메뉴 건너뛰기




Volumn 216, Issue 12, 2011, Pages 1239-1247

A cytotoxic humanized anti-ganglioside antibody produced in a murine cell line defective of N-glycolylated-glycoconjugates

Author keywords

Cmah; Cytotoxic antibody; Gangliosides; Humanization; N glycolyl GM3; ShRNA

Indexed keywords

ANTINEOPLASTIC AGENT; CHIMERIC PROTEIN; EPITOPE; GANGLIOSIDE ANTIBODY; GLYCOCONJUGATE; GLYCOLYTIC ENZYME; MONOCLONAL ANTIBODY 14F7; UNCLASSIFIED DRUG;

EID: 80054944831     PISSN: 01712985     EISSN: 18783279     Source Type: Journal    
DOI: 10.1016/j.imbio.2011.07.004     Document Type: Article
Times cited : (30)

References (66)
  • 1
    • 23844455213 scopus 로고    scopus 로고
    • Mechanisms for the apoptosis of small cell lung cancer cells induced by anti-GD2 monoclonal antibodies: roles of anoikis
    • Aixinjueluo W., Furukawa K., Zhang Q., Hamamura K., Tokuda N., Yoshida S., Ueda R. Mechanisms for the apoptosis of small cell lung cancer cells induced by anti-GD2 monoclonal antibodies: roles of anoikis. J. Biol. Chem. 2005, 280(33):29828-29836.
    • (2005) J. Biol. Chem. , vol.280 , Issue.33 , pp. 29828-29836
    • Aixinjueluo, W.1    Furukawa, K.2    Zhang, Q.3    Hamamura, K.4    Tokuda, N.5    Yoshida, S.6    Ueda, R.7
  • 3
    • 38449104580 scopus 로고    scopus 로고
    • Humanization of antibodies
    • Almagro J.C., Fransson J. Humanization of antibodies. Front. Biosci. 2008, 13:1619-1633.
    • (2008) Front. Biosci. , vol.13 , pp. 1619-1633
    • Almagro, J.C.1    Fransson, J.2
  • 4
    • 0026573630 scopus 로고
    • Glycolipid depletion using a ceramide analogue (PDMP) alters growth, adhesion, and membrane lipid organization in human A431 cells
    • Barbour S., Edidin M., Felding-Habermann B., Taylor-Norton J., Radin N.S., Fenderson B.A. Glycolipid depletion using a ceramide analogue (PDMP) alters growth, adhesion, and membrane lipid organization in human A431 cells. J. Cell. Physiol. 1992, 150(3):610-619.
    • (1992) J. Cell. Physiol. , vol.150 , Issue.3 , pp. 610-619
    • Barbour, S.1    Edidin, M.2    Felding-Habermann, B.3    Taylor-Norton, J.4    Radin, N.S.5    Fenderson, B.A.6
  • 5
    • 14244266499 scopus 로고    scopus 로고
    • Mechanism of uptake and incorporation of the non-human sialic acid N-glycolylneuraminic acid into human cells
    • Bardor M., Nguyen D.H., Diaz S., Varki A. Mechanism of uptake and incorporation of the non-human sialic acid N-glycolylneuraminic acid into human cells. J. Biol. Chem. 2005, 280(6):4228-4237.
    • (2005) J. Biol. Chem. , vol.280 , Issue.6 , pp. 4228-4237
    • Bardor, M.1    Nguyen, D.H.2    Diaz, S.3    Varki, A.4
  • 6
    • 77950461287 scopus 로고    scopus 로고
    • Evaluation of a combinatorial cell engineering approach to overcome apoptotic effects in XBP-1(s) expressing cells
    • Becker E., Florin L., Pfizenmaier K., Kaufmann H. Evaluation of a combinatorial cell engineering approach to overcome apoptotic effects in XBP-1(s) expressing cells. J. Biotechnol. 2010, 146(4):198-206.
    • (2010) J. Biotechnol. , vol.146 , Issue.4 , pp. 198-206
    • Becker, E.1    Florin, L.2    Pfizenmaier, K.3    Kaufmann, H.4
  • 8
    • 0033624355 scopus 로고    scopus 로고
    • A mouse IgG1 monoclonal antibody specific for N-glycolyl GM3 ganglioside recognized breast and melanoma tumors
    • Carr A., Mullet A., Mazorra Z., Vazquez A.M., Alfonso M., Mesa C., Rengifo E., Perez R., Fernandez L.E. A mouse IgG1 monoclonal antibody specific for N-glycolyl GM3 ganglioside recognized breast and melanoma tumors. Hybridoma 2000, 19(3):241-247.
