Engineered CHO cells for production of diverse, homogeneous glycoproteins

Biopharmaceutical benchmarks 2014

Walsh, G. (2014) · Nature Biotechnology · doi:10.1038/nbt.3040 · Cited by 1,008 · see citing works

The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line

Xu, X., Nagarajan, H., Lewis, N. E., Pan, S., Cai, Z., Liu, X., Chen, W., Xie, M., Wang, W., Hammond, S., et al. (2011) · Nature Biotechnology · doi:10.1038/nbt.1932 · Cited by 785 · see citing works

Establishment of <i>FUT8</i> knockout Chinese hamster ovary cells: An ideal host cell line for producing completely defucosylated antibodies with enhanced antibody‐dependent cellular cytotoxicity

Yamane‐Ohnuki, N., Kinoshita, S., Inoue‐Urakubo, M., Kusunoki, M., Iida, S., Nakano, R., Wakitani, M., Niwa, R., Sakurada, M., Uchida, K., et al. (2004) · Biotechnology and Bioengineering · doi:10.1002/bit.20151 · Cited by 572 · see citing works

Humanization of yeast to produce complex terminally sialylated glycoproteins

Hamilton, S. R., Davidson, R. C., Sethuraman, N., Nett, J. H., Jiang, Y., Rios, S., Bobrowicz, P., Stadheim, T. A., Li, H., Choi, B.-K., et al. (2006) · Science · doi:10.1126/science.1130256 · Cited by 511 · see citing works

Glycoengineering: The effect of glycosylation on the properties of therapeutic proteins

Sinclair, A. M., & Elliott, S. (2005) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.20319 · Cited by 461 · see citing works

Survival of recombinant erythropoietin in the circulation: the role of carbohydrates

Fukuda, M., Sasaki, H., Lopez, L. B., & Fukuda, M. (1989) · Blood · doi:10.1182/blood.v73.1.84.84 · Cited by 386 · see citing works

Genomic landscapes of Chinese hamster ovary cell lines as revealed by the Cricetulus griseus draft genome

Lewis, N. E., Liu, X., Li, Y., Nagarajan, H., Yerganian, G., O'Brien, E., Bordbar, A., Roth, A. M., Rosenbloom, J., Bian, C., et al. (2013) · Nature Biotechnology · doi:10.1038/nbt.2624 · Cited by 380 · see citing works

Obligate Ligation-Gated Recombination (ObLiGaRe): Custom-designed nuclease-mediated targeted integration through nonhomologous end joiningPreprint

Maresca, M., Lin, V. G., Guo, N., & Yang, Y. (2012) · Genome Research · doi:10.1101/gr.145441.112 · Cited by 310 · see citing works

Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions

Amado, M., Almeida, R., Schwientek, T., & Clausen, H. (1999) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(99)00168-3 · Cited by 300 · see citing works

Post-translational modifications of protein biopharmaceuticals

Walsh, G. (2010) · Drug Discovery Today · doi:10.1016/j.drudis.2010.06.009 · Cited by 263 · see citing works

Lectin-resistant CHO glycosylation mutants

Patnaik, S. K., & Stanley, P. (2006) · Methods in Enzymology · doi:10.1016/s0076-6879(06)16011-5 · Cited by 218 · see citing works

Glycomics profiling of Chinese hamster ovary cell glycosylation mutants reveals N-glycans of a novel size and complexity

North, S. J., Huang, H.-H., Sundaram, S., Jang-Lee, J., Etienne, A. T., Trollope, A., Chalabi, S., Dell, A., Stanley, P., & Haslam, S. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.068353 · Cited by 207 · see citing works

Fast and sensitive detection of indels induced by precise gene targeting

Zhang, Y., Steentoft, C., Hauge, C., Hansen, L. H., Lind-Thomsen, A., Niola, F., Vester-Christensen, M. B., Frödin, M., Clausen, H., Wandall, H. H., et al. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv126 · Cited by 191 · 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

Highly efficient deletion of <i>FUT8</i> in CHO cell lines using zinc‐finger nucleases yields cells that produce completely nonfucosylated antibodies

Malphettes, L., Freyvert, Y., Chang, J., Liu, P., Chan, E., Miller, J. C., Zhou, Z., Nguyen, T., Tsai, C., Snowden, A. W., et al. (2010) · Biotechnology and Bioengineering · doi:10.1002/bit.22751 · Cited by 164 · see citing works

