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Volumn 5, Issue JUL, 2014, Pages

Protein N-glycosylation in eukaryotic microalgae and its impact on the production of nuclear expressed biopharmaceuticals

Author keywords

Biopharmaceuticals; Chlamydomonas reinhardtii; Endoplasmic reticulum; Glycan; Glycosylation pathway; Golgi apparatus; Microalgae; Phaeodactylum tricornutum

Indexed keywords


EID: 84979738497     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2014.00359     Document Type: Review
Times cited : (80)

References (138)
  • 1
    • 0029085691 scopus 로고
    • Insect cells contain an unusual, membrane-bound-N-acetylglucosaminidase probably involved in the processing of protein N-glycans
    • Altmann, F., Schwihla, H., Staudacher, E., Glössl, J., and März, L. (1995). Insect cells contain an unusual, membrane-bound-N-acetylglucosaminidase probably involved in the processing of protein N-glycans. J. Biol. Chem. 270, 17344-17349. doi: 10.1074/jbc.270.29.17344
    • (1995) J. Biol. Chem , vol.270 , pp. 17344-17349
    • Altmann, F.1    Schwihla, H.2    Staudacher, E.3    Glössl, J.4    März, L.5
  • 3
    • 0029966913 scopus 로고    scopus 로고
    • Stable nuclear transformation of the diatomPhaeodactylum tricornutum
    • Apt, K. E., Grossman, A. R., and Kroth-Pancic, P. G. (1996). Stable nuclear transformation of the diatomPhaeodactylum tricornutum. Mol. Gen. Genet. 252, 572-579.
    • (1996) Mol. Gen. Genet , vol.252 , pp. 572-579
    • Apt, K.E.1    Grossman, A.R.2    Kroth-Pancic, P.G.3
  • 4
    • 79953186622 scopus 로고    scopus 로고
    • N-glycans of Phaeodactylum tricornutum diatom and functional characterization of its N-acetylglucosaminyltransferase I enzyme
    • Baïet, B., Burel, C., Saint-Jean, B., Louvet, R., Menu-Bouaouiche, L., Kiefer-Meyer, M.-C., et al. (2011). N-glycans of Phaeodactylum tricornutum diatom and functional characterization of its N-acetylglucosaminyltransferase I enzyme. J. Biol. Chem. 286, 6152-6164. doi: 10.1074/jbc.M110.175711
    • (2011) J. Biol. Chem , vol.286 , pp. 6152-6164
    • Baïet, B.1    Burel, C.2    Saint-Jean, B.3    Louvet, R.4    Menu-Bouaouiche, L.5    Kiefer-Meyer, M.-C.6
  • 5
    • 84873866373 scopus 로고    scopus 로고
    • A new strategy to produce a defensin: Stable production of mutated NP-1 in nitrate reductase-deficient chlorella ellipsoidea
    • Bai, L.-L., Yin, W.-B., Chen, Y.-H., Niu, L.-L., Sun, Y.-R., Zhao, S.-M., et al. (2013). A new strategy to produce a defensin: stable production of mutated NP-1 in nitrate reductase-deficient chlorella ellipsoidea. PLoS ONE 8:e54966. doi: 10.1371/journal.pone.0054966
    • (2013) Plos ONE , vol.8
    • Bai, L.-L.1    Yin, W.-B.2    Chen, Y.-H.3    Niu, L.-L.4    Sun, Y.-R.5    Zhao, S.-M.6
  • 7
    • 33646737444 scopus 로고    scopus 로고
    • An antibody produced in tobacco expressing a hybrid β-1, 4-galactosyltransferase is essentially devoid of plant carbohydrate epitopes
    • Bakker, H., Rouwendal, G. J., Karnoup, A. S., Florack, D. E., Stoopen, G. M., Helsper, J. P., et al. (2006). An antibody produced in tobacco expressing a hybrid β-1, 4-galactosyltransferase is essentially devoid of plant carbohydrate epitopes. Proc. Natl. Acad. Sci. U.S.A. 103, 7577-7582. doi: 10.1073/pnas.0600879103
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 7577-7582
    • Bakker, H.1    Rouwendal, G.J.2    Karnoup, A.S.3    Florack, D.E.4    Stoopen, G.M.5    Helsper, J.P.6
  • 8
    • 0025030291 scopus 로고
    • The oligosaccharides of the glycoprotein pheromone of Volvox carteri f. Nagariensis Iyengar (Chlorophyceae)
    • Balshüsemann, D., and Jaenicke, L. (1990). The oligosaccharides of the glycoprotein pheromone of Volvox carteri f. nagariensis Iyengar (Chlorophyceae). Eur. J. Biochem. 192, 231-237. doi: 10.1111/j.1432-1033.1990.tb19220.x
    • (1990) Eur. J. Biochem , vol.192 , pp. 231-237
    • Balshüsemann, D.1    Jaenicke, L.2
  • 9
    • 0038581900 scopus 로고    scopus 로고
    • Immunoreactivity in mammals of two typical plant glyco-epitopes, core α (1,3)-fucose and core xylose
    • Bardor, M., Faveeuw, C., Fitchette, A.-C., Gilbert, D., Galas, L., Trottein, F., et al. (2003). Immunoreactivity in mammals of two typical plant glyco-epitopes, core α (1,3)-fucose and core xylose. Glycobiology 13, 427-434. doi: 10.1093/glycob/cwg024
    • (2003) Glycobiology , vol.13 , pp. 427-434
    • Bardor, M.1    Faveeuw, C.2    Fitchette, A.-C.3    Gilbert, D.4    Galas, L.5    Trottein, F.6
  • 10
    • 67649757166 scopus 로고    scopus 로고
    • Engineering algae for biohydrogen and biofuel production
    • Beer, L. L., Boyd, E. S., Peters, J. W., and Posewitz, M. C. (2009). Engineering algae for biohydrogen and biofuel production. Curr. Opin. Biotechnol. 20, 264-271. doi: 10.1016/j.copbio.2009.06.002
    • (2009) Curr. Opin. Biotechnol , vol.20 , pp. 264-271
    • Beer, L.L.1    Boyd, E.S.2    Peters, J.W.3    Posewitz, M.C.4
  • 11
    • 84861408399 scopus 로고    scopus 로고
    • The genome of the polar eukaryotic microalga Coccomyxa subellipsoidea reveals traits of cold adaptation
    • Blanc, G., Agarkova, I., Grimwood, J., Kuo, A., Brueggeman, A., Dunigan, D. D., et al. (2012). The genome of the polar eukaryotic microalga Coccomyxa subellipsoidea reveals traits of cold adaptation. Genome Biol. 13:R39. doi: 10.1186/gb-2012-13-5-r39
    • (2012) Genome Biol , vol.13
    • Blanc, G.1    Agarkova, I.2    Grimwood, J.3    Kuo, A.4    Brueggeman, A.5    Dunigan, D.D.6
  • 12
    • 78049477633 scopus 로고    scopus 로고
    • The Chlorella variabilis NC64A genome reveals adaptation to photosymbiosis, coevolution with viruses, and cryptic sex
    • Blanc, G., Duncan, G., Agarkova, I., Borodovsky, M., Gurnon, J., Kuo, A., et al. (2010). The Chlorella variabilis NC64A genome reveals adaptation to photosymbiosis, coevolution with viruses, and cryptic sex. Plant Cell Online 22, 2943-2955. doi: 10.1105/tpc.110.076406
    • (2010) Plant Cell Online , vol.22 , pp. 2943-2955
    • Blanc, G.1    Duncan, G.2    Agarkova, I.3    Borodovsky, M.4    Gurnon, J.5    Kuo, A.6
  • 13
    • 84890968181 scopus 로고    scopus 로고
    • Reconstruction of the lipid metabolism for the microalga Monoraphidium neglectum from its genome sequence reveals characteristics suitable for biofuel production
    • Bogen, C., Al-Dilaimi, A., Albersmeier, A., Wichmann, J., Grundmann, M., Rupp, O., et al. (2013). Reconstruction of the lipid metabolism for the microalga Monoraphidium neglectum from its genome sequence reveals characteristics suitable for biofuel production. BMC Genomics 14:926. doi: 10.1186/1471-2164-14-926
    • (2013) BMC Genomics , vol.14 , pp. 926
    • Bogen, C.1    Al-Dilaimi, A.2    Albersmeier, A.3    Wichmann, J.4    Grundmann, M.5    Rupp, O.6
  • 14
    • 0032904470 scopus 로고    scopus 로고
    • The dolichol pathway of N-linked glycosylation
    • Burda, P., and Aebi, M. (1999). The dolichol pathway of N-linked glycosylation. Biochim. Biophys. Acta 1426, 239-257. doi: 10.1016/S0304-4165(98)00127-5
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 239-257
    • Burda, P.1    Aebi, M.2
  • 15
    • 84899462929 scopus 로고    scopus 로고
    • Downstream processing of biopharmaceutical proteins produced in plants: The pros and cons of flocculants
    • Buyel, J. F., and Fischer, R. (2014). Downstream processing of biopharmaceutical proteins produced in plants: the pros and cons of flocculants. Bioengineered 5, 138-142. doi: 10.4161/bioe.28061
    • (2014) Bioengineered , vol.5 , pp. 138-142
    • Buyel, J.F.1    Fischer, R.2
  • 16
    • 59449106108 scopus 로고    scopus 로고
    • La production de biocarburant lipidique avec des microalgues: Promesses et défis
    • Cadoret, J.-P., and Bernard, O. (2008). La production de biocarburant lipidique avec des microalgues: promesses et défis. J. Soc. Biol. 202, 201-211. doi: 10.1051/jbio:2008022
    • (2008) J. Soc. Biol , vol.202 , pp. 201-211
    • Cadoret, J.-P.1    Bernard, O.2
  • 17
    • 84872844872 scopus 로고    scopus 로고
    • Generation of biologically active multi-sialylated recombinant human EPOFc in plants
    • Castilho, A., Neumann, L., Gattinger, P., Strasser, R., Vorauer-Uhl, K., Sterovsky, T., et al. (2013). Generation of biologically active multi-sialylated recombinant human EPOFc in plants. PLoS ONE 8:e54836. doi: 10.1371/journal.pone.0054836
    • (2013) Plos ONE , vol.8
    • Castilho, A.1    Neumann, L.2    Gattinger, P.3    Strasser, R.4    Vorauer-Uhl, K.5    Sterovsky, T.6
  • 18
    • 50649089667 scopus 로고    scopus 로고
    • Construction of a functional CMP-sialic acid biosynthesis pathway in Arabidopsis
    • Castilho, A., Pabst, M., Leonard, R., Veit, C., Altmann, F., Mach, L., et al. (2008). Construction of a functional CMP-sialic acid biosynthesis pathway in Arabidopsis. Plant Physiol. 147, 331-339. doi: 10.1104/pp.108.117572
    • (2008) Plant Physiol , vol.147 , pp. 331-339
