Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity

Tight control of gene expression in mammalian cells by tetracycline-responsive promoters.

Gossen, M., & Bujard, H. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.12.5547 · Cited by 4,943 · cited 1×

Depletion of B cells in vivo by a chimeric mouse human monoclonal antibody to CD20

Reff, M., Carner, K., Chambers, K., Chinn, P., Leonard, J., Raab, R., Newman, R., Hanna, N., & Anderson, D. (1994) · Blood · doi:10.1182/blood.v83.2.435.435 · Cited by 1,996

Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides

Schachter, H. (1986) · Biochemistry and Cell Biology · doi:10.1139/o86-026 · Cited by 526

Biosynthetic Controls That Determine the Branching and Microheterogeneity of Protein-Bound Oligosaccharides

Schachter, H. (1986) · Advances in experimental medicine and biology · doi:10.1007/978-1-4684-5209-9_2 · Cited by 510

Sequencing of N-Linked Oligosaccharides Directly from Protein Gels: In-Gel Deglycosylation Followed by Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry and Normal-Phase High-Performance Liquid Chromatography

Küster, B., Wheeler, S. F., Hunter, A. P., Dwek, R. A., & Harvey, D. J. (1997) · Analytical Biochemistry · doi:10.1006/abio.1997.2199 · Cited by 358

Effect of glycosylation on antibody function: implications for genetic engineering

Wright, A. M., & Morrison, S. L. (1997) · Trends in biotechnology · doi:10.1016/s0167-7799(96)10062-7 · Cited by 317

Quantitative aspects of the matrix‐assisted laser desorption mass spectrometry of complex oligosaccharides

Harvey, D. J. (1993) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.1290070712 · Cited by 265

In Pursuit of the Optimal Fed‐Batch Process for Monoclonal Antibody Production

Bibila, T. A., & Robinson, D. K. (1995) · Biotechnology Progress · doi:10.1021/bp00031a001 · Cited by 251

Overlapping distribution of two glycosyltransferases in the Golgi apparatus of HeLa cells.

Nilsson, T., Pypaert, M., Hoe, M. H., Slusarewicz, P., Berger, E. G., & Warren, W. G. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.120.1.5 · Cited by 222

Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human Fc γ receptor I and influence the synthesis of its oligosaccharide chains

Lund, J., Takahashi, N., Pound, J. D., Goodall, M. D., & Jefferis, R. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.157.11.4963 · Cited by 216

Targeted killing of colorectal cancer cell lines by a humanised IgG1 monoclonal antibody that binds to membrane-bound carcinoembryonic antigen

Conaghan, P. J., Ashraf, S. Q., Tytherleigh, M. G., Wilding, J. L., Tchilian, E. Z., Bicknell, D. C., Mortensen, N., & Bodmer, W. F. (2008) · British Journal of Cancer · doi:10.1038/sj.bjc.6604289 · Cited by 30

N-Glycosylation of Serum IgG and Total Glycoproteins in MAN1B1 Deficiency

Saldova, R., Stöckmann, H., O’Flaherty, R., Lefeber, D. J., Jaeken, J., & Rudd, P. M. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00709 · Cited by 30

IgG Fc variant cross-reactivity between human and rhesus macaque FcγRs

Boesch, A. W., Miles, A., Chan, Y. N., Osei‐Owusu, N. Y., & Ackerman, M. E. (2017) · mAbs · doi:10.1080/19420862.2016.1274845 · Cited by 33

Development of a pre-glycoengineered CHO-K1 host cell line for the expression of antibodies with enhanced Fc mediated effector function

Popp, O., Moser, S., Zielonka, J., Rüger, P., Hansen, S., & Plöttner, O. (2017) · mAbs · doi:10.1080/19420862.2017.1405203 · Cited by 30

A CD19-specific single-chain immunotoxin mediates potent apoptosis of B-lineage leukemic cells

Schwemmlein, M., Stieglmaier, J., Kellner, C., Peipp, M., Saul, D., Oduncu, F. S., Emmerich, B., Stockmeyer, B., Lang, P., Beck, J. D., et al. (2007) · Leukemia · doi:10.1038/sj.leu.2404687 · Cited by 29

Application of partial‐filling capillary electrophoresis using lectins and glycosidases for the characterization of oligosaccharides in a therapeutic antibody

Yagi, Y., Yamamoto, S., Kakehi, K., Hayakawa, T., Ohyama, Y., & Suzuki, S. (2011) · Electrophoresis · doi:10.1002/elps.201100126 · Cited by 29

Therapeutic antibodies — Delivering the promise?