    • (2000) Hybridoma , vol.19 , Issue.3 , pp. 241-247
    • Carr, A.1    Mullet, A.2    Mazorra, Z.3    Vazquez, A.M.4    Alfonso, M.5    Mesa, C.6    Rengifo, E.7    Perez, R.8    Fernandez, L.E.9
  • 10
    • 0026654187 scopus 로고
    • Novel vectors for the expression of antibody molecules using variable regions generated by polymerase chain reaction
    • Coloma M.J., Hastings A., Wims L.A., Morrison S.L. Novel vectors for the expression of antibody molecules using variable regions generated by polymerase chain reaction. J. Immunol. Methods 1992, 152(1):89-104.
    • (1992) J. Immunol. Methods , vol.152 , Issue.1 , pp. 89-104
    • Coloma, M.J.1    Hastings, A.2    Wims, L.A.3    Morrison, S.L.4
  • 12
    • 41149148210 scopus 로고    scopus 로고
    • Differential influence of the tumour-specific non-human sialic acid containing GM3 ganglioside on CD4+CD25- effector and naturally occurring CD4+CD25+ regulatory T cells function
    • de Leon J., Fernandez A., Clavell M., Labrada M., Bebelagua Y., Mesa C., Fernandez L.E. Differential influence of the tumour-specific non-human sialic acid containing GM3 ganglioside on CD4+CD25- effector and naturally occurring CD4+CD25+ regulatory T cells function. Int. Immunol. 2008, 20(4):591-600.
    • (2008) Int. Immunol. , vol.20 , Issue.4 , pp. 591-600
    • de Leon, J.1    Fernandez, A.2    Clavell, M.3    Labrada, M.4    Bebelagua, Y.5    Mesa, C.6    Fernandez, L.E.7
  • 13
    • 30444446808 scopus 로고    scopus 로고
    • Role of tumour-associated N-glycolylated variant of GM3 ganglioside in cancer progression: effect over CD4 expression on T cells
    • de Leon J., Fernandez A., Mesa C., Clavel M., Fernandez L.E. Role of tumour-associated N-glycolylated variant of GM3 ganglioside in cancer progression: effect over CD4 expression on T cells. Cancer Immunol. Immunother. 2006, 55(4):443-450.
    • (2006) Cancer Immunol. Immunother. , vol.55 , Issue.4 , pp. 443-450
    • de Leon, J.1    Fernandez, A.2    Mesa, C.3    Clavel, M.4    Fernandez, L.E.5
  • 14
    • 77951555640 scopus 로고    scopus 로고
    • Microarray and proteomics expression profiling identifies several candidates, including the valosin-containing protein (VCP), involved in regulating high cellular growth rate in production CHO cell lines
    • Doolan P., Meleady P., Barron N., Henry M., Gallagher R., Gammell P., Melville M., Sinacore M., McCarthy K., Leonard M., Charlebois T., Clynes M. Microarray and proteomics expression profiling identifies several candidates, including the valosin-containing protein (VCP), involved in regulating high cellular growth rate in production CHO cell lines. Biotechnol. Bioeng. 2010, 106(1):42-56.
    • (2010) Biotechnol. Bioeng. , vol.106 , Issue.1 , pp. 42-56
    • Doolan, P.1    Meleady, P.2    Barron, N.3    Henry, M.4    Gallagher, R.5    Gammell, P.6    Melville, M.7    Sinacore, M.8    McCarthy, K.9    Leonard, M.10    Charlebois, T.11    Clynes, M.12
  • 15
    • 77955436442 scopus 로고    scopus 로고
    • Implications of the presence of N-glycolylneuraminic acid in recombinant therapeutic glycoproteins
    • Ghaderi D., Taylor R.E., Padler-Karavani V., Diaz S., Varki A. Implications of the presence of N-glycolylneuraminic acid in recombinant therapeutic glycoproteins. Nat. Biotechnol. 2010, 28(8):863-867.
