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Volumn 30, Issue 2, 2012, Pages 410-418

Post-translational modification of plant-made foreign proteins; glycosylation and beyond

Author keywords

Glycosylation; Lipidation; Plant made proteins; Post translational modification; Proline hydroxylation; Recombinant proteins

Indexed keywords

DEGREE OF TOLERANCE; DYNAMIC INTERACTION; EXPRESSION SYSTEM; HIGH QUALITY; LIPIDATION; LOCALISATION; NATIVE PROTEINS; POST-TRANSLATIONAL MODIFICATION; POST-TRANSLATIONAL MODIFICATIONS; PROTEIN ACTIVITY; PROTEIN ENGINEERING; PROTEIN PROCESSING; RATIONAL DESIGN; RECOMBINANT PROTEIN;

EID: 84856958234     PISSN: 07349750     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biotechadv.2011.07.015     Document Type: Review
Times cited : (67)

References (111)
  • 2
    • 33846187538 scopus 로고    scopus 로고
    • The role of protein glycosylation in allergy
    • Altmann F. The role of protein glycosylation in allergy. Int Arch Allergy Immunol 2007, 142:99-115.
    • (2007) Int Arch Allergy Immunol , vol.142 , pp. 99-115
    • Altmann, F.1
  • 3
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler R., Hermjakob H., Sharon N. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim Biophys Acta 1999, 1473:4-8.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 5
    • 33646737444 scopus 로고    scopus 로고
    • An antibody produced in tobacco expressing a hybrid beta-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. An antibody produced in tobacco expressing a hybrid beta-1,4-galactosyltransferase is essentially devoid of plant carbohydrate epitopes. Proc Natl Acad Sci U S A 2006, 103:7577-7582.
    • (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
  • 6
  • 7
    • 77955262351 scopus 로고    scopus 로고
    • Plant glycans: friend or foe in vaccine development?
    • Bosch D., Schots A. Plant glycans: friend or foe in vaccine development?. Expert Rev Vaccines 2010, 9:835-842.
    • (2010) Expert Rev Vaccines , vol.9 , pp. 835-842
    • Bosch, D.1    Schots, A.2
  • 8
    • 33747362656 scopus 로고    scopus 로고
    • Optimisation of the cellular metabolism of glycosylation for recombinant proteins produced by mammalian cell systems
    • Butler M. Optimisation of the cellular metabolism of glycosylation for recombinant proteins produced by mammalian cell systems. Cytotechnology 2006, 50:57-76.
    • (2006) Cytotechnology , vol.50 , pp. 57-76
    • Butler, M.1
  • 10
    • 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. Construction of a functional CMP-sialic acid biosynthesis pathway in Arabidopsis. Plant Physiol 2008, 147:331-339.
    • (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
  • 11
    • 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. In planta protein sialylation through overexpression of the respective mammalian pathway. J Biol Chem 2010, 285:15923-15930.
    • (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
  • 12
    • 79956093771 scopus 로고    scopus 로고
    • N-Glycosylation engineering of plants for the biosynthesis of glycoproteins with bisected and branched complex N-glycans
    • Castilho A., Gattinger P., Grass J., Jez J., Pabst M., Altmann F., et al. N-Glycosylation engineering of plants for the biosynthesis of glycoproteins with bisected and branched complex N-glycans. Glycobiology 2011, 21:813-823.
    • (2011) Glycobiology , vol.21 , pp. 813-823
    • Castilho, A.1    Gattinger, P.2    Grass, J.3    Jez, J.4    Pabst, M.5    Altmann, F.6
  • 13
    • 0028896496 scopus 로고
    • The macroheterogeneity of recombinant human interferon-gamma produced by Chinese-hamster ovary cells is affected by the protein and lipid content of the culture medium
    • Castro P.M., Ison A.P., Hayter P.M., Bull A.T. The macroheterogeneity of recombinant human interferon-gamma produced by Chinese-hamster ovary cells is affected by the protein and lipid content of the culture medium. Biotechnol Appl Biochem 1995, 21:87-100.
    • (1995) Biotechnol Appl Biochem , vol.21 , pp. 87-100
    • Castro, P.M.1    Ison, A.P.2    Hayter, P.M.3    Bull, A.T.4
  • 14
    • 40849142102 scopus 로고    scopus 로고
    • Cetuximab-induced anaphylaxis and IgE specific for galactose-alpha-1,3-galactose
    • Chung C.H., Mirakhur B., Chan E., Le Q.T., Berlin J., Morse M., et al. Cetuximab-induced anaphylaxis and IgE specific for galactose-alpha-1,3-galactose. N Engl J Med 2008, 358:1109-1117.
    • (2008) N Engl 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
  • 15
    • 70449698030 scopus 로고    scopus 로고
    • Anaphylaxis syndromes related to a new mammalian cross-reactive carbohydrate determinant
    • Commins S.P., Platts-Mills T.A. Anaphylaxis syndromes related to a new mammalian cross-reactive carbohydrate determinant. J Allergy Clin Immunol 2009, 124:652-657.
    • (2009) J Allergy Clin Immunol , vol.124 , pp. 652-657
    • Commins, S.P.1    Platts-Mills, T.A.2
  • 16
    • 64349107859 scopus 로고    scopus 로고
    • The Arabidopsis thaliana putative sialyltransferase resides in the Golgi apparatus but lacks the ability to transfer sialic acid
    • Daskalova S.M., Pah A.R., Baluch D.P., Lopez L.C. The Arabidopsis thaliana putative sialyltransferase resides in the Golgi apparatus but lacks the ability to transfer sialic acid. Plant Biol 2009, 11:284-299.
    • (2009) Plant Biol , vol.11 , pp. 284-299
    • Daskalova, S.M.1    Pah, A.R.2    Baluch, D.P.3    Lopez, L.C.4
  • 17
    • 77955812183 scopus 로고    scopus 로고
    • Engineering of N. benthamiana plants for production of N-acetylgalactosamine-glycosylated proteins-towards development of a plant-based platform for production of protein therapeutics with mucin type O-glycosylation
    • Daskalova S.M., Radder J.E., Cichacz Z.A., Olsen S.H., Tsaprailis G., Mason H., et al. Engineering of N. benthamiana plants for production of N-acetylgalactosamine-glycosylated proteins-towards development of a plant-based platform for production of protein therapeutics with mucin type O-glycosylation. BMC Biotechnol 2010, 10:62.