Hale, G. (2006) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2006.03.010 · Cited by 29

Recombinant antibodies for cancer therapy

Deonarain, M. P. (2008) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.8.8.1123 · Cited by 29

Interferon-α alters host glycosylation machinery during treated HIV infection

Giron, L. B., Colomb, F., Papasavvas, E., Azzoni, L., Yin, X., Fair, M. G., Anzurez, A., Damra, M., Mounzer, K., Kostman, J. R., et al. (2020) · EBioMedicine · doi:10.1016/j.ebiom.2020.102945 · Cited by 29

Humanised IgG1 antibody variants targeting membrane-bound carcinoembryonic antigen by antibody-dependent cellular cytotoxicity and phagocytosis

Ashraf, S. Q., Umaña, P., Mössner, E., Ntouroupi, T. G., Brünker, P., Schmidt, C., Wilding, J. L., Mortensen, N. J. M. C., & Bodmer, W. F. (2009) · British Journal of Cancer · doi:10.1038/sj.bjc.6605355 · Cited by 28

Influence of Variable N-Glycosylation on the Cytolytic Potential of Chimeric CD19 Antibodies

Barbin, K., Stieglmaier, J., Saul, D., Stieglmaier, K., Stockmeyer, B., Pfeiffer, M. M., Lang, P., & Fey, G. H. (2006) · Journal of Immunotherapy · doi:10.1097/01.cji.0000175684.28615.7b · Cited by 28

Overexpression of YY1 increases the protein production in mammalian cells

Tastanova, A., Schulz, A., Folcher, M., Tolstrup, A. B., Puklowski, A., Kaufmann, H., & Fussenegger, M. (2015) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2015.12.005 · Cited by 28

Protein N-Glycosylation in Cardiovascular Diseases and Related Risk Factors

Gudelj, I., & Lauc, G. (2018) · Current Cardiovascular Risk Reports · doi:10.1007/s12170-018-0579-4 · Cited by 28

Heterologous protein production capacity of mammalian cells cultivated as monolayers and microtissues

Sánchez-Bustamante, C. D., Kelm, J. M., Guarino, B., & Fussenegger, M. (2005) · Biotechnology and Bioengineering · doi:10.1002/bit.20679 · Cited by 28

Modulation of IgG1 immunoeffector function by glycoengineering of the GDP‐fucose biosynthesis pathway

Kelly, R. M., Kowle, R. L., Lian, Z., Strifler, B. A., Witcher, D. R., Parekh, B. S., Wang, T., & Frye, C. C. (2017) · Biotechnology and Bioengineering · doi:10.1002/bit.26496 · Cited by 29

An Engineered Human Fc variant With Exquisite Selectivity for FcγRIIIaV158 Reveals That Ligation of FcγRIIIa Mediates Potent Antibody Dependent Cellular Phagocytosis With GM-CSF-Differentiated Macrophages

Kang, T. H., Lee, C., Delidakis, G., Jung, J., Goff, O. R.-L., Lee, J., Kim, J. E., Charab, W., Bruhns, P., & Georgiou, G. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00562 · Cited by 27

Intratumoral delivery of CpG-conjugated anti-MUC1 antibody enhances NK cell anti-tumor activity

Schettini, J. L., Kidiyoor, A., Besmer, D. M., Tinder, T. L., Roy, L. D., Lustgarten, J., Gendler, S. J., & Mukherjee, P. (2012) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-012-1264-y · Cited by 27

Glyco-engineered anti-EGFR mAb elicits ADCC by NK cells from colorectal cancer patients irrespective of chemotherapy