    • Castilho, A.1    Pabst, M.2    Leonard, R.3    Veit, C.4    Altmann, F.5    Mach, L.6
  • 19
    • 77952408200 scopus 로고    scopus 로고
    • In planta protein sialylation through overexpression of the respective mammalian pathway
    • Castilho, A., Strasser, R., Stadlmann, J., Grass, J., Jez, J., Gattinger, P., et al. (2010). In planta protein sialylation through overexpression of the respective mammalian pathway. J. Biol. Chem. 285, 15923-15930. doi: 10.1074/jbc.M109.088401
    • (2010) J. Biol. Chem , vol.285 , pp. 15923-15930
    • Castilho, A.1    Strasser, R.2    Stadlmann, J.3    Grass, J.4    Jez, J.5    Gattinger, P.6
  • 20
    • 0031153996 scopus 로고    scopus 로고
    • Epigenetic silencing of a foreign gene in nuclear transformants of Chlamydomonas
    • Cerutti, H., Johnson, A. M., Gillham, N. W., and Boynton, J. E. (1997). Epigenetic silencing of a foreign gene in nuclear transformants of Chlamydomonas. Plant Cell 9, 925-945. doi: 10.1105/tpc.9.6.925
    • (1997) Plant Cell , vol.9 , pp. 925-945
    • Cerutti, H.1    Johnson, A.M.2    Gillham, N.W.3    Boynton, J.E.4
  • 21
    • 80052388966 scopus 로고    scopus 로고
    • RNA-mediated silencing in algae: Biological roles and tools for analysis of gene function
    • Cerutti, H., Ma, X., Msanne, J., and Repas, T. (2011). RNA-mediated silencing in algae: biological roles and tools for analysis of gene function. Eukaryot Cell 10, 1164-1172. doi: 10.1128/EC.05106-11
    • (2011) Eukaryot Cell , vol.10 , pp. 1164-1172
    • Cerutti, H.1    Ma, X.2    Msanne, J.3    Repas, T.4
  • 22
    • 84872499682 scopus 로고    scopus 로고
    • Expression of soybean Kunitz trypsin inhibitor gene SKTI in Dunaliella salina
    • Chai, X.-J., Chen, H.-X., Xu, W.-Q., and Xu, Y.-W. (2013). Expression of soybean Kunitz trypsin inhibitor gene SKTI in Dunaliella salina. J. Appl. Phycol. 25, 139-144. doi: 10.1007/s10811-012-9847-8
    • (2013) J. Appl. Phycol , vol.25 , pp. 139-144
    • Chai, X.-J.1    Chen, H.-X.2    Xu, W.-Q.3    Xu, Y.-W.4
  • 23
    • 0034864815 scopus 로고    scopus 로고
    • Highly efficient expression of rabbit neutrophil peptide-1 gene in Chlorella ellipsoidea cells
    • Chen, Y., Wang, Y., Sun, Y., Zhang, L., and Li, W. (2001). Highly efficient expression of rabbit neutrophil peptide-1 gene in Chlorella ellipsoidea cells. Curr. Genet. 39, 365-370. doi: 10.1007/s002940100205
    • (2001) Curr. Genet , vol.39 , pp. 365-370
    • Chen, Y.1    Wang, Y.2    Sun, Y.3    Zhang, L.4    Li, W.5
  • 24
    • 40849142102 scopus 로고    scopus 로고
    • Cetuximab-induced anaphylaxis and IgE specific for galactose-α-1, 3-galactose. New Engl
    • Chung, C. H., Mirakhur, B., Chan, E., Le, Q.-T., Berlin, J., Morse, M., et al. (2008). Cetuximab-induced anaphylaxis and IgE specific for galactose-α-1, 3-galactose. New Engl. J. Med. 358, 1109-1117. doi: 10.1056/NEJMoa074943
    • (2008) J. Med , vol.358 , pp. 1109-1117
    • Chung, C.H.1    Mirakhur, B.2    Chan, E.3    Le, Q.-T.4    Berlin, J.5    Morse, M.6
  • 25
    • 77950628448 scopus 로고    scopus 로고
    • Optimisation of contained Nicotiana tabacum cultivation for the production of recombinant protein pharmaceuticals
    • Colgan, R., Atkinson, C. J., Paul, M., Hassan, S., Drake, P. M. W., Sexton, A. L., et al. (2010). Optimisation of contained Nicotiana tabacum cultivation for the production of recombinant protein pharmaceuticals. Transgenic Res. 19, 241-256. doi: 10.1007/s11248-009-9303-y
    • (2010) Transgenic Res , vol.19 , pp. 241-256
    • Colgan, R.1    Atkinson, C.J.2    Paul, M.3    Hassan, S.4    Drake, P.M.W.5    Sexton, A.L.6
  • 26
    • 33845711353 scopus 로고    scopus 로고
    • Glycan optimization of a human monoclonal antibody in the aquatic plant Lemna minor
    • Cox, K. M., Sterling, J. D., Regan, J. T., Gasdaska, J. R., Frantz, K. K., Peele, C. G., et al. (2006). Glycan optimization of a human monoclonal antibody in the aquatic plant Lemna minor. Nat. Biotechnol. 24, 1591-1597. doi: 10.1038/nbt1260
    • (2006) Nat. Biotechnol , vol.24 , pp. 1591-1597
    • Cox, K.M.1    Sterling, J.D.2    Regan, J.T.3    Gasdaska, J.R.4    Frantz, K.K.5    Peele, C.G.6
  • 27
    • 33747890974 scopus 로고    scopus 로고
    • Inhibition of hybrid- and complex-type glycosylation reveals the presence of the GlcNAc transferase I-independent fucosylation pathway
    • Crispin, M., Harvey, D. J., Chang, V. T., Yu, C., Aricescu, A. R., Jones, E. Y., et al. (2006). Inhibition of hybrid- and complex-type glycosylation reveals the presence of the GlcNAc transferase I-independent fucosylation pathway. Glycobiology 16, 748-756. doi: 10.1093/glycob/cwj119
    • (2006) Glycobiology , vol.16 , pp. 748-756
    • Crispin, M.1    Harvey, D.J.2    Chang, V.T.3    Yu, C.4    Aricescu, A.R.5    Jones, E.Y.6
  • 28
    • 84856970614 scopus 로고    scopus 로고
    • Glycoprotein production in moss bioreactors
    • Decker, E. L., and Reski, R. (2012). Glycoprotein production in moss bioreactors. Plant Cell Rep. 31, 453-460. doi: 10.1007/s00299-011-1152-5
    • (2012) Plant Cell Rep , vol.31 , pp. 453-460
    • Decker, E.L.1    Reski, R.2
  • 29
    • 61349178501 scopus 로고    scopus 로고
    • Production of recombinant proteins by microbes and higher organisms. Biotechnol
    • Demain, A. L., and Vaishnav, P. (2009). Production of recombinant proteins by microbes and higher organisms. Biotechnol. Adv. 27, 297-306. doi: 10.1016/j.biotechadv.2009.01.008
    • (2009) Adv , vol.27 , pp. 297-306
    • Demain, A.L.1    Vaishnav, P.2
  • 30
    • 84876587491 scopus 로고    scopus 로고
    • A chlamydomonas-derived human papillomavirus 16 E7 vaccine induces specific tumor protection
    • Demurtas, O. C., Massa, S., Ferrante, P., Venuti, A., Franconi, R., and Giuliano, G. (2013). A chlamydomonas-derived human papillomavirus 16 E7 vaccine induces specific tumor protection. PLoS ONE 8:e61473. doi: 10.1371/journal.pone.0061473
    • (2013) Plos ONE , vol.8
    • Demurtas, O.C.1    Massa, S.2    Ferrante, P.3    Venuti, A.4    Franconi, R.5    Giuliano, G.6
  • 31
    • 77953999126 scopus 로고    scopus 로고
    • Production of antibodies in plants: Status after twenty years
    • De Muynck, B., Navarre, C., and Boutry, M. (2010). Production of antibodies in plants: status after twenty years. Plant Biotechnol. J. 8, 529-563. doi: 10.1111/j.1467-7652.2009.00494.x
    • (2010) Plant Biotechnol. J , vol.8 , pp. 529-563
    • De Muynck, B.1    Navarre, C.2    Boutry, M.3
  • 33
    • 70349695698 scopus 로고    scopus 로고
    • Development of rhizosecretion as a production system for recombinant proteins from hydroponic cultivated tobacco
    • Drake, P. M. W., Barbi, T., Sexton, A., McGowan, E., Stadlmann, J., Navarre, C., et al. (2009). Development of rhizosecretion as a production system for recombinant proteins from hydroponic cultivated tobacco. FASEB J. 23, 3581-3589. doi: 10.1096/fj.09-131771
    • (2009) FASEB J , vol.23 , pp. 3581-3589
    • Drake, P.M.W.1    Barbi, T.2    Sexton, A.3    McGowan, E.4    Stadlmann, J.5    Navarre, C.6
  • 34
    • 61349114218 scopus 로고    scopus 로고
    • Strategies to facilitate transgene expression in Chlamydomonas reinhardtii
    • Eichler-Stahlberg, A., Weisheit, W., Ruecker, O., and Heitzer, M. (2009). Strategies to facilitate transgene expression in Chlamydomonas reinhardtii. Planta 229, 873-883. doi: 10.1007/s00425-008-0879-x
    • (2009) Planta , vol.229 , pp. 873-883
    • Eichler-Stahlberg, A.1    Weisheit, W.2    Ruecker, O.3    Heitzer, M.4
  • 35
    • 67651115703 scopus 로고    scopus 로고
    • Improvement of efficiency of genetic transformation for Dunaliella salina by glass beads method
    • Feng, S., Xue, L., Liu, H., and Lu, P. (2009). Improvement of efficiency of genetic transformation for Dunaliella salina by glass beads method. Mol. Biol. Rep. 36, 1433-1439. doi: 10.1007/s11033-008-9333-1
    • (2009) Mol. Biol. Rep , vol.36 , pp. 1433-1439
    • Feng, S.1    Xue, L.2    Liu, H.3    Lu, P.4
  • 36
    • 0034888190 scopus 로고    scopus 로고
    • The flanking regions of PsaD drive efficient gene expression in the nucleus of the green alga Chlamydomonas reinhardtii
    • Fischer, N., and Rochaix, J.-D. (2001). The flanking regions of PsaD drive efficient gene expression in the nucleus of the green alga Chlamydomonas reinhardtii. Mol. Genet. Genomics 265, 888-894. doi: 10.1007/s004380100485
    • (2001) Mol. Genet. Genomics , vol.265 , pp. 888-894
    • Fischer, N.1    Rochaix, J.-D.2
  • 37
    • 34748885169 scopus 로고    scopus 로고
    • Plant Proteomics and Glycosylation
    • eds H. Thiellement, M. Zivy, C. Damerval, and V. Méchin (Humana Press), Accessed June 16, 2014
    • Fitchette, A.-C., Dinh, O. T., Faye, L., and Bardor, M. (2007). “Plant Proteomics and Glycosylation,” in Plant Proteomics Methods in Molecular Biology, eds H. Thiellement, M. Zivy, C. Damerval, and V. Méchin (Humana Press), 317-342. Available online at: http://link.springer.com/protocol/10.1385/1-59745-227-0%3A317 [Accessed June 16, 2014].