    • (2010) Nat. Biotechnol. , vol.28 , Issue.8 , pp. 863-867
    • Ghaderi, D.1    Taylor, R.E.2    Padler-Karavani, V.3    Diaz, S.4    Varki, A.5
  • 16
    • 0033511863 scopus 로고    scopus 로고
    • Antibody engineering via genetic engineering of the mouse: XenoMouse strains are a vehicle for the facile generation of therapeutic human monoclonal antibodies
    • Green L.L. Antibody engineering via genetic engineering of the mouse: XenoMouse strains are a vehicle for the facile generation of therapeutic human monoclonal antibodies. J. Immunol. Methods 1999, 231(1-2):11-23.
    • (1999) J. Immunol. Methods , vol.231 , Issue.1-2 , pp. 11-23
    • Green, L.L.1
  • 17
    • 0030480250 scopus 로고    scopus 로고
    • Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism
    • Hakomori S. Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism. Cancer Res. 1996, 56(23):5309-5318.
    • (1996) Cancer Res. , vol.56 , Issue.23 , pp. 5309-5318
    • Hakomori, S.1
  • 18
    • 16244378911 scopus 로고    scopus 로고
    • Gangliosides as carbohydrate antigens associated with cancer and their possible use in tumor immunotherapy
    • Horwacik I. Gangliosides as carbohydrate antigens associated with cancer and their possible use in tumor immunotherapy. Przegl. Lek. 2004, 61(Suppl. 2):14-19.
    • (2004) Przegl. Lek. , vol.61 , Issue.SUPPL. 2 , pp. 14-19
    • Horwacik, I.1
  • 19
    • 17644378667 scopus 로고    scopus 로고
    • Immunogenicity of engineered antibodies
    • Hwang W.Y., Foote J. Immunogenicity of engineered antibodies. Methods 2005, 36(1):3-10.
    • (2005) Methods , vol.36 , Issue.1 , pp. 3-10
    • Hwang, W.Y.1    Foote, J.2
  • 20
    • 0037274318 scopus 로고    scopus 로고
    • Modulation of cell cycle for enhancement of antibody productivity in perfusion culture of NS0 cells
    • Ibarra N., Watanabe S., Bi J.X., Shuttleworth J., Al-Rubeai M. Modulation of cell cycle for enhancement of antibody productivity in perfusion culture of NS0 cells. Biotechnol. Prog. 2003, 19(1):224-228.
    • (2003) Biotechnol. Prog. , vol.19 , Issue.1 , pp. 224-228
    • Ibarra, N.1    Watanabe, S.2    Bi, J.X.3    Shuttleworth, J.4    Al-Rubeai, M.5
  • 21
    • 0032546785 scopus 로고    scopus 로고
    • The molecular basis for the absence of N-glycolylneuraminic acid in humans
    • Irie A., Koyama S., Kozutsumi Y., Kawasaki T., Suzuki A. The molecular basis for the absence of N-glycolylneuraminic acid in humans. J. Biol. Chem. 1998, 273(25):15866-15871.
    • (1998) J. Biol. Chem. , vol.273 , Issue.25 , pp. 15866-15871
    • Irie, A.1    Koyama, S.2    Kozutsumi, Y.3    Kawasaki, T.4    Suzuki, A.5
  • 23
    • 0024346633 scopus 로고
    • Rapid insertional mutagenesis of DNA by polymerase chain reaction (PCR)
    • Kammann M., Laufs J., Schell J., Gronenborn B. Rapid insertional mutagenesis of DNA by polymerase chain reaction (PCR). Nucleic Acids Res. 1989, 17(13):5404.
    • (1989) Nucleic Acids Res. , vol.17 , Issue.13 , pp. 5404
    • Kammann, M.1    Laufs, J.2    Schell, J.3    Gronenborn, B.4
  • 24
    • 40749118374 scopus 로고    scopus 로고
    • Current relevance of incomplete synthesis and neo-synthesis for cancer-associated alteration of carbohydrate determinants - Hakomori's concepts revisited
    • Kannagi R., Yin J., Miyazaki K., Izawa M. Current relevance of incomplete synthesis and neo-synthesis for cancer-associated alteration of carbohydrate determinants - Hakomori's concepts revisited. Biochim. Biophys. Acta 2008, 1780(3):525-531.