Oppenheim, D. E., Spreafico, R., Etuk, A., Malone, D., Amofah, E., Peña-Murillo, C., Murray, T. J., McLaughlin, L., Choi, B., Allan, S., et al. (2014) · British Journal of Cancer · doi:10.1038/bjc.2014.35 · Cited by 27

Applicability of predictive toxicology methods for monoclonal antibody therapeutics: status Quo and scope

Kizhedath, A., Wilkinson, S. C., & Glassey, J. (2016) · Archives of Toxicology · doi:10.1007/s00204-016-1876-7 · Cited by 29

The transgenic chicken derived anti-CD20 monoclonal antibodies exhibits greater anti-cancer therapeutic potential with enhanced Fc effector functions

Kim, Y. M., Park, J. S., Kim, S. K., Jung, K. M., Hwang, Y. S., Han, M., Lee, H. J., Seo, H. W., Suh, J., Han, B. K., et al. (2018) · Biomaterials · doi:10.1016/j.biomaterials.2018.03.021 · Cited by 28

Fc receptor targeting in the treatment of allergy, autoimmune diseases and cancer

Nakamura, A., Akiyama, K., & Takai, T. (2005) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.9.1.169 · Cited by 27

Epigenetic Engineering of Ribosomal RNA Genes Enhances Protein Production

Santoro, R., Lienemann, P. S., & Fussenegger, M. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006653 · Cited by 28

Applying quality by design to glycoprotein therapeutics: experimental and computational efforts of process control

Jedrzejewski, P., del Val, I. J., Polizzi, K. M., & Kontoravdi, C. (2013) · Pharmaceutical Bioprocessing · doi:10.4155/pbp.13.4 · Cited by 27

mAbs N-glycosylation: Implications for biotechnology and analytics

Wang, T., Liu, L., & Voglmeir, J. (2022) · Carbohydrate Research · doi:10.1016/j.carres.2022.108541 · Cited by 25

Antibodies for angiogenesis inhibition, vascular targeting and endothelial cell transcytosis

Trachsel, E., & Neri, D. (2006) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2005.11.002 · Cited by 26

Improving monoclonal antibodies for cancer therapy

Robinson, M. K., Weiner, L. M., & Adams, G. P. (2004) · Drug Development Research · doi:10.1002/ddr.10345 · Cited by 27

Sialylated IgG induces the transcription factor REST in alveolar macrophages to protect against lung inflammation and severe influenza disease

Chakraborty, S., Cheng, B. Y.-L., Edwards, D. L., González, J. C., Chiu, D. K., Zheng, H., Scallan, C., Guo, X., Tan, G. S., Coffey, G., et al. (2024) · Immunity · doi:10.1016/j.immuni.2024.10.002 · Cited by 24

Reduction of N-linked xylose and fucose by expression of rat β1,4-N-acetylglucosaminyltransferase III in tobacco BY-2 cells depends on Golgi enzyme localization domain and genetic elements used for expression

Karg, S. R., Frey, A. D., & Kallio, P. T. (2010) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2010.01.005 · Cited by 25

The Potential Role of Fc-Receptor Functions in the Development of a Universal Influenza Vaccine

Jegaskanda, S. (2018) · Vaccines · doi:10.3390/vaccines6020027 · Cited by 24

A new approach for identifying positional isomers of glycans cleaved from monoclonal antibodies

Dyukova, I., Faleh, A. B., Warnke, S., Yalovenko, N., Yatsyna, V., Bansal, P., & Rizzo, T. R. (2021) · The Analyst · doi:10.1039/d1an00780g · Cited by 26

Transient Production of scFv-Fc Fusion Proteins in Mammalian Cells

Schirrmann, T., & Büssow, K. (2010) · Springer eBooks · doi:10.1007/978-3-642-01147-4_30 · Cited by 24

Fc-Receptor Targeted Therapies for the Treatment of Myasthenia gravis

Keller, C. W., Pawlitzki, M., Wiendl, H., & Lünemann, J. D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115755 · Cited by 25

Antibodies for HIV Treatment and Prevention: Window of Opportunity?