    • (2010) BMC Biotechnol , vol.10 , pp. 62
    • Daskalova, S.M.1    Radder, J.E.2    Cichacz, Z.A.3    Olsen, S.H.4    Tsaprailis, G.5    Mason, H.6
  • 18
    • 77956440770 scopus 로고    scopus 로고
    • Commercialization of whole-plant systems for biomanufacturing of protein products: evolution and prospects
    • Davies H.M. Commercialization of whole-plant systems for biomanufacturing of protein products: evolution and prospects. Plant Biotechnol J 2010, 8:845-861.
    • (2010) Plant Biotechnol J , vol.8 , pp. 845-861
    • Davies, H.M.1
  • 19
    • 36148950459 scopus 로고    scopus 로고
    • Moss bioreactors producing improved biopharmaceuticals
    • Decker E.L., Reski R. Moss bioreactors producing improved biopharmaceuticals. Curr Opin Biotechnol 2007, 18:393-398.
    • (2007) Curr Opin Biotechnol , vol.18 , pp. 393-398
    • Decker, E.L.1    Reski, R.2
  • 20
    • 0034997401 scopus 로고    scopus 로고
    • Development and characterization of novel erythropoiesis stimulating protein (NESP)
    • Egrie J.C., Browne J.K. Development and characterization of novel erythropoiesis stimulating protein (NESP). Br J Cancer 2001, 84(Suppl. 1):3-10.
    • (2001) Br J Cancer , vol.84 , Issue.SUPPL. 1 , pp. 3-10
    • Egrie, J.C.1    Browne, J.K.2
  • 21
    • 68849113455 scopus 로고    scopus 로고
    • Production of a recombinant full-length collagen type I alpha-1 and of a 45-kda collagen type I alpha-1 fragment in barley seeds
    • Eskelin K., Ritala A., Suntio T., Blumer S., Holkeri H., Wahlstrom E.H., et al. Production of a recombinant full-length collagen type I alpha-1 and of a 45-kda collagen type I alpha-1 fragment in barley seeds. Plant Biotechnol J 2009, 7:657-672.
    • (2009) Plant Biotechnol J , vol.7 , pp. 657-672
    • Eskelin, K.1    Ritala, A.2    Suntio, T.3    Blumer, S.4    Holkeri, H.5    Wahlstrom, E.H.6
  • 22
    • 70449370975 scopus 로고    scopus 로고
    • Influence of elastin-like peptide fusions on the quantity and quality of a tobacco-derived human immunodeficiency virus-neutralizing antibody
    • Floss D.M., Sack M., Arcalis E., Stadlmann J., Quendler H., Rademacher T., et al. Influence of elastin-like peptide fusions on the quantity and quality of a tobacco-derived human immunodeficiency virus-neutralizing antibody. Plant Biotechnol J 2009, 7:899-913.
    • (2009) Plant Biotechnol J , vol.7 , pp. 899-913
    • Floss, D.M.1    Sack, M.2    Arcalis, E.3    Stadlmann, J.4    Quendler, H.5    Rademacher, T.6
  • 23
    • 34248137611 scopus 로고    scopus 로고
    • Production of mouse monoclonal antibody with galactose-extended sugar chain by suspension cultured tobacco BY2 cells expressing human beta(1,4)-galactosyltransferase
    • Fujiyama K., Furukawa A., Katsura A., Misaki R., Omasa T., Seki T. Production of mouse monoclonal antibody with galactose-extended sugar chain by suspension cultured tobacco BY2 cells expressing human beta(1,4)-galactosyltransferase. Biochem Biophys Res Commun 2007, 358:85-91.
    • (2007) Biochem Biophys Res Commun , vol.358 , pp. 85-91
    • Fujiyama, K.1    Furukawa, A.2    Katsura, A.3    Misaki, R.4    Omasa, T.5    Seki, T.6
  • 24
    • 77953161781 scopus 로고    scopus 로고
    • Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes
    • Gill D.J., Chia J., Senewiratne J., Bard F. Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes. J Cell Biol 2010, 189:843-858.
    • (2010) J Cell Biol , vol.189 , pp. 843-858
    • Gill, D.J.1    Chia, J.2    Senewiratne, J.3    Bard, F.4
  • 25
    • 79952106660 scopus 로고    scopus 로고
    • Location, location, location: new insights into O-GalNAc protein glycosylation
    • Gill D.J., Clausen H., Bard F. Location, location, location: new insights into O-GalNAc protein glycosylation. Trends Cell Biol 2011, 21:149-158.
    • (2011) Trends Cell Biol , vol.21 , pp. 149-158
    • Gill, D.J.1    Clausen, H.2    Bard, F.3
  • 27
    • 79958837668 scopus 로고    scopus 로고
    • High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans
    • Goetze A.M., Liu Y.D., Zhang Z., Shah B., Lee E., Bondarenko P.V., et al. High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans. Glycobiol 2011, 21:949-959.
    • (2011) Glycobiol , vol.21 , pp. 949-959
    • Goetze, A.M.1    Liu, Y.D.2    Zhang, Z.3    Shah, B.4    Lee, E.5    Bondarenko, P.V.6
  • 28
    • 1542291118 scopus 로고    scopus 로고
    • Posttranslational modification of therapeutic proteins in plants
    • Gomord V., Faye L. Posttranslational modification of therapeutic proteins in plants. Curr Opin Plant Biol 2004, 7:171-181.
    • (2004) Curr Opin Plant Biol , vol.7 , pp. 171-181
    • Gomord, V.1    Faye, L.2
  • 31
    • 34447322721 scopus 로고    scopus 로고
    • Glycosylation design in transgenic moss for better product efficacy
    • Gorr G., Jost W. Glycosylation design in transgenic moss for better product efficacy. Bioprocess J 2005, 4:26-30.