    • (2007) Plant Proteomics Methods in Molecular Biology , pp. 317-342
    • Fitchette, A.-C.1    Dinh, O.T.2    Faye, L.3    Bardor, M.4
  • 38
    • 0033179996 scopus 로고    scopus 로고
    • A synthetic gene coding for the green fluorescent protein (GFP) is a versatile reporter in Chlamydomonas reinhardtii
    • Fuhrmann, M., Oertel, W., and Hegemann, P. (1999). A synthetic gene coding for the green fluorescent protein (GFP) is a versatile reporter in Chlamydomonas reinhardtii. Plant J. 19, 353-361. doi: 10.1046/j.1365-313X.1999.00526.x
    • (1999) Plant J , vol.19 , pp. 353-361
    • Fuhrmann, M.1    Oertel, W.2    Hegemann, P.3
  • 39
    • 0032763888 scopus 로고    scopus 로고
    • Evolutionary considerations in relating oligosaccharide diversity to biological function
    • Gagneux, P., and Varki, A. (1999). Evolutionary considerations in relating oligosaccharide diversity to biological function. Glycobiology 9, 747-755. doi: 10.1093/glycob/9.8.747
    • (1999) Glycobiology , vol.9 , pp. 747-755
    • Gagneux, P.1    Varki, A.2
  • 40
    • 0347380967 scopus 로고    scopus 로고
    • Stable expression of hepatitis B surface antigen gene in Dunaliella salina (Chlorophyta)
    • Geng, D., Wang, Y., Wang, P., Li, W., and Sun, Y. (2003). Stable expression of hepatitis B surface antigen gene in Dunaliella salina (Chlorophyta). J. Appl. Phycol. 15, 451-456. doi: 10.1023/B:JAPH.0000004298.89183.e5
    • (2003) J. Appl. Phycol , vol.15 , pp. 451-456
    • Geng, D.1    Wang, Y.2    Wang, P.3    Li, W.4    Sun, Y.5
  • 41
    • 66249114347 scopus 로고    scopus 로고
    • N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant Protein C
    • Gil, G.-C., Velander, W. H., and Van Cott, K. E. (2009). N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant Protein C. Proteomics 9, 2555-2567. doi: 10.1002/pmic.200800775
    • (2009) Proteomics , vol.9 , pp. 2555-2567
    • Gil, G.-C.1    Velander, W.H.2    Van Cott, K.E.3
  • 42
    • 0033849052 scopus 로고    scopus 로고
    • Flagellar membrane proteins of Tetraselmis striata butcher (Chlorophyta)
    • Gödel, S., Becker, B., and Melkonian, M. (2000). Flagellar membrane proteins of Tetraselmis striata butcher (Chlorophyta). Protist 151, 147-159. doi: 10.1078/1434-4610-00015
    • (2000) Protist , vol.151 , pp. 147-159
    • Gödel, S.1    Becker, B.2    Melkonian, M.3
  • 44
    • 80053054984 scopus 로고    scopus 로고
    • A single peroxisomal targeting signal mediates matrix protein import in diatoms
    • Gonzalez, N. H., Felsner, G., Schramm, F. D., Klingl, A., Maier, U.-G., and Bolte, K. (2011). A single peroxisomal targeting signal mediates matrix protein import in diatoms. PLoS ONE 6:e25316. doi: 10.1371/journal.pone.0025316
    • (2011) Plos ONE , vol.6
    • Gonzalez, N.H.1    Felsner, G.2    Schramm, F.D.3    Klingl, A.4    Maier, U.-G.5    Bolte, K.6
  • 45
    • 84899630021 scopus 로고    scopus 로고
    • Taliglucerase alfa: An enzyme replacement therapy using plant cell expression technology
    • Grabowski, G. A., Golembo, M., and Shaaltiel, Y. (2014). Taliglucerase alfa: an enzyme replacement therapy using plant cell expression technology. Mol. Genet. Metab. 112, 1-8. doi: 10.1016/j.ymgme.2014.02.011
    • (2014) Mol. Genet. Metab , vol.112 , pp. 1-8
    • Grabowski, G.A.1    Golembo, M.2    Shaaltiel, Y.3
  • 46
    • 79953211111 scopus 로고    scopus 로고
    • Discovery and structural characterization of fucosylated oligomannosidic N-glycans in mushrooms
    • Grass, J., Pabst, M., Kolarich, D., Poltl, G., Leonard, R., Brecker, L., et al. (2011). Discovery and structural characterization of fucosylated oligomannosidic N-glycans in mushrooms. J. Biol. Chem. 286, 5977-5984. doi: 10.1074/jbc.M110.191304
    • (2011) J. Biol. Chem , vol.286 , pp. 5977-5984
    • Grass, J.1    Pabst, M.2    Kolarich, D.3    Poltl, G.4    Leonard, R.5    Brecker, L.6
  • 47
    • 0027184317 scopus 로고
    • Isolation and characterization of the Golgi apparatus of a flagellate scaly green alga
    • Grunow, A., Becker, B., and Melkonian, M. (1993). Isolation and characterization of the Golgi apparatus of a flagellate scaly green alga. Eur. J. Cell Biol. 61, 10-10.
    • (1993) Eur. J. Cell Biol , vol.61 , pp. 10-110
    • Grunow, A.1    Becker, B.2    Melkonian, M.3
  • 49
    • 0032994028 scopus 로고    scopus 로고
    • Expression of human growth hormone by the eukaryotic alga, Chlorella
    • Hawkins, R. L., and Nakamura, M. (1999). Expression of human growth hormone by the eukaryotic alga, Chlorella. Curr. Microbiol. 38, 335-341. doi: 10.1007/PL00006813
    • (1999) Curr. Microbiol , vol.38 , pp. 335-341
    • Hawkins, R.L.1    Nakamura, M.2
  • 50
    • 84863398445 scopus 로고    scopus 로고
    • Production of active human glucocerebrosidase in seeds of Arabidopsis thaliana complex-glycan-deficient (Cgl) plants
    • He, X., Galpin, J. D., Tropak, M. B., Mahuran, D., Haselhorst, T., von Itzstein, M., et al. (2012). Production of active human glucocerebrosidase in seeds of Arabidopsis thaliana complex-glycan-deficient (cgl) plants. Glycobiology 22, 492-503. doi: 10.1093/glycob/cwr157
    • (2012) Glycobiology , vol.22 , pp. 492-503
    • He, X.1    Galpin, J.D.2    Tropak, M.B.3    Mahuran, D.4    Haselhorst, T.5    Von Itzstein, M.6
  • 51
    • 38549102642 scopus 로고    scopus 로고
    • Influence of codon bias on the expression of foreign genes in microalgae
    • Springer, Accessed December 1, 2013
    • Heitzer, M., Eckert, A., Fuhrmann, M., and Griesbeck, C. (2007). “Influence of codon bias on the expression of foreign genes in microalgae,” in Transgenic Microalgae as Green Cell Factories (Springer), 46-53. Available online at: http://link.springer.com/chapter/10.1007/978-0-387-75532-8_5 [Accessed December 1, 2013].