Huber, M., Olson, W. C., & Trkola, A. (2007) · Current topics in microbiology and immunology · doi:10.1007/978-3-540-72146-8_2 · Cited by 24

Intramolecular N-Glycan/Polypeptide Interactions Observed at Multiple N-Glycan Remodeling Steps through [13C,15N]-N-Acetylglucosamine Labeling of Immunoglobulin G1

Barb, A. W. (2014) · Biochemistry · doi:10.1021/bi501380t · Cited by 24

The Biological Role and Therapeutic Potential of NK Cells in Hematological and Solid Tumors

Velichinskii, R. A., Streltsova, M. A., Kust, S. A., Sapozhnikov, A. M., & Kovalenko, E. I. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111385 · Cited by 23

Strategies for Engineering Protein N-Glycosylation Pathways in Mammalian Cells

Wang, Q., Stuczynski, M. C., Gao, Y., & Betenbaugh, M. J. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2760-9_20 · Cited by 27

Plug-plug kinetic capillary electrophoresis for in-capillary exoglycosidase digestion as a profiling tool for the analysis of glycoprotein glycans

Maki, Y., Matsui, Y., Hayakawa, T., Yamamoto, S., Kinoshita, M., & Suzuki, S. (2017) · Journal of Chromatography A · doi:10.1016/j.chroma.2017.03.019 · Cited by 22

Mammalian Stable Expression of Biotherapeutics

Jostock, T., & Knopf, H. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-921-1_15 · Cited by 24

The Role of Glycosylation in Therapeutic Antibodies

Spearman, M. A., Dionne, B., & Butler, M. (2011) · Cell engineering · doi:10.1007/978-94-007-1257-7_12 · Cited by 24

Comprehensive analysis of human IgG Fc N-glycopeptides and construction of a screening model for colorectal cancer

Zou, Y., Hu, J., Jie, J., Lai, J., Li, M., Liu, Z., & Zou, X. (2019) · Journal of Proteomics · doi:10.1016/j.jprot.2019.103616 · Cited by 23

Homogeneous production and characterization of recombinant N-GlcNAc-protein in Pichia pastoris

Wang, S., Rong, Y., Wang, Y., Kong, D., Wang, P. G., Chen, M., & Kong, Y. (2020) · Microbial Cell Factories · doi:10.1186/s12934-020-1280-0 · Cited by 22

Biotinylation of the Fcγ receptor ectodomains by mammalian cell co-transfection: application to the development of a surface plasmon resonance-based assay

Dorion-Thibaudeau, J., St‐Laurent, G., Raymond, C., Crescenzo, G. D., & Durocher, Y. (2015) · Journal of Molecular Recognition · doi:10.1002/jmr.2495 · Cited by 24

A novel mammalian cell-based approach for the discovery of anticancer drugs with reduced cytotoxicity on non-dividing cells

Gonzalez‐Nicolini, V., Fux, C., & Fussenegger, M. (2004) · Investigational New Drugs · doi:10.1023/b:drug.0000026251.00854.77 · Cited by 22

Antibody Engineering Principles and Applications

Loo, L., Robinson, M. K., & Adams, G. P. (2008) · The Cancer Journal · doi:10.1097/ppo.0b013e318173a5d5 · Cited by 22

Variability factors in the clinical response to recombinant antibodies and IgG Fc-containing fusion proteins

Watier, H. (2005) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.5.1.s29 · Cited by 26

Characterization of N-Linked Glycosylation on Recombinant Glycoproteins Produced in Pichia pastoris Using ESI-MS and MALDI-TOF

Gong, B., Cukan, M. C., Fisher, R., Li, H., Stadheim, T. A., & Gerngross, T. U. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-022-5_16 · Cited by 22

Fc Engineering: Design, Expression, and Functional Characterization of Antibody Variants with Improved Effector Function

Derer, S., Kellner, C., Berger, S., Valerius, T., & Peipp, M. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-974-7_30 · Cited by 20

Solid‐Phase Enzymatic Remodeling Produces High Yields of Single Glycoform Antibodies

Tayi, V. S., & Butler, M. (2017) · Biotechnology Journal · doi:10.1002/biot.201700381 · Cited by 18