    • (2005) Bioprocess J , vol.4 , pp. 26-30
    • Gorr, G.1    Jost, W.2
  • 33
    • 0037362655 scopus 로고    scopus 로고
    • Effect of PEGylation on pharmaceuticals
    • Harris J.M., Chess R.B. Effect of PEGylation on pharmaceuticals. Nat Rev Drug Discov 2003, 2:214-221.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 214-221
    • Harris, J.M.1    Chess, R.B.2
  • 34
    • 44649139158 scopus 로고    scopus 로고
    • Multiple roles for protein palmitoylation in plants
    • Hemsley P.A., Grierson C.S. Multiple roles for protein palmitoylation in plants. Trends Plant Sci 2008, 13:295-302.
    • (2008) Trends Plant Sci , vol.13 , pp. 295-302
    • Hemsley, P.A.1    Grierson, C.S.2
  • 35
    • 35448994846 scopus 로고    scopus 로고
    • Expression of the recombinant bacterial outer surface protein A in tobacco chloroplasts leads to thylakoid localisation and loss of photosynthesis
    • Hennig A., Bonfig K., Roitsch T., Warzecha H. Expression of the recombinant bacterial outer surface protein A in tobacco chloroplasts leads to thylakoid localisation and loss of photosynthesis. FEBS J 2007, 274:5749-5758.
    • (2007) FEBS J , vol.274 , pp. 5749-5758
    • Hennig, A.1    Bonfig, K.2    Roitsch, T.3    Warzecha, H.4
  • 36
    • 84856967996 scopus 로고    scopus 로고
    • Assessment of different expression strategies for the production of a recombinant lipoprotein vaccine in plants
    • Hennig A., Reinders Y., Giritch A., Reinders J., Warzecha H. Assessment of different expression strategies for the production of a recombinant lipoprotein vaccine in plants. Open Biotechnol J 2008, 2:51-55.
    • (2008) Open Biotechnol J , vol.2 , pp. 51-55
    • Hennig, A.1    Reinders, Y.2    Giritch, A.3    Reinders, J.4    Warzecha, H.5
  • 37
    • 77949266037 scopus 로고    scopus 로고
    • Carbohydrate analysis throughout the development of a protein therapeutic
    • Higgins E. Carbohydrate analysis throughout the development of a protein therapeutic. Glycoconj J 2010, 27:211-225.
    • (2010) Glycoconj J , vol.27 , pp. 211-225
    • Higgins, E.1
  • 38
    • 0028256486 scopus 로고
    • Role of N-linked oligosaccharide chains in the processing and antigenicity of measles virus haemagglutinin protein
    • Hu A., Cattaneo R., Schwartz S., Norrby E. Role of N-linked oligosaccharide chains in the processing and antigenicity of measles virus haemagglutinin protein. J Gen Virol 1994, 75:1043-1052.
    • (1994) J Gen Virol , vol.75 , pp. 1043-1052
    • Hu, A.1    Cattaneo, R.2    Schwartz, S.3    Norrby, E.4
  • 39
    • 70350544173 scopus 로고    scopus 로고
    • N-glycosylation engineering of biopharmaceutical expression systems
    • Jacobs P.P., Callewaert N. N-glycosylation engineering of biopharmaceutical expression systems. Curr Mol Med 2009, 9:774-800.
    • (2009) Curr Mol Med , vol.9 , pp. 774-800
    • Jacobs, P.P.1    Callewaert, N.2
  • 40
    • 40549118514 scopus 로고    scopus 로고
    • A plant-derived human monoclonal antibody induces an anti-carbohydrate immune response in rabbits
    • Jin C., Altmann F., Strasser R., Mach L., Schahs M., Kunert R., et al. A plant-derived human monoclonal antibody induces an anti-carbohydrate immune response in rabbits. Glycobiology 2008, 18:235-241.
    • (2008) Glycobiology , vol.18 , pp. 235-241
    • Jin, C.1    Altmann, F.2    Strasser, R.3    Mach, L.4    Schahs, M.5    Kunert, R.6
  • 41
    • 79959861065 scopus 로고    scopus 로고
    • O-linked glycosylation leads to decreased thermal stability of interferon alpha 2b as measured by two orthogonal techniques
    • Johnston M.J., Frahm G., Li X., Durocher Y., Hefford M.A. O-linked glycosylation leads to decreased thermal stability of interferon alpha 2b as measured by two orthogonal techniques. Pharm Res 2011, 28:1661-1667.
    • (2011) Pharm Res , vol.28 , pp. 1661-1667
    • Johnston, M.J.1    Frahm, G.2    Li, X.3    Durocher, Y.4    Hefford, M.A.5
  • 42
    • 27244433853 scopus 로고    scopus 로고
    • O-linked glycosylation in maize-expressed human iga1
    • Karnoup A.S., Turkelson V., Anderson W.H. O-linked glycosylation in maize-expressed human iga1. Glycobiology 2005, 15:965-981.
    • (2005) Glycobiology , vol.15 , pp. 965-981
    • Karnoup, A.S.1    Turkelson, V.2    Anderson, W.H.3
  • 43
    • 0034794126 scopus 로고    scopus 로고
    • Synthetic genes for the elucidation of glycosylation codes for arabinogalactan-proteins and other hydroxyproline-rich glycoproteins
    • Kieliszewski M.J., Shpak E. Synthetic genes for the elucidation of glycosylation codes for arabinogalactan-proteins and other hydroxyproline-rich glycoproteins. Cell Mol Life Sci 2001, 58:1386-1398.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 1386-1398
    • Kieliszewski, M.J.1    Shpak, E.2
  • 44
    • 34547611335 scopus 로고    scopus 로고
    • Methods of producing peptides/proteins and peptides/proteins produced thereby
    • United State Patent, Publication No. US-20060026719
    • Kieliszewski MJ, Xu J. Methods of producing peptides/proteins and peptides/proteins produced thereby. United State Patent, Publication No. US-20060026719, 2006.