    • (2008) Biochim. Biophys. Acta , vol.1780 , Issue.3 , pp. 525-531
    • Kannagi, R.1    Yin, J.2    Miyazaki, K.3    Izawa, M.4
  • 25
    • 0028322123 scopus 로고
    • Biosynthesis of N-glycolylneuraminic acid-containing glycoconjugates. Purification and characterization of the key enzyme of the cytidine monophospho-N-acetylneuraminic acid hydroxylation system
    • Kawano T., Kozutsumi Y., Kawasaki T., Suzuki A. Biosynthesis of N-glycolylneuraminic acid-containing glycoconjugates. Purification and characterization of the key enzyme of the cytidine monophospho-N-acetylneuraminic acid hydroxylation system. J. Biol. Chem. 1994, 269(12):9024-9029.
    • (1994) J. Biol. Chem. , vol.269 , Issue.12 , pp. 9024-9029
    • Kawano, T.1    Kozutsumi, Y.2    Kawasaki, T.3    Suzuki, A.4
  • 26
  • 27
    • 0014963871 scopus 로고
    • Three variable-gene pools common to IgM, IgG and IgA immunoglobulins
    • Kohler H., Shimizu A., Paul C., Moore V., Putnam F.W. Three variable-gene pools common to IgM, IgG and IgA immunoglobulins. Nature 1970, 227(5265):1318-1320.
    • (1970) Nature , vol.227 , Issue.5265 , pp. 1318-1320
    • Kohler, H.1    Shimizu, A.2    Paul, C.3    Moore, V.4    Putnam, F.W.5
  • 28
    • 77956230926 scopus 로고    scopus 로고
    • Methods in mammalian cell line engineering: from random mutagenesis to sequence-specific approaches
    • Kramer O., Klausing S., Noll T. Methods in mammalian cell line engineering: from random mutagenesis to sequence-specific approaches. Appl. Microbiol. Biotechnol. 2010, 88(2):425-436.
    • (2010) Appl. Microbiol. Biotechnol. , vol.88 , Issue.2 , pp. 425-436
    • Kramer, O.1    Klausing, S.2    Noll, T.3
  • 30
    • 0347297482 scopus 로고    scopus 로고
    • Transfection of NS0 myeloma fusion partner cells with HSP70 gene results in higher hybridoma yield by improving cellular resistance to apoptosis
    • Lasunskaia E.B., Fridlianskaia I.I., Darieva Z.A., da Silva M.S., Kanashiro M.M., Margulis B.A. Transfection of NS0 myeloma fusion partner cells with HSP70 gene results in higher hybridoma yield by improving cellular resistance to apoptosis. Biotechnol. Bioeng. 2003, 81(4):496-504.
    • (2003) Biotechnol. Bioeng. , vol.81 , Issue.4 , pp. 496-504
    • Lasunskaia, E.B.1    Fridlianskaia, I.I.2    Darieva, Z.A.3    da Silva, M.S.4    Kanashiro, M.M.5    Margulis, B.A.6
  • 31
    • 41149097757 scopus 로고    scopus 로고
    • Engineering therapeutic monoclonal antibodies
    • Liu X.Y., Pop L.M., Vitetta E.S. Engineering therapeutic monoclonal antibodies. Immunol. Rev. 2008, 222:9-27.
    • (2008) Immunol. Rev. , vol.222 , pp. 9-27
    • Liu, X.Y.1    Pop, L.M.2    Vitetta, E.S.3
  • 33
    • 0034844959 scopus 로고    scopus 로고
    • N-glycolylneuraminic acid in human tumours
    • Malykh Y.N., Schauer R., Shaw L. N-glycolylneuraminic acid in human tumours. Biochimie 2001, 83(7):623-634.
    • (2001) Biochimie , vol.83 , Issue.7 , pp. 623-634
    • Malykh, Y.N.1    Schauer, R.2    Shaw, L.3
  • 34
    • 0023098573 scopus 로고
    • Prediction of immunodominant helper T cell antigenic sites from the primary sequence
    • Margalit H., Spouge J.L., Cornette J.L., Cease K.B., Delisi C., Berzofsky J.A. Prediction of immunodominant helper T cell antigenic sites from the primary sequence. J. Immunol. 1987, 138(7):2213-2229.
