosaccharides of apolipophorin III from the insect
  publication-title: Biochemistry
– volume: 55
  start-page: 591
  year: 1962
  end-page: 597
  ident: bb0075
  article-title: The biology of
  publication-title: Ann. Entomol. Soc. Am.
– volume: 23
  start-page: 778
  year: 2013
  end-page: 796
  ident: bb0220
  article-title: Mucin-type proteins produced in the
  publication-title: Glycobiology
– volume: 110
  start-page: 386
  year: 2010
  end-page: 391
  ident: bb0350
  article-title: Cloning and characterization of a β-N-acetylglucosaminidase (BmFDL) from silkworm
  publication-title: J. Biosci. Bioeng.
– volume: 1503
  start-page: 167
  year: 2017
  end-page: 184
  ident: bb0110
  article-title: Analysis of invertebrate and protist N-glycans
  publication-title: Methods Mol. Biol.
– volume: 17
  start-page: 11
  year: 2005
  end-page: 16
  ident: bb0420
  article-title: Subversion of immunological signalling by a filarial nematode phosphorylcholine-containing secreted product
  publication-title: Cell. Signal.
– volume: 13
  start-page: 539
  year: 2003
  end-page: 548
  ident: bb0265
  article-title: N-glycan structures of human transferrin produced by
  publication-title: Glycobiology
– volume: 163
  start-page: 489
  year: 1987
  end-page: 499
  ident: bb0200
  article-title: Structural analysis of N-linked oligosaccharides by a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography
  publication-title: Anal. Biochem.
– volume: 282
  start-page: 9127
  year: 2007
  end-page: 9142
  ident: bb0050
  article-title: Dynamic developmental elaboration of N-linked glycan complexity in the
  publication-title: J. Biol. Chem.
– volume: 36
  start-page: 1314
  year: 2015
  end-page: 1329
  ident: bb0120
  article-title: Comparison of RP-HPLC modes to analyse the N-glycome of the free-living nematode
  publication-title: Electrophoresis
– volume: 42
  start-page: 279
  year: 2012
  end-page: 285
  ident: bb0145
  article-title: Mass spectrometric analysis of the immunodominant glycan epitope of
  publication-title: Int. J. Parasitol.
– volume: 15
  start-page: 73
  year: 2016
  end-page: 92
  ident: bb0165
  article-title: More than just oligomannose: An N-glycomic comparison of
  publication-title: Mol. Cell. Proteomics
– volume: 308
  start-page: 148
  year: 1994
  end-page: 157
  ident: bb0030
  article-title: Structures of the N-linked oligosaccharides of the membrane glycoproteins from three lepidopteran cell lines (Sf-21, IZD-Mb-0503, Bm-N)
  publication-title: Arch. Biochem. Biophys.
– volume: 7
  year: 2012
  ident: bb0090
  article-title: Resistance of
  publication-title: PLoS One
– volume: 402
  start-page: 105
  year: 2007
  end-page: 115
  ident: bb0300
  article-title: Towards abolition of immunogenic structures in insect cells: characterization of a honey-bee (
  publication-title: Biochem. J.
– volume: 14
  start-page: 5291
  year: 2015
  end-page: 5305
  ident: bb0280
  article-title: Comparisons of
  publication-title: J. Proteome Res.
– volume: 480
  start-page: 297
  year: 2010
  end-page: 321
  ident: bb0055
  article-title: The glycomics of glycan glucuronylation in
  publication-title: Methods Enzymol.
– volume: 171
  start-page: 73
  year: 1988
  end-page: 90
  ident: bb0275
  article-title: Analyses of N-linked oligosaccharides using a two-dimensional mapping technique
  publication-title: Anal. Biochem.
– volume: 259
  start-page: 2375
  year: 1984
  end-page: 2382
  ident: bb0010
  article-title: Regulation of asparagine-linked oligosaccharide processing. Oligosaccharide processing in
  publication-title: J. Biol. Chem.
– volume: 279
  start-page: 49588
  year: 2004
  end-page: 49598
  ident: bb0140
  article-title: Molecular basis of anti-horseradish peroxidase staining in
  publication-title: J. Biol. Chem.
– volume: 450
  start-page: 953
  year: 2014
  end-page: 960
  ident: bb0310
  article-title: Cloning, expression and characterization of
  publication-title: Biochem. Biophys. Res. Commun.
– volume: 22
  start-page: 300
  year: 2012
  end-page: 313
  ident: bb0105
  article-title: The N-glycans of
  publication-title: Glycobiology
– volume: 263
  start-page: 18253
  year: 1988
  end-page: 18268
  ident: bb0185
  article-title: The asparagine-linked oligosaccharides on bovine fetuin. Structural analysis of N-glycanase-released oligosaccharides by 500-megahertz
  publication-title: J. Biol. Chem.