    • (2006)
    • Kieliszewski, M.J.1    Xu, J.2
  • 46
    • 0033570069 scopus 로고    scopus 로고
    • Glutelin basic subunits have a mammalian mucin-type O-linked disaccharide side chain
    • Kishimoto T., Watanabe M., Mitsui T., Hori H. Glutelin basic subunits have a mammalian mucin-type O-linked disaccharide side chain. Arch Biochem Biophys 1999, 370:271-277.
    • (1999) Arch Biochem Biophys , vol.370 , pp. 271-277
    • Kishimoto, T.1    Watanabe, M.2    Mitsui, T.3    Hori, H.4
  • 49
    • 53849096006 scopus 로고    scopus 로고
    • The importance of proline residues in the structure, stability and susceptibility to proteolytic degradation of collagens
    • Krane S.M. The importance of proline residues in the structure, stability and susceptibility to proteolytic degradation of collagens. Amino Acids 2008, 35:703-710.
    • (2008) Amino Acids , vol.35 , pp. 703-710
    • Krane, S.M.1
  • 50
    • 0036966210 scopus 로고    scopus 로고
    • A complete alpha1,3-galactosyltransferase gene is present in the human genome and partially transcribed
    • Lanteri M., Giordanengo V., Vidal F., Gaudray P., Lefebvre J.C. A complete alpha1,3-galactosyltransferase gene is present in the human genome and partially transcribed. Glycobiology 2002, 12:785-792.
    • (2002) Glycobiology , vol.12 , pp. 785-792
    • Lanteri, M.1    Giordanengo, V.2    Vidal, F.3    Gaudray, P.4    Lefebvre, J.C.5
  • 51
    • 84975742481 scopus 로고    scopus 로고
    • Genomics meets glycomics-the first GWAS study of human N-glycome identifies hNF1alpha as a master regulator of plasma protein fucosylation
    • Lauc G., Essafi A., Huffman J.E., Hayward C., Knezevic A., Kattla J.J., et al. Genomics meets glycomics-the first GWAS study of human N-glycome identifies hNF1alpha as a master regulator of plasma protein fucosylation. PLoS Genet 2011, 6:e1001256.
    • (2011) PLoS Genet , vol.6
    • Lauc, G.1    Essafi, A.2    Huffman, J.E.3    Hayward, C.4    Knezevic, A.5    Kattla, J.J.6
  • 52
    • 70449732650 scopus 로고    scopus 로고
    • Pharmacological significance of glycosylation in therapeutic proteins
    • Li H., d'Anjou M. Pharmacological significance of glycosylation in therapeutic proteins. Curr Opin Biotechnol 2009, 20:678-684.
    • (2009) Curr Opin Biotechnol , vol.20 , pp. 678-684
    • Li, H.1    d'Anjou, M.2
  • 53
    • 77955240271 scopus 로고    scopus 로고
    • Current status of plant-made vaccines for veterinary purposes
    • Ling H.Y., Pelosi A., Walmsley A.M. Current status of plant-made vaccines for veterinary purposes. Expert Rev Vaccines 2010, 9:971-982.
    • (2010) Expert Rev Vaccines , vol.9 , pp. 971-982
    • Ling, H.Y.1    Pelosi, A.2    Walmsley, A.M.3
  • 54
    • 52249107853 scopus 로고    scopus 로고
    • Stable high volumetric production of glycosylated human recombinant IFNalpha2b in HEK293 cells
    • Loignon M., Perret S., Kelly J., Boulais D., Cass B., Bisson L., et al. Stable high volumetric production of glycosylated human recombinant IFNalpha2b in HEK293 cells. BMC Biotechnol 2008, 8:65.
    • (2008) BMC Biotechnol , vol.8 , pp. 65
    • Loignon, M.1    Perret, S.2    Kelly, J.3    Boulais, D.4    Cass, B.5    Bisson, L.6
  • 55
    • 33847788546 scopus 로고    scopus 로고
    • Expression, intracellular targeting and purification of HIV Nef variants in tobacco cells
    • Marusic C., Nuttall J., Buriani G., Lico C., Lombardi R., Baschieri S., et al. Expression, intracellular targeting and purification of HIV Nef variants in tobacco cells. BMC Biotechnol 2007, 7:12.
    • (2007) BMC Biotechnol , vol.7 , pp. 12
    • Marusic, C.1    Nuttall, J.2    Buriani, G.3    Lico, C.4    Lombardi, R.5    Baschieri, S.6
  • 56
    • 16244383185 scopus 로고    scopus 로고
    • Monoclonal antibodies to plant cell wall xylans and arabinoxylans
    • McCartney L., Marcus S.E., Knox J.P. Monoclonal antibodies to plant cell wall xylans and arabinoxylans. J Histochem Cytochem 2005, 53:543-546.
    • (2005) J Histochem Cytochem , vol.53 , pp. 543-546
    • McCartney, L.1    Marcus, S.E.2    Knox, J.P.3
  • 57
    • 46849114454 scopus 로고    scopus 로고
    • Protein lipidation meets proteomics
    • Meinnel T., Giglione C. Protein lipidation meets proteomics. Front Biosci 2008, 13:6326-6340.
    • (2008) Front Biosci , vol.13 , pp. 6326-6340
    • Meinnel, T.1    Giglione, C.2
  • 58
    • 0037181489 scopus 로고    scopus 로고
    • Hydroxylated human homotrimeric collagen I in Agrobacterium tumefaciens-mediated transient expression and in transgenic tobacco plant
    • Merle C., Perret S., Lacour T., Jonval V., Hudaverdian S., Garrone R., et al. Hydroxylated human homotrimeric collagen I in Agrobacterium tumefaciens-mediated transient expression and in transgenic tobacco plant. FEBS Lett 2002, 515:114-118.
    • (2002) FEBS Lett , vol.515 , pp. 114-118
    • Merle, C.1    Perret, S.2    Lacour, T.3    Jonval, V.4    Hudaverdian, S.5    Garrone, R.6
  • 59
    • 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., Seki T. Expression of human CMP-N-acetylneuraminic acid synthetase and CMP-sialic acid transporter in tobacco suspension-cultured cell. Biochem Biophys Res Commun 2006, 339:1184-1189.