Cell Culture Media in Bioprocessing

Whitford, W. G., Lundgren, M., & Fairbank, A. (2018) · Elsevier eBooks · doi:10.1016/b978-0-08-100623-8.00008-6 · Cited by 26

Anti-CD20 monoclonal antibodies in Systemic Lupus Erythematosus

Shah, K., Cragg, M. S., Leandro, M. J., & Reddy, V. R. (2020) · Biologicals · doi:10.1016/j.biologicals.2020.11.002 · Cited by 23

Expression of glycoproteins bearing complex human-like glycans with galactose terminal in Hansenula polymorpha

Wang, H., Song, H., Wang, Q., & Qiu, B. (2012) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-012-1197-9 · Cited by 20

Systematic analysis of Fc mutations designed to enhance binding to Fc-gamma receptors

Hale, G., Davy, A. D., & Wilkinson, I. (2024) · mAbs · doi:10.1080/19420862.2024.2406539 · Cited by 20

The antibody paradigm: present and future development as a scaffold for biopharmaceutical drugs

Jefferis, R. (2009) · Biotechnology and Genetic Engineering Reviews · doi:10.5661/bger-26-1 · Cited by 22

Molecular engineering to improve antibodies’ anti-lymphoma activity

Peipp, M., van de Winkel, J. G. J., & Valerius, T. (2011) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2011.03.004 · Cited by 19

Plant-Derived Monoclonal Antibodies for Prevention and Treatment of Infectious Disease

Hiatt, A., Whaley, K. J., & Zeitlin, L. (2014) · Microbiology Spectrum · doi:10.1128/microbiolspec.aid-0004-2012 · Cited by 20

Functional glycomics and evidence for gain- and loss-of-functions of target proteins for glycosyltransferases involved in N-glycan biosynthesis: their pivotal roles in growth and development, cancer metastasis and antibody therapy against cancer

Taniguchi, N., Gu, J., Takahashi, M., & Miyoshi, E. (2004) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.80.82 · Cited by 20

Composition of the immunoglobulin G glycome associates with the severity of COVID-19Preprint

Petrović, T., Alves, I., Bugada, D., Pascual, J., Vučković, F., Skelin, A., Gaifem, J., Villar-García, J., Vicente, M. M., Fernandes, Â., et al. (2020) · medRxiv · doi:10.1101/2020.10.17.20214205 · Cited by 20

Antitumor Efficacy of Anti-GD2 IgG1 Is Enhanced by Fc Glyco-Engineering

Xu, H., Guo, H.-F., Cheung, I. Y., & Cheung, N. V. (2016) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-15-0221 · Cited by 19

Advances in analytical methodologies to guide bioprocess engineering for bio-therapeutics

Saldova, R., Kilcoyne, M., Stöckmann, H., Millán‐Martín, S., Lewis, A. M., Tuite, C. M. E., Gerlach, J. Q., Berre, M. L., Borys, M., Li, Z. J., et al. (2016) · Methods · doi:10.1016/j.ymeth.2016.11.002 · Cited by 19

Characterization of Endogenous Human FcγRIII by Mass Spectrometry Reveals Site, Allele and Sequence Specific Glycosylation*

Washburn, N., Meccariello, R., Duffner, J. L., Getchell, K. M., Holte, K., Prod’homme, T., Srinivasan, K., Prenovitz, R., Lansing, J. C., Capila, I., et al. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.001142 · Cited by 19

Dilute-and-shoot analysis of therapeutic monoclonal antibody variants in fermentation broth: a method capability study

Regl, C., Wohlschlager, T., Esser‐Skala, W., Wagner, I., Samonig, M., Holzmann, J., & Huber, C. G. (2019) · mAbs · doi:10.1080/19420862.2018.1563034 · Cited by 19

Fc gamma receptor IIIb binding of individual antibody proteoforms resolved by affinity chromatography–mass spectrometry

Lippold, S., Knaupp, A., de Ru, A. H., Tjokrodirijo, R. T. N., van Veelen, P. A., van Puijenbroek, E., de Taeye, S. W., Reusch, D., Vidarsson, G., Wuhrer, M., et al. (2021) · mAbs · doi:10.1080/19420862.2021.1982847 · Cited by 19

