Production platforms for biotherapeutic glycoproteins. Occurrence impact, and challenges of non-human sialylation
Open accessAbstract
One of the fastest growing fields in the pharmaceutical industry is the market for therapeutic glycoproteins. Today, these molecules play a major role in the treatment of various diseases, and include several protein classes, i.e., clotting factors, hormones, cytokines, antisera, enzymes, enzyme inhibitors, Ig-Fc-Fusion proteins, and monoclonal antibodies. Optimal glycosylation is critical for therapeutic glycoproteins, as glycans can influence their yield, immunogenicity and efficacy, which impact the costs and success of such treatments. While several mammalian cell expression systems currently used can produce therapeutic glycoproteins that are mostly decorated with human-like glycans, they can differ from human glycans by presenting two structures at the terminal and therefore most exposed position. First, natural human N-glycans are lacking the terminal Gal 1-3Gal (alpha-Gal) modification; and second, they do not contain the non-human sialic acid N-glycolylneuraminic acid (Neu5Gc). All humans spontaneously express antibodies against both of these glycan structures, risking increased immunogenicity of biotherapeutics carrying such non-human glycan epitopes. However, in striking contrast to the alpha-Gal epitope, exogenous Neu5Gc can be metabolically incorporated into human cells and presented on expressed glycoproteins in several possible epitopes. Recent work has demonstrated that this non-human sialic acid is found in widely varying amounts on biotherapeutic glycoproteins approved for treatment of various medical conditions. Neu5Gc on glycans of these medical agents likely originates from the production process involving the non-human mammalian cell lines and/or the addition of animal-derived tissue culture supplements. Further studies are needed to fully understand the impact of Neu5Gc in biotherapeutic agents. Similar concerns apply to human cells prepared for allo- or auto-transplantation, that have been grown in animal-derived tissue culture supplements.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Plants produce core α1,3-fructose and β1,2-xylose, which are completely absent in human cells and could be immunogenic.
“Indeed, plants produce core α1,3-fructose and β1,2-xylose, which are completely absent in human cells and could be immunogenic (Karg et al., 2009;Ghaderi et al., 2012).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Ghaderi et al., 2012
The plant-based expression systems section says plant N-glycans may carry β1,2-xylose and α1,3-fucose residues that are absent in humans and may be immunogenic. The claim says “fructose” rather than the paper’s “fucose,” so that component is not supported as written. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Wiederschain, G. Y. (2009) · Biochemistry (Moscow) · doi:10.1134/s0006297909090156 · Cited by 4,089 · see citing works
Siglecs and their roles in the immune system
Crocker, P. R., Paulson, J. C., & Varki, A. P. (2007) · Nature reviews. Immunology · doi:10.1038/nri2056 · Cited by 2,032 · see citing works
Self-citationCetuximab-Induced Anaphylaxis and IgE Specific for Galactose-α-1,3-Galactose
Chung, C. H., Mirakhur, B., Chan, E., Le, Q.-T., Berlin, J., Morse, M., Murphy, B. A., Satinover, S. M., Hosen, J., Mauro, D., et al. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa074943 · Cited by 1,521 · see citing works
The Impact of Glycosylation on the Biological Function and Structure of Human Immunoglobulins
Arnold, J. N., Wormald, M. R., Sim, R. B., Rudd, P. M., & Dwek, R. A. (2006) · Annual Review of Immunology · doi:10.1146/annurev.immunol.25.022106.141702 · Cited by 1,308 · see citing works
Chemical Diversity in the Sialic Acids and Related α-Keto Acids: An Evolutionary Perspective
Angata, T., & Varki, A. P. (2002) · Chemical Reviews · doi:10.1021/cr000407m · Cited by 1,232 · see citing works
Self-citationProduction of α1,3-Galactosyltransferase-Deficient Pigs
Phelps, C. J., Koike, C., Vaught, T. D., Boone, J. T., Wells, K. D., Chen, S.-H., Ball, S. F., Specht, S. M., Polejaeva, I. A., Monahan, J. A., et al. (2003) · Science · doi:10.1126/science.1078942 · Cited by 1,111 · see citing works
Baculovirus as versatile vectors for protein expression in insect and mammalian cells
Kost, T. A., Condreay, J. P., & Jarvis, D. L. (2005) · Nature Biotechnology · doi:10.1038/nbt1095 · Cited by 1,014 · see citing works
Human embryonic stem cells express an immunogenic nonhuman sialic acid
Martin, M. J., Muotri, A. R., Gage, F. H., & Varki, A. P. (2005) · Nature Medicine · doi:10.1038/nm1181 · Cited by 932 · see citing works
Self-citationJournal of the National Cancer Institute
(1993) · Journal of the American Dietetic Association · doi:10.1016/0002-8223(93)92324-q · Cited by 913 · see citing works
Wiseman, M. J. (2008) · Proceedings of The Nutrition Society · doi:10.1017/s002966510800712x · Cited by 902 · see citing works
Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins
Varki, A. P. (2007) · Nature · doi:10.1038/nature05816 · Cited by 855 · see citing works
Self-citationN-Linked Glycosylation in Campylobacter jejuni and Its Functional Transfer into E. coli
Wacker, M., Linton, D., Hitchen, P. G., Lazar, M. N., Haslam, S. M., North, S. J., Panico, M., Morris, H. R., Dell, A., Wren, B. W., et al. (2002) · Science · doi:10.1126/science.298.5599.1790 · Cited by 780 · see citing works
Kuwaki, K., Tseng, Y., Dor, F. J. M. F., Shimizu, A., Houser, S. L., Sanderson, T. M., Lancos, C. J., Prabharasuth, D., Cheng, J. J., Moran, K., et al. (2004) · Nature Medicine · doi:10.1038/nm1171 · Cited by 693 · see citing works
Galili, U. (1993) · Immunology Today · doi:10.1016/0167-5699(93)90261-i · Cited by 665 · see citing works
Human uptake and incorporation of an immunogenic nonhuman dietary sialic acid
Tangvoranuntakul, P., Gagneux, P., Diaz, S., Bardor, M., Varki, N., Varki, A., & Muchmore, E. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2131556100 · Cited by 625 · see citing works
Self-citationRose, D., Boyar, A. P., & Wynder, E. L. (1986) · Cancer · doi:10.1002/1097-0142(19861201)58:11 · Cited by 593 · see citing works
A mutation in human CMP-sialic acid hydroxylase occurred after the Homo-Pan divergence
Chou, H.-H., Takematsu, H., Diaz, S. L., Iber, J. C., Nickerson, E., Wright, K. L., Muchmore, E. A., Nelson, D. L., Warren, S. T., & Varki, A. P. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.20.11751 · Cited by 576 · see citing works
Self-citationAchievements and challenges of sialic acid research
Schauer, R. (2000) · Glycoconjugate Journal · doi:10.1023/a:1011062223612 · Cited by 572 · see citing works
Readily Available Tissue-Engineered Vascular Grafts
Dahl, S. L. M., Kypson, A. P., Lawson, J. H., Blum, J. L., Strader, J. T., Li, Y., Manson, R. J., Tente, W. E., DiBernardo, L. R., Hensley, M. T., et al. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3001426 · Cited by 563 · see citing works
Pera, M. F., Reubinoff, B. E., & Trounson, A. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.1.5 · Cited by 557 · see citing works
Immunogenicity of protein therapeutics
Groot, A. S. D., & Scott, D. W. (2007) · Trends in Immunology · doi:10.1016/j.it.2007.07.011 · Cited by 545 · see citing works