– volume: 6
  start-page: 157
  year: 1996
  end-page: 164
  ident: bb0370
  article-title: Glycosylation in lepidopteran insect cells: identification of a β1
  publication-title: Glycobiology
– volume: 126
  start-page: 172
  year: 2015
  end-page: 188
  ident: bb0065
  article-title: Targetted release and fractionation reveal glucuronylated and sulphated N- and O-glycans in larvae of dipteran insects
  publication-title: J. Proteome
– volume: 276
  start-page: 28058
  year: 2001
  end-page: 28067
  ident: bb0040
  article-title: Identification of core α1,3-fucosylated glycans and the requisite fucosyltransferase in
  publication-title: J. Biol. Chem.
– volume: 283
  start-page: 11330
  year: 2008
  end-page: 11339
  ident: bb0340
  article-title: A
  publication-title: J. Biol. Chem.
– volume: 15
  start-page: 463
  year: 2005
  end-page: 474
  ident: bb0295
  article-title: Fucosyltransferase substrate specificity and the order of fucosylation in invertebrates
  publication-title: Glycobiology
– volume: 8
  start-page: 391
  year: 1992
  end-page: 396
  ident: bb0085
  article-title: Screening of insect cell lines for the production of recombinant proteins and infectious virus in the baculovirus expression system
  publication-title: Biotechnol. Prog.
– volume: 278
  start-page: 9116
  year: 2003
  end-page: 9124
  ident: bb0390
  article-title: Identification and characterization of three
  publication-title: J. Biol. Chem.
– volume: 26
  start-page: 230
  year: 2015
  end-page: 250
  ident: bb0070
  article-title: Structural characterization and biological implications of sulfated N-glycans in a serine protease from the neotropical moth
  publication-title: Glycobiology
– volume: 330
  start-page: 130
  year: 2008
  end-page: 136
  ident: bb0440
  article-title: False positive reactivity of recombinant, diagnostic, glycoproteins produced in High Five insect cells: effect of glycosylation
  publication-title: J. Immunol. Methods
– volume: 18
  start-page: 2
  year: 2001
  end-page: 13
  ident: bb0445
  article-title: Genetic differences between humans and great apes
  publication-title: Mol. Phylogenet. Evol.
– volume: 408
  start-page: 461
  year: 2016
  end-page: 471
  ident: bb0135
  article-title: Sweet secrets of a therapeutic worm: mass spectrometric N-glycomic analysis of
  publication-title: Anal. Bioanal. Chem.
– volume: 291
  start-page: 11064
  year: 2016
  end-page: 11071
  ident: bb0410
  article-title: Mammalian α1,6-fucosyltransferase (FUT8) is the sole enzyme responsible for the N-acetylglucosaminyltransferase I-independent core fucosylation of high-mannose N-glycans
  publication-title: J. Biol. Chem.
– volume: 8
  start-page: 1838
  year: 2009
  end-page: 1848
  ident: bb0430
  article-title: Homodimeric alkaline phosphatase located at
  publication-title: J. Proteome Res.
– volume: 16
  start-page: 650
  year: 2000
  end-page: 656
  ident: bb0245
  article-title: Influence of baculovirus-host cell interactions on complex N-linked glycosylation of a recombinant human protein
  publication-title: Biotechnol. Prog.
– volume: 272
  start-page: 9062
  year: 1997
  end-page: 9070
  ident: bb0035
  article-title: Differential
  publication-title: J. Biol. Chem.
– volume: 26
  start-page: 34
  year: 2010
  end-page: 44
  ident: bb0345
  article-title: Identification of genes encoding N-glycan processing β-N-acetylglucosaminidases in
  publication-title: Biotechnol. Prog.
– volume: 15
  start-page: 573
  year: 2016
  end-page: 597
  ident: bb0100
  article-title: Multi-step fractionation and mass spectrometry reveals zwitterionic and anionic modifications of the N- and O-glycans of a marine snail
  publication-title: Mol. Cell. Proteomics
– volume: 9
  year: 2014
  ident: bb0305
  article-title: The α1,6-fucosyltransferase gene (fut8) from the Sf9 lepidopteran insect cell line: insights into fut8 evolution
  publication-title: PLoS One
– volume: 15
  year: 2015
  ident: bb0315
  article-title: Identification of core α1,3-fucosyltransferase gene from silkworm: an insect popularly used to express mammalian proteins
  publication-title: J. Insect Sci.
– volume: 281
  start-page: 4867
  year: 2006
  end-page: 4875
  ident: bb0335
  article-title: The
  publication-title: J. Biol. Chem.
– volume: 276
  start-page: 16335
  year: 2001
  end-page: 16340
  ident: bb0365
  article-title: Insect cells encode a class II α-mannosidase with unique properties
  publication-title: J. Biol. Chem.