    • (2006) Biochem Biophys Res Commun , vol.339 , pp. 1184-1189
    • Misaki, R.1    Fujiyama, K.2    Seki, T.3
  • 60
    • 65249168279 scopus 로고    scopus 로고
    • Recombinant collagen trimers from insect cells and yeast
    • Myllyharju J. Recombinant collagen trimers from insect cells and yeast. Methods Mol Biol 2009, 522:51-62.
    • (2009) Methods Mol Biol , vol.522 , pp. 51-62
    • Myllyharju, J.1
  • 61
    • 79952303673 scopus 로고    scopus 로고
    • Production of complex multiantennary N-glycans in Nicotiana benthamiana plants
    • Nagels B., Van Damme E.J., Pabst M., Callewaert N., Weterings K. Production of complex multiantennary N-glycans in Nicotiana benthamiana plants. Plant Physiol 2011, 155:1103-1112.
    • (2011) Plant Physiol , vol.155 , pp. 1103-1112
    • Nagels, B.1    Van Damme, E.J.2    Pabst, M.3    Callewaert, N.4    Weterings, K.5
  • 62
    • 0034861890 scopus 로고    scopus 로고
    • Heterogeneity of O-glycosylation in the hinge region of human IgA1
    • Novak J., Tomana M., Kilian M., Coward L., Kulhavy R., Barnes S., et al. Heterogeneity of O-glycosylation in the hinge region of human IgA1. Mol Immunol 2000, 37:1047-1056.
    • (2000) Mol Immunol , vol.37 , pp. 1047-1056
    • Novak, J.1    Tomana, M.2    Kilian, M.3    Coward, L.4    Kulhavy, R.5    Barnes, S.6
  • 63
    • 0037470515 scopus 로고    scopus 로고
    • EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin
    • Oda Y., Hosokawa N., Wada I., Nagata K. EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 2003, 299:1394-1397.
    • (2003) Science , vol.299 , pp. 1394-1397
    • Oda, Y.1    Hosokawa, N.2    Wada, I.3    Nagata, K.4
  • 64
    • 0033551250 scopus 로고    scopus 로고
    • Stable expression of human beta1,4-galactosyltransferase in plant cells modifies N-linked glycosylation patterns
    • Palacpac N.Q., Yoshida S., Sakai H., Kimura Y., Fujiyama K., Yoshida T., et al. Stable expression of human beta1,4-galactosyltransferase in plant cells modifies N-linked glycosylation patterns. Proc Natl Acad Sci U S A 1999, 96:4692-4697.
    • (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
  • 65
    • 79952543170 scopus 로고    scopus 로고
    • Correcting a public health fiasco: the need for a new vaccine against Lyme disease
    • Plotkin S.A. Correcting a public health fiasco: the need for a new vaccine against Lyme disease. Clin Infect Dis 2011, 52(Suppl. 3):s271-s275.
    • (2011) Clin Infect Dis , vol.52 , Issue.SUPPL. 3
    • Plotkin, S.A.1
  • 66
    • 53249085819 scopus 로고    scopus 로고
    • Impact of glycans on T-cell tolerance to glycosylated self-antigens
    • Purcell A.W., van Driel I.R., Gleeson P.A. Impact of glycans on T-cell tolerance to glycosylated self-antigens. Immunol Cell Biol 2008, 86:574-579.
    • (2008) Immunol Cell Biol , vol.86 , pp. 574-579
    • Purcell, A.W.1    van Driel, I.R.2    Gleeson, P.A.3
  • 67
    • 48549090941 scopus 로고    scopus 로고
    • Terminal sugars of Fc glycans influence antibody effector functions of IgGs
    • Raju T.S. Terminal sugars of Fc glycans influence antibody effector functions of IgGs. Curr Opin Immunol 2008, 20:471-478.
    • (2008) Curr Opin Immunol , vol.20 , pp. 471-478
    • Raju, T.S.1
  • 68
    • 0031692464 scopus 로고    scopus 로고
    • Gly-X-Y tripeptide frequencies in collagen: a context for host-guest triple-helical peptides
    • Ramshaw J.A., Shah N.K., Brodsky B. Gly-X-Y tripeptide frequencies in collagen: a context for host-guest triple-helical peptides. J Struct Biol 1998, 122:86-91.
    • (1998) J Struct Biol , vol.122 , pp. 86-91
    • Ramshaw, J.A.1    Shah, N.K.2    Brodsky, B.3
  • 69
    • 0031826473 scopus 로고    scopus 로고
    • The protein N-glycosylation in plants
    • Rayon C., Lerouge P., Faye L. The protein N-glycosylation in plants. J Exp Biol 1998, 49:1463-1472.
    • (1998) J Exp Biol , vol.49 , pp. 1463-1472
    • Rayon, C.1    Lerouge, P.2    Faye, L.3
  • 71
    • 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. Efficient introduction of a bisecting GlcNAc residue in tobacco N-glycans by expression of the gene encoding human N-acetylglucosaminyltransferase III. Glycobiology 2007, 17:334-344.
    • (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
  • 72
    • 34250346068 scopus 로고    scopus 로고
    • From planta to pharma with glycosylation in the toolbox
    • Saint-Jore-Dupas C., Faye L., Gomord V. From planta to pharma with glycosylation in the toolbox. Trends Biotechnol 2007, 25:317-323.
    • (2007) Trends Biotechnol , vol.25 , pp. 317-323
    • Saint-Jore-Dupas, C.1    Faye, L.2    Gomord, V.3
  • 73
    • 78650718836 scopus 로고    scopus 로고
    • The intracellular dynamic of protein palmitoylation
    • Salaun C., Greaves J., Chamberlain L.H. The intracellular dynamic of protein palmitoylation. J Cell Biol 2010, 191:1229-1238.