Production of afucosylated antibodies in CHO cells by coexpression of an anti‐FUT8 intrabody

Joubert, S., Guimond, J., Perret, S., Malenfant, F., Elahi, S. M., Marcil, A., Parat, M., Gilbert, M., Lenferink, A. E. G., Baardsnes, J., et al. (2022) · Biotechnology and Bioengineering · doi:10.1002/bit.28127 · Cited by 21

Engineered therapeutic antibodies with enhanced effector functions: Clinical application of the Potelligent® Technology

Matsushita, T. (2011) · The Korean Journal of Hematology · doi:10.5045/kjh.2011.46.3.148 · Cited by 19

Monoclonal antibody-based therapeutics for leukemia

Li, Y., & Zhu, Z. (2007) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.7.3.319 · Cited by 20

Anti-D monoclonal antibodies from 23 human and rodent cell lines display diverse IgG Fc-glycosylation profiles that determine their clinical efficacy

Kumpel, B. M., Saldova, R., Koeleman, C. A. M., Abrahams, J. L., Ederveen, A. L. H., Armour, K. L., Olovnikova, N. I., Vidarsson, G., Kapur, R., Rudd, P. M., et al. (2020) · Scientific Reports · doi:10.1038/s41598-019-57393-9 · Cited by 19

Commercial interest grows in glycan analysis

Sheridan, C. (2007) · Nature Biotechnology · doi:10.1038/nbt0207-145 · Cited by 19

Investigation of the causal relationships between human IgG N-glycosylation and 12 common diseases associated with changes in the IgG N-glycome

Zaytseva, O. O., Sharapov, S., Perola, M., Esko, T., Landini, A., Hayward, C., Wilson, J. F., Lauc, G., Aulchenko, Y. S., Klarić, L., et al. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab335 · Cited by 19

Activating and inhibitory Fcγ receptors in immunotherapy: being the actor or being the target

Abès, R., Dutertre, C., Agnelli, L., & Teillaud, J. (2009) · Expert Review of Clinical Immunology · doi:10.1586/eci.09.57 · Cited by 18

Tear N‐glycomics in vernal and atopic keratoconjunctivitis

Messina, A., Palmigiano, A., Tosto, C., Romeo, D. A., Sturiale, L., Garozzo, D., & Leonardi, A. (2021) · Allergy · doi:10.1111/all.14775 · Cited by 18

The structure of Fc receptor/Ig complexes: considerations on stoichiometry and potential inhibitors

Sondermann, P., & Oosthuizen, V. (2002) · Immunology Letters · doi:10.1016/s0165-2478(02)00018-4 · Cited by 18

Change of fucosylated IgG2 Fc-glycoforms in pancreatitis and pancreatic adenocarcinoma: a promising disease-classification model

Chen, G., Li, H., Qiu, L., Qin, X., Liu, H., & Li, Z. (2013) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-013-7439-3 · Cited by 18

Implementation of Glycan Remodeling to Plant-Made Therapeutic Antibodies

Bennett, L. D., Yang, Q., Berquist, B. R., Giddens, J. P., Ren, Z., Kommineni, V., Murray, R. C., White, E. L., Holtz, B. R., Wang, L., et al. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020421 · Cited by 18

A novel system for glycosylation engineering by natural and artificial miRNAs

Klingler, F., Naumann, L., Schlossbauer, P., Dreyer, L., Burkhart, M., Handrick, R., Junker, H.-D., Hesse, F., Neusüß, C., & Otte, K. (2023) · Metabolic Engineering · doi:10.1016/j.ymben.2023.03.004 · Cited by 20

Differential influence on antibody dependent cellular phagocytosis by different glycoforms on therapeutic Monoclonal antibodies

Kuhns, S. T., Shu, J., Xiang, C. D., Guzman, R. D., Zhang, Q., Bretzlaff, W., Miscalichi, N., Kalenian, K., & Joubert, M. K. (2020) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2020.04.017 · Cited by 19

Glycomic Signatures on Serum IgGs for Prediction of Postvaccination Response

Wang, J., Guan, W., Yau, L., Gao, W., Zhan, Y., Liu, L., Yang, Z., & Jiang, Z. (2015) · Scientific Reports · doi:10.1038/srep07648 · Cited by 17