– volume: 10
  start-page: 837
  year: 2000
  ident: 10.1016/j.bbagen.2017.01.009_bb0250
  article-title: N-glycan patterns of human transferrin produced in Trichoplusia ni insect cells: effects of mammalian galactosyltransferase
  publication-title: Glycobiology
  doi: 10.1093/glycob/10.8.837
– volume: 14
  start-page: 5291
  year: 2015
  ident: 10.1016/j.bbagen.2017.01.009_bb0280
  article-title: Comparisons of Caenorhabditis fucosyltransferase mutants reveal a multiplicity of isomeric N-glycan structures
  publication-title: J. Proteome Res.
  doi: 10.1021/acs.jproteome.5b00746
– volume: 25
  start-page: 448
  year: 2015
  ident: 10.1016/j.bbagen.2017.01.009_bb0130
  article-title: Enzymatic properties and subtle differences in the substrate specificity of phylogenetically distinct invertebrate N-glycan processing hexosaminidases
  publication-title: Glycobiology
  doi: 10.1093/glycob/cwu132
– volume: 282
  start-page: 9127
  year: 2007
  ident: 10.1016/j.bbagen.2017.01.009_bb0050
  article-title: Dynamic developmental elaboration of N-linked glycan complexity in the Drosophila melanogaster embryo
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M606711200
– volume: 32
  start-page: 766
  year: 1993
  ident: 10.1016/j.bbagen.2017.01.009_bb0235
  article-title: Structure of the Asn-linked oligosaccharides of apolipophorin III from the insect Locusta migratoria. Carbohydrate- linked 2-aminoethylphosphonate as a constituent of a glycoprotein
  publication-title: Biochemistry
  doi: 10.1021/bi00054a005
– volume: 276
  start-page: 16335
  year: 2001
  ident: 10.1016/j.bbagen.2017.01.009_bb0365
  article-title: Insect cells encode a class II α-mannosidase with unique properties
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M100119200
– volume: 163
  start-page: 489
  year: 1987
  ident: 10.1016/j.bbagen.2017.01.009_bb0200
  article-title: Structural analysis of N-linked oligosaccharides by a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography
  publication-title: Anal. Biochem.
  doi: 10.1016/0003-2697(87)90253-3
– volume: 110
  start-page: 386
  year: 2010
  ident: 10.1016/j.bbagen.2017.01.009_bb0350
  article-title: Cloning and characterization of a β-N-acetylglucosaminidase (BmFDL) from silkworm Bombyx mori
  publication-title: J. Biosci. Bioeng.
  doi: 10.1016/j.jbiosc.2010.04.008
– volume: 13
  start-page: 539
  year: 2003
  ident: 10.1016/j.bbagen.2017.01.009_bb0265
  article-title: N-glycan structures of human transferrin produced by Lymantria dispar (gypsy moth) cells using the LdMNPV expression system
  publication-title: Glycobiology
  doi: 10.1093/glycob/cwg071
– volume: 340
  start-page: 1852
  year: 2005
  ident: 10.1016/j.bbagen.2017.01.009_bb0230
  article-title: Major O-glycans from the nest of Vespula germanica contain phospho-ethanolamine
  publication-title: Carbohydr. Res.
  doi: 10.1016/j.carres.2005.05.008
– volume: 283
  start-page: 11330
  year: 2008
  ident: 10.1016/j.bbagen.2017.01.009_bb0340
  article-title: A fused lobes gene encodes the processing β-N-acetylglucosaminidase in Sf9 cells
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M710279200
– volume: 13
  start-page: 213
  year: 1977
  ident: 10.1016/j.bbagen.2017.01.009_bb0155
  article-title: The establishment of two cell lines from the insect Spodoptera frugiperda (Lepidoptera; Noctuidae)
  publication-title: In Vitro
  doi: 10.1007/BF02615077
– volume: 15
  start-page: 573
  year: 2016
  ident: 10.1016/j.bbagen.2017.01.009_bb0100
  article-title: Multi-step fractionation and mass spectrometry reveals zwitterionic and anionic modifications of the N- and O-glycans of a marine snail
  publication-title: Mol. Cell. Proteomics
  doi: 10.1074/mcp.M115.051573
– volume: 36
  start-page: 1314
  year: 2015
  ident: 10.1016/j.bbagen.2017.01.009_bb0120
  article-title: Comparison of RP-HPLC modes to analyse the N-glycome of the free-living nematode Pristionchus pacificus
  publication-title: Electrophoresis
  doi: 10.1002/elps.201400528
– volume: 343
  start-page: 2041
  year: 2008
  ident: 10.1016/j.bbagen.2017.01.009_bb0210
  article-title: The N-glycosylation pattern of Caenorhabditis elegans
  publication-title: Carbohydr. Res.