Advances in the Biology and Chemistry of Sialic Acids
Chen, X., & Varki, A. P. (2009) · ACS Chemical Biology · doi:10.1021/cb900266r · Cited by 544 · see citing works
Self-citationProtein glycosylation in bacteria: sweeter than ever
Nothaft, H., & Szymanski, C. M. (2010) · Nature Reviews Microbiology · doi:10.1038/nrmicro2383 · Cited by 531 · see citing works
Diversity in cell surface sialic acid presentations: implications for biology and disease
Varki, N. M., & Varki, A. P. (2007) · Laboratory Investigation · doi:10.1038/labinvest.3700656 · Cited by 516 · see citing works
Self-citationMeat consumption and colorectal cancer risk: Dose‐response meta‐analysis of epidemiological studies
Norat, T., Lukanova, A., Ferrari, P., & Ríboli, E. (2001) · International Journal of Cancer · doi:10.1002/ijc.10126 · Cited by 499 · see citing works
Fraser, G. E. (1999) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/70.3.532s · Cited by 489 · see citing works
Key, T. J., Fraser, G. E., Thorogood, M., Appleby, P. N., Beral, V., Reeves, G., Burr, M. L., Chang-Claude, J., Frentzel-Beyme, R., Kuzma, J. W., et al. (1999) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/70.3.516s · Cited by 484 · see citing works
Plant‐specific glycosylation patterns in the context of therapeutic protein production
Gomord, V., Fitchette, A., Menu‐Bouaouiche, L., Saint‐Jore‐Dupas, C., Plasson, C., Michaud, D., & Faye, L. J.-Y. (2010) · Plant Biotechnology Journal · doi:10.1111/j.1467-7652.2009.00497.x · Cited by 419 · see citing works
The Molecular Basis for the Absence ofN-Glycolylneuraminic Acid in Humans
Irie, A., Koyama, S., Kozutsumi, Y., Kawasaki, T., & Suzuki, A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15866 · Cited by 405 · see citing works
Process economics of industrial monoclonal antibody manufacture
Farid, S. S. (2006) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.07.037 · Cited by 396 · see citing works
Bardor, M., Nguyen, D., Diaz, S. L., & Varki, A. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m412040200 · Cited by 390 · see citing works
Self-citationExpression systems for therapeutic glycoprotein production
Durocher, Y., & Butler, M. (2009) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2009.10.008 · Cited by 386 · see citing works
Implications of the presence of N-glycolylneuraminic acid in recombinant therapeutic glycoproteins
Ghaderi, D., Taylor, R. E., Padler-Karavani, V., Diaz, S., & Varki, A. (2010) · Nature Biotechnology · doi:10.1038/nbt.1651 · Cited by 372 · see citing works
Self-citationChou, H.-H., Hayakawa, T., Diaz, S. L., Krings, M., Indriati, E., Leakey, M. G., Pääbo, S., Satta, Y., Takahata, N., & Varki, A. P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.182257399 · Cited by 351 · see citing works
Self-citationKoren, E., Smith, H. W., Shores, E., Shankar, G., Finco-Kent, D., Rup, B., Barrett, Y., Devanarayan, V., Gorovits, B., Gupta, S., et al. (2008) · JIM - Journal of Immunological Methods · doi:10.1016/j.jim.2008.01.001 · Cited by 332 · see citing works
Varki, A. P. (2001) · American Journal of Physical Anthropology · doi:10.1002/ajpa.10018 · Cited by 324 · see citing works
Self-citationPadler-karavani, V., Yu, H., Cao, H.-Z., Chokhawala, H. A., Karp, F., Varki, N., Chen, X., & Varki, A. (2008) · Glycobiology · doi:10.1093/glycob/cwn072 · Cited by 322 · see citing works
Self-citationGlycosylation engineering in yeast: the advent of fully humanized yeast
Hamilton, S. R., & Gerngross, T. U. (2007) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2007.09.001 · Cited by 322 · see citing works
The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach
Harduin‐Lepers, A., Mollicone, R., Delannoy, P., & Oriol, R. (2005) · Glycobiology · doi:10.1093/glycob/cwi063 · Cited by 302 · see citing works
Regulation of Macropinocytosis by p21-activated Kinase-1
Dharmawardhane, S., Schürmann, A., Sells, M. A., Chernoff, J., Schmid, S. L., & Bokoch, G. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.10.3341 · Cited by 290 · see citing works
Qian, J., Liu, T., Yang, L., Daus, A., Crowley, R., & Zhou, Q.-W. (2007) · Analytical Biochemistry · doi:10.1016/j.ab.2007.01.023 · Cited by 286 · see citing works
Iliopoulou, E. G., Kountourakis, P., Karamouzis, M. V., Doufexis, D., Ardavanis, A. S., Baxevanis, C. N., Rigatos, G. A., Papamichail, M., & Perez, S. A. (2010) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-010-0904-3 · Cited by 277 · see citing works
Malykh, Y. N., Schauer, R., & Shaw, L. (2001) · Biochimie · doi:10.1016/s0300-9084(01)01303-7 · Cited by 275 · see citing works
Anti‐N‐glycolylneuraminic acid antibodies identified in healthy human serum
Zhu, A., & Hurst, R. (2002) · Xenotransplantation · doi:10.1034/j.1399-3089.2002.02138.x · Cited by 274 · see citing works
Shankar, G., Pendley, C. E., & Stein, K. E. (2007) · Nature Biotechnology · doi:10.1038/nbt1303 · Cited by 262 · see citing works
Willett, W. C. (2000) · The Oncologist · doi:10.1634/theoncologist.5-5-393 · Cited by 245 · see citing works
Diet: Fat, Meat, and Prostate Cancer
Kolonel, L. N. (2001) · Epidemiologic Reviews · doi:10.1093/oxfordjournals.epirev.a000798 · Cited by 237 · see citing works
Seed‐based expression systems for plant molecular farming
Boothe, J. G., Nykiforuk, C. L., Shen, Y., Zaplachinski, S., Szarka, S. J., Kuhlman, P. S., Murray, E. W., Morck, D. W., & Moloney, M. M. (2010) · Plant Biotechnology Journal · doi:10.1111/j.1467-7652.2010.00511.x · Cited by 235 · see citing works
In Planta Protein Sialylation through Overexpression of the Respective Mammalian Pathway
Castilho, A., Strasser, R., Stadlmann, J., Grass, J., Jeż, J., Gattinger, P., Kunert, R., Quendler, H., Pabst, M., Leonard, R., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.088401 · Cited by 230 · see citing works
Multiple changes in sialic acid biology during human evolution
Varki, A. P. (2008) · Glycoconjugate Journal · doi:10.1007/s10719-008-9183-z · Cited by 220 · see citing works
Self-citationHeiskanen, A., Satomaa, T., Tiitinen, S. L., Laitinen, A., Mannelin, S., Impola, U., Mikkola, M., Olsson, C., Miller‐Podraza, H., Blomqvist, M., et al. (2006) · Stem Cells · doi:10.1634/stemcells.2006-0444 · Cited by 215 · see citing works
Fucose in N-glycans: from plant to man
Staudacher, E. (1999) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(99)00181-6 · Cited by 213 · see citing works
Hedlund, M., Padler‐Karavani, V., Varki, N. M., & Varki, A. P. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803943105 · Cited by 199 · see citing works
Self-citationN -Glycolylneuraminic Acid Deficiency in Mice: Implications for Human Biology and Evolution
Hedlund, M., Tangvoranuntakul, P., Takematsu, H., Long, J. M., Housley, G. D., Kozutsumi, Y., Suzuki, A., Wynshaw-Boris, A. J., Ryan, A. F., Gallo, R. L., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00379-07 · Cited by 197 · see citing works
Self-citationModifications of cell surface sialic acids modulate cell adhesion mediated by sialoadhesin and CD22
Kelm, S., Schauer, R., Manuguerra, J., Groß, H., & Crocker, P. R. (1994) · Glycoconjugate Journal · doi:10.1007/bf00731309 · Cited by 196 · see citing works
Mortality among California Seventh-Day Adventists for selected cancer sites.