    • (2007) Transgenic Microalgae as Green Cell Factories , pp. 46-53
    • Heitzer, M.1    Eckert, A.2    Fuhrmann, M.3    Griesbeck, C.4
  • 52
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius, A., and Aebi, M. (2001). Intracellular functions of N-linked glycans. Science 291, 2364-2369. doi: 10.1126/science.291.5512.2364
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 54
    • 82555187161 scopus 로고    scopus 로고
    • Algae as protein factories: Expression of a human antibody and the respective antigen in the diatom phaeodactylum tricornutum
    • Hempel, F., Lau, J., Klingl, A., and Maier, U. G. (2011b). Algae as protein factories: expression of a human antibody and the respective antigen in the diatom phaeodactylum tricornutum. PLoS ONE 6:e28424. doi: 10.1371/journal.pone.0028424
    • (2011) Plos ONE , vol.6
    • Hempel, F.1    Lau, J.2    Klingl, A.3    Maier, U.G.4
  • 55
    • 84866084599 scopus 로고    scopus 로고
    • An engineered diatom acting like a plasma cell secreting human IgG antibodies with high efficiency
    • Hempel, F., and Maier, U. G. (2012). An engineered diatom acting like a plasma cell secreting human IgG antibodies with high efficiency. Microb. Cell Fact. 11:126. doi: 10.1186/1475-2859-11-126
    • (2012) Microb. Cell Fact , vol.11 , pp. 126
    • Hempel, F.1    Maier, U.G.2
  • 56
    • 84877962654 scopus 로고    scopus 로고
    • Comparison of internal ribosome entry site (IRES) and Furin-2A (F2A) for monoclonal antibody expression level and quality in CHO cells
    • Ho, S. C. L., Bardor, M., Li, B., Lee, J. J., Song, Z., Tong, Y. W., et al. (2013). Comparison of internal ribosome entry site (IRES) and Furin-2A (F2A) for monoclonal antibody expression level and quality in CHO cells. PLoS ONE 8:e63247. doi: 10.1371/journal.pone.0063247
    • (2013) Plos ONE , vol.8
    • Ho, S.C.L.1    Bardor, M.2    Li, B.3    Lee, J.J.4    Song, Z.5    Tong, Y.W.6
  • 57
    • 0031775473 scopus 로고    scopus 로고
    • Stable expression of mammalian beta 1,4-galactosyltransferase extends the N-glycosylation pathway in insect cells
    • Hollister, J. R., Shaper, J. H., and Jarvis, D. L. (1998). Stable expression of mammalian beta 1,4-galactosyltransferase extends the N-glycosylation pathway in insect cells. Glycobiology 8, 473-480. doi: 10.1093/glycob/8.5.473
    • (1998) Glycobiology , vol.8 , pp. 473-480
    • Hollister, J.R.1    Shaper, J.H.2    Jarvis, D.L.3
  • 58
    • 68749110765 scopus 로고    scopus 로고
    • Optimal and consistent protein glycosylation in mammalian cell culture
    • Hossler, P., Khattak, S. F., and Li, Z. J. (2009). Optimal and consistent protein glycosylation in mammalian cell culture. Glycobiology 19, 936-949. doi: 10.1093/glycob/cwp079
    • (2009) Glycobiology , vol.19 , pp. 936-949
    • Hossler, P.1    Khattak, S.F.2    Li, Z.J.3
  • 59
    • 84863303532 scopus 로고    scopus 로고
    • Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements
    • Huang, C.-J., Lin, H., and Yang, X. (2012). Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements. J. Ind. Microbiol. Biotechnol. 39, 383-399. doi: 10.1007/s10295-011-1082-9
    • (2012) J. Ind. Microbiol. Biotechnol , vol.39 , pp. 383-399
    • Huang, C.-J.1    Lin, H.2    Yang, X.3
  • 60
    • 20144372901 scopus 로고    scopus 로고
    • Glyco-Engineering of Moss Lacking Plant-Specific Sugar Residues
    • Huether, C. M., Lienhart, O., Baur, A., Stemmer, C., Gorr, G., Reski, R., et al. (2005). Glyco-Engineering of Moss Lacking Plant-Specific Sugar Residues. Plant Biol. 7, 292-299. doi: 10.1055/s-2005-837653
    • (2005) Plant Biol , vol.7 , pp. 292-299
    • Huether, C.M.1    Lienhart, O.2    Baur, A.3    Stemmer, C.4    Gorr, G.5    Reski, R.6
  • 61
    • 0028012014 scopus 로고
    • Mice lacking N-acetylglucosaminyltransferase I activity die at mid-gestation, revealing an essential role for complex or hybrid N-linked carbohydrates
    • Ioffe, E., and Stanley, P. (1994). Mice lacking N-acetylglucosaminyltransferase I activity die at mid-gestation, revealing an essential role for complex or hybrid N-linked carbohydrates. Proc. Natl. Acad. Sci. U.S.A. 91, 728-732. doi: 10.1073/pnas.91.2.728
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 728-732
    • Ioffe, E.1    Stanley, P.2
  • 62
    • 0025906543 scopus 로고
    • Transient expression of firefly luciferase in protoplasts of the green alga Chlorella ellipsoidea
    • Jarvis, E. E., and Brown, L. M. (1991). Transient expression of firefly luciferase in protoplasts of the green alga Chlorella ellipsoidea. Curr. Genet. 19, 317-321. doi: 10.1007/BF00355062
    • (1991) Curr. Genet , vol.19 , pp. 317-321
    • Jarvis, E.E.1    Brown, L.M.2
  • 63
    • 66749102794 scopus 로고    scopus 로고
    • Agrobacterium_mediated transformation in the green alga Haematococcus pluvilais (Chlorophyceae, Volvocales) 1
    • Kathiresan, S., Chandrashekar, A., Ravishankar, G. A., and Sarada, R. (2009). Agrobacterium_mediated transformation in the green alga Haematococcus pluvilais (Chlorophyceae, Volvocales) 1. J. Phycol. 45, 642-649. doi: 10.1111/j.1529-8817.2009.00688.x
    • (2009) J. Phycol , vol.45 , pp. 642-649
    • Kathiresan, S.1    Chandrashekar, A.2    Ravishankar, G.A.3    Sarada, R.4
  • 64
    • 0036204864 scopus 로고    scopus 로고
    • Stable integration and functional expression of flounder growth hormone gene in transformed microalga, Chlorella ellipsoidea
    • Kim, D.-H., Kim, Y. T., Cho, J. J., Bae, J.-H., Hur, S.-B., Hwang, I., et al. (2002). Stable integration and functional expression of flounder growth hormone gene in transformed microalga, Chlorella ellipsoidea. Mar. Biotechnol. 4, 63-73. doi: 10.1007/s1012601-0070-x
    • (2002) Mar. Biotechnol , vol.4 , pp. 63-73
    • Kim, D.-H.1    Kim, Y.T.2    Cho, J.J.3    Bae, J.-H.4    Hur, S.-B.5    Hwang, I.6
  • 65
    • 0031721160 scopus 로고    scopus 로고
    • High-frequency nuclear transformation of Chlamydomonas reinhardtii
    • ed L. McIntosh (Academic Press), Accessed January 20, 2014
    • Kindle, K. L. (1998). “High-frequency nuclear transformation of Chlamydomonas reinhardtii,” in Methods in Enzymology Photosynthesis: Molecular Biology of Energy Capture, ed L. McIntosh (Academic Press), 27-38. Available online at: http://www.sciencedirect.com/science/article/pii/S0076687998970057 [Accessed January 20, 2014].
    • (1998) Methods in Enzymology Photosynthesis: Molecular Biology of Energy Capture , pp. 27-38
    • Kindle, K.L.1
  • 66
    • 84888262073 scopus 로고    scopus 로고
    • Evaluating nuclear transgene expression systems in Chlamydomonas reinhardtii
    • Kumar, A., Falcao, V. R., and Sayre, R. T. (2013). Evaluating nuclear transgene expression systems in Chlamydomonas reinhardtii. Algal Res. 2, 321-332. doi: 10.1016/j.algal.2013.09.002
    • (2013) Algal Res , vol.2 , pp. 321-332
    • Kumar, A.1    Falcao, V.R.2    Sayre, R.T.3
  • 67
    • 84857507922 scopus 로고    scopus 로고
    • Microalgae biofuels: A critical review of issues, problems and the way forward
    • Lam, M. K., and Lee, K. T. (2012). Microalgae biofuels: a critical review of issues, problems and the way forward. Biotechnol. Adv. 30, 673-690. doi: 10.1016/j.biotechadv.2011.11.008
    • (2012) Biotechnol. Adv , vol.30 , pp. 673-690
    • Lam, M.K.1    Lee, K.T.2
  • 68
    • 84881026402 scopus 로고    scopus 로고
    • Efficient recombinant protein production and secretion from nuclear transgenes in Chlamydomonas reinhardtii
    • Lauersen, K. J., Berger, H., Mussgnug, J. H., and Kruse, O. (2013a). Efficient recombinant protein production and secretion from nuclear transgenes in Chlamydomonas reinhardtii. J. Biotechnol. 167, 101-110. doi: 10.1016/j.jbiotec.2012.10.010
    • (2013) J. Biotechnol , vol.167 , pp. 101-110
    • Lauersen, K.J.1    Berger, H.2    Mussgnug, J.H.3    Kruse, O.4
  • 69
    • 84888432657 scopus 로고    scopus 로고
    • Ice recrystallization inhibition mediated by a nuclear-expressed and -secreted recombinant ice-binding protein in the microalga Chlamydomonas reinhardtii
    • Lauersen, K. J., Vanderveer, T. L., Berger, H., Kaluza, I., Mussgnug, J. H., Walker, V. K., et al. (2013b). Ice recrystallization inhibition mediated by a nuclear-expressed and -secreted recombinant ice-binding protein in the microalga Chlamydomonas reinhardtii. Appl. Microbiol. Biotechnol. 97, 9763-9772. doi: 10.1007/s00253-013-5226-x
    • (2013) Appl. Microbiol. Biotechnol , vol.97 , pp. 9763-9772
    • Lauersen, K.J.1    Vanderveer, T.L.2    Berger, H.3    Kaluza, I.4    Mussgnug, J.H.5    Walker, V.K.6
  • 70
    • 0032169762 scopus 로고    scopus 로고
    • N-glycoprotein biosynthesis in plants: Recent developments and future trends
    • Springer, Accessed December 1, 2013
    • Lerouge, P., Cabanes-Macheteau, M., Rayon, C., Fischette-Lainé, A.-C., Gomord, V., and Faye, L. (1998). “N-glycoprotein biosynthesis in plants: recent developments and future trends,” in Protein Trafficking in Plant Cells (Springer), 31-48. Available online at: http://link.springer.com/chapter/10.1007/978-94-011-5298-3_2 [Accessed December 1, 2013].