Site-specific glycosylation of human recombinant erythropoietin: analysis of glycopeptides or peptides at each glycosylation site by fast atom bombardment-mass spectrometry

Sasaki, H., Ochi, N., Dell, A., & Fukuda, M. (1988) · Biochemistry · doi:10.1021/bi00423a017 · Cited by 122 · see citing works

High-efficiency genome editing via 2A-coupled co-expression of fluorescent proteins and zinc finger nucleases or CRISPR/Cas9 nickase pairs

Duda, K., Lonowski, L. A., Kofoed-Nielsen, M., Ibarra, A., Delay, C. M., Kang, Q., Yang, Z., Pruett‐Miller, S. M., Bennett, E., Wandall, H. H., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku251 · Cited by 76 · see citing works

Human glycogene cloning: focus on β3-glycosyltransferase and β4-glycosyltransferase families

Narimatsu, H. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.09.001 · Cited by 66 · see citing works

Precision genome editing: A small revolution for glycobiology

Steentoft, C., Bennett, E., Schjoldager, K. T.-B. G., Vakhrushev, S. Y., Wandall, H. H., & Clausen, H. (2014) · Glycobiology · doi:10.1093/glycob/cwu046 · Cited by 59 · see citing works

Engineering a Human-Like Glycosylation to Produce Therapeutic Glycoproteins Based on 6-Linked Sialylation in CHO Cells

Maï, N. E., Donadio, S., Iss, C., Calabro, V., & Ronin, C. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-327-5_2 · Cited by 21 · see citing works

Global view of human protein glycosylation pathways and functions

Schjoldager, K. T.-B. G., Narimatsu, Y., Joshi, H. J., & Clausen, H. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00294-x · Cited by 1,322 · see citing works

High-Resolution Native Mass Spectrometry

Tamara, S., den Boer, M. A., & Heck, A. J. R. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00212 · Cited by 511 · see citing works

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442 · see citing works

Decoding the Human Immunoglobulin G-Glycan Repertoire Reveals a Spectrum of Fc-Receptor- and Complement-Mediated-Effector Activities

Dekkers, G., Treffers, L. W., Plomp, R., Bentlage, A. E. H., de Boer, M., Koeleman, C. A. M., Lissenberg‐Thunnissen, S. N., Visser, R., Brouwer, M. C., Mok, J. Y., et al. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00877 · Cited by 359 · 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

An Atlas of Human Glycosylation Pathways Enables Display of the Human Glycome by Gene Engineered Cells

Narimatsu, Y., Joshi, H. J., Nason, R., Coillie, J. V., Karlsson, R. T. G., Sun, L., Ye, Z., Chen, Y., Schjoldager, K. T.-B. G., Steentoft, C., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.05.017 · Cited by 277 · see citing works

Global aspects of viral glycosylation

Bagdonaite, I., & Wandall, H. H. (2018) · Glycobiology · doi:10.1093/glycob/cwy021 · Cited by 234 · 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

Oligosaccharide Synthesis and Translational Innovation

Krasnova, L. B., & Wong, C. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.8b11005 · Cited by 202 · see citing works

Recent advances in CHO cell line development for recombinant protein production

Tihanyi, B., & Nyitray, L. (2020) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2021.02.003 · Cited by 201 · see citing works

Microbial consortia: a critical look at microalgae co-cultures for enhanced biomanufacturing

Padmaperuma, G., Kapoore, R. V., Gilmour, D. J., & Vaidyanathan, S. (2017) · Critical Reviews in Biotechnology · doi:10.1080/07388551.2017.1390728 · Cited by 184 · see citing works

Hybrid mass spectrometry approaches in glycoprotein analysis and their usage in scoring biosimilarity

Yang, Y., Liu, F., Franc, V., Halim, L. A., Schellekens, H., & Heck, A. J. R. (2016) · Nature Communications · doi:10.1038/ncomms13397 · Cited by 152 · see citing works

The GAGOme: a cell-based library of displayed glycosaminoglycans

Chen, Y., Narimatsu, Y., Clausen, T. M., Gomes, C., Karlsson, R. T. G., Steentoft, C., Spliid, C. B., Gustavsson, T., Salanti, A., Persson, A., et al. (2018) · Nature Methods · doi:10.1038/s41592-018-0086-z · Cited by 143 · see citing works

A cell-free biosynthesis platform for modular construction of protein glycosylation pathways