Phillips, R. L., Garfinkel, L., Kuzma, J. W., Beeson, W. L., Lotz, T. M., & Brin, B. N. (1980) · PubMed · Cited by 188 · see citing works
Mortality among California Seventh-Day Adventists for selected cancer sites.
Phillips, R. L., Garfinkel, L., Kuzma, J., Beeson, W., Lotz, T., & Brin, B. N. (1980) · Journal of the National Cancer Institute · doi:10.1093/jnci/65.5.1097 · Cited by 187
A combined method for producing homogeneous glycoproteins with eukaryotic N-glycosylation
Schwarz, F., Huang, W., Li, C., Schulz, B. L., Lizak, C., Palumbo, A., Numao, S., Neri, D., Aebi, M., & Wang, L. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.314 · Cited by 186 · see citing works
Higashi, H., Hirabayashi, Y., Fukui, Y., Naiki, M., Matsumoto, M., Ueda, S., & Kato, S. (1985) · PubMed · Cited by 178 · see citing works
Higashi, H., NAIKI, M., Matuo, S., & OKOUCHI, K. (1977) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(77)90169-3 · Cited by 174 · see citing works
GlycoPEGylation of recombinant therapeutic proteins produced in Escherichia coli
DeFrees, S. A., Wang, Z., Xing, R., Scott, A. E., Wang, J., Zopf, D., Gouty, D. L., Sjoberg, E. R., Panneerselvam, K., der Linden, E. C. M. B.-V., et al. (2006) · Glycobiology · doi:10.1093/glycob/cwl004 · Cited by 174 · see citing works
Cao, H., & Crocker, P. R. (2010) · Immunology · doi:10.1111/j.1365-2567.2010.03368.x · Cited by 172 · see citing works
Brooks, S. A. (2004) · Molecular Biotechnology · doi:10.1385/mb:28:3:241 · Cited by 166 · see citing works
Factors controlling the glycosylation potential of the Golgi apparatus
Varki, A. P. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(97)01198-7 · Cited by 165 · see citing works
Self-citationPadler‐Karavani, V., & Varki, A. (2011) · Xenotransplantation · doi:10.1111/j.1399-3089.2011.00622.x · Cited by 162 · see citing works
Self-citationEngineering of glycosylation in yeast and other fungi: current state and perspectives
Pourcq, K. D., Schutter, K. D., & Callewaert, N. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2721-1 · Cited by 160 · see citing works
Yin, J., Hashimoto, A., Izawa, M., Miyazaki, K., Chen, G.-Y., Takematsu, H., Kozutsumi, Y., Suzuki, A., Furuhata, K., Cheng, F.-L., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-2615 · Cited by 160 · see citing works
Chinese hamster ovary cells can produce galactose-α-1,3-galactose antigens on proteins
Bosques, C. J., Collins, B. E., Meador, J. W., Sarvaiya, H., Murphy, J. L., DelloRusso, G., Bulik, D. A., Hsu, I.-H., Washburn, N., Sipsey, S. F., et al. (2010) · Nature Biotechnology · doi:10.1038/nbt1110-1153 · Cited by 159 · see citing works
Loss of N-Glycolylneuraminic Acid in Human Evolution
der Linden, E. C. M. B.-V., Sjoberg, E. R., Juneja, L. R., Crocker, P. R., Varki, N. M., & Varki, A. P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.8633 · Cited by 158 · see citing works
Self-citationTaylor, R. E., Gregg, C. J., Padler‐Karavani, V., Ghaderi, D., Yu, H., Huang, S., Sorensen, R. U., Chen, X., Jaime Inostroza, S., Nizet, V., et al. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem.20100575 · Cited by 156 · see citing works
Self-citationAlu -mediated inactivation of the human CMP- N -acetylneuraminic acid hydroxylase gene
Hayakawa, T., Satta, Y., Gagneux, P., Varki, A. P., & Takahata, N. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.191268198 · Cited by 154 · see citing works
Self-citationNucleotide sugar transporters of the Golgi apparatus
Berninsone, P. M., & Hirschberg, C. B. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00128-7 · Cited by 151 · see citing works
Byrne, B. J., Donohoe, G. G., & O’Kennedy, R. J. (2007) · Drug Discovery Today · doi:10.1016/j.drudis.2007.02.010 · Cited by 148 · see citing works
Diaz, S. L., Padler‐Karavani, V., Ghaderi, D., Hurtado‐Ziola, N., Yu, H., Chen, X., der Linden, E. C. M. B.-V., Varki, A. P., & Varki, N. M. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004241 · Cited by 146 · see citing works
Self-citationNguyen, D. H., Tangvoranuntakul, P., & Varki, A. P. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.1.228 · Cited by 145 · see citing works
Self-citationShaw, L., & Schauer, R. (1988) · Biological Chemistry Hoppe-Seyler · doi:10.1515/bchm3.1988.369.1.477 · Cited by 139 · see citing works
Lewis, A. L., Desa, N., Hansen, E. E., Knirel, Y. A., Gordon, J. I., Gagneux, P., Nizet, V., & Varki, A. P. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902431106 · Cited by 138 · see citing works
Self-citationCastilho, A., Gattinger, P., Grass, J., Jeż, J., Pabst, M., Altmann, F., Gorfer, M., Strasser, R., & Steinkellner, H. (2011) · Glycobiology · doi:10.1093/glycob/cwr009 · Cited by 135 · see citing works
Padler‐Karavani, V., Hurtado‐Ziola, N., Pu, M., Yu, H., Huang, S., Muthana, S. M., Chokhawala, H. A., Cao, H., Secrest, P., Friedmann‐Morvinski, D., et al. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-4102 · Cited by 133 · see citing works
Self-citationGenetic engineering of recombinant glycoproteins and glycosylation pathway in mammalian host cells
Grabenhorst, E., Schlenke, P., Pohl, S., Nimtz, M., & Conradt, H. S. (1999) · Glycoconjugate Journal · doi:10.1023/a:1026466408042 · Cited by 131 · see citing works
Merrick, J. M., Zadarlik, K., & Milgrom, F. (2009) · International Archives of Allergy and Applied Immunology · doi:10.1159/000232140 · Cited by 127 · see citing works
Characterization of Mouse Sialyltransferase Genes: Their Evolution and Diversity
Takashima, S. (2008) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.80025 · Cited by 125 · see citing works
Hamadeh, R. M., Jarvis, G. A., Galili, U., Mandrell, R. E., Zhou, P., & Griffiss, J. M. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115706 · Cited by 125 · see citing works
Insect cell technology is a versatile and robust vaccine manufacturing platform
Mena, J. A., & Kamen, A. (2011) · Expert Review of Vaccines · doi:10.1586/erv.11.24 · Cited by 122 · see citing works
Biosynthesis of N-Glycolyneuraminic Acid
Muchmore, E. A., Milewski, M., Varki, A. P., & Diaz, S. L. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47049-x · Cited by 118 · see citing works