  doi: 10.1016/j.carres.2007.12.018
– volume: 259
  start-page: 2375
  year: 1984
  ident: 10.1016/j.bbagen.2017.01.009_bb0010
  article-title: Regulation of asparagine-linked oligosaccharide processing. Oligosaccharide processing in Aedes albopictus mosquito cells
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(17)43362-X
– volume: 213
  start-page: 1193
  year: 1993
  ident: 10.1016/j.bbagen.2017.01.009_bb0025
  article-title: Primary structures of the N-linked carbohydrate chains from honeybee venom phospholipase A2
  publication-title: Eur. J. Biochem.
  doi: 10.1111/j.1432-1033.1993.tb17870.x
– volume: 23
  start-page: 778
  year: 2013
  ident: 10.1016/j.bbagen.2017.01.009_bb0220
  article-title: Mucin-type proteins produced in the Trichoplusia ni and Spodoptera frugiperda insect cell lines carry novel O-glycans with phosphocholine and sulfate substitutions
  publication-title: Glycobiology
  doi: 10.1093/glycob/cwt015
– volume: 288
  start-page: 24410
  year: 2013
  ident: 10.1016/j.bbagen.2017.01.009_bb0285
  article-title: Haemocytes and plasma of the eastern oyster (Crassostrea virginica) display a diverse repertoire of sulphated and blood group A-modified N-glycans
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M113.478933
– volume: 281
  start-page: 4867
  year: 2006
  ident: 10.1016/j.bbagen.2017.01.009_bb0335
  article-title: The Drosophila fused lobes gene encodes an N-acetylglucosaminidase involved in N-glycan processing
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M511023200
– volume: 112
  start-page: 3319
  year: 1999
  ident: 10.1016/j.bbagen.2017.01.009_bb0360
  article-title: The Drosophila GMII gene encodes a Golgi α-mannosidase II
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.112.19.3319
– volume: 279
  start-page: 33501
  year: 2004
  ident: 10.1016/j.bbagen.2017.01.009_bb0375
  article-title: Molecular cloning and functional characterization of a Lepidopteran insect β4-N-acetylgalactosaminyltransferase with broad substrate specificity, a functional role in glycoprotein biosynthesis, and a potential functional role in glycolipid biosynthesis
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M404925200
– year: 2007
  ident: 10.1016/j.bbagen.2017.01.009_bb0080
– volume: 114
  start-page: 76
  year: 2013
  ident: 10.1016/j.bbagen.2017.01.009_bb0425
  article-title: Cross-order and cross-phylum activity of Bacillus thuringiensis pesticidal proteins
  publication-title: J. Invertebr. Pathol.
  doi: 10.1016/j.jip.2013.05.010
– volume: 640
  start-page: 655
  year: 1981
  ident: 10.1016/j.bbagen.2017.01.009_bb0005
  article-title: Isolation and characterisation of mosquito cell membrane glycoproteins
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0005-2736(81)90096-1
– volume: 7
  start-page: 373
  year: 2016
  ident: 10.1016/j.bbagen.2017.01.009_bb0290
  article-title: Transcriptome analyses of insect cells to facilitate baculovirus-insect expression
  publication-title: Protein Cell
  doi: 10.1007/s13238-016-0260-y
– volume: 279
  start-page: 4346
  year: 2004
  ident: 10.1016/j.bbagen.2017.01.009_bb0045
  article-title: Functional characterization of Drosophila sialyltransferase
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M309912200
– volume: 126
  start-page: 172
  year: 2015
  ident: 10.1016/j.bbagen.2017.01.009_bb0065
  article-title: Targetted release and fractionation reveal glucuronylated and sulphated N- and O-glycans in larvae of dipteran insects
  publication-title: J. Proteome
  doi: 10.1016/j.jprot.2015.05.030
– volume: 55
  start-page: 591
  year: 1962
  ident: 10.1016/j.bbagen.2017.01.009_bb0075
  article-title: The biology of Trichoplusia ni (Lepidoptera: Noctuidae). I. Life history and behavior
  publication-title: Ann. Entomol. Soc. Am.
  doi: 10.1093/aesa/55.5.591
– volume: 10
  start-page: 2199
  year: 2015
  ident: 10.1016/j.bbagen.2017.01.009_bb0190
  article-title: Modifying an insect cell N-glycan processing pathway using CRISPR-Cas technology
  publication-title: ACS Chem. Biol.
  doi: 10.1021/acschembio.5b00340
– volume: 16
  start-page: 650
  year: 2000
  ident: 10.1016/j.bbagen.2017.01.009_bb0245
  article-title: Influence of baculovirus-host cell interactions on complex N-linked glycosylation of a recombinant human protein
  publication-title: Biotechnol. Prog.