Kightlinger, W., Duncker, K. E., Ramesh, A., Thames, A. H., Natarajan, A., Stark, J. C., Yang, A., Liang, L., Mrksich, M., DeLisa, M. P., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12024-9 · Cited by 135 · see citing works

Understanding the Chemistry and Biology of Glycosylation with Glycan Synthesis

Krasnova, L. B., & Wong, C. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-034420 · Cited by 134 · see citing works

Cell Factory Engineering

Davy, A. M., Kildegaard, H. F., & Andersen, M. R. (2017) · Cell Systems · doi:10.1016/j.cels.2017.02.010 · Cited by 133 · see citing works

The benefits of hybrid fragmentation methods for glycoproteomics

Reiding, K. R., Bondt, A., Franc, V., & Heck, A. J. R. (2018) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2018.09.007 · Cited by 129 · see citing works

Design of glycosylation sites by rapid synthesis and analysis of glycosyltransferases

Kightlinger, W., Liang, L., Rosztoczy, M., Li, W., DeLisa, M. P., Mrksich, M., & Jewett, M. C. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0051-2 · Cited by 126 · see citing works

Cell-based glycan arrays for probing glycan–glycan binding protein interactions

Briard, J. G., Jiang, H., Moremen, K. W., Macauley, M. S., & Wu, P. (2018) · Nature Communications · doi:10.1038/s41467-018-03245-5 · Cited by 123 · see citing works

Translating the ‘Sugar Code’ into Immune and Vascular Signaling Programs

Cerliani, J. P., Blidner, A. G., Toscano, M. A., Croci, D. O., & Rabinovich, G. A. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.11.003 · Cited by 119 · see citing works

Multi-level glyco-engineering techniques to generate IgG with defined Fc-glycans

Dekkers, G., Plomp, R., Koeleman, C. A. M., Visser, R., von Horsten, H. H., Sandig, V., Rispens, T., Wuhrer, M., & Vidarsson, G. (2016) · Scientific Reports · doi:10.1038/srep36964 · Cited by 118 · see citing works

Conformational analysis of complex protein states by hydrogen/deuterium exchange mass spectrometry (HDX-MS): Challenges and emerging solutions

Trabjerg, E., Nazari, Z. E., & Rand, K. D. (2018) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2018.06.008 · Cited by 117 · see citing works

Engineering of complex protein sialylation in plants

Kallolimath, S., Castilho, A., Strasser, R., Grünwald-Gruber, C., Altmann, F., Strubl, S., Galuska, C. E., Zlatina, K., Galuska, S. P., Werner, S., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604371113 · Cited by 113 · see citing works

Genome editing using FACS enrichment of nuclease-expressing cells and indel detection by amplicon analysis

Lonowski, L. A., Narimatsu, Y., Riaz, A., Delay, C. M., Yang, Z., Niola, F., Duda, K., Ober, E. A., Clausen, H., Wandall, H. H., et al. (2017) · Nature Protocols · doi:10.1038/nprot.2016.165 · Cited by 109 · see citing works

Genetic glycoengineering in mammalian cells

Narimatsu, Y., Büll, C., Chen, Y., Wandall, H. H., Yang, Z., & Clausen, H. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100448 · Cited by 100 · see citing works

CHO-omics review: the impact of current and emerging technologies on Chinese hamster ovary based bioproduction

Stolfa, G., Smonskey, M. T., Boniface, R., Hachmann, A., Gulde, P., Joshi, A. D., Pierce, A. P., Jacobia, S. J., & Campbell, A. (2018) · Biotechnology Journal · doi:10.1002/biot.201700227 · Cited by 97 · see citing works

A Markov chain model for N-linked protein glycosylation – towards a low-parameter tool for model-driven glycoengineering

Spahn, P. N., Hansen, A. H., Hansen, H. G., Arnsdorf, J., Kildegaard, H. F., & Lewis, N. E. (2015) · Metabolic Engineering · doi:10.1016/j.ymben.2015.10.007 · Cited by 96 · see citing works

Antibody glycoengineering strategies in mammalian cells

Wang, Q., Chung, C., Chough, S., & Betenbaugh, M. J. (2018) · Biotechnology and Bioengineering · doi:10.1002/bit.26567 · Cited by 94 · see citing works

A validated gRNA library for CRISPR/Cas9 targeting of the human glycosyltransferase genome