    • (2010) J Cell Biol , vol.191 , pp. 1229-1238
    • Salaun, C.1    Greaves, J.2    Chamberlain, L.H.3
  • 75
    • 34250826510 scopus 로고    scopus 로고
    • The biology of arabinogalactan proteins
    • Seifert G.J., Roberts K. The biology of arabinogalactan proteins. Annu Rev Plant Biol 2007, 58:137-161.
    • (2007) Annu Rev Plant Biol , vol.58 , pp. 137-161
    • Seifert, G.J.1    Roberts, K.2
  • 76
    • 0033592904 scopus 로고    scopus 로고
    • Synthetic genes for glycoprotein design and the elucidation of hydroxyproline-O-glycosylation codes
    • Shpak E., Leykam J.F., Kieliszewski M.J. Synthetic genes for glycoprotein design and the elucidation of hydroxyproline-O-glycosylation codes. Proc Natl Acad Sci U S A 1999, 96:14736-14741.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 14736-14741
    • Shpak, E.1    Leykam, J.F.2    Kieliszewski, M.J.3
  • 77
    • 0035815610 scopus 로고    scopus 로고
    • Contiguous hydroxyproline residues direct hydroxyproline arabinosylation in Nicotiana tabacum
    • Shpak E., Barbar E., Leykam J.F., Kieliszewski M.J. Contiguous hydroxyproline residues direct hydroxyproline arabinosylation in Nicotiana tabacum. J Biol Chem 2001, 276:11272-11278.
    • (2001) J Biol Chem , vol.276 , pp. 11272-11278
    • Shpak, E.1    Barbar, E.2    Leykam, J.F.3    Kieliszewski, M.J.4
  • 78
    • 25444435396 scopus 로고    scopus 로고
    • Glycoengineering: the effect of glycosylation on the properties of therapeutic proteins
    • Sinclair A.M., Elliott S. Glycoengineering: the effect of glycosylation on the properties of therapeutic proteins. J Pharm Sci 2005, 94:1626-1635.
    • (2005) J Pharm Sci , vol.94 , pp. 1626-1635
    • Sinclair, A.M.1    Elliott, S.2
  • 79
    • 70450277084 scopus 로고    scopus 로고
    • Targeting glycan modified OVA to murine DC-SIGN transgenic dendritic cells enhances MHC class I and II presentation
    • Singh S.K., Stephani J., Schaefer M., Kalay H., Garcia-Vallejo J.J., den Haan J., et al. Targeting glycan modified OVA to murine DC-SIGN transgenic dendritic cells enhances MHC class I and II presentation. Mol Immunol 2009, 47:164-174.
    • (2009) Mol Immunol , vol.47 , pp. 164-174
    • Singh, S.K.1    Stephani, J.2    Schaefer, M.3    Kalay, H.4    Garcia-Vallejo, J.J.5    den Haan, J.6
  • 80
    • 3543099503 scopus 로고    scopus 로고
    • Palmitoylation of intracellular signalling proteins: regulation and function
    • Smotrys J.E., Linder M.E. Palmitoylation of intracellular signalling proteins: regulation and function. Annu Rev Biochem 2004, 73:559-587.
    • (2004) Annu Rev Biochem , vol.73 , pp. 559-587
    • Smotrys, J.E.1    Linder, M.E.2
  • 82
    • 0036320685 scopus 로고    scopus 로고
    • N-glycans on the receptor for advanced glycation end products influence amphoterin binding and neurite outgrowth
    • Srikrishna G., Huttunen H.J., Johansson L., Weigle B., Yamaguchi Y., Rauvala H., et al. N-glycans on the receptor for advanced glycation end products influence amphoterin binding and neurite outgrowth. J Neurochem 2002, 80:998-1008.
    • (2002) J Neurochem , vol.80 , pp. 998-1008
    • Srikrishna, G.1    Huttunen, H.J.2    Johansson, L.3    Weigle, B.4    Yamaguchi, Y.5    Rauvala, H.6
  • 83
    • 70349170207 scopus 로고    scopus 로고
    • Production of bioactive, post-translationally modified, heterotrimeric, human recombinant type-I collagen in transgenic tobacco
    • Stein H., Wilensky M., Tsafrir Y., Rosenthal M., Amir R., Avraham T., et al. Production of bioactive, post-translationally modified, heterotrimeric, human recombinant type-I collagen in transgenic tobacco. Biomacromolecules 2009, 10:2640-2645.
    • (2009) Biomacromolecules , vol.10 , pp. 2640-2645
    • Stein, H.1    Wilensky, M.2    Tsafrir, Y.3    Rosenthal, M.4    Amir, R.5    Avraham, T.6
  • 84
    • 1542358140 scopus 로고    scopus 로고
    • Generation of Arabidopsis thaliana plants with complex N-glycans lacking beta1,2-linked xylose and core alpha1,3-linked fucose
    • Strasser R., Altmann F., Mach L., Glossl J., Steinkellner H. Generation of Arabidopsis thaliana plants with complex N-glycans lacking beta1,2-linked xylose and core alpha1,3-linked fucose. FEBS Lett 2004, 561:132-136.
    • (2004) FEBS Lett , vol.561 , pp. 132-136
    • Strasser, R.1    Altmann, F.2    Mach, L.3    Glossl, J.4    Steinkellner, H.5
  • 85
    • 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., Schahs M., Stiegler G., Quendler H., Mach L., et al. Generation of glyco-engineered Nicotiana benthamiana for the production of monoclonal antibodies with a homogeneous human-like N-glycan structure. Plant Biotechnol J 2008, 6:392-402.
    • (2008) Plant Biotechnol J , vol.6 , pp. 392-402
    • Strasser, R.1    Stadlmann, J.2    Schahs, M.3    Stiegler, G.4    Quendler, H.5    Mach, L.6
  • 86
    • 68949137116 scopus 로고    scopus 로고
    • Improved virus neutralization by plant-produced anti-HIV antibodies with a homogeneous beta1,4-galactosylated N-glycan profile
    • Strasser R., Castilho A., Stadlmann J., Kunert R., Quendler H., Gattinger P., et al. Improved virus neutralization by plant-produced anti-HIV antibodies with a homogeneous beta1,4-galactosylated N-glycan profile. J Biol Chem 2009, 284:20479-20485.