    • (1998) Protein Trafficking in Plant Cells , pp. 31-48
    • Lerouge, P.1    Cabanes-Macheteau, M.2    Rayon, C.3    Fischette-Lainé, A.-C.4    Gomord, V.5    Faye, L.6
  • 71
    • 79958694107 scopus 로고    scopus 로고
    • Unique N-glycan moieties of the 66-kDa cell wall glycoprotein from the red microalga Porphyridium sp
    • Levy-Ontman, O., Arad, S. M., Harvey, D. J., Parsons, T. B., Fairbanks, A., and Tekoah, Y. (2011). Unique N-glycan moieties of the 66-kDa cell wall glycoprotein from the red microalga Porphyridium sp. J. Biol. Chem. 286, 21340-21352. doi: 10.1074/jbc.M110.175042
    • (2011) J. Biol. Chem , vol.286 , pp. 21340-21352
    • Levy-Ontman, O.1    Arad, S.M.2    Harvey, D.J.3    Parsons, T.B.4    Fairbanks, A.5    Tekoah, Y.6
  • 72
    • 84893658783 scopus 로고    scopus 로고
    • Genes involved in the endoplasmic reticulum N-glycosylation pathway of the red microalga Porphyridium sp.: A bioinformatic study
    • Levy-Ontman, O., Fisher, M., Shotland, Y., Weinstein, Y., Tekoah, Y., and Arad, S. M. (2014). Genes involved in the endoplasmic reticulum N-glycosylation pathway of the red microalga Porphyridium sp.: a bioinformatic study. Int. J. Mol. Sci. 15, 2305-2326. doi: 10.3390/ijms15022305
    • (2014) Int. J. Mol. Sci , vol.15 , pp. 2305-2326
    • Levy-Ontman, O.1    Fisher, M.2    Shotland, Y.3    Weinstein, Y.4    Tekoah, Y.5    Arad, S.M.6
  • 73
    • 84870698615 scopus 로고    scopus 로고
    • The sweet tooth of biopharmaceuticals: Importance of recombinant protein glycosylation analysis
    • Lingg, N., Zhang, P., Song, Z., and Bardor, M. (2012). The sweet tooth of biopharmaceuticals: importance of recombinant protein glycosylation analysis. Biotechnol. J. 7, 1462-1472. doi: 10.1002/biot.201200078
    • (2012) Biotechnol. J , vol.7 , pp. 1462-1472
    • Lingg, N.1    Zhang, P.2    Song, Z.3    Bardor, M.4
  • 74
    • 0031830846 scopus 로고    scopus 로고
    • Efficient foreign gene expression in Chlamydomonas reinhardtii mediated by an endogenous intron
    • Lumbreras, V., Stevens, D. R., and Purton, S. (1998). Efficient foreign gene expression in Chlamydomonas reinhardtii mediated by an endogenous intron. Plant J. 14, 441-447. doi: 10.1046/j.1365-313X.1998.00145.x
    • (1998) Plant J , vol.14 , pp. 441-447
    • Lumbreras, V.1    Stevens, D.R.2    Purton, S.3
  • 75
    • 70349505956 scopus 로고    scopus 로고
    • Microalgae for biodiesel production and other applications: A review
    • Mata, T. M., Martins, A. A., and Caetano, N. S. (2010). Microalgae for biodiesel production and other applications: a review. Renew. Sust. Energ. Rev. 14, 217-232. doi: 10.1016/j.rser.2009.07.020
    • (2010) Renew. Sust. Energ. Rev , vol.14 , pp. 217-232
    • Mata, T.M.1    Martins, A.A.2    Caetano, N.S.3
  • 76
    • 84887106619 scopus 로고    scopus 로고
    • Exploring the N-glycosylation pathway in chlamydomonas reinhardtii unravels novel complex structures
    • Mathieu-Rivet, E., Scholz, M., Arias, C., Dardelle, F., Schulze, S., Le Mauff, F., et al. (2013). Exploring the N-glycosylation pathway in chlamydomonas reinhardtii unravels novel complex structures. Mol. Cell. Proteomics 12, 3160-3183. doi: 10.1074/mcp.M113.028191
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 3160-3183
    • Mathieu-Rivet, E.1    Scholz, M.2    Arias, C.3    Dardelle, F.4    Schulze, S.5    Le Mauff, F.6
  • 77
    • 79960270958 scopus 로고    scopus 로고
    • N-glycosylation at noncanonical Asn-X-Cys sequences in plant cells
    • Matsui, T., Takita, E., Sato, T., Kinjo, S., Aizawa, M., Sugiura, Y., et al. (2011). N-glycosylation at noncanonical Asn-X-Cys sequences in plant cells. Glycobiology 21, 994-999. doi: 10.1093/glycob/cwq198
    • (2011) Glycobiology , vol.21 , pp. 994-999
    • Matsui, T.1    Takita, E.2    Sato, T.3    Kinjo, S.4    Aizawa, M.5    Sugiura, Y.6
  • 78
    • 84860738853 scopus 로고    scopus 로고
    • Drug-making plant blooms
    • Maxmen, A. (2012). Drug-making plant blooms. Nature 485, 160-160. doi: 10.1038/485160a
    • (2012) Nature , vol.485 , pp. 160-1160
    • Maxmen, A.1
  • 79
    • 0037457888 scopus 로고    scopus 로고
    • Expression and assembly of a fully active antibody in algae
    • Mayfield, S. P., Franklin, S. E., and Lerner, R. A. (2003). Expression and assembly of a fully active antibody in algae. Proc. Natl. Acad. Sci. 100, 438-442. doi: 10.1073/pnas.0237108100
    • (2003) Proc. Natl. Acad. Sci , vol.100 , pp. 438-442
    • Mayfield, S.P.1    Franklin, S.E.2    Lerner, R.A.3
  • 80
    • 84861984680 scopus 로고    scopus 로고
    • TAG, You're it! Chlamydomonas as a reference organism for understanding algal triacylglycerol accumulation
    • Merchant, S. S., Kropat, J., Liu, B., Shaw, J., and Warakanont, J. (2012). TAG, You're it! Chlamydomonas as a reference organism for understanding algal triacylglycerol accumulation. Curr. Opin. Biotechnol. 23, 352-363. doi: 10.1016/j.copbio.2011.12.001
    • (2012) Curr. Opin. Biotechnol , vol.23 , pp. 352-363
    • Merchant, S.S.1    Kropat, J.2    Liu, B.3    Shaw, J.4    Warakanont, J.5
  • 81
    • 35348896591 scopus 로고    scopus 로고
    • The Chlamydomonas genome reveals the evolution of key animal and plant functions
    • Merchant, S. S., Prochnik, S. E., Vallon, O., Harris, E. H., Karpowicz, S. J., Witman, G. B., et al. (2007). The Chlamydomonas genome reveals the evolution of key animal and plant functions. Science 318, 245-250. doi: 10.1126/science.1143609
    • (2007) Science , vol.318 , pp. 245-250
    • Merchant, S.S.1    Prochnik, S.E.2    Vallon, O.3    Harris, E.H.4    Karpowicz, S.J.5    Witman, G.B.6
  • 82
    • 0028213962 scopus 로고
    • Complex asparagine-linked oligosaccharides are required for morphogenic events during post-implantation development
    • Metzler, M., Gertz, A., Sarkar, M., Schachter, H., Schrader, J. W., and Marth, J. D. (1994). Complex asparagine-linked oligosaccharides are required for morphogenic events during post-implantation development. EMBO J. 13, 2056-2065.