Narimatsu, Y., Joshi, H. J., Yang, Z., Gomes, C., Chen, Y., Lorenzetti, F. C., Furukawa, S., Schjoldager, K. T.-B. G., Hansen, L. H., Clausen, H., et al. (2017) · Glycobiology · doi:10.1093/glycob/cwx101 · Cited by 93 · see citing works

Protein glycosylation in gastric and colorectal cancers: Toward cancer detection and targeted therapeutics

Ferreira, J. A., Magalhães, A., Gomes, J., Peixoto, A., Gaiteiro, C., Fernandes, E., Santos, L. L., & Reis, C. A. (2016) · Cancer Letters · doi:10.1016/j.canlet.2016.01.044 · Cited by 92 · see citing works

Galectin binding to cells and glycoproteins with genetically modified glycosylation reveals galectin–glycan specificities in a natural context

Nielsen, M. I., Stegmayr, J., Grant, O. C., Yang, Z., Nilsson, U. J., Boos, I., Carlsson, M. C., Woods, R. J., Unverzagt, C., Leffler, H., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004636 · Cited by 89 · see citing works

Plant glyco-biotechnology

Schoberer, J., & Strasser, R. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.07.005 · Cited by 86 · see citing works

Direct quality control of glycoengineered erythropoietin variants

Čaval, T., Tian, W., Yang, Z., Clausen, H., & Heck, A. J. R. (2018) · Nature Communications · doi:10.1038/s41467-018-05536-3 · Cited by 84 · see citing works

Combined metabolomics and proteomics reveals hypoxia as a cause of lower productivity on scale-up to a 5000-liter CHO bioprocess

Gao, Y., Ray, S., Dai, S., Ivanov, A. R., Abu‐Absi, N. R., Lewis, A. M., Huang, Z., Xing, Z., Borys, M. C., Li, Z. J., et al. (2016) · Biotechnology Journal · doi:10.1002/biot.201600030 · Cited by 76 · 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

The emerging role of systems biology for engineering protein production in CHO cells

Kuo, C., Chiang, A. W. T., Shamie, I., Samoudi, M., Gutierrez, J. M., & Lewis, N. E. (2017) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2017.11.015 · Cited by 80 · see citing works

Harnessing the potential of artificial neural networks for predicting protein glycosylation

Kotidis, P., & Kontoravdi, C. (2020) · Metabolic Engineering Communications · doi:10.1016/j.mec.2020.e00131 · Cited by 80 · see citing works

Molecular basis for fibroblast growth factor 23 O-glycosylation by GalNAc-T3

Rivas, M. D. L., Daniel, E. J. P., Narimatsu, Y., Compañón, I., Kato, K., Hermosilla, P., Thureau, A., Ceballos-Laita, L., Coelho, H., Bernadó, P., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-019-0444-x · Cited by 76 · see citing works

Glycoengineered antibodies: towards the next-generation of immunotherapeutics

Mastrangeli, R., Palinsky, W., & Bierau, H. (2018) · Glycobiology · doi:10.1093/glycob/cwy092 · Cited by 74 · see citing works

De novo expression of human polypeptide N-acetylgalactosaminyltransferase 6 (GalNAc-T6) in colon adenocarcinoma inhibits the differentiation of colonic epithelium

Lavrsen, K., Dabelsteen, S., Vakhrushev, S. Y., Rudjord-Levann, A. M., Haue, A. D., Dylander, A., Mandel, U., Hansen, L. H., Frödin, M., Bennett, E., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.812826 · Cited by 73 · see citing works

Small-molecule control of antibody N-glycosylation in engineered mammalian cells

Chang, M. M., Gaidukov, L., Jung, G., Tseng, W. A., Scarcelli, J. J., Cornell, R. J., Marshall, J. K., Lyles, J. L., Sakorafas, P., Chu, A. A., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0288-4 · Cited by 73 · 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

Dissecting structure-function of 3-O-sulfated heparin and engineered heparan sulfates

Karlsson, R. T. G., Chopra, P., Joshi, A., Yang, Z., Vakhrushev, S. Y., Clausen, T. M., Painter, C. D., Szekeres, G. P., Chen, Y., Sandoval, D. R., et al. (2021) · Science Advances · doi:10.1126/sciadv.abl6026 · Cited by 66 · see citing works

Selective N-glycan editing on living cell surfaces to probe glycoconjugate function

Tang, F., Zhou, M., Qin, K., Shi, W., Yashinov, A., Yang, Y., LiYun, Y., Guan, D., Zhao, L., Tang, Y., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0551-8 · Cited by 68 · see citing works