    • (2009) J Biol Chem , vol.284 , pp. 20479-20485
    • Strasser, R.1    Castilho, A.2    Stadlmann, J.3    Kunert, R.4    Quendler, H.5    Gattinger, P.6
  • 87
    • 33845756751 scopus 로고    scopus 로고
    • Approaches to achieve high-level heterologous protein production in plants
    • Streatfield S.J. Approaches to achieve high-level heterologous protein production in plants. Plant Biotechnol J 2007, 5:2-15.
    • (2007) Plant Biotechnol J , vol.5 , pp. 2-15
    • Streatfield, S.J.1
  • 88
    • 45149098473 scopus 로고    scopus 로고
    • Post-translational modification of host proteins in pathogen-triggered defence signalling in plants
    • Stulemeijer I.J., Joosten M.H. Post-translational modification of host proteins in pathogen-triggered defence signalling in plants. Mol Plant Pathol 2008, 9:545-560.
    • (2008) Mol Plant Pathol , vol.9 , pp. 545-560
    • Stulemeijer, I.J.1    Joosten, M.H.2
  • 89
    • 77955279149 scopus 로고    scopus 로고
    • The role of mucin-type o-glycans in eukaryotic development
    • Tabak L.A. The role of mucin-type o-glycans in eukaryotic development. Semin Cell Dev Biol 2010, 21:616-621.
    • (2010) Semin Cell Dev Biol , vol.21 , pp. 616-621
    • Tabak, L.A.1
  • 90
    • 62449106207 scopus 로고    scopus 로고
    • Recent insights into the biological roles of mucin-type O-glycosylation
    • Tian E., Ten Hagen K.G. Recent insights into the biological roles of mucin-type O-glycosylation. Glycoconj J 2009, 26:325-334.
    • (2009) Glycoconj J , vol.26 , pp. 325-334
    • Tian, E.1    Ten Hagen, K.G.2
  • 91
    • 0033044588 scopus 로고    scopus 로고
    • Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity
    • Umana P., Jean-Mairet J., Moudry R., Amstutz H., Bailey J.E. Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity. Nat Biotechnol 1999, 17:176-180.
    • (1999) Nat Biotechnol , vol.17 , pp. 176-180
    • Umana, P.1    Jean-Mairet, J.2    Moudry, R.3    Amstutz, H.4    Bailey, J.E.5
  • 92
    • 9144237471 scopus 로고    scopus 로고
    • Protein N-glycosylation is similar in the moss Physcomitrella patens and in higher plants
    • Vietor R., Loutelier-Bourhis C., Fitchette A.-C., Margerie P., Gonneau M., Faye L., et al. Protein N-glycosylation is similar in the moss Physcomitrella patens and in higher plants. Planta 2003, 218:269-275.
    • (2003) Planta , vol.218 , pp. 269-275
    • Vietor, R.1    Loutelier-Bourhis, C.2    Fitchette, A.-C.3    Margerie, P.4    Gonneau, M.5    Faye, L.6
  • 93
    • 24144490427 scopus 로고    scopus 로고
    • Recombinant pharmaceuticals from plants: the plant endomembrane system as bioreactor
    • Vitale A., Pedrazzini E. Recombinant pharmaceuticals from plants: the plant endomembrane system as bioreactor. Mol Interv 2005, 5:216-225.
    • (2005) Mol Interv , vol.5 , pp. 216-225
    • Vitale, A.1    Pedrazzini, E.2
  • 94
    • 77956458110 scopus 로고    scopus 로고
    • Post-translational modifications of protein biopharmaceuticals
    • Walsh G. Post-translational modifications of protein biopharmaceuticals. Drug Discov Today 2010, 15:773-780.
    • (2010) Drug Discov Today , vol.15 , pp. 773-780
    • Walsh, G.1
  • 95
    • 0032191992 scopus 로고    scopus 로고
    • Targeting of active sialyltransferase to the plant Golgi apparatus
    • Wee E.G., Sherrier D.J., Prime T.A., Dupree P. Targeting of active sialyltransferase to the plant Golgi apparatus. Plant Cell 1998, 10:1759-1768.
    • (1998) Plant Cell , vol.10 , pp. 1759-1768
    • Wee, E.G.1    Sherrier, D.J.2    Prime, T.A.3    Dupree, P.4
  • 96
    • 0027978073 scopus 로고
    • Biological activities of native and recombinant Borrelia burgdorferi outer surface protein A: dependence on lipid modification
    • Weis J.J., Ma Y., Erdile L.F. Biological activities of native and recombinant Borrelia burgdorferi outer surface protein A: dependence on lipid modification. Infect Immun 1994, 62:4632-4636.
    • (1994) Infect Immun , vol.62 , pp. 4632-4636
    • Weis, J.J.1    Ma, Y.2    Erdile, L.F.3
  • 97
    • 34147185919 scopus 로고    scopus 로고
    • High-level expression of secreted complex glycosylated recombinant human erythropoietin in the Physcomitrella δ-fuc-t δ-xyl-t mutant
    • Weise A., Altmann F., Rodriguez-Franco M., Sjoberg E.R., Bäumer W., Launhardt H., et al. High-level expression of secreted complex glycosylated recombinant human erythropoietin in the Physcomitrella δ-fuc-t δ-xyl-t mutant. Plant Biotech J 2007, 5:389-401.
    • (2007) Plant Biotech J , vol.5 , pp. 389-401
    • Weise, A.1    Altmann, F.2    Rodriguez-Franco, M.3    Sjoberg, E.R.4    Bäumer, W.5    Launhardt, H.6
  • 98
    • 33745107170 scopus 로고    scopus 로고
    • Strategies to improve plasma half life time of peptide and protein drugs
    • Werle M., Bernkop-Schnurch A. Strategies to improve plasma half life time of peptide and protein drugs. Amino Acids 2006, 30:351-367.