Comparison of two glycoengineering strategies to control the fucosylation of a monoclonal antibody

Mishra, N., Spearman, M. A., Donald, L. J., Perreault, H., & Butler, M. (2020) · Journal of Biotechnology · doi:10.1016/j.btecx.2020.100015 · Cited by 18

Metabolic engineering II. Eukaryotic systems

Fussenegger, M., & Betenbaugh, M. J. (2002) · Biotechnology and Bioengineering · doi:10.1002/bit.10405 · Cited by 17

Gas-inducible product gene expression in bioreactors

Weber, W., Rimann, M., de Glutz, F.-N., Weber, E., Memmert, K., & Fussenegger, M. (2005) · Metabolic Engineering · doi:10.1016/j.ymben.2005.01.003 · Cited by 17

Manufacture of Recombinant Biopharmaceutical Proteins by Cultivated Mammalian Cells in Bioreactors

Wurm, F. M. (2005) · Wiley eBooks · doi:10.1002/9783527620982.ch31 · Cited by 17

A Chinese hamster transcription start site atlas that enables targeted editing of CHO cells

Shamie, I., Duttke, S. H. C., Karottki, K. J. L. C., Han, C. Z., Hansen, A. H., Hefzi, H., Xiong, K., Li, S., Roth, S. J., Tao, J., et al. (2021) · NAR Genomics and Bioinformatics · doi:10.1093/nargab/lqab061 · Cited by 16

Facts and Hopes: Immunocytokines for Cancer Immunotherapy

Pabani, A., & Gainor, J. F. (2023) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-22-1837 · Cited by 17

The analysis of N-glycans of cell membrane proteins from human hematopoietic cell lines reveals distinctions in their pattern

Reinke, S. O., Bayer, M., Berger, M., Hinderlich, S., & Blanchard, V. (2012) · Biological Chemistry · doi:10.1515/hsz-2012-0195 · Cited by 16

Isotype‐specific glycosylation analysis of mouse IgG by LC‐MS

Maresch, D., & Altmann, F. (2016) · PROTEOMICS · doi:10.1002/pmic.201500367 · Cited by 16

Glycosylation decreases aggregation and immunogenicity of adalimumab Fab secreted fromPichia pastoris

Nakamura, H., Kiyoshi, M., Anraku, M., Hashii, N., Oda‐Ueda, N., Ueda, T., & Ohkuri, T. (2020) · The Journal of Biochemistry · doi:10.1093/jb/mvaa116 · Cited by 16

Effect of the conserved oligosaccharides of recombinant monoclonal antibodies on the separation by protein A and protein G chromatography

Gaza‐Bulseco, G., Hickman, K., Sinicropi-Yao, S. L., Hurkmans, K., Chumsae, C. M., & Liu, H. (2009) · Journal of Chromatography A · doi:10.1016/j.chroma.2009.01.014 · Cited by 16

Glycosylation Analysis of Therapeutic Glycoproteins Produced in CHO Cells

Carillo, S., Mittermayr, S., Farrell, A., Albrecht, S., & Bones, J. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6972-2_15 · Cited by 16

Antibody Structures

Yamaguchi, Y., Takahashi, N., & Kato, K. (2007) · Elsevier eBooks · doi:10.1016/b978-044451967-2/00072-6 · Cited by 17

Bioprocess applications of a Sindbis virus‐based temperature‐inducible expression system

Boorsma, M., Hoenke, S., Marrero, A., Fischer, R. W., Bailey, J. E., Renner, W. A., & Bachmann, M. F. (2002) · Biotechnology and Bioengineering · doi:10.1002/bit.10311 · Cited by 16

Recent advances in antibody glycoengineering for the gain of functions

Liu, Z., Zou, X., Tang, F., & Huang, W. (2024) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2023.102420 · Cited by 15

Large-scale multicenter study reveals anticitrullinated SR-A peptide antibody as a biomarker and exacerbator for rheumatoid arthritis