    • (1994) EMBO J , vol.13 , pp. 2056-2065
    • Metzler, M.1    Gertz, A.2    Sarkar, M.3    Schachter, H.4    Schrader, J.W.5    Marth, J.D.6
  • 83
    • 29044433720 scopus 로고    scopus 로고
    • Expression of human CMP-N-acetylneuraminic acid synthetase and CMP-sialic acid transporter in tobacco suspension-cultured cell
    • Misaki, R., Fujiyama, K., and Seki, T. (2006). Expression of human CMP-N-acetylneuraminic acid synthetase and CMP-sialic acid transporter in tobacco suspension-cultured cell. Biochem. Biophys. Res. Commun. 339, 1184-1189. doi: 10.1016/j.bbrc.2005.11.130
    • (2006) Biochem. Biophys. Res. Commun , vol.339 , pp. 1184-1189
    • Misaki, R.1    Fujiyama, K.2    Seki, T.3
  • 84
    • 21044452598 scopus 로고    scopus 로고
    • Cyanidioschyzon merolae genome. A tool for facilitating comparable studies on organelle biogenesis in photosynthetic eukaryotes
    • Misumi, O., Matsuzaki, M., Nozaki, H., Miyagishima, S., Mori, T., Nishida, K., et al. (2005). Cyanidioschyzon merolae genome. A tool for facilitating comparable studies on organelle biogenesis in photosynthetic eukaryotes. Plant Physiol. 137, 567-585. doi: 10.1104/pp.104.053991
    • (2005) Plant Physiol , vol.137 , pp. 567-585
    • Misumi, O.1    Matsuzaki, M.2    Nozaki, H.3    Miyagishima, S.4    Mori, T.5    Nishida, K.6
  • 85
    • 62149107922 scopus 로고    scopus 로고
    • Generation of Chlamydomonas strains that efficiently express nuclear transgenes
    • Neupert, J., Karcher, D., and Bock, R. (2009). Generation of Chlamydomonas strains that efficiently express nuclear transgenes. Plant J. 57, 1140-1150. doi: 10.1111/j.1365-313X.2008.03746.x
    • (2009) Plant J , vol.57 , pp. 1140-1150
    • Neupert, J.1    Karcher, D.2    Bock, R.3
  • 86
    • 33845760011 scopus 로고    scopus 로고
    • Engineering of a sialic acid synthesis pathway in transgenic plants by expression of bacterial Neu5Ac-synthesizing enzymes
    • Paccalet, T., Bardor, M., Rihouey, C., Delmas, F., Chevalier, C., D'Aoust, M.-A., et al. (2007). Engineering of a sialic acid synthesis pathway in transgenic plants by expression of bacterial Neu5Ac-synthesizing enzymes. Plant Biotechnol. J. 5, 16-25. doi: 10.1111/j.1467-7652.2006.00211.x
    • (2007) Plant Biotechnol. J , vol.5 , pp. 16-25
    • Paccalet, T.1    Bardor, M.2    Rihouey, C.3    Delmas, F.4    Chevalier, C.5    D'aoust, M.-A.6
  • 87
    • 53049100695 scopus 로고    scopus 로고
    • Diversity in specificity, abundance, and composition of anti-Neu5Gc antibodies in normal humans: Potential implications for disease
    • Padler-Karavani, V., Yu, H., Cao, H., Chokhawala, H., Karp, F., Varki, N., et al. (2008). Diversity in specificity, abundance, and composition of anti-Neu5Gc antibodies in normal humans: potential implications for disease. Glycobiology 18, 818-830. doi: 10.1093/glycob/cwn072
    • (2008) Glycobiology , vol.18 , pp. 818-830
    • Padler-Karavani, V.1    Yu, H.2    Cao, H.3    Chokhawala, H.4    Karp, F.5    Varki, N.6
  • 88
    • 0033551250 scopus 로고    scopus 로고
    • Stable expression of human β1, 4-galactosyltransferase in plant cells modifies N-linked glycosylation patterns
    • Palacpac, N. Q., Yoshida, S., Sakai, H., Kimura, Y., Fujiyama, K., Yoshida, T., et al. (1999). Stable expression of human β1, 4-galactosyltransferase in plant cells modifies N-linked glycosylation patterns. Proc. Natl. Acad. Sci. U.S.A. 96, 4692-4697. doi: 10.1073/pnas.96.8.4692
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 4692-4697
    • Palacpac, N.Q.1    Yoshida, S.2    Sakai, H.3    Kimura, Y.4    Fujiyama, K.5    Yoshida, T.6
  • 89
    • 34250689932 scopus 로고    scopus 로고
    • The tiny eukaryote Ostreococcus provides genomic insights into the paradox of plankton speciation
    • Palenik, B., Grimwood, J., Aerts, A., Rouzé, P., Salamov, A., Putnam, N., et al. (2007). The tiny eukaryote Ostreococcus provides genomic insights into the paradox of plankton speciation. Proc. Natl. Acad. Sci. U.S.A. 104, 7705-7710. doi: 10.1073/pnas.0611046104
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 7705-7710
    • Palenik, B.1    Grimwood, J.2    Aerts, A.3    Rouzé, P.4    Salamov, A.5    Putnam, N.6
  • 90
    • 84891159705 scopus 로고    scopus 로고
    • Expression of the high light-inducible Dunaliella LIP promoter in Chlamydomonas reinhardtii
    • Park, S., Lee, Y., Lee, J.-H., and Jin, E. (2013). Expression of the high light-inducible Dunaliella LIP promoter in Chlamydomonas reinhardtii. Planta 238, 1147-1156. doi: 10.1007/s00425-013-1955-4
    • (2013) Planta , vol.238 , pp. 1147-1156
    • Park, S.1    Lee, Y.2    Lee, J.-H.3    Jin, E.4
  • 91
    • 84864500496 scopus 로고    scopus 로고
    • Moss-based production of asialo-erythropoietin devoid of Lewis A and other plant-typical carbohydrate determinants
    • Parsons, J., Altmann, F., Arrenberg, C. K., Koprivova, A., Beike, A. K., Stemmer, C., et al. (2012). Moss-based production of asialo-erythropoietin devoid of Lewis A and other plant-typical carbohydrate determinants. Plant Biotechnol. J. 10, 851-861. doi: 10.1111/j.1467-7652.2012.00704.x
    • (2012) Plant Biotechnol. J , vol.10 , pp. 851-861
    • Parsons, J.1    Altmann, F.2    Arrenberg, C.K.3    Koprivova, A.4    Beike, A.K.5    Stemmer, C.6
  • 92
    • 77957019344 scopus 로고    scopus 로고
    • Strategies for high-level recombinant protein expression in transgenic microalgae: A review
    • Potvin, G., and Zhang, Z. (2010). Strategies for high-level recombinant protein expression in transgenic microalgae: a review. Biotechnol. Adv. 28, 910-918. doi: 10.1016/j.biotechadv.2010.08.006
    • (2010) Biotechnol. Adv , vol.28 , pp. 910-918
    • Potvin, G.1    Zhang, Z.2
  • 93
    • 22144456432 scopus 로고    scopus 로고
    • A new molecular tool for transgenic diatoms
    • Poulsen, N., and Kröger, N. (2005). A new molecular tool for transgenic diatoms. Febs J. 272, 3413-3423. doi: 10.1111/j.1742-4658.2005.04760.x
    • (2005) Febs J , vol.272 , pp. 3413-3423
    • Poulsen, N.1    Kröger, N.2
  • 94
    • 84857701617 scopus 로고    scopus 로고
    • Draft genome sequence and genetic transformation of the oleaginous alga Nannochloropis gaditana
    • Radakovits, R., Jinkerson, R. E., Fuerstenberg, S. I., Tae, H., Settlage, R. E., Boore, J. L., et al. (2012). Draft genome sequence and genetic transformation of the oleaginous alga Nannochloropis gaditana. Nat. Commun. 3:686. doi: 10.1038/ncomms1688
    • (2012) Nat. Commun , vol.3 , pp. 686
    • Radakovits, R.1    Jinkerson, R.E.2    Fuerstenberg, S.I.3    Tae, H.4    Settlage, R.E.5    Boore, J.L.6
  • 95
    • 84865281597 scopus 로고    scopus 로고
    • Robust expression and secretion of Xylanase1 in chlamydomonas reinhardtii by fusion to a selection gene and processing with the FMDV 2A peptide
    • Rasala, B. A., Lee, P. A., Shen, Z., Briggs, S. P., Mendez, M., and Mayfield, S. P. (2012). Robust expression and secretion of Xylanase1 in chlamydomonas reinhardtii by fusion to a selection gene and processing with the FMDV 2A peptide. PLoS ONE 7:e43349. doi: 10.1371/journal.pone.0043349
    • (2012) Plos ONE , vol.7
    • Rasala, B.A.1    Lee, P.A.2    Shen, Z.3    Briggs, S.P.4    Mendez, M.5    Mayfield, S.P.6
  • 96
    • 78751624437 scopus 로고    scopus 로고
    • The microalga Chlamydomonas reinhardtii as a platform for the production of human protein therapeutics
    • Rasala, B. A., and Mayfield, S. P. (2011). The microalga Chlamydomonas reinhardtii as a platform for the production of human protein therapeutics. Bioengineered 2, 50-54. doi: 10.4161/bbug.2.1.13423
    • (2011) Bioengineered , vol.2 , pp. 50-54
    • Rasala, B.A.1    Mayfield, S.P.2
  • 97
    • 84896409512 scopus 로고    scopus 로고
    • Photosynthetic biomanufacturing in green algae; production of recombinant proteins for industrial, nutritional, and medical uses
    • Epub ahead of print
    • Rasala, B. A., and Mayfield, S. P. (2014). Photosynthetic biomanufacturing in green algae; production of recombinant proteins for industrial, nutritional, and medical uses. Photosyn. Res. doi: 10.1007/s11120-014-9994-7. [Epub ahead of print].