    • (2006) Amino Acids , vol.30 , pp. 351-367
    • Werle, M.1    Bernkop-Schnurch, A.2
  • 99
    • 79953718390 scopus 로고    scopus 로고
    • Emerging antibody products and Nicotiana manufacturing
    • Whaley K.J., Hiatt A., Zeitlin L. Emerging antibody products and Nicotiana manufacturing. Hum Vaccin 2011, 7.
    • (2011) Hum Vaccin , vol.7
    • Whaley, K.J.1    Hiatt, A.2    Zeitlin, L.3
  • 100
    • 0032029408 scopus 로고    scopus 로고
    • Generation of monoclonal antibody specific to (1→5)-alpha-l-arabinan
    • Willats W.G., Marcus S.E., Knox J.P. Generation of monoclonal antibody specific to (1→5)-alpha-l-arabinan. Carbohydr Res 1998, 308:149-152.
    • (1998) Carbohydr Res , vol.308 , pp. 149-152
    • Willats, W.G.1    Marcus, S.E.2    Knox, J.P.3
  • 101
    • 0036816556 scopus 로고    scopus 로고
    • Glycosylation of proteins in plants and invertebrates
    • Wilson I.B.H. Glycosylation of proteins in plants and invertebrates. Curr Opin Struct Biol 2002, 12:569-577.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 569-577
    • Wilson, I.B.H.1
  • 102
    • 34547590342 scopus 로고    scopus 로고
    • High-yields and extended serum half-life of human interferon alpha2b expressed in tobacco cells as arabinogalactan-protein fusions
    • Xu J., Tan L., Goodrum K.J., Kieliszewski M.J. High-yields and extended serum half-life of human interferon alpha2b expressed in tobacco cells as arabinogalactan-protein fusions. Biotechnol Bioeng 2007, 97:997-1008.
    • (2007) Biotechnol Bioeng , vol.97 , pp. 997-1008
    • Xu, J.1    Tan, L.2    Goodrum, K.J.3    Kieliszewski, M.J.4
  • 103
    • 42749083259 scopus 로고    scopus 로고
    • The O-hyp glycosylation code in tobacco and Arabidopsis and a proposed role of Hyp-glycans in secretion
    • Xu J., Tan L., Lamport D.T., Showalter A.M., Kieliszewski M.J. The O-hyp glycosylation code in tobacco and Arabidopsis and a proposed role of Hyp-glycans in secretion. Phytochemistry 2008, 69:1631-1640.
    • (2008) Phytochemistry , vol.69 , pp. 1631-1640
    • Xu, J.1    Tan, L.2    Lamport, D.T.3    Showalter, A.M.4    Kieliszewski, M.J.5
  • 104
    • 77956468443 scopus 로고    scopus 로고
    • Human growth hormone expressed in tobacco cells as an arabinogalactan-protein fusion glycoprotein has a prolonged serum life
    • Xu J., Okada S., Tan L., Goodrum K.J., Kopchick J.J., Kieliszewski M.J. Human growth hormone expressed in tobacco cells as an arabinogalactan-protein fusion glycoprotein has a prolonged serum life. Transgenic Res 2010, 19:849-867.
    • (2010) Transgenic Res , vol.19 , pp. 849-867
    • Xu, J.1    Okada, S.2    Tan, L.3    Goodrum, K.J.4    Kopchick, J.J.5    Kieliszewski, M.J.6
  • 105
    • 79952699968 scopus 로고    scopus 로고
    • Towards high-yield production of pharmaceutical proteins with plant cell suspension cultures
    • Xu J., Ge X., Dolan M.C. Towards high-yield production of pharmaceutical proteins with plant cell suspension cultures. Biotechnol Adv 2011, 29:278-299.
    • (2011) Biotechnol Adv , vol.29 , pp. 278-299
    • Xu, J.1    Ge, X.2    Dolan, M.C.3
  • 106
    • 77957222651 scopus 로고    scopus 로고
    • Modification-specific proteomics in plant biology
    • Ytterberg A.J., Jensen O.N. Modification-specific proteomics in plant biology. J Proteomics 2010, 73:2249-2266.
    • (2010) J Proteomics , vol.73 , pp. 2249-2266
    • Ytterberg, A.J.1    Jensen, O.N.2
  • 107
    • 33744484016 scopus 로고    scopus 로고
    • Sialic acid concentrations in plants are in the range of inadvertent contamination
    • Zeleny R., Kolarich D., Strasser R., Altmann F. Sialic acid concentrations in plants are in the range of inadvertent contamination. Planta 2006, 224:222-227.
    • (2006) Planta , vol.224 , pp. 222-227
    • Zeleny, R.1    Kolarich, D.2    Strasser, R.3    Altmann, F.4
  • 108
    • 61449207344 scopus 로고    scopus 로고
    • Purification and characterization of a 44-kda recombinant collagen I alpha 1 fragment from corn grain
    • Zhang C., Baez J., Glatz C.E. Purification and characterization of a 44-kda recombinant collagen I alpha 1 fragment from corn grain. J Agric Food Chem 2009, 57:880-887.
    • (2009) J Agric Food Chem , vol.57 , pp. 880-887
    • Zhang, C.1    Baez, J.2    Glatz, C.E.3
  • 109
    • 68849104340 scopus 로고    scopus 로고
    • Purification and characterization of a transgenic corn grain-derived recombinant collagen type I alpha 1
    • Zhang C., Baez J., Pappu K.M., Glatz C.E. Purification and characterization of a transgenic corn grain-derived recombinant collagen type I alpha 1. Biotechnol Prog 2009, 25:1660-1668.
    • (2009) Biotechnol Prog , vol.25 , pp. 1660-1668
    • Zhang, C.1    Baez, J.2    Pappu, K.M.3    Glatz, C.E.4
  • 111
    • 67549097000 scopus 로고    scopus 로고
    • Regulatory aspects of biosimilars in Europe
    • Zuniga L., Calvo B. Regulatory aspects of biosimilars in Europe. Trends Biotechnol 2009, 27:385-387.
    • (2009) Trends Biotechnol , vol.27 , pp. 385-387
    • Zuniga, L.1    Calvo, B.2


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