Self-citationHara, S., Yamaguchi, M., Takemori, Y., Nakamura, M., & Ohkura, Y. (1986) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(00)80766-5 · Cited by 115 · see citing works
Varki, N. M., Strobert, E. A., Dick, E. J., Benirschke, K., & Varki, A. P. (2011) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-011110-130315 · Cited by 114 · see citing works
Self-citationYuen, C., Storring, P. L., Tiplady, R. J., Izquierdo, M., Wait, R., Gee, C. K., Gerson, P., Lloyd, P., & Cremata, J. A. (2003) · British Journal of Haematology · doi:10.1046/j.1365-2141.2003.04307.x · Cited by 106 · see citing works
Hokke, C. H., Bergwerff, A. A., van Dedem, G. W. K., van Oostrum, J., Kamerling, J. P., & Vliegenthart, J. F. G. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)81427-p · Cited by 101 · see citing works
Carbohydrate analysis throughout the development of a protein therapeutic
Higgins, E. A. (2009) · Glycoconjugate Journal · doi:10.1007/s10719-009-9261-x · Cited by 99 · see citing works
Xenotransplantation: the importance of the Galα1,3Gal epitope in hyperacute vascular rejection
Joziasse, D. H., & Oriol, R. (1999) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(99)00056-3 · Cited by 98 · see citing works
Über die Erzeugung heterospezifischer Hämagglutinine durch Injektion artfremden Serums
Deicher, H. (1926) · Medical Microbiology and Immunology · doi:10.1007/bf02176298 · Cited by 94 · see citing works
Success stories in molecular farming—a brief overview
Faye, L. J.-Y., & Gomord, V. (2010) · Plant Biotechnology Journal · doi:10.1111/j.1467-7652.2010.00521.x · Cited by 93 · see citing works
N-glycosylation Engineering of Biopharmaceutical Expression Systems
Jacobs, P. P., & Callewaert, N. (2009) · Current Molecular Medicine · doi:10.2174/156652409789105552 · Cited by 92 · see citing works
Evidence for efficient uptake and incorporation of sialic acid by eukaryotic cells
Oetke, C., Hinderlich, S., Brossmer, R., Reutter, W. G., Pawlita, M., & Keppler, O. T. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02379.x · Cited by 90 · see citing works
Ailor, E., Takahashi, N., Tsukamoto, Y., Masuda, K., Rahman, B. A., Jarvis, D. L., Lee, Y. C., & Betenbaugh, M. J. (2000) · Glycobiology · doi:10.1093/glycob/10.8.837 · Cited by 85 · see citing works
Borys, M., Dalal, N. G., Abu‐Absi, N. R., Khattak, S. F., Jing, Y., Xing, Z., & Li, Z. J. (2009) · Biotechnology and Bioengineering · doi:10.1002/bit.22644 · Cited by 83 · see citing works
The perspectives for porcine-to-human xenografts
Petersen, B., Carnwath, J. W., & Niemann, H. (2008) · Comparative Immunology Microbiology and Infectious Diseases · doi:10.1016/j.cimid.2007.11.014 · Cited by 82 · see citing works
Participation of Cytochrome b5 in CMP-N- Acetylneuraminic Acid Hydroxylation in Mouse Liver Cytosol1
Kozutsumi, Y., Kawano, T., Yamakawa, T., & Suzuki, A. (1990) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a123268 · Cited by 74 · see citing works
Hanganutziu-Deicher Antigen and Antibody in Pathologic Sera and Tissues
Nishimaki, T., Kano, K., & Milgrom, F. (1979) · The Journal of Immunology · doi:10.4049/jimmunol.122.6.2314 · Cited by 73 · see citing works
A Comprehensive Phylogenetic Analysis of Rieske and Rieske-Type Iron-Sulfur Proteins
Schmidt, C. L., & Shaw, L. (2001) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005616505962 · Cited by 71 · see citing works
Validation of immunoassays used to assess immunogenicity to therapeutic monoclonal antibodies
Geng, D., Shankar, G., Schantz, A., Rajadhyaksha, M., Davis, H. M., & Wagner, C. L. (2005) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2005.04.045 · Cited by 71 · see citing works
What's fueling the biotech engine—2009–2010
Aggarwal, S. (2010) · Nature Biotechnology · doi:10.1038/nbt1110-1165 · Cited by 70 · see citing works
Fu, D., & van HALBEEK, H. (1992) · Analytical Biochemistry · doi:10.1016/s0003-2697(05)80010-7 · Cited by 70 · see citing works
Production of Complex Multiantennary N-Glycans in Nicotiana benthamiana Plants
Nagels, B., Damme, E. J. M. V., Pabst, M., Callewaert, N., & Weterings, K. (2011) · PLANT PHYSIOLOGY · doi:10.1104/pp.110.168773 · Cited by 68 · see citing works
Glycan Engineering and Production of 'Humanized' Glycoprotein in Yeast Cells
Chiba, Y., & Akeboshi, H. (2009) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.32.786 · Cited by 67 · see citing works
Sonnenburg, J. L. (2003) · Glycobiology · doi:10.1093/glycob/cwh039 · Cited by 65 · see citing works
Kim, Y. K., Shin, H. S., Tomiya, N., Lee, Y. C., Betenbaugh, M. J., & Chi, H. J. (2005) · Biotechnology and Bioengineering · doi:10.1002/bit.20605 · Cited by 64 · see citing works
Evolution of Glycan DiversityPreprint
Varki, A. P., Freeze, H. H., & Gagneux, P. (2009) · Europe PMC (PubMed Central) · doi:10.1101/glycobiology.3e.020 · Cited by 62 · see citing works
Self-citationYoo, E. M., Chintalacharuvu, K. R., Penichet, M. L., & Morrison, S. L. (2002) · Journal of Immunological Methods · doi:10.1016/s0022-1759(01)00559-2 · Cited by 61 · see citing works
Chenu, S., Grégoire, A., Malykh, Y. N., Visvikis, A., Monaco, L., Shaw, L., Schauer, R., Marc, A., & Goergen, J. (2003) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(03)00137-5 · Cited by 45 · see citing works
Zhang, J., & Kesteloot, H. (2005) · Nutrition and Cancer · doi:10.1207/s15327914nc5301_8 · Cited by 43 · see citing works
Tahara, H., Ide, K., Basnet, N. B., Tanaka, Y., Matsuda, H., Takematsu, H., Kozutsumi, Y., & Ohdan, H. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0902857 · Cited by 41 · see citing works
The influence of natural antibody specificity on antigen immunogenicity
Benatuil, L., Kaye, J., Rich, R. F., Fishman, J. A., Green, W. R., & Iacomini, J. (2005) · European Journal of Immunology · doi:10.1002/eji.200526146 · Cited by 41 · see citing works
Malykh, Y. N., Shaw, L., & Schauer, R. (1998) · Glycoconjugate Journal · doi:10.1023/a:1006959016011 · Cited by 41 · see citing works
Hanganutziu-Deicher antibodies in infectious mononucleosis and other diseases.