    • (2014) Photosyn. Res
    • Rasala, B.A.1    Mayfield, S.P.2
  • 98
    • 77956729072 scopus 로고    scopus 로고
    • Production of therapeutic proteins in algae, analysis of expression of seven human proteins in the chloroplast of Chlamydomonas reinhardtii: Production of therapeutic proteins in algae
    • Rasala, B. A., Muto, M., Lee, P. A., Jager, M., Cardoso, R. M. F., Behnke, C. A., et al. (2010). Production of therapeutic proteins in algae, analysis of expression of seven human proteins in the chloroplast of Chlamydomonas reinhardtii: production of therapeutic proteins in algae. Plant Biotechnol. J. 8, 719-733. doi: 10.1111/j.1467-7652.2010.00503.x
    • (2010) Plant Biotechnol. J , vol.8 , pp. 719-733
    • Rasala, B.A.1    Muto, M.2    Lee, P.A.3    Jager, M.4    Cardoso, R.M.F.5    Behnke, C.A.6
  • 99
    • 33847396507 scopus 로고    scopus 로고
    • Efficient introduction of a bisecting GlcNAc residue in tobacco N-glycans by expression of the gene encoding human N-acetylglucosaminyltransferase III
    • Rouwendal, G. J., Wuhrer, M., Florack, D. E., Koeleman, C. A., Deelder, A. M., Bakker, H., et al. (2007). Efficient introduction of a bisecting GlcNAc residue in tobacco N-glycans by expression of the gene encoding human N-acetylglucosaminyltransferase III. Glycobiology 17, 334-344. doi: 10.1093/glycob/cwl078
    • (2007) Glycobiology , vol.17 , pp. 334-344
    • Rouwendal, G.J.1    Wuhrer, M.2    Florack, D.E.3    Koeleman, C.A.4    Deelder, A.M.5    Bakker, H.6
  • 100
    • 48349095382 scopus 로고    scopus 로고
    • Gaussia-luciferase as a sensitive reporter gene for monitoring promoter activity in the nucleus of the green alga Chlamydomonas reinhardtii
    • Ruecker, O., Zillner, K., Groebner-Ferreira, R., and Heitzer, M. (2008). Gaussia-luciferase as a sensitive reporter gene for monitoring promoter activity in the nucleus of the green alga Chlamydomonas reinhardtii. Mol. Genet. Genomics 280, 153-162. doi: 10.1007/s00438-008-0352-3
    • (2008) Mol. Genet. Genomics , vol.280 , pp. 153-162
    • Ruecker, O.1    Zillner, K.2    Groebner-Ferreira, R.3    Heitzer, M.4
  • 101
    • 84862636812 scopus 로고    scopus 로고
    • Microalgae in the postgenomic era: A blooming reservoir for new natural products
    • Sasso, S., Pohnert, G., Lohr, M., Mittag, M., and Hertweck, C. (2012). Microalgae in the postgenomic era: a blooming reservoir for new natural products. FEMS Microbiol. Rev. 36, 761-785. x doi: 10.1111/j.1574-6976.2011.00304.x
    • (2012) FEMS Microbiol. Rev , vol.36 , pp. 761-785
    • Sasso, S.1    Pohnert, G.2    Lohr, M.3    Mittag, M.4    Hertweck, C.5
  • 103
    • 84881355568 scopus 로고    scopus 로고
    • Molecular farming of pharmaceutical proteins using plant suspension cell and tissue cultures
    • Schillberg, S., Raven, N., Fischer, R., Twyman, R., and Schiermeyer, A. (2013). Molecular farming of pharmaceutical proteins using plant suspension cell and tissue cultures. Curr. Pharm. Des. 19, 5531-5542. doi: 10.2174/1381612811319310008
    • (2013) Curr. Pharm. Des , vol.19 , pp. 5531-5542
    • Schillberg, S.1    Raven, N.2    Fischer, R.3    Twyman, R.4    Schiermeyer, A.5
  • 104
    • 0342680049 scopus 로고    scopus 로고
    • The HSP70A promoter as a tool for the improved expression of transgenes in Chlamydomonas
    • Schroda, M., Blöcker, D., and Beck, C. F. (2000). The HSP70A promoter as a tool for the improved expression of transgenes in Chlamydomonas. Plant J. 21, 121-131. doi: 10.1046/j.1365-313x.2000.00652.x
    • (2000) Plant J , vol.21 , pp. 121-131
    • Schroda, M.1    Blöcker, D.2    Beck, C.F.3
  • 106
    • 34547586616 scopus 로고    scopus 로고
    • Production of glucocerebrosidase with terminal mannose glycans for enzyme replacement therapy of Gaucher's disease using a plant cell system
    • Shaaltiel, Y., Bartfeld, D., Hashmueli, S., Baum, G., Brill-Almon, E., Galili, G., et al. (2007). Production of glucocerebrosidase with terminal mannose glycans for enzyme replacement therapy of Gaucher's disease using a plant cell system. Plant Biotechnol. J. 5, 579-590. doi: 10.1111/j.1467-7652.2007.00263.x
    • (2007) Plant Biotechnol. J , vol.5 , pp. 579-590
    • Shaaltiel, Y.1    Bartfeld, D.2    Hashmueli, S.3    Baum, G.4    Brill-Almon, E.5    Galili, G.6
  • 107
    • 77954676296 scopus 로고    scopus 로고
    • Origin of the polycomb repressive complex 2 and gene silencing by an E(Z) homolog in the unicellular alga Chlamydomonas
    • Shaver, S., Casas-Mollano, J. A., Cerny, R. L., and Cerutti, H. (2010). Origin of the polycomb repressive complex 2 and gene silencing by an E(z) homolog in the unicellular alga Chlamydomonas. Epigenetics 5, 301-312. doi: 10.4161/epi.5.4.11608
    • (2010) Epigenetics , vol.5 , pp. 301-312
    • Shaver, S.1    Casas-Mollano, J.A.2    Cerny, R.L.3    Cerutti, H.4
  • 108
    • 77956747852 scopus 로고    scopus 로고
    • Micro-algae come of age as a platform for recombinant protein production
    • Specht, E., Miyake-Stoner, S., and Mayfield, S. (2010). Micro-algae come of age as a platform for recombinant protein production. Biotechnol. Lett. 32, 1373-1383. doi: 10.1007/s10529-010-0326-5
    • (2010) Biotechnol. Lett , vol.32 , pp. 1373-1383
    • Specht, E.1    Miyake-Stoner, S.2    Mayfield, S.3
  • 110
    • 84867768757 scopus 로고    scopus 로고
    • Methylation—an uncommon modification of glycans
    • Staudacher, E. (2012). Methylation—an uncommon modification of glycans. Biol. Chem. 393, 675-685. doi: 10.1515/hsz-2012-0132
    • (2012) Biol. Chem , vol.393 , pp. 675-685
    • Staudacher, E.1
  • 111
    • 17044406723 scopus 로고    scopus 로고
    • Sowing the seeds of success: Pharmaceutical proteins from plants
    • Stoger, E., Ma, J. K.-C., Fischer, R., and Christou, P. (2005). Sowing the seeds of success: pharmaceutical proteins from plants. Curr. Opin. Biotechnol. 16, 167-173. doi: 10.1016/j.copbio.2005.01.005
    • (2005) Curr. Opin. Biotechnol , vol.16 , pp. 167-173
    • Stoger, E.1    Ma, J.K.2    Fischer, R.3    Christou, P.4
  • 112
    • 84870414392 scopus 로고    scopus 로고
    • Distribution of the SELMA translocon in secondary plastids of red algal origin and predicted uncoupling of ubiquitin-dependent translocation from degradation
    • Stork, S., Moog, D., Przyborski, J. M., Wilhelmi, I., Zauner, S., and Maier, U. G. (2012). Distribution of the SELMA translocon in secondary plastids of red algal origin and predicted uncoupling of ubiquitin-dependent translocation from degradation. Eukaryotic Cell 11, 1472-1481. doi: 10.1128/EC.00183-12
    • (2012) Eukaryotic Cell , vol.11 , pp. 1472-1481
    • Stork, S.1    Moog, D.2    Przyborski, J.M.3    Wilhelmi, I.4    Zauner, S.5    Maier, U.G.6
  • 113
    • 0034696932 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of beta1, 2-xylosyltransferase cDNA from Arabidopsis thaliana
    • Strasser, R., Mucha, J., Mach, L., Altmann, F., Wilson, I. B., Glössl, J., et al. (2000). Molecular cloning and functional expression of beta1, 2-xylosyltransferase cDNA from Arabidopsis thaliana. FEBS Lett. 472, 105-108. doi: 10.1016/S0014-5793(00)01443-5
    • (2000) FEBS Lett. , vol.472 , pp. 105-108
    • Strasser, R.1    Mucha, J.2    Mach, L.3    Altmann, F.4    Wilson, I.B.5    Glössl, J.6
  • 114
    • 41749105290 scopus 로고    scopus 로고
    • Generation of glyco-engineered Nicotiana benthamiana for the production of monoclonal antibodies with a homogeneous human-like N-glycan structure
    • Strasser, R., Stadlmann, J., Schähs, M., Stiegler, G., Quendler, H., Mach, L., et al. (2008). Generation of glyco-engineered Nicotiana benthamiana for the production of monoclonal antibodies with a homogeneous human-like N-glycan structure. Plant Biotechnol. J. 6, 392-402. doi: 10.1111/j.1467-7652.2008.00330.x
    • (2008) Plant Biotechnol. J , vol.6 , pp. 392-402
    • Strasser, R.1    Stadlmann, J.2    Schähs, M.3    Stiegler, G.4    Quendler, H.5    Mach, L.6
  • 115
  • 117
    • 70350507228 scopus 로고    scopus 로고
    • Synthesis and assembly of a full-length human monoclonal antibody in algal chloroplasts. Biotechnol
    • Tran, M., Zhou, B., Pettersson, P. L., Gonzalez, M. J., and Mayfield, S. P. (2009). Synthesis and assembly of a full-length human monoclonal antibody in algal chloroplasts. Biotechnol. Bioeng. 104, 663-673. doi: 10.1002/bit.22446
    • (2009) Bioeng , vol.104 , pp. 663-673
    • Tran, M.1    Zhou, B.2    Pettersson, P.L.3    Gonzalez, M.J.4    Mayfield, S.P.5
  • 118
    • 84881347629 scopus 로고    scopus 로고
    • Optimizing the yield of recombinant pharmaceutical proteins in plants
    • Twyman, R., Schillberg, S., and Fischer, R. (2013). Optimizing the yield of recombinant pharmaceutical proteins in plants. Curr. Pharm. Des. 19, 5486-5494. doi: 10.2174/1381612811319310004