Xie, Y., Wei, C., Fu, D., Zhang, W., Du, Y., Huang, C., Liu, S., Yao, R., He, Z., Zhang, S., et al. (2025) · Science Advances · doi:10.1126/sciadv.adr8078 · Cited by 15

Antibody-drug conjugates for cancer therapy: An up-to-date review on the chemistry and pharmacology

Gholap, A. D., Gupta, J. S., Kamandar, P. A., Banchhod, G. V., & Hatvate, N. T. (2023) · Comprehensive analytical chemistry · doi:10.1016/bs.coac.2023.02.007 · Cited by 18

Next generation of antibody therapy for cancer

Zhu, Z., & Li, Y. (2011) · 癌症：英文版 · doi:10.5732/cjc.011.10123 · Cited by 15

Capillary (Gel) Electrophoresis-Based Methods for Immunoglobulin (G) Glycosylation Analysis

Cajic, S., Hennig, R., Burock, R., & Rapp, E. (2021) · Experientia supplementum · doi:10.1007/978-3-030-76912-3_4 · Cited by 15

The War Is on: The Immune System against Glioblastoma—How Can NK Cells Drive This Battle?

da Silva, L. H. R., Catharino, L. C. C., da Silva, V. J., Evangelista, G. C. M., & Barbuto, J. A. M. (2022) · Biomedicines · doi:10.3390/biomedicines10020400 · Cited by 16

Overview of Biopharmaceuticals and Comparison with Small-molecule Drug Development

Reynolds, T., de Zafra, C., Kim, A., & Gelzleichter, T. R. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-394810-6.00001-0 · Cited by 16

Expression of Antibody in Mammalian Cells

Jostock, T. (2011) · Cell engineering · doi:10.1007/978-94-007-1257-7_1 · Cited by 16

Genetic Engineering of Crop Plants for Abiotic Stress Tolerance

Goel, S., & Madan, B. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-800876-8.00005-9 · Cited by 15

Direct targeting of cancer cells with antibodies: What can we learn from the successes and failure of unconjugated antibodies for lymphoid neoplasias?

Golay, J. (2017) · Journal of Autoimmunity · doi:10.1016/j.jaut.2017.06.002 · Cited by 15

Antibody Engineering

Lo, K.-M., Léger, O. J. P., & Hock, B. M. (2014) · Microbiology Spectrum · doi:10.1128/microbiolspec.aid-0007-12 · Cited by 14

Influence of Variable N-Glycosylation on the Cytolytic Potential of Chimeric CD19 Antibodies

Barbin, K., Stieglmaier, J., Saul, D., Stieglmaier, K., Stockmeyer, B., Pfeiffer, M. M., Lang, P., & Fey, G. H. (2006) · Journal of Immunotherapy · doi:10.1097/01.cji.0000175684.28615.7b · Cited by 28

Expression of GnTIII in a recombinant anti‐CD20 CHO production cell line: Expression of antibodies with altered glycoforms leads to an increase in ADCC through higher affinity for FCγRIII

Davies, J., Jiang, L., Pan, L., LaBarre, M. J., Anderson, D., & Reff, M. (2001) · Biotechnology and Bioengineering · doi:10.1002/bit.1119 · Cited by 327

Modulation of therapeutic antibody effector functions by glycosylation engineering: Influence of Golgi enzyme localization domain and co‐expression of heterologous β1, 4‐N‐acetylglucosaminyltransferase III and Golgi α‐mannosidase II

Ferrara, C., Brünker, P., Suter, T., Moser, S., Püntener, U., & Umaña, P. (2006) · Biotechnology and Bioengineering · doi:10.1002/bit.20777 · Cited by 305

Improved Effector Functions of a Therapeutic Monoclonal Lewis Y-Specific Antibody by Glycoform Engineering

Schuster, M., Umaña, P., Ferrara, C., Brünker, P., Gerdes, C. A., Waxenecker, G., Wiederkum, S., Schwager, C., Loibner, H., Himmler, G., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4212 · Cited by 91

Engineering of protein glycosylation in Chinese hamster ovary cells

Umaña, P. (2005) · CaltechTHESIS (California Institute of Technology) · doi:10.7907/6ceh-kt92 · Cited by 1