Morito, T., Kano, K., & Milgrom, F. (1982) · The Journal of Immunology · doi:10.4049/jimmunol.129.6.2524 · Cited by 40 · see citing works
(2013) · Glycoconjugate Journal · doi:10.1007/10719.1573-4986 · Cited by 33 · see citing works
Jiang, Y., Li, F., Zha, D., Potgieter, T. I., Mitchell, T., Moore, R., Cukan, M. C., Houston-Cummings, N. R., Nylen, A., Drummond, J. E., et al. (2010) · Protein Expression and Purification · doi:10.1016/j.pep.2010.11.004 · Cited by 28 · see citing works
Survey of Hanganutziu and Deicher Antibodies in Operated Patients
HIGASHIHARA, T., Takeshima, T., Anzai, M., Tomioka, M., Matsumoto, K., Nishida, K., Kitamura, Y., Okinaga, K., & Naiki, M. (2009) · International Archives of Allergy and Applied Immunology · doi:10.1159/000235434 · Cited by 25 · see citing works
Kim, Y. K., Kim, K. R., Kang, D. G., Jang, S. Y., Kim, Y. H., & Chi, H. J. (2011) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2011.03.021 · Cited by 24 · see citing works
Immunological studies on Kawasaki disease. I. Appearance of Hanganutziu-Deicher antibodies.
Takiguchi, M., Tamura, T., Goto, M., Kusakawa, S., Milgrom, F., & Kano, K. (1984) · PubMed Central · Cited by 22 · see citing works
Genetically Modified Animals and Pharmacological Research
Wells, D. J. (2010) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-10324-7_9 · Cited by 22 · see citing works
Panitumumab: A Fully Human Monoclonal Antibody with Activity in Metastatic Colorectal Cancer
Saadeh, C. E., & Lee, H. S. (2007) · Annals of Pharmacotherapy · doi:10.1345/aph.1h492 · Cited by 20 · see citing works
Studies on Hanganutziu-Deicher Antigens-Antibodies
MORITO, T., Nishimaki, T., Masaki, M., Yoshida, H., Kasukawa, R., Nakarai, H., & Kano, K. (2009) · International Archives of Allergy and Applied Immunology · doi:10.1159/000234135 · Cited by 19 · see citing works
Heterophile Hanganutziu-Deicher Antigen in Ganglioside Fractions of Human Melanoma Tissues
Kawachi, S., Saida, T., Uhara, H., Uemura, K., Taketomi, T., & Kano, K. (2009) · International Archives of Allergy and Applied Immunology · doi:10.1159/000234536 · Cited by 18 · see citing works
Hillar, A., & Jarvis, D. L. (2010) · Glycobiology · doi:10.1093/glycob/cwq099 · Cited by 12 · see citing works
Manufacturing of Biopharmaceuticals and Implications for Biosimilars
Wurm, F. M. (2007) · Kidney & Blood Pressure Research · doi:10.1159/000107094 · Cited by 5 · see citing works
Human Embryonic Stem Cells Contaminated
Hampton, T. (2005) · JAMA · doi:10.1001/jama.293.7.789 · Cited by 1 · see citing works
Hemispheric difference in human skin color
Chaplin, G., & Jablonski, N. G. (1998) · American Journal of Physical Anthropology · doi:10.1002/(sici)1096-8644(199810)107:2
Self-citation
Flagged first, then by citations
Research works printed but not linked: 2
- MALYKH, YN, SCHAUER, R,SHAW, L (2001), 'N-Glycolylneuraminic Acid in Human Tumours.', Biochimie, 83 (7), 623-34.
- STANLEY, P, H SCHACHTER,N TANIGUCHI (2009), 'N-Glycans', in VARKI, A, RD CUMMINGS, JD ESKO, HH FREEZE, P STANLEY, CR BERTOZZI, GW HART,ME ETZLER (eds.), Essentials of Glycobiology (2nd edn., Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press), 101-14.
Cited by
Sorted by citations
Human cell lines for biopharmaceutical manufacturing: history, status, and future perspectives
Dumont, J., Euwart, D., Mei, B., Estes, S., & Kshirsagar, R. (2016) · Critical Reviews in Biotechnology · doi:10.3109/07388551.2015.1084266 · Cited by 483 · see citing works
Chemically modified and conjugated antimicrobial peptides against superbugs
Li, W., Separovic, F., O’brien-simpson, N. M., & Wade, J. D. (2021) · Chemical Society Reviews · doi:10.1039/d0cs01026j · Cited by 440 · see citing works
Liu, L. (2015) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.24444 · Cited by 428 · see citing works
Emerging principles for the therapeutic exploitation of glycosylation
Dalziel, M., Crispin, M., Scanlan, C. N., Zitzmann, N., & Dwek, R. A. (2014) · Science · doi:10.1126/science.1235681 · Cited by 447 · see citing works
The art of CHO cell engineering: A comprehensive retrospect and future perspectives
Fischer, S., Handrick, R., & Otte, K. (2015) · Biotechnology Advances · doi:10.1016/j.biotechadv.2015.10.015 · Cited by 314 · see citing works
Therapeutic glycoprotein production in mammalian cells
Lalonde, M.-E., & Durocher, Y. (2017) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2017.04.028 · Cited by 296 · see citing works
Advances in Mammalian cell line development technologies for recombinant protein production
Lai, T., Yang, Y., & Ng, S. (2013) · Pharmaceuticals · doi:10.3390/ph6050579 · Cited by 322 · see citing works
Fc-fusion proteins and FcRn: structural insights for longer-lasting and more effective therapeutics
Räth, T., Baker, K., Dumont, J. A., Peters, R., Jiang, H., Qiao, S., Lencer, W. I., Pierce, G. F., & Blumberg, R. S. (2013) · Critical Reviews in Biotechnology · doi:10.3109/07388551.2013.834293 · Cited by 282 · see citing works
Design and Production of Bispecific Antibodies
Wang, Q., Chen, Y., Park, J., Liu, X., Hu, Y., Wang, T., McFarland, K. S., & Betenbaugh, M. J. (2019) · Antibodies · doi:10.3390/antib8030043 · Cited by 280 · see citing works
Impact of host cell line choice on glycan profile
Goh, J. B., & Ng, S. K. (2017) · Critical Reviews in Biotechnology · doi:10.1080/07388551.2017.1416577 · Cited by 226 · see citing works
Overview of the Purification of Recombinant Proteins
Wingfield, P. T. (2015) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps0601s80 · Cited by 220 · see citing works
Therapeutic recombinant protein production in plants: Challenges and opportunities
Burnett, M., & Burnett, A. C. (2019) · Plants People Planet · doi:10.1002/ppp3.10073 · Cited by 222 · see citing works
Zhang, P., Woen, S., Wang, T., Liau, B., Zhao, S., Chen, C., Yang, Y., Song, Z., Wormald, M. R., Yu, C., et al. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.01.006 · Cited by 212 · see citing works
Glycan analysis of therapeutic glycoproteins