    • (1987) J. Immunol. , vol.138 , Issue.7 , pp. 2213-2229
    • Margalit, H.1    Spouge, J.L.2    Cornette, J.L.3    Cease, K.B.4    Delisi, C.5    Berzofsky, J.A.6
  • 36
    • 0034532441 scopus 로고    scopus 로고
    • Removal of amphipathic epitopes from genetically engineered antibodies: production of modified immunoglobulins with reduced immunogenicity
    • Mateo C., Lombardero J., Moreno E., Morales A., Bombino G., Coloma J., Wims L., Morrison S.L., Perez R. Removal of amphipathic epitopes from genetically engineered antibodies: production of modified immunoglobulins with reduced immunogenicity. Hybridoma 2000, 19(6):463-471.
    • (2000) Hybridoma , vol.19 , Issue.6 , pp. 463-471
    • Mateo, C.1    Lombardero, J.2    Moreno, E.3    Morales, A.4    Bombino, G.5    Coloma, J.6    Wims, L.7    Morrison, S.L.8    Perez, R.9
  • 37
    • 0030910482 scopus 로고    scopus 로고
    • Humanization of a mouse monoclonal antibody that blocks the epidermal growth factor receptor: recovery of antagonistic activity
    • Mateo C., Moreno E., Amour K., Lombardero J., Harris W., Perez R. Humanization of a mouse monoclonal antibody that blocks the epidermal growth factor receptor: recovery of antagonistic activity. Immunotechnology 1997, 3(1):71-81.
    • (1997) Immunotechnology , vol.3 , Issue.1 , pp. 71-81
    • Mateo, C.1    Moreno, E.2    Amour, K.3    Lombardero, J.4    Harris, W.5    Perez, R.6
  • 39
    • 0021716682 scopus 로고
    • Chimeric human antibody molecules: mouse antigen-binding domains with human constant region domains
    • Morrison S.L., Johnson M.J., Herzenberg L.A., Oi V.T. Chimeric human antibody molecules: mouse antigen-binding domains with human constant region domains. Proc. Natl. Acad. Sci. U.S.A. 1984, 81(21):6851-6855.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , Issue.21 , pp. 6851-6855
    • Morrison, S.L.1    Johnson, M.J.2    Herzenberg, L.A.3    Oi, V.T.4
  • 42
    • 21244478903 scopus 로고    scopus 로고
    • Effects of natural human antibodies against a nonhuman sialic acid that metabolically incorporates into activated and malignant immune cells
    • Nguyen D.H., Tangvoranuntakul P., Varki A. Effects of natural human antibodies against a nonhuman sialic acid that metabolically incorporates into activated and malignant immune cells. J. Immunol. 2005, 175(1):228-236.
    • (2005) J. Immunol. , vol.175 , Issue.1 , pp. 228-236
    • Nguyen, D.H.1    Tangvoranuntakul, P.2    Varki, A.3
  • 44
    • 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., Chen X., Varki A. Diversity in specificity, abundance, and composition of anti-Neu5Gc antibodies in normal humans: potential implications for disease. Glycobiology 2008, 18(10):818-830.
    • (2008) Glycobiology , vol.18 , Issue.10 , pp. 818-830
    • Padler-Karavani, V.1    Yu, H.2    Cao, H.3    Chokhawala, H.4    Karp, F.5    Varki, N.6    Chen, X.7    Varki, A.8
  • 45
    • 66349092892 scopus 로고    scopus 로고
    • Ceramide-induced autophagy: to junk or to protect cells?
    • Pattingre S., Bauvy C., Levade T., Levine B., Codogno P. Ceramide-induced autophagy: to junk or to protect cells?. Autophagy 2009, 5(4):558-560.
    • (2009) Autophagy , vol.5 , Issue.4 , pp. 558-560
    • Pattingre, S.1    Bauvy, C.2    Levade, T.3    Levine, B.4    Codogno, P.5
  • 47
    • 22244491314 scopus 로고    scopus 로고
    • Characterization of a proapoptotic antiganglioside GM2 monoclonal antibody and evaluation of its therapeutic effect on melanoma and small cell lung carcinoma xenografts
    • Retter M.W., Johnson J.C., Peckham D.W., Bannink J.E., Bangur C.S., Dresser K., Cai F., Foy T.M., Fanger N.A., Fanger G.R., Woda B., Rock K.L. Characterization of a proapoptotic antiganglioside GM2 monoclonal antibody and evaluation of its therapeutic effect on melanoma and small cell lung carcinoma xenografts. Cancer Res. 2005, 65(14):6425-6434.