Global Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr Virus

Bagdonaite, I., Nordén, R., Joshi, H. J., King, S. L., Vakhrushev, S. Y., Olofsson, S., & Wandall, H. H. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.721746 · Cited by 68 · see citing works

Customized protein glycosylation to improve biopharmaceutical function and targeting

Van Landuyt, L., Lonigro, C., Meuris, L., & Callewaert, N. (2019) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2018.11.017 · Cited by 66 · see citing works

Development of Antibody Therapeutics against Flaviviruses

Sun, H., Chen, Q., & Lai, H. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms19010054 · Cited by 65 · see citing works

Industrial bioprocessing perspectives on managing therapeutic protein charge variant profiles

Chung, S., Tian, J., Tan, Z., Chen, J., Lee, J., Borys, M., & Li, Z. J. (2018) · Biotechnology and Bioengineering · doi:10.1002/bit.26587 · Cited by 66 · see citing works

Recombinant protein production from stable mammalian cell lines and pools

Hacker, D. L., & Balasubramanian, S. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.06.005 · Cited by 65 · see citing works

The glycosylation design space for recombinant lysosomal replacement enzymes produced in CHO cells

Tian, W., Ye, Z., Wang, S., Schulz, M. A., Coillie, J. V., Sun, L., Chen, Y., Narimatsu, Y., Hansen, L. H., Kristensen, C., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09809-3 · Cited by 63 · see citing works

Reduced paucimannosidic N‐glycan formation by suppression of a specific β‐hexosaminidase from Nicotiana benthamiana

Shin, Y., Castilho, A., Dicker, M., Sádio, F., Vavra, U., Grünwald‐Gruber, C., Kwon, T., Altmann, F., Steinkellner, H., & Strasser, R. (2016) · Plant Biotechnology Journal · doi:10.1111/pbi.12602 · Cited by 58 · see citing works

Essential Functions of Glycans in Human Epithelia Dissected by a CRISPR-Cas9-Engineered Human Organotypic Skin Model

Dabelsteen, S., Pallesen, E. M. H., Marinova, I. N., Nielsen, M. I., Adamopoulou, M., Rømer, T. B., Rudjord-Levann, A. M., Aasted, M. K. M., Ye, Z., Thein, D., et al. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.06.039 · Cited by 56 · see citing works

Antibody glycosylation: impact on antibody drug characteristics and quality control

Wang, Z., Zhu, J., & Lu, H. (2020) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-020-10368-7 · Cited by 55 · see citing works

Perfusion culture of Chinese Hamster Ovary cells for bioprocessing applications

MacDonald, M. A., Nöbel, M., Roche Recinos, D., Martínez, V. S., Schulz, B. L., Howard, C. B., Baker, K., Shave, E., Lee, Y. Y., Marcellin, E., et al. (2022) · Critical Reviews in Biotechnology · doi:10.1080/07388551.2021.1998821 · Cited by 55 · see citing works

Fine-Tuning Limited Proteolysis: A Major Role for Regulated Site-Specific O-Glycosylation

Goth, C. K., Vakhrushev, S. Y., Joshi, H. J., Clausen, H., & Schjoldager, K. T.-B. G. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.02.005 · Cited by 55 · see citing works

Glyco-engineered CHO cell lines producing alpha-1-antitrypsin and C1 esterase inhibitor with fully humanized N-glycosylation profiles

Amann, T., Hansen, A. H., Kol, S., Hansen, H. G., Arnsdorf, J., Nallapareddy, S., Voldborg, B. G. R., Lee, G. M., Andersen, M. R., & Kildegaard, H. F. (2018) · Metabolic Engineering · doi:10.1016/j.ymben.2018.11.014 · Cited by 55 · see citing works

Towards next generation CHO cell line development and engineering by systems approaches

Hong, J. K., Lakshmanan, M., Goudar, C. T., & Lee, D. (2018) · Current Opinion in Chemical Engineering · doi:10.1016/j.coche.2018.08.002 · Cited by 53 · see citing works

Engineering Challenges in Therapeutic Protein Product and Process Design

Papathanasiou, M. M., & Kontoravdi, C. (2020) · Current Opinion in Chemical Engineering · doi:10.1016/j.coche.2019.11.010 · Cited by 54 · see citing works

FUT8-Directed Core Fucosylation of N-glycans Is Regulated by the Glycan Structure and Protein Environment