  doi: 10.1021/bp000057p
– volume: 8
  start-page: 7
  year: 2008
  ident: 10.1016/j.bbagen.2017.01.009_bb0170
  article-title: The glycosylation capacity of insect cells
  publication-title: Croat. Chem. Acta
– volume: 276
  start-page: 28058
  year: 2001
  ident: 10.1016/j.bbagen.2017.01.009_bb0040
  article-title: Identification of core α1,3-fucosylated glycans and the requisite fucosyltransferase in Drosophila melanogaster. Potential basis of the neural anti-horseradish peroxidase epitope
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M100573200
– volume: 6
  start-page: 157
  year: 1996
  ident: 10.1016/j.bbagen.2017.01.009_bb0370
  article-title: Glycosylation in lepidopteran insect cells: identification of a β1→4-N-acetylgalactosaminyltransferase involved in the synthesis of complex-type oligosaccharide chains
  publication-title: Glycobiology
  doi: 10.1093/glycob/6.2.157
– volume: 32
  start-page: 141
  year: 2015
  ident: 10.1016/j.bbagen.2017.01.009_bb0380
  article-title: Identification of β1,3-galactosyltransferases responsible for biosynthesis of insect complex-type N-glycans containing a T-antigen unit in the honeybee
  publication-title: Glycoconj. J.
  doi: 10.1007/s10719-015-9585-7
– volume: 408
  start-page: 461
  year: 2016
  ident: 10.1016/j.bbagen.2017.01.009_bb0135
  article-title: Sweet secrets of a therapeutic worm: mass spectrometric N-glycomic analysis of Trichuris suis
  publication-title: Anal. Bioanal. Chem.
  doi: 10.1007/s00216-015-9154-8
– volume: 8
  start-page: 391
  year: 1992
  ident: 10.1016/j.bbagen.2017.01.009_bb0085
  article-title: Screening of insect cell lines for the production of recombinant proteins and infectious virus in the baculovirus expression system
  publication-title: Biotechnol. Prog.
  doi: 10.1021/bp00017a003
– volume: 26
  start-page: 34
  year: 2010
  ident: 10.1016/j.bbagen.2017.01.009_bb0345
  article-title: Identification of genes encoding N-glycan processing β-N-acetylglucosaminidases in Trichoplusia ni and Bombyx mori: implications for glycoengineering of baculovirus expression systems
  publication-title: Biotechnol. Prog.
  doi: 10.1002/btpr.298
– volume: 330
  start-page: 130
  year: 2008
  ident: 10.1016/j.bbagen.2017.01.009_bb0440
  article-title: False positive reactivity of recombinant, diagnostic, glycoproteins produced in High Five insect cells: effect of glycosylation
  publication-title: J. Immunol. Methods
  doi: 10.1016/j.jim.2007.08.002
– volume: 12
  start-page: 1173
  year: 2013
  ident: 10.1016/j.bbagen.2017.01.009_bb0115
  article-title: Mass spectrometric analysis of neutral and anionic N-glycans from a Dictyostelium discoideum model for human congenital disorder of glycosylation CDG IL
  publication-title: J. Proteome Res.
  doi: 10.1021/pr300806b
– volume: 7
  year: 2012
  ident: 10.1016/j.bbagen.2017.01.009_bb0255
  article-title: SweetBac: a new approach for the production of mammalianised glycoproteins in insect cells
  publication-title: PLoS One
  doi: 10.1371/annotation/bd906c17-a44b-443d-9051-7d31d8e47afa
– volume: 153
  start-page: 160
  year: 2011
  ident: 10.1016/j.bbagen.2017.01.009_bb0415
  article-title: Insect cells for antibody production: evaluation of an efficient alternative
  publication-title: J. Biotechnol.
  doi: 10.1016/j.jbiotec.2011.02.009
– volume: 73
  start-page: 1357
  year: 2013
  ident: 10.1016/j.bbagen.2017.01.009_bb0435
  article-title: Recombinant trivalent influenza vaccine (FluBlok®): a review of its use in the prevention of seasonal influenza in adults
  publication-title: Drugs
  doi: 10.1007/s40265-013-0103-6
– volume: 281
  start-page: 3343
  year: 2006
  ident: 10.1016/j.bbagen.2017.01.009_bb0175
  article-title: Modulation of neural carbohydrate epitope expression in Drosophila melanogaster cells
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M508334200
– volume: 16
  start-page: 629
  year: 1999
  ident: 10.1016/j.bbagen.2017.01.009_bb0240
  article-title: Monosaccharide compositions of Danaus plexippus (monarch butterfly) and Trichoplusia ni (cabbage looper) egg glycoproteins
  publication-title: Glycoconj. J.
  doi: 10.1023/A:1007029017400
– volume: 171
  start-page: 73
  year: 1988
  ident: 10.1016/j.bbagen.2017.01.009_bb0275
  article-title: Analyses of N-linked oligosaccharides using a two-dimensional mapping technique
  publication-title: Anal. Biochem.
  doi: 10.1016/0003-2697(88)90126-1
– volume: 88
  start-page: 13781
  year: 2014
  ident: 10.1016/j.bbagen.2017.01.009_bb0150
  article-title: Transcriptome responses of the host Trichoplusia ni to infection by the baculovirus autographa californica multiple nucleopolyhedrovirus
  publication-title: J. Virol.