    • (2013) Curr. Pharm. Des , vol.19 , pp. 5486-5494
    • Twyman, R.1    Schillberg, S.2    Fischer, R.3
  • 119
    • 84870704743 scopus 로고    scopus 로고
    • Minimizing immunogenicity of biopharmaceuticals by controlling critical quality attributes of proteins
    • Van Beers, M. M. C., and Bardor, M. (2012). Minimizing immunogenicity of biopharmaceuticals by controlling critical quality attributes of proteins. Biotechnol. J. 7, 1473-1484. doi: 10.1002/biot.201200065
    • (2012) Biotechnol. J , vol.7 , pp. 1473-1484
    • Van Beers, M.M.C.1    Bardor, M.2
  • 120
    • 34447309572 scopus 로고    scopus 로고
    • Effect of mannose chain length on targeting of glucocerebrosidase for enzyme replacement therapy of Gaucher disease
    • Van Patten, S. M., Hughes, H., Huff, M. R., Piepenhagen, P. A., Waire, J., Qiu, H., et al. (2007). Effect of mannose chain length on targeting of glucocerebrosidase for enzyme replacement therapy of Gaucher disease. Glycobiology 17, 467-478. doi: 10.1093/glycob/cwm008
    • (2007) Glycobiology , vol.17 , pp. 467-478
    • Van Patten, S.M.1    Hughes, H.2    Huff, M.R.3    Piepenhagen, P.A.4    Waire, J.5    Qiu, H.6
  • 121
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. (1993). Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3, 97-130. doi: 10.1093/glycob/3.2.97
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 122
    • 84863860723 scopus 로고    scopus 로고
    • Evolutionary forces shaping the Golgi glycosylation machinery: Why cell surface glycans are universal to living cells
    • Varki, A. (2011). Evolutionary forces shaping the Golgi glycosylation machinery: why cell surface glycans are universal to living cells. Cold Spring Harb. Perspect. Biol. 3:a005462. doi: 10.1101/cshperspect.a005462
    • (2011) Cold Spring Harb. Perspect. Biol , vol.3
    • Varki, A.1
  • 124
    • 65549122945 scopus 로고    scopus 로고
    • Transient co-expression for fast and high-yield production of antibodies with human-like N-glycans in plants
    • Vézina, L.-P., Faye, L., Lerouge, P., D'Aoust, M.-A., Marquet-Blouin, E., Burel, C., et al. (2009). Transient co-expression for fast and high-yield production of antibodies with human-like N-glycans in plants. Plant Biotechnol. J. 7, 442-455. doi: 10.1111/j.1467-7652.2009.00414.x
    • (2009) Plant Biotechnol. J , vol.7 , pp. 442-455
    • Vézina, L.-P.1    Faye, L.2    Lerouge, P.3    D'aoust, M.-A.4    Marquet-Blouin, E.5    Burel, C.6
  • 125
    • 84870681271 scopus 로고    scopus 로고
    • Genome, functional gene annotation, and nuclear transformation of the heterokont oleaginous alga nannochloropsis oceanica CCMP1779
    • Vieler, A., Wu, G., Tsai, C.-H., Bullard, B., Cornish, A. J., Harvey, C., et al. (2012). Genome, functional gene annotation, and nuclear transformation of the heterokont oleaginous alga nannochloropsis oceanica CCMP1779. PLoS Genet. 8:e1003064. doi: 10.1371/journal.pgen.1003064
    • (2012) Plos Genet , vol.8
    • Vieler, A.1    Wu, G.2    Tsai, C.-H.3    Bullard, B.4    Cornish, A.J.5    Harvey, C.6
  • 126
    • 0021274996 scopus 로고
    • Transient N-acetylglucosamine in the biosynthesis of phytohemagglutinin: Attachment in the Golgi apparatus and removal in protein bodies
    • Vitale, A., and Chrispeels, M. J. (1984). Transient N-acetylglucosamine in the biosynthesis of phytohemagglutinin: attachment in the Golgi apparatus and removal in protein bodies. J. Cell Biol. 99, 133-140. doi: 10.1083/jcb.99.1.133
    • (1984) J. Cell Biol , vol.99 , pp. 133-140
    • Vitale, A.1    Chrispeels, M.J.2
  • 127
    • 77956690413 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks 2010
    • Walsh, G. (2010). Biopharmaceutical benchmarks 2010. Nat. Biotechnol. 28, 917-924. doi: 10.1038/nbt0910-917
    • (2010) Nat. Biotechnol , vol.28 , pp. 917-924
    • Walsh, G.1
  • 128
    • 33646892873 scopus 로고    scopus 로고
    • Asparagine-linked protein glycosylation: From eukaryotic to prokaryotic systems
    • Weerapana, E., and Imperiali, B. (2006). Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems. Glycobiology 16, 91R-101R. doi: 10.1093/glycob/cwj099
    • (2006) Glycobiology , vol.16 , pp. 91R-101R
    • Weerapana, E.1    Imperiali, B.2
  • 130
    • 0034958453 scopus 로고    scopus 로고
    • Analysis of Asn-linked glycans from vegetable foodstuffs: Widespread occurrence of Lewis a, core α1,3−linked fucose and xylose substitutions
    • Wilson, I. B. H., Zeleny, R., Kolarich, D., Staudacher, E., Stroop, C. J. M., Kamerling, J. P., et al. (2001). Analysis of Asn-linked glycans from vegetable foodstuffs: widespread occurrence of Lewis a, core α1,3−linked fucose and xylose substitutions. Glycobiology 11, 261-274. doi: 10.1093/glycob/11.4.261
    • (2001) Glycobiology , vol.11 , pp. 261-274
    • Wilson, I.B.H.1    Zeleny, R.2    Kolarich, D.3    Staudacher, E.4    Stroop, C.J.M.5    Kamerling, J.P.6
  • 131
    • 19544380240 scopus 로고    scopus 로고
    • Protein glycosylation: New challenges and opportunities
    • Wong, C.-H. (2005). Protein glycosylation: new challenges and opportunities. J. Org. Chem. 70, 4219-4225. doi: 10.1021/jo050278f
    • (2005) J. Org. Chem , vol.70 , pp. 4219-4225
    • Wong, C.-H.1
  • 132
    • 64849088316 scopus 로고    scopus 로고
    • Green evolution and dynamic adaptations revealed by genomes of the marine picoeukaryotes micromonas
    • Worden, A. Z., Lee, J.-H., Mock, T., Rouze, P., Simmons, M. P., Aerts, A. L., et al. (2009). Green evolution and dynamic adaptations revealed by genomes of the marine picoeukaryotes micromonas. Science 324, 268-272. doi: 10.1126/science.1167222
    • (2009) Science , vol.324 , pp. 268-272
    • Worden, A.Z.1    Lee, J.-H.2    Mock, T.3    Rouze, P.4    Simmons, M.P.5    Aerts, A.L.6
  • 133
    • 84864941692 scopus 로고    scopus 로고
    • Green factory: Plants as bioproduction platforms for recombinant proteins
    • Xu, J., Dolan, M. C., Medrano, G., Cramer, C. L., and Weathers, P. J. (2012). Green factory: plants as bioproduction platforms for recombinant proteins. Biotechnol. Adv. 30, 1171-1184. doi: 10.1016/j.biotechadv.2011.08.020
    • (2012) Biotechnol. Adv , vol.30 , pp. 1171-1184
    • Xu, J.1    Dolan, M.C.2    Medrano, G.3    Cramer, C.L.4    Weathers, P.J.5
  • 134
    • 0033855410 scopus 로고    scopus 로고
    • Transformation of the diatom Phaeodactylum tricornutum (Bacillariophyceae) with a variety of selectable marker and reporter genes
    • Zaslavskaia, L. A., Lippmeier, J. C., Kroth, P. G., Grossman, A. R., and Apt, K. E. (2000). Transformation of the diatom Phaeodactylum tricornutum (Bacillariophyceae) with a variety of selectable marker and reporter genes. J. Phycol. 36, 379-386. doi: 10.1046/j.1529-8817.2000.99164.x
    • (2000) J. Phycol , vol.36 , pp. 379-386
    • Zaslavskaia, L.A.1    Lippmeier, J.C.2    Kroth, P.G.3    Grossman, A.R.4    Apt, K.E.5
  • 135
    • 33744484016 scopus 로고    scopus 로고
    • Sialic acid concentrations in plants are in the range of inadvertent contamination
    • Zeleny, R., Kolarich, D., Strasser, R., and Altmann, F. (2006). Sialic acid concentrations in plants are in the range of inadvertent contamination. Planta 224, 222-227. doi: 10.1007/s00425-005-0206-8
    • (2006) Planta , vol.224 , pp. 222-227
    • Zeleny, R.1    Kolarich, D.2    Strasser, R.3    Altmann, F.4
  • 136
    • 63349106223 scopus 로고    scopus 로고
    • Gene silencing by artificial microRNAs in Chlamydomonas
    • Zhao, T., Wang, W., Bai, X., and Qi, Y. (2009). Gene silencing by artificial microRNAs in Chlamydomonas. Plant J. 58, 157-164. doi: 10.1111/j.1365-313X.2008.03758.x
    • (2009) Plant J , vol.58 , pp. 157-164
    • Zhao, T.1    Wang, W.2    Bai, X.3    Qi, Y.4
  • 137
    • 4744347867 scopus 로고    scopus 로고
    • Caenorhabditis elegans triple null mutant lacking UDP-N-acetyl-D-glucosamine:α-3-D-mannoside β1,2-N-acetylglucosaminyltransferase I
    • Zhu, S., Hanneman, A., Reinhold, V. N., Spence, A. M., and Schachter, H. (2004). Caenorhabditis elegans triple null mutant lacking UDP-N-acetyl-D-glucosamine:α-3-D-mannoside β1,2-N-acetylglucosaminyltransferase I. Biochem. J. 382, 995-1001. doi: 10.1042/BJ20040793
    • (2004) Biochem. J , vol.382 , pp. 995-1001
    • Zhu, S.1    Hanneman, A.2    Reinhold, V.N.3    Spence, A.M.4    Schachter, H.5
  • 138
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska, D. F., Gnad, F., Wiśniewski, J. R., and Mann, M. (2010). Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell 141, 897-907. doi: 10.1016/j.cell.2010.04.012
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wiśniewski, J.R.3    Mann, M.4


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