García‐García, A., Serna, S., Yang, Z., Delso, I., Taleb, V., Hicks, T., Artschwager, R., Vakhrushev, S. Y., Clausen, H., Angulo, J., et al. (2021) · ACS Catalysis · doi:10.1021/acscatal.1c01698 · Cited by 52 · see citing works

Development of plant-made monoclonal antibodies against viral infections

Chen, Q. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.12.005 · Cited by 49 · see citing works

Role of N-Glycosylation in FcγRIIIa interaction with IgG

Coillie, J. V., Schulz, M. A., Bentlage, A. E. H., de Haan, N., Ye, Z., Geerdes, D. M., van Esch, W. J. E., Hafkenscheid, L., Miller, R. L., Narimatsu, Y., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.987151 · Cited by 48 · see citing works

Integrated Genome and Protein Editing Swaps α‐2,6 Sialylation for α‐2,3 Sialic Acid on Recombinant Antibodies from CHO

Chung, C., Wang, Q., Yang, S., Yin, B., Zhang, H., & Betenbaugh, M. J. (2016) · Biotechnology Journal · doi:10.1002/biot.201600502 · Cited by 48 · see citing works

A knockout cell library of GPI biosynthetic genes for functional studies of GPI-anchored proteins

Liu, S., Liu, Y., Guo, X., Murakami, Y., Yang, G., Gao, X., Kinoshita, T., & Fujita, M. (2021) · Communications Biology · doi:10.1038/s42003-021-02337-1 · Cited by 48 · see citing works

Systems Glycobiology: Integrating Glycogenomics, Glycoproteomics, Glycomics, and Other ‘Omics Data Sets to Characterize Cellular Glycosylation Processes

Bennun, S. V., Hızal, D. B., Heffner, K. M., Can, Ö., Zhang, H., & Betenbaugh, M. J. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.07.005 · Cited by 47 · see citing works

Genetic engineering approaches to improve posttranslational modification of biopharmaceuticals in different production platforms

Amann, T., Schmieder, V., Faustrup Kildegaard, H., Borth, N., & Andersen, M. R. (2019) · Biotechnology and Bioengineering · doi:10.1002/bit.27101 · Cited by 46 · see citing works

Comprehensive Glycoproteomic Analysis of Chinese Hamster Ovary Cells

Yang, G., Hu, Y., Sun, S., OuYang, C., Yang, W., Wang, Q., Betenbaugh, M. J., & Zhang, H. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b03520 · Cited by 45 · see citing works

The contributions of individual galactosyltransferases to protein specific N-glycan processing in Chinese Hamster Ovary cells

Bydlinski, N., Maresch, D., Schmieder, V., Klanert, G., Strasser, R., & Borth, N. (2018) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2018.07.015 · Cited by 45 · see citing works

Cytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies

Tytgat, H. L. P., Lin, C., Levasseur, M. D., Tomek, M. B., Rutschmann, C., Mock, J., Liebscher, N., Terasaka, N., Azuma, Y., Wetter, M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13283-2 · Cited by 45 · see citing works

Correcting for sparsity and interdependence in glycomics by accounting for glycan biosynthesis

Bao, B., Kellman, B. P., Chiang, A. W. T., Zhang, Y., Sorrentino, J. T., York, A. K., Mohammad, M. A., Haymond, M. W., Bode, L., & Lewis, N. E. (2021) · Nature Communications · doi:10.1038/s41467-021-25183-5 · Cited by 45 · see citing works

From Efficiency to Yield: Exploring Recent Advances in CHO Cell Line Development for Monoclonal Antibodies

Majumdar, S., Desai, R., Hans, A. K., Dandekar, P. P., & Jain, R. D. (2024) · Molecular Biotechnology · doi:10.1007/s12033-024-01060-6 · Cited by 43 · see citing works

Site-specific O-Glycosylation by Polypeptide N-Acetylgalactosaminyltransferase 2 (GalNAc-transferase T2) Co-regulates β1-Adrenergic Receptor N-terminal Cleavage

Goth, C. K., Tuhkanen, H. E., Khan, H., Lackman, J. J., Wang, S., Narimatsu, Y., Hansen, L. H., Overall, C. M., Clausen, H., Schjoldager, K. T.-B. G., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.730614 · Cited by 43 · see citing works

Production of homogeneous glycoprotein with multisite modifications by an engineered N-glycosyltransferase mutant