Zhang, L., Luo, S., & Zhang, B. (2016) · mAbs · doi:10.1080/19420862.2015.1117719 · Cited by 207 · see citing works
Involvement of a Non-Human Sialic Acid in Human Cancer
Samraj, A. N., Läubli, H., Varki, N., & Varki, A. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00033 · Cited by 196 · see citing works
Self-citationExploiting metabolic glycoengineering to advance healthcare
Agatemor, C., Buettner, M. J., Ariss, R., Muthiah, K., Saeui, C. T., & Yarema, K. J. (2019) · Nature Reviews Chemistry · doi:10.1038/s41570-019-0126-y · Cited by 185 · see citing works
The choice of mammalian cell host and possibilities for glycosylation engineering
Butler, M., & Spearman, M. (2014) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2014.06.010 · Cited by 175 · see citing works
In vitro and in vivo modifications of recombinant and human IgG antibodies
Liu, H., Ponniah, G., Zhang, H., Nowak, C., Neill, A., Gonzalez, N., Patel, R., Cheng, G. C., Kita, A., & Andrien, B. A. (2014) · mAbs · doi:10.4161/mabs.29883 · Cited by 169 · see citing works
Kolter, T. (2012) · ISRN Biochemistry · doi:10.5402/2012/506160 · Cited by 167 · see citing works
Rumachik, N. G., Malaker, S. A., Poweleit, N., Maynard, L. H., Adams, C. M., Leib, R. D., Cirolia, G., Thomas, D. R., Stamnes, S. J., Holt, K. H., et al. (2020) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2020.05.018 · Cited by 155 · see citing works
Therapeutic Fc‐fusion proteins: Current analytical strategies
Duivelshof, B. L., Murisier, A., Camperi, J., Fekete, S., Beck, A., Guillarme, D., & D’Atri, V. (2020) · Journal of Separation Science · doi:10.1002/jssc.202000765 · Cited by 153 · see citing works
Integrating plant molecular farming and materials research for next-generation vaccines
Chung, Y. H., Church, D. C., Koellhoffer, E. C., Osota, E. O., Shukla, S., Rybicki, E. P., Pokorski, J. K., & Steinmetz, N. F. (2021) · Nature Reviews Materials · doi:10.1038/s41578-021-00399-5 · Cited by 149 · see citing works
Dhar, C., Sasmal, A., & Varki, A. P. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00807 · Cited by 122 · see citing works
Self-citationGlycans in immune recognition and response
Amon, R., Reuven, E. M., Ben‐Arye, S. L., & Padler‐Karavani, V. (2014) · Carbohydrate Research · doi:10.1016/j.carres.2014.02.004 · Cited by 115 · see citing works
Kaur, H. (2021) · Critical Reviews in Biotechnology · doi:10.1080/07388551.2020.1869684 · Cited by 100 · see citing works
Engineering of Sialylated Mucin-type O-Glycosylation in Plants
Castilho, A., Neumann, L., Daskalova, S. M., Mason, H. S., Steinkellner, H., Altmann, F., & Strasser, R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.402685 · Cited by 96 · see citing works
Glycosylation control technologies for recombinant therapeutic proteins
Gupta, S. K., & Shukla, P. (2018) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-018-9430-6 · Cited by 94 · see citing works
Kastberg, L. L. B., Ard, R., Jensen, M. K., & Workman, C. T. (2022) · Frontiers in Fungal Biology · doi:10.3389/ffunb.2022.827704 · Cited by 92 · see citing works
The use of lectin microarray for assessing glycosylation of therapeutic proteins
Zhang, L., Luo, S., & Zhang, B. (2016) · mAbs · doi:10.1080/19420862.2016.1149662 · Cited by 90 · see citing works
Molecular farming on rescue of pharma industry for next generations
Moustafa, K., Makhzoum, A. B., & Trémouillaux‐Guiller, J. (2015) · Critical Reviews in Biotechnology · doi:10.3109/07388551.2015.1049934 · Cited by 88 · see citing works
Using glyco-engineering to produce therapeutic proteins
Dicker, M., & Strasser, R. (2015) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2015.1069271 · Cited by 73 · see citing works
Synthetic Glycobiology: Parts, Systems, and Applications
Kightlinger, W., Warfel, K. F., DeLisa, M. P., & Jewett, M. C. (2020) · ACS Synthetic Biology · doi:10.1021/acssynbio.0c00210 · Cited by 80 · see citing works
Padler‐Karavani, V. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.10.005 · Cited by 79 · see citing works
Biopharmaceutical Manufacturing: Historical Perspectives and Future Directions
Szkodny, A. C., & Lee, K. H. (2022) · Annual Review of Chemical and Biomolecular Engineering · doi:10.1146/annurev-chembioeng-092220-125832 · Cited by 83 · see citing works
Ling, A. J. W., Chang, L. S., Babji, A. S., Latip, J., Koketsu, M., & Lim, S. J. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.130755 · Cited by 78 · see citing works
Applications and analysis of hydrolysates in animal cell culture
Ho, Y. Y., Lu, H., Lim, Z. F. S., Lim, H. W., Ho, Y. S., & Ng, S. K. (2021) · Bioresources and Bioprocessing · doi:10.1186/s40643-021-00443-w · Cited by 77 · see citing works
Synthesis of N-Glycolylneuraminic Acid (Neu5Gc) and Its Glycosides
Kooner, A. S., Yu, H., & Chen, X. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02004 · Cited by 73 · see citing works
Glycosylated Biotherapeutics: Immunological Effects of N-Glycolylneuraminic Acid
Yehuda, S., & Padler-Karavani, V. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00021 · Cited by 71 · see citing works
Glycoengineering in CHO cells: advances in systems biology
Tejwani, V., Andersen, M. R., Nam, J. H., & Sharfstein, S. T. (2018) · Biotechnology Journal · doi:10.1002/biot.201700234 · Cited by 70 · see citing works
Cell-Free Synthesis Meets Antibody Production: A Review
Stech, M., Kubick, S., & Ohtake, S. (2015) · Antibodies · doi:10.3390/antib4010012 · Cited by 60 · see citing works
Röhrig, C. H., Choi, S. S. H., & Baldwin, N. J. (2015) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2015.1040113 · Cited by 70 · see citing works
Perspectives for Glyco-Engineering of Recombinant Biopharmaceuticals from Microalgae
Barolo, L., Abbriano, R. M., Commault, A. S., George, J., Kahlke, T., Fabris, M., Padula, M. P., Lopez, A., Ralph, P. J., & Pernice, M. (2020) · Cells · doi:10.3390/cells9030633 · Cited by 65 · see citing works
Vainauskas, S., Guntz, H., McLeod, E., McClung, C. M., Ruse, C. I., Shi, X., & Taron, C. H. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c04055 · Cited by 67 · see citing works