  doi: 10.1128/JVI.02243-14
– volume: 7
  year: 2012
  ident: 10.1016/j.bbagen.2017.01.009_bb0090
  article-title: Resistance of Trichoplusia ni to Bacillus thuringiensis toxin Cry1Ac is independent of alteration of the cadherin-like receptor for cry toxins
  publication-title: PLoS One
– volume: 480
  start-page: 297
  year: 2010
  ident: 10.1016/j.bbagen.2017.01.009_bb0055
  article-title: The glycomics of glycan glucuronylation in Drosophila melanogaster
  publication-title: Methods Enzymol.
  doi: 10.1016/S0076-6879(10)80014-X
– volume: 9
  year: 2014
  ident: 10.1016/j.bbagen.2017.01.009_bb0305
  article-title: The α1,6-fucosyltransferase gene (fut8) from the Sf9 lepidopteran insect cell line: insights into fut8 evolution
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0110422
– volume: 17
  start-page: 11
  year: 2005
  ident: 10.1016/j.bbagen.2017.01.009_bb0420
  article-title: Subversion of immunological signalling by a filarial nematode phosphorylcholine-containing secreted product
  publication-title: Cell. Signal.
  doi: 10.1016/j.cellsig.2004.05.014
– volume: 25
  start-page: 1441
  year: 2015
  ident: 10.1016/j.bbagen.2017.01.009_bb0270
  article-title: Sialylation potentials of the silkworm, Bombyx mori; B. mori possesses an active α2,6-sialyltransferase
  publication-title: Glycobiology
  doi: 10.1093/glycob/cwv060
– volume: 308
  start-page: 148
  year: 1994
  ident: 10.1016/j.bbagen.2017.01.009_bb0030
  article-title: Structures of the N-linked oligosaccharides of the membrane glycoproteins from three lepidopteran cell lines (Sf-21, IZD-Mb-0503, Bm-N)
  publication-title: Arch. Biochem. Biophys.
  doi: 10.1006/abbi.1994.1021
– volume: 287
  start-page: 7084
  year: 2012
  ident: 10.1016/j.bbagen.2017.01.009_bb0330
  article-title: Substrate specificities and intracellular distributions of three N-glycan processing enzymes functioning at a key branch point in the insect N-glycosylation pathway
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M111.296814
– volume: 26
  start-page: 230
  year: 2015
  ident: 10.1016/j.bbagen.2017.01.009_bb0070
  article-title: Structural characterization and biological implications of sulfated N-glycans in a serine protease from the neotropical moth Hylesia metabus (Cramer [1775]) (Lepidoptera: Saturniidae)
  publication-title: Glycobiology
– volume: 67
  start-page: 2055
  year: 2003
  ident: 10.1016/j.bbagen.2017.01.009_bb0205
  article-title: 350-kDa royal jelly glycoprotein (apisin), which stimulates proliferation of human monocytes, bears the β1-3galactosylated N-glycan: analysis of the N-glycosylation site
  publication-title: Biosci. Biotechnol. Biochem.
  doi: 10.1271/bbb.67.2055
– volume: 1259
  start-page: 220
  year: 1995
  ident: 10.1016/j.bbagen.2017.01.009_bb0215
  article-title: Structural elucidation of two novel amphoteric glycosphingolipids from the earthworm, Pheretima hilgendorfi
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0005-2760(95)00168-9
– volume: 18
  start-page: 2
  year: 2001
  ident: 10.1016/j.bbagen.2017.01.009_bb0445
  article-title: Genetic differences between humans and great apes
  publication-title: Mol. Phylogenet. Evol.
  doi: 10.1006/mpev.2000.0799
– volume: 279
  start-page: 49588
  year: 2004
  ident: 10.1016/j.bbagen.2017.01.009_bb0140
  article-title: Molecular basis of anti-horseradish peroxidase staining in Caenorhabditis elegans
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M408978200
– volume: 83
  start-page: 115
  year: 2013
  ident: 10.1016/j.bbagen.2017.01.009_bb0355
  article-title: Biochemical characterization of a novel β-N-acetylhexosaminidase from the insect Ostrinia furnacalis
  publication-title: Arch. Insect Biochem. Physiol.
  doi: 10.1002/arch.21099
– volume: 15
  year: 2015
  ident: 10.1016/j.bbagen.2017.01.009_bb0315
  article-title: Identification of core α1,3-fucosyltransferase gene from silkworm: an insect popularly used to express mammalian proteins
  publication-title: J. Insect Sci.
  doi: 10.1093/jisesa/iev088
– volume: 382
  start-page: 67
  year: 2004
  ident: 10.1016/j.bbagen.2017.01.009_bb0385
  article-title: The Drosophila melanogaster homologue of the humna histo-blood group Pk gene encodes a glycolipid-modifying α1,4-N-acetylgalactosaminyltransferase
  publication-title: Biochem. J.