Song, Q., Wu, Z., Fan, Y., Song, W., Zhang, P., Wang, L., Wang, F., Xu, Y., Wang, P. G., & Cheng, J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.777383 · Cited by 42 · see citing works

Sequential Glycosylation of Proteins with Substrate-Specific N-Glycosyltransferases

Liang, L., Kightlinger, W., Prabhu, S. K., Hockenberry, A. J., Li, C., Wang, L., Jewett, M. C., & Mrksich, M. (2020) · ACS Central Science · doi:10.1021/acscentsci.9b00021 · Cited by 41 · see citing works

Improvements in protein production in mammalian cells from targeted metabolic engineering

Richelle, A., & Lewis, N. E. (2017) · Current Opinion in Systems Biology · doi:10.1016/j.coisb.2017.05.019 · Cited by 40 · see citing works

A flow cytometric approach to engineering Escherichia coli for improved eukaryotic protein glycosylation

Glasscock, C. J., Yates, L. E., Jaroentomeechai, T., Wilson, J. D., Merritt, J. H., Lucks, J. B., & DeLisa, M. P. (2018) · Metabolic Engineering · doi:10.1016/j.ymben.2018.04.014 · Cited by 40 · see citing works

Targeted Gene Deletion Using DNA-Free RNA-Guided Cas9 Nuclease Accelerates Adaptation of CHO Cells to Suspension Culture

Lee, N., Shin, J., Park, J. H., Lee, G. M., Cho, S., & Cho, B. (2016) · ACS Synthetic Biology · doi:10.1021/acssynbio.5b00249 · Cited by 41 · see citing works

A Knowledge-Based System for Display and Prediction of O-Glycosylation Network Behaviour in Response to Enzyme Knockouts

McDonald, A. G., Tipton, K. F., & Davey, G. P. (2016) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004844 · Cited by 39 · 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

Glycoengineering design options for IgG1 in CHO cells using precise gene editing

Schulz, M. A., Tian, W., Mao, Y., Coillie, J. V., Sun, L., Larsen, J. S., Chen, Y., Kristensen, C., Vakhrushev, S. Y., Clausen, H., et al. (2018) · Glycobiology · doi:10.1093/glycob/cwy022 · Cited by 39 · 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

Predictive glycoengineering of biosimilars using a Markov chain glycosylation model

Spahn, P. N., Hansen, A. H., Kol, S., Voldborg, B. G. R., & Lewis, N. E. (2016) · Biotechnology Journal · doi:10.1002/biot.201600489 · Cited by 37 · see citing works

CRISPR/Cas9‐Multiplexed Editing of Chinese Hamster Ovary B4Gal‐T1, 2, 3, and 4 Tailors N‐Glycan Profiles of Therapeutics and Secreted Host Cell Proteins

Amann, T., Hansen, A. H., Kol, S., Lee, G. M., Andersen, M. R., & Kildegaard, H. F. (2018) · Biotechnology Journal · doi:10.1002/biot.201800111 · Cited by 37 · see citing works

NMR of glycoproteins: profiling, structure, conformation and interactions

Unione, L., Ardá, A., Jiménez‐Barbero, J., & Millet, Ó. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.09.009 · Cited by 37 · see citing works

Model Transferability and Reduced Experimental Burden in Cell Culture Process Development Facilitated by Hybrid Modeling and Intensified Design of Experiments

Bayer, B., Duerkop, M., Striedner, G., & Sissolak, B. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.740215 · Cited by 38 · see citing works

Glycoengineering of plants yields glycoproteins with polysialylation and other defined N-glycoforms

Chen, Q. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1610803113 · Cited by 37 · see citing works

A synthetic transcription platform for programmable gene expression in mammalian cells

Chen, W. C. W., Gaidukov, L., Lai, Y., Wu, M.-R., Cao, J., Gutbrod, M. J., Choi, G. C. G., Utomo, R. P., Chen, Y.-C., Wróblewska, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33287-9 · Cited by 36 · see citing works

Multiplexed engineering glycosyltransferase genes in CHO cells via targeted integration for producing antibodies with diverse complex-type N-glycans

Nguyen, N., Lin, J., Tay, S. J., Mariati, Yeo, J. H. M., Nguyen‐Khuong, T., & Yang, Y. (2021) · Scientific Reports · doi:10.1038/s41598-021-92320-x · Cited by 36 · see citing works

Understanding glycoprotein structural heterogeneity and interactions: Insights from native mass spectrometry

Wu, D., & Robinson, C. V. (2022) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102351 · Cited by 36 · see citing works

Adolescent meal patterns: grazing habits in the west of Scotland.