Improving Immunotherapy Through Glycodesign
Buettner, M. J., Shah, S. R., Saeui, C. T., Ariss, R., & Yarema, K. J. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02485 · Cited by 66 · see citing works
Strategies for Glycoengineering Therapeutic Proteins
Dammen-Brower, K., Epler, P., Zhu, S., Bernstein, Z. J., Stabach, P., Braddock, D., Spangler, J. B., & Yarema, K. (2022) · Frontiers in Chemistry · doi:10.3389/fchem.2022.863118 · Cited by 54 · see citing works
The CAG promoter maintains high‐level transgene expression in HEK293 cells
Dou, Y.-Y., Lin, Y., Wang, T., Wang, X., Jia, Y., & Zhao, C. (2020) · FEBS Open Bio · doi:10.1002/2211-5463.13029 · Cited by 63 · see citing works
Therapeutic proteins: developments, progress, challenges, and future perspectives
Kumar, V., Barwal, A., Sharma, N., Mir, D. S., Kumar, P., & Kumar, V. (2024) · 3 Biotech · doi:10.1007/s13205-024-03958-z · Cited by 62 · see citing works
Therapeutic peptides: chemical strategies fortify peptides for enhanced disease treatment efficacy
Li, Q., Chao, W., & Qiu, L. (2025) · Amino Acids · doi:10.1007/s00726-025-03454-5 · Cited by 60 · see citing works
Serum-Free Medium for Recombinant Protein Expression in Chinese Hamster Ovary Cells
Li, W., Fan, Z., Lin, Y., & Wang, T. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.646363 · Cited by 58 · see citing works
Khan, T., Islam, R., Jerin, T. J., Mahmud, A., Khatun, S., Kobir, A., Islam, M. N., Akter, A., & Mondal, S. I. (2021) · PLoS ONE · doi:10.1371/journal.pone.0253393 · Cited by 57 · see citing works
N-Glycosylation of Extracellular Vesicles from HEK-293 and Glioma Cell Lines
Costa, J., Gatermann, M., Nimtz, M., Kandzia, S., Glatzel, M., & Conradt, H. S. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.7b05455 · Cited by 56 · see citing works
Cuccui, J., & Wren, B. W. (2014) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.12321 · Cited by 55 · see citing works
Product Quality Considerations for Mammalian Cell Culture Process Development and Manufacturing
Gramer, M. J. (2013) · Advances in biochemical engineering, biotechnology · doi:10.1007/10_2013_214 · Cited by 54 · see citing works
The present state of the art in expression, production and characterization of monoclonal antibodies
Gaughan, C. L. (2015) · Molecular Diversity · doi:10.1007/s11030-015-9625-z · Cited by 53 · see citing works
Song, T., Ozcan, S., Becker, A., & Lebrilla, C. (2014) · Analytical Chemistry · doi:10.1021/ac501102t · Cited by 46 · see citing works
Human cell lines for the production of recombinant proteins: on the horizon
Fliedl, L., Grillari, J., & Grillari‐Voglauer, R. (2014) · New Biotechnology · doi:10.1016/j.nbt.2014.11.005 · Cited by 50 · see citing works
Manufacturing process used to produce long-acting recombinant factor VIII Fc fusion protein
McCue, J. T., Kshirsagar, R., Selvitelli, K., Lü, Q., Zhang, M., Mei, B., Peters, R., Pierce, G. F., Dumont, J., Raso, S. W., et al. (2015) · Biologicals · doi:10.1016/j.biologicals.2015.05.012 · Cited by 48 · see citing works
Self-citationLuo, S., & Zhang, B. (2023) · Pharmaceutical Research · doi:10.1007/s11095-023-03628-4 · Cited by 46 · see citing works
Characterization of anti-CD20 monoclonal antibody produced by transgenic silkworms (Bombyx mori)
Tada, M., Tatematsu, K., Ishii‐Watabe, A., Harazono, A., Takakura, D., Hashii, N., Sezutsu, H., & Kawasaki, N. (2015) · mAbs · doi:10.1080/19420862.2015.1078054 · Cited by 46 · see citing works
Blondeel, E. J. M., & Aucoin, M. G. (2018) · Biotechnology Advances · doi:10.1016/j.biotechadv.2018.06.008 · Cited by 46 · see citing works
Evolution of sialic acids: Implications in xenotransplant biology
Paul, A., & Padler‐Karavani, V. (2018) · Xenotransplantation · doi:10.1111/xen.12424 · Cited by 45 · see citing works
Zhao, C., Guo, X. H., Chen, S.-J., Li, C., Yang, Y., Zhang, J., Chen, S.-N., Jia, Y., & Wang, T. (2017) · Scientific Reports · doi:10.1038/srep42805 · Cited by 44 · see citing works
Varki, A. P. (2017) · Journal of Autoimmunity · doi:10.1016/j.jaut.2017.07.011 · Cited by 43 · see citing works
Self-citationFermentanomics informed amino acid supplementation of an antibody producing mammalian cell culture
Read, E. K., Bradley, S. A., Smitka, T. A., Agarabi, C. D., Lute, S. C., & Brorson, K. (2013) · Biotechnology Progress · doi:10.1002/btpr.1728 · Cited by 42 · see citing works
Lin, P.-C., Chan, K. F., Kieß, I. A., Tan, J. L., Shahreel, W., Wong, S.-Y., & Song, Z. (2019) · mAbs · doi:10.1080/19420862.2019.1612690 · Cited by 42 · see citing works
Glycosylation of Therapeutic Proteins: A Critical Quality Attribute
Delobel, A. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1241-5_1 · Cited by 42 · see citing works
Patrucco, L., Chiesa, A. D., Soluri, M. F., Fasolo, F., Takahashi, H., Carninci, P., Zucchelli, S., Santoro, C., Gustincich, S., Sblattero, D., et al. (2015) · Gene · doi:10.1016/j.gene.2015.05.070 · Cited by 42 · see citing works
Generation of cattle knockout for galactose‐α1,3‐galactose and N‐glycolylneuraminic acid antigens
Perota, A., Lagutina, I., Duchi, R., Zanfrini, E., Lazzari, G., Judor, J., Conchon, S., Bach, J., Bottio, T., Gerosa, G., et al. (2019) · Xenotransplantation · doi:10.1111/xen.12524 · Cited by 41 · see citing works
Oldenburg, J., Lacroix‐Desmazes, S., & Lillicrap, D. (2015) · Haematologica · doi:10.3324/haematol.2014.112821 · Cited by 40 · see citing works
Glycoengineering of CHO Cells to Improve Product Quality
Wang, Q., Yin, B., Chung, C., & Betenbaugh, M. J. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6972-2_2 · Cited by 40 · see citing works
An Effective Bacterial Fucosidase for Glycoprotein Remodeling
Tsai, T.-I., Li, S., Liu, C.-P., Chen, K. Y., Shivatare, S. S., Lin, C., Liao, S.-F., Lin, C.-W., Hsu, T.-L., Wu, Y., et al. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00821 · Cited by 38 · see citing works
Production of recombinant coagulation factors: Are humans the best host cells?