  doi: 10.1042/BJ20040535
– volume: 263
  start-page: 18253
  year: 1988
  ident: 10.1016/j.bbagen.2017.01.009_bb0185
  article-title: The asparagine-linked oligosaccharides on bovine fetuin. Structural analysis of N-glycanase-released oligosaccharides by 500-megahertz 1H NMR spectroscopy
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(19)81354-6
– volume: 265
  start-page: 9737
  year: 1990
  ident: 10.1016/j.bbagen.2017.01.009_bb0195
  article-title: Novel phosphorus-containing glycosphingolipids from the blowfly Calliphora vicina Meigen. Structural analysis by 1H and 1H[31P]-edited NMR spectroscopy at 600 and 500MHz
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(19)38733-2
– volume: 402
  start-page: 105
  year: 2007
  ident: 10.1016/j.bbagen.2017.01.009_bb0300
  publication-title: Biochem. J.
  doi: 10.1042/BJ20060964
– volume: 8
  start-page: 1838
  year: 2009
  ident: 10.1016/j.bbagen.2017.01.009_bb0430
  article-title: Homodimeric alkaline phosphatase located at Helicoverpa armigera midgut, a putative receptor of Cry1Ac contains α-GalNAc in terminal glycan structure as interactive epitope
  publication-title: J. Proteome Res.
  doi: 10.1021/pr8006528
– volume: 12
  start-page: 77
  year: 1995
  ident: 10.1016/j.bbagen.2017.01.009_bb0020
  article-title: The asparagine-linked carbohydrate of honeybee venom hyaluronidase
  publication-title: Glycoconj. J.
  doi: 10.1007/BF00731872
– start-page: 165
  year: 2009
  ident: 10.1016/j.bbagen.2017.01.009_bb0060
  article-title: Insect cell glycosylation patterns in the context of biopharmaceuticals
– volume: 1503
  start-page: 167
  year: 2017
  ident: 10.1016/j.bbagen.2017.01.009_bb0110
  article-title: Analysis of invertebrate and protist N-glycans
  publication-title: Methods Mol. Biol.
  doi: 10.1007/978-1-4939-6493-2_13
– volume: 22
  start-page: 300
  year: 2012
  ident: 10.1016/j.bbagen.2017.01.009_bb0105
  article-title: The N-glycans of Trichomonas vaginalis contain variable core and antennal modifications
  publication-title: Glycobiology
  doi: 10.1093/glycob/cwr149
– volume: 450
  start-page: 953
  year: 2014
  ident: 10.1016/j.bbagen.2017.01.009_bb0310
  article-title: Cloning, expression and characterization of Bombyx mori α1,6-fucosyltransferase
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2014.06.087
– volume: 1075
  start-page: 146
  year: 1991
  ident: 10.1016/j.bbagen.2017.01.009_bb0015
  article-title: Characterisation of oligosaccharides from Drosophila melanogaster glycoproteins
  publication-title: Biochim. Biophys. Acta Gen. Subj.
  doi: 10.1016/0304-4165(91)90245-C
– volume: 267
  start-page: 3549
  year: 2000
  ident: 10.1016/j.bbagen.2017.01.009_bb0225
  article-title: Zwitterionic and acidic glycosphingolipids of the Drosophila melanogaster embryo
  publication-title: Eur. J. Biochem.
  doi: 10.1046/j.1432-1327.2000.01383.x
– volume: 25
  start-page: 1323
  year: 2015
  ident: 10.1016/j.bbagen.2017.01.009_bb0125
  article-title: Symbol nomenclature for graphical representations of glycans
  publication-title: Glycobiology
  doi: 10.1093/glycob/cwv091
– volume: 15
  start-page: 73
  year: 2016
  ident: 10.1016/j.bbagen.2017.01.009_bb0165
  article-title: More than just oligomannose: An N-glycomic comparison of Penicillium species
  publication-title: Mol. Cell. Proteomics
  doi: 10.1074/mcp.M115.055061
– volume: 273
  start-page: 466
  year: 1998
  ident: 10.1016/j.bbagen.2017.01.009_bb0180
  article-title: Structural elucidation and monokine-inducing activity of two biologically active zwitterionic glycosphingolipids derived from the porcine parasitic nematode Ascaris suum
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.273.1.466
– volume: 58
  start-page: 535
  year: 2009
  ident: 10.1016/j.bbagen.2017.01.009_bb0395
  article-title: Molecular cloning and expression of a novel cholinephosphotransferase involved in glycoglycerophospholipid biosynthesis of mycoplasma fermentans
  publication-title: Curr. Microbiol.