    • (2005) Cancer Res. , vol.65 , Issue.14 , pp. 6425-6434
    • Retter, M.W.1    Johnson, J.C.2    Peckham, D.W.3    Bannink, J.E.4    Bangur, C.S.5    Dresser, K.6    Cai, F.7    Foy, T.M.8    Fanger, N.A.9    Fanger, G.R.10    Woda, B.11    Rock, K.L.12
  • 48
    • 0023911111 scopus 로고
    • Reshaping human antibodies for therapy
    • Riechmann L., Clark M., Waldmann H., Winter G. Reshaping human antibodies for therapy. Nature 1988, 332(6162):323-327.
    • (1988) Nature , vol.332 , Issue.6162 , pp. 323-327
    • Riechmann, L.1    Clark, M.2    Waldmann, H.3    Winter, G.4
  • 49
    • 0344825770 scopus 로고    scopus 로고
    • Generation and characterization of an anti-idiotype monoclonal antibody related to GM3(NeuGc) ganglioside
    • Rodriguez M., Llanes L., Perez A., Perez R., Vazquez A.M. Generation and characterization of an anti-idiotype monoclonal antibody related to GM3(NeuGc) ganglioside. Hybrid. Hybridomics 2003, 22(5):307-314.
    • (2003) Hybrid. Hybridomics , vol.22 , Issue.5 , pp. 307-314
    • Rodriguez, M.1    Llanes, L.2    Perez, A.3    Perez, R.4    Vazquez, A.M.5
  • 51
    • 7944222460 scopus 로고    scopus 로고
    • Light-chain shuffling results in successful phage display selection of functional prokaryotic-expressed antibody fragments to N-glycolyl GM3 ganglioside
    • Rojas G., Talavera A., Munoz Y., Rengifo E., Krengel U., Angstrom J., Gavilondo J., Moreno E. Light-chain shuffling results in successful phage display selection of functional prokaryotic-expressed antibody fragments to N-glycolyl GM3 ganglioside. J. Immunol. Methods 2004, 293(1-2):71-83.
    • (2004) J. Immunol. Methods , vol.293 , Issue.1-2 , pp. 71-83
    • Rojas, G.1    Talavera, A.2    Munoz, Y.3    Rengifo, E.4    Krengel, U.5    Angstrom, J.6    Gavilondo, J.7    Moreno, E.8
  • 53
    • 0042838162 scopus 로고    scopus 로고
    • Humanization of predicted T-cell epitopes reduces the immunogenicity of chimeric antibodies: new evidence supporting a simple method
    • Roque-Navarro L., Mateo C., Lombardero J., Mustelier G., Fernandez A., Sosa K., Morrison S.L., Perez R. Humanization of predicted T-cell epitopes reduces the immunogenicity of chimeric antibodies: new evidence supporting a simple method. Hybrid. Hybridomics 2003, 22(4):245-257.
    • (2003) Hybrid. Hybridomics , vol.22 , Issue.4 , pp. 245-257
    • Roque-Navarro, L.1    Mateo, C.2    Lombardero, J.3    Mustelier, G.4    Fernandez, A.5    Sosa, K.6    Morrison, S.L.7    Perez, R.8
  • 54
    • 0028276873 scopus 로고
    • Human-engineered monoclonal antibodies retain full specific binding activity by preserving non-CDR complementarity-modulating residues
    • Studnicka G.M., Soares S., Better M., Williams R.E., Nadell R., Horwitz A.H. Human-engineered monoclonal antibodies retain full specific binding activity by preserving non-CDR complementarity-modulating residues. Protein Eng. 1994, 7(6):805-814.
    • (1994) Protein Eng. , vol.7 , Issue.6 , pp. 805-814
    • Studnicka, G.M.1    Soares, S.2    Better, M.3    Williams, R.E.4    Nadell, R.5    Horwitz, A.H.6
  • 55
    • 0024849163 scopus 로고
    • Glycosphingolipids: structure, biological source, and properties
    • Stults C.L., Sweeley C.C., Macher B.A. Glycosphingolipids: structure, biological source, and properties. Methods Enzymol. 1989, 179:167-214.