Swiech, K., Picanço‐Castro, V., & Covas, D. T. (2017) · Bioengineered · doi:10.1080/21655979.2017.1279767 · Cited by 38 · see citing works
Glycoengineering Chinese hamster ovary cells: a short history
Donini, R., Haslam, S. M., & Kontoravdi, C. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200840 · Cited by 37 · see citing works
Ni, W., Bones, J., & Karger, B. L. (2013) · Analytical Chemistry · doi:10.1021/ac3031898 · Cited by 36 · see citing works
Shapiro, A. D. (2013) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2013.819339 · Cited by 36 · see citing works
Müller-Kräuter, H., Fehling, S. K., Dorna, J., Urbanowicz, R. A., Oestereich, L., Krebs, Y., Kolesnikova, L., Schauflinger, M., Krähling, V., Magassouba, N., et al. (2020) · npj Vaccines · doi:10.1038/s41541-020-00219-x · Cited by 36 · see citing works
Furukawa, J., Tsuda, M., Okada, K., Kimura, T., Piao, J., Tanaka, S., & Shinohara, Y. (2015) · PLoS ONE · doi:10.1371/journal.pone.0128300 · Cited by 36 · see citing works
Liu, J., Wang, J., Li, F., Chen, X., Hu, D., Deng, X., Poon, H. F., Wang, H., Liu, X., & Tan, W. (2015) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-015-1864-8 · Cited by 36 · see citing works
Radoman, B., Grünwald‐Gruber, C., Schmelzer, B., Zavec, D., Gasser, B., Altmann, F., & Mattanovich, D. (2020) · Biotechnology Journal · doi:10.1002/biot.202000266 · Cited by 35 · see citing works
Fernández‐Tejada, A., Vadola, P. A., & Danishefsky, S. J. (2014) · Journal of the American Chemical Society · doi:10.1021/ja503545r · Cited by 35 · see citing works
Dong, Q., Yan, X., Liang, Y., & Stein, S. E. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b01046 · Cited by 34 · see citing works
Cell Surface and Membrane Engineering: Emerging Technologies and Applications
Saeui, C. T., Mathew, M. P., Liu, L., Urias, E., & Yarema, K. J. (2015) · Journal of Functional Biomaterials · doi:10.3390/jfb6020454 · Cited by 32 · see citing works
Synthesis of the Antimicrobial S‐Linked Glycopeptide, Glycocin F
Brimble, M. A., Edwards, P. J. B., Harris, P. W. R., Norris, G. E., Patchett, M. L., Wright, T. H., Yang, S., & Carley, S. E. (2015) · Chemistry - A European Journal · doi:10.1002/chem.201405692 · Cited by 33 · see citing works
Stutz, H. (2022) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2022.115089 · Cited by 33 · see citing works
Improving recombinant protein production in CHO cells using the CRISPR-Cas system
Kalkan, A. K., Palaz, F., Semeniuk, S., Elmousa, N., Ledezma, Y., Cachat, É., & Rios‐Solis, L. (2023) · Biotechnology Advances · doi:10.1016/j.biotechadv.2023.108115 · Cited by 32 · see citing works
McCue, J. T., Osborne, D., Dumont, J., Peters, R., Mei, B., Pierce, G. F., Kobayashi, K., & Euwart, D. (2014) · Haemophilia · doi:10.1111/hae.12451 · Cited by 32 · see citing works
Orthogonal Technologies for NISTmAb N-Glycan Structure Elucidation and Quantitation
Prien, J. M., Stöckmann, H., Albrecht, S., Millán‐Martín, S., Varatta, M., Furtado, M., Hosselet, S., Wang, M., Formolo, T., Rudd, P. M., et al. (2015) · ACS symposium series · doi:10.1021/bk-2015-1201.ch004 · Cited by 32 · see citing works
Study of structure‐dependent chromatographic behavior of glycopeptides using reversed phase nanoLC
Kozlík, P., Goldman, R., & Šanda, M. (2017) · Electrophoresis · doi:10.1002/elps.201600547 · Cited by 32 · see citing works
Glycoengineering of Mammalian Expression Systems on a Cellular Level
Heffner, K. M., Wang, Q., Hızal, D. B., Can, Ö., & Betenbaugh, M. J. (2018) · Advances in biochemical engineering, biotechnology · doi:10.1007/10_2017_57 · Cited by 34 · see citing works
Binz, R. L., Tian, E., Sadhukhan, R., Zhou, D., Hauer‐Jensen, M., & Pathak, R. (2019) · Scientific Reports · doi:10.1038/s41598-019-47002-0 · Cited by 32 · see citing works
Gibbons, L. A., Rafferty, C., Robinson, K., Abad, M. C., Maslanka, F., Le, N., Mo, J., Clark, K., Madden, F., Hayes, R., et al. (2021) · Biotechnology Progress · doi:10.1002/btpr.3223 · Cited by 32 · see citing works
Sialic acids in infection and their potential use in detection and protection against pathogens
Dedola, S., Ahmadipour, S., de Andrade, P., Baker, A. N., Boshra, A. N., Chessa, S., Gibson, M. I., Hernando, P. J., Ivanova, I. M., Lloyd, J., et al. (2023) · RSC Chemical Biology · doi:10.1039/d3cb00155e · Cited by 31 · see citing works
Wei, M., Mi, C., Jing, C., & Wang, T. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.879222 · Cited by 31 · see citing works
Compte, M., Álvarez‐Cienfuegos, A., Nuñez‐Prado, N., Sainz-Pastor, N., Blanco‐Toribio, A., Pescador, N., Sanz, L., & Álvarez‐Vallina, L. (2014) · OncoImmunology · doi:10.4161/onci.28810 · Cited by 31 · see citing works
Blondeel, E. J. M., Braasch, K., McGill, T., Chang, D., Engel, C., Spearman, M. A., Butler, M., & Aucoin, M. G. (2015) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2015.09.014 · Cited by 29 · see citing works
Serum-free suspension culturing of human cells: adaptation, growth, and cryopreservation
Biaggio, R. T., Abreu-Neto, M. S., Covas, D. T., & Swiech, K. (2015) · Bioprocess and Biosystems Engineering · doi:10.1007/s00449-015-1392-9 · Cited by 29 · see citing works
Engineering of human-type O-glycosylation in Nicotiana benthamiana plants
Strasser, R. (2012) · Bioengineered · doi:10.4161/bioe.22857 · Cited by 28 · see citing works
Бекхановна, Б. З., Анатольевна, В. Л., Fetisova, Y., Александровна, М. Н., Ovchinnikova, M. M., Tischenko, M., Scherbatyuk, Y., Kolotovkina, A., Miskun, A. A., Kasyanova, G. V., et al. (2019) · European Journal of Obstetrics & Gynecology and Reproductive Biology · doi:10.1016/j.ejogrb.2019.07.032 · Cited by 29 · see citing works
Koenitzer, J. D., Müller, M. M., Leparc, G., Pauers, M., Bechmann, J., Schulz, P., Schaub, J., Enenkel, B., Hildebrandt, T., Hampel, M., et al. (2015) · Biotechnology Journal · doi:10.1002/biot.201400652 · Cited by 28 · see citing works
Stable Protein Sialylation in Physcomitrella
Bohlender, L. L., Parsons, J., Hoernstein, S. N. W., Rempfer, C., Ruiz-Molina, N., Lorenz, T., Rodríguez-Jahnke, F., Figl, R., Fode, B., Altmann, F., et al. (2020) · Frontiers in Plant Science · doi:10.3389/fpls.2020.610032 · Cited by 28 · see citing works
- Authors
- Ghaderi, D., Zhang, M., Hurtado-Ziola, N., & Varki, A.
- Affiliations
- University of California San Diego (US)
- Corresponding author
- Varki, Ajit
- Venue
- Biotechnology and Genetic Engineering Reviews
- Publisher
- Informa UK Limited
- Published
- 2012-01
- Volume
- 28
- Issue
- 1
- Pages
- 147-176
- ISSN
- 0264-8725 (ISSN-L)
- 2046-5556
- OpenAlex
- W1997984454
- Cited by
- 320
- References
- 128
- Citations by year
- 2026: 9 · 2025: 11 · 2024: 15 · 2023: 13 · 2022: 22 · 2021: 29 · 2020: 29 · 2019: 30 · 2018: 25 · 2017: 30 · 2016: 24 · 2015: 36 · 2014: 23 · 2013: 21 · 2012: 3
- FWCI
- 10.68
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biotechnology and Genetic Engineering Reviews (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Transgenic Plants and Applications
- Keywords
- N-glycolylneuraminic acid, alpha-gal epitope, therapeutic glycoproteins, biologic therapy, N-glycosylation, immunogenicity, sialic acid, monoclonal antibodies
- MeSH terms
- Animals, Antibodies, Monoclonal, Epitopes, Biotechnology, Carbohydrate Sequence, Cattle, Cells, Cultured, Culture Media, Disaccharides, Glycoproteins, Glycosylation, Cricetinae, Humans, Insecta, Rabbits, Recombinant Proteins, Sialic Acids, Swine, Cell Culture Techniques, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