  doi: 10.1007/s00284-009-9362-6
– volume: 291
  start-page: 11064
  year: 2016
  ident: 10.1016/j.bbagen.2017.01.009_bb0410
  article-title: Mammalian α1,6-fucosyltransferase (FUT8) is the sole enzyme responsible for the N-acetylglucosaminyltransferase I-independent core fucosylation of high-mannose N-glycans
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M116.720789
– volume: 42
  start-page: 279
  year: 2012
  ident: 10.1016/j.bbagen.2017.01.009_bb0145
  article-title: Mass spectrometric analysis of the immunodominant glycan epitope of Echinococcus granulosus antigen Ag5
  publication-title: Int. J. Parasitol.
  doi: 10.1016/j.ijpara.2012.01.002
– volume: 193
  start-page: 90
  year: 1991
  ident: 10.1016/j.bbagen.2017.01.009_bb0160
  article-title: Calculated two-dimensional sugar map of pyridylaminated oligosaccharides: elucidation of the jack bean α-mannosidase digestion pathway of Man9GlcNAc2
  publication-title: Anal. Biochem.
  doi: 10.1016/0003-2697(91)90047-W
– volume: 382
  start-page: 209
  year: 2001
  ident: 10.1016/j.bbagen.2017.01.009_bb0325
  article-title: Cloning and expression of Drosophila melanogaster UDP-N-acetylglucosamine: α-6-D-mannoside-β-1,2-N-acetylglucosaminyltransferase I
  publication-title: Biol. Chem.
  doi: 10.1515/BC.2001.028
– volume: 278
  start-page: 9116
  year: 2003
  ident: 10.1016/j.bbagen.2017.01.009_bb0390
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M209344200
– volume: 13
  start-page: 6144
  year: 2014
  ident: 10.1016/j.bbagen.2017.01.009_bb0400
  article-title: Rapid analysis of cell surface N-glycosylation from living cells using mass spectrometry
  publication-title: J. Proteome Res.
  doi: 10.1021/pr5003005
– volume: 68
  start-page: 52
  year: 2016
  ident: 10.1016/j.bbagen.2017.01.009_bb0320
  article-title: The fucomic potential of mosquitoes: fucosylated N-glycan epitopes and their cognate fucosyltransferases
  publication-title: Insect Biochem. Mol. Biol.
  doi: 10.1016/j.ibmb.2015.11.001
– volume: 72
  start-page: 909
  year: 1976
  ident: 10.1016/j.bbagen.2017.01.009_bb0405
  article-title: The control of glycoprotein synthesis. N-acetylglucosamine linkage to a mannose residue as a signal for the attachment of L-fucose to the asparagine-linked N-acetylglucosamine of glycopeptide from α1-acid glycoprotein
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/S0006-291X(76)80218-5
– volume: 272
  start-page: 9062
  year: 1997
  ident: 10.1016/j.bbagen.2017.01.009_bb0035
  article-title: Differential N-glycan patterns of secreted and intracellular IgG produced in Trichoplusia ni cells
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.272.14.9062
– volume: 8
  start-page: 741
  year: 1998
  ident: 10.1016/j.bbagen.2017.01.009_bb0260
  article-title: N-linked glycosylation of a baculovirus-expressed recombinant glycoprotein in insect larvae and tissue culture cells
  publication-title: Glycobiology
  doi: 10.1093/glycob/8.7.741
– start-page: 599
  year: 1981
  ident: 10.1016/j.bbagen.2017.01.009_bb0095
  article-title: Development of mass-rearing technology
– volume: 15
  start-page: 463
  year: 2005
  ident: 10.1016/j.bbagen.2017.01.009_bb0295
  article-title: Fucosyltransferase substrate specificity and the order of fucosylation in invertebrates
  publication-title: Glycobiology
  doi: 10.1093/glycob/cwi028
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Snippet Insects are significant to the environment, agriculture, health and biotechnology. Many of these aspects display some relationship to glycosylation, e.g., in...
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SubjectTerms Animals
antennae
antibodies
biotechnology
Cell Line
factories
Glucuronic acid
Glycolipids
glycoproteins
Glycoproteins - metabolism
Glycosylation
Insect
insects
Lepidoptera - metabolism
Lepidoptera - physiology
Lymantria dispar
mammals
Moths - metabolism
Moths - physiology
N-linked oligosaccharides
Nematoda
pathogens
Phosphorylcholine
Phosphorylcholine - metabolism
polysaccharides
Polysaccharides - metabolism
Sulfates - metabolism
Sulphate
Trichoplusia ni
zwitterions
Title The underestimated N-glycomes of lepidopteran species
URI https://dx.doi.org/10.1016/j.bbagen.2017.01.009
https://www.ncbi.nlm.nih.gov/pubmed/28077298
https://www.proquest.com/docview/1858108862
https://www.proquest.com/docview/2000379427
https://pubmed.ncbi.nlm.nih.gov/PMC5330436
Volume 1861
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