Anderson, A. S., MacIntyre, S., & West, P. (1993) · PubMed · Cited by 35 · see citing works

Understanding of decreased sialylation of Fc‐fusion protein in hyperosmotic recombinant Chinese hamster ovary cell culture: <i>N</i>‐glycosylation gene expression and <i>N</i>‐linked glycan antennary profile

Lee, J. H., Jeong, Y. R., Kim, Y., & Lee, G. M. (2017) · Biotechnology and Bioengineering · doi:10.1002/bit.26284 · Cited by 34 · see citing works

Cell-Free Synthetic Glycobiology: Designing and Engineering Glycomolecules Outside of Living Cells

Jaroentomeechai, T., Taw, M. N., Li, M., Aquino, A. K., Agashe, N., Chung, S. S., Jewett, M. C., & DeLisa, M. P. (2020) · Frontiers in Chemistry · doi:10.3389/fchem.2020.00645 · Cited by 35 · see citing works

Identification of global inhibitors of cellular glycosylation

Sørensen, D. M., Büll, C., Madsen, T. D., Lira‐Navarrete, E., Clausen, T. M., Clark, A. E., Garretson, A. F., Karlsson, R. T. G., Pijnenborg, J. F. A., Yin, X., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36598-7 · Cited by 35 · see citing works

Droplet size influences division of mammalian cell factories in droplet microfluidic cultivation

Rajeswari, P. K. P., Joensson, H. N., & Svahn, H. A. (2016) · Electrophoresis · doi:10.1002/elps.201600316 · Cited by 34 · see citing works

Activity of N-acylneuraminate-9-phosphatase (NANP) is not essential for de novo sialic acid biosynthesis

Willems, A. P., Sun, L., Schulz, M. A., Tian, W., Ashikov, A., van Scherpenzeel, M., Hermans, E., Clausen, H., Yang, Z., & Lefeber, D. J. (2019) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2019.05.011 · Cited by 33 · see citing works

ANALYSIS OF CARBOHYDRATES AND GLYCOCONJUGATES BY MATRIX‐ASSISTED LASER DESORPTION/IONIZATION MASS SPECTROMETRY: AN UPDATE FOR 2015–2016

Harvey, D. J. (2021) · Mass Spectrometry Reviews · doi:10.1002/mas.21651 · Cited by 33 · see citing works

N‐glycan maturation mutants in Lotus japonicus for basic and applied glycoprotein research

Pedersen, C. T., Loke, I., Lorentzen, A. M., Wolf, S., Kamble, M., Kristensen, S. K., Munch, D., Radutoiu, S., Spillner, E., Roepstorff, P., et al. (2017) · The Plant Journal · doi:10.1111/tpj.13570 · Cited by 33 · see citing works

CRISPR Technologies in Chinese Hamster Ovary Cell Line Engineering

Glinšek, K., Bozovičar, K., & Bratkovič, T. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24098144 · Cited by 35 · 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

Zinc supplementation decreases galactosylation of recombinant IgG in CHO cells

Prabhu, A., Gadre, R. V., & Gadgil, M. (2018) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-018-9064-8 · Cited by 32 · see citing works

Design of Optimal CHO Protein N-glycosylation Profiles

Amann, T. (2018) · Technical University of Denmark, DTU Orbit (Technical University of Denmark, DTU)

Systems Glycoengineering: Integrated Analyses of Glycomics, Transcriptomics and Phenotypic Data Reveal Complex Cellular Response to Glycoengineering in CHO Cells

Chiang, W.-T., Gazestani, V., Bao, B., Liang, C., Sorrention, J. T., Kellman, B. P., Ménard, P., Arnsdorf, J., Sukhova, Z., Bjørn, S. P., et al. (2020) · The FASEB Journal · doi:10.1096/fasebj.2020.34.s1.07419

Glycosylation engineering in chinese hamster ovary (CHO) cells

Prati, E. G. P. (1999) · Repository for Publications and Research Data (ETH Zurich) · doi:10.3929/ethz-a-003880454

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

Optimizing Chinese hamster ovary cell line development via targeted control of N-glycosylation

Alves, C. S., & Prajapati, S. (2015) · Pharmaceutical Bioprocessing · doi:10.4155/pbp.15.25 · Cited by 4 · see citing works