    • (1989) Methods Enzymol. , vol.179 , pp. 167-214
    • Stults, C.L.1    Sweeley, C.C.2    Macher, B.A.3
  • 59
    • 0029586061 scopus 로고
    • Generation of a murine monoclonal antibody specific for N-glycolylneuraminic acid-containing gangliosides that also recognizes sulfated glycolipids
    • Vazquez A.M., Alfonso M., Lanne B., Karlsson K.A., Carr A., Barroso O., Fernandez L.E., Rengifo E., Lanio M.E., Alvarez C., et al. Generation of a murine monoclonal antibody specific for N-glycolylneuraminic acid-containing gangliosides that also recognizes sulfated glycolipids. Hybridoma 1995, 14(6):551-556.
    • (1995) Hybridoma , vol.14 , Issue.6 , pp. 551-556
    • Vazquez, A.M.1    Alfonso, M.2    Lanne, B.3    Karlsson, K.A.4    Carr, A.5    Barroso, O.6    Fernandez, L.E.7    Rengifo, E.8    Lanio, M.E.9    Alvarez, C.10
  • 60
    • 0032412454 scopus 로고    scopus 로고
    • Syngeneic anti-idiotypic monoclonal antibodies to an anti-NeuGc-containing ganglioside monoclonal antibody
    • Vazquez A.M., Perez A., Hernandez A.M., Macias A., Alfonso M., Bombino G., Perez R. Syngeneic anti-idiotypic monoclonal antibodies to an anti-NeuGc-containing ganglioside monoclonal antibody. Hybridoma 1998, 17(6):527-534.
    • (1998) Hybridoma , vol.17 , Issue.6 , pp. 527-534
    • Vazquez, A.M.1    Perez, A.2    Hernandez, A.M.3    Macias, A.4    Alfonso, M.5    Bombino, G.6    Perez, R.7
  • 62
    • 0027078548 scopus 로고
    • Genetically engineered antibodies: progress and prospects
    • Wright A., Shin S.U., Morrison S.L. Genetically engineered antibodies: progress and prospects. Crit. Rev. Immunol. 1992, 12(3-4):125-168.
    • (1992) Crit. Rev. Immunol. , vol.12 , Issue.3-4 , pp. 125-168
    • Wright, A.1    Shin, S.U.2    Morrison, S.L.3
  • 63
    • 0033584995 scopus 로고    scopus 로고
    • Humanization of a murine monoclonal antibody by simultaneous optimization of framework and CDR residues
    • Wu H., Nie Y., Huse W.D., Watkins J.D. Humanization of a murine monoclonal antibody by simultaneous optimization of framework and CDR residues. J. Mol. Biol. 1999, 294(1):151-162.
    • (1999) J. Mol. Biol. , vol.294 , Issue.1 , pp. 151-162
    • Wu, H.1    Nie, Y.2    Huse, W.D.3    Watkins, J.D.4
  • 64
    • 67349211749 scopus 로고    scopus 로고
    • RNA interference technology to improve recombinant protein production in Chinese hamster ovary cells
    • Wu S.C. RNA interference technology to improve recombinant protein production in Chinese hamster ovary cells. Biotechnol. Adv. 2009, 27(4):417-422.
    • (2009) Biotechnol. Adv. , vol.27 , Issue.4 , pp. 417-422
    • Wu, S.C.1
  • 65
    • 34249693089 scopus 로고    scopus 로고
    • Novel antibodies as anticancer agents
    • Zafir-Lavie I., Michaeli Y., Reiter Y. Novel antibodies as anticancer agents. Oncogene 2007, 26(25):3714-3733.
    • (2007) Oncogene , vol.26 , Issue.25 , pp. 3714-3733
    • Zafir-Lavie, I.1    Michaeli, Y.2    Reiter, Y.3
  • 66
    • 38449115463 scopus 로고    scopus 로고
    • Development of a simple and rapid method for producing non-fucosylated oligomannose containing antibodies with increased effector function
    • Zhou Q., Shankara S., Roy A., Qiu H., Estes S., McVie-Wylie A., Culm-Merdek K., Park A., Pan C., Edmunds T. Development of a simple and rapid method for producing non-fucosylated oligomannose containing antibodies with increased effector function. Biotechnol. Bioeng. 2008, 99(3):652-665.
    • (2008) Biotechnol. Bioeng. , vol.99 , Issue.3 , pp. 652-665
    • Zhou, Q.1    Shankara, S.2    Roy, A.3    Qiu, H.4    Estes, S.5    McVie-Wylie, A.6    Culm-Merdek, K.7    Park, A.8    Pan, C.9    Edmunds, T.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.