GlycoDelete engineering of mammalian cells simplifies N-glycosylation of recombinant proteins

Skyline: an open source document editor for creating and analyzing targeted proteomics experiments

MacLean, B., Tomazela, D. M., Shulman, N., Chambers, M., Finney, G. L., Frewen, B., Kern, R., Tabb, D. L., Liebler, D. C., & MacCoss, M. J. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq054 · Cited by 4,697

FcRn: the neonatal Fc receptor comes of age

Roopenian, D. C., & Akilesh, S. (2007) · Nature Reviews Immunology · doi:10.1038/nri2155 · Cited by 2,346

Increasing the efficacy of CD20 antibody therapy through the engineering of a new type II anti-CD20 antibody with enhanced direct and immune effector cell–mediated B-cell cytotoxicity

Mössner, E., Brünker, P., Moser, S., Püntener, U., Schmidt, C., Herter, S., Grau, R., Gerdes, C. A., Nopora, A., van Puijenbroek, E., et al. (2010) · Blood · doi:10.1182/blood-2009-06-225979 · Cited by 983

An improved colorimetric assay for interleukin 2

Tada, H., Shiho, O., Kuroshima, K.-I., Koyama, M., & Tsukamoto, K. (1986) · Journal of Immunological Methods · doi:10.1016/0022-1759(86)90183-3 · Cited by 871

Thermofluor-based high-throughput stability optimization of proteins for structural studies

Ericsson, U. B., Hällberg, B. M., DeTitta, G. T., Dekker, N., & Nordlund, P. (2006) · Analytical Biochemistry · doi:10.1016/j.ab.2006.07.027 · Cited by 840

Glycosylation as a strategy to improve antibody-based therapeutics

Jefferis, R. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2804 · Cited by 829

Establishment and characterization of a unique human cell line that proliferates dependently on GM‐CSF, IL‐3, or erythropoietin

Kitamura, T., Tange, T., Terasawa, T., Chiba, S., Kuwaki, T., Miyagawa, K., Piao, Y., Miyazono, K., Urabe, A., & Takaku, F. (1989) · Journal of Cellular Physiology · doi:10.1002/jcp.1041400219 · Cited by 784

Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N -acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line

Reeves, P. J., Callewaert, N., Contreras, R., & Khorana, H. G. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212519299 · Cited by 641

Intracellular Signaling by the Unfolded Protein Response

Bernales, S., Papa, F. R., & Walter, P. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.21.122303.120200 · Cited by 543

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 1,353

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 365

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

Glycoconjugates: Synthesis, Functional Studies, and Therapeutic Developments

Shivatare, S. S., Shivatare, V. S., & Wong, C. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c01032 · Cited by 266

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 243

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

Single-pot glycoprotein biosynthesis using a cell-free transcription-translation system enriched with glycosylation machinery

Jaroentomeechai, T., Stark, J. C., Natarajan, A., Glasscock, C. J., Yates, L. E., Hsu, K. J., Mrksich, M., Jewett, M. C., & DeLisa, M. P. (2018) · Nature Communications · doi:10.1038/s41467-018-05110-x · Cited by 201

Cell-Free Synthetic Biology: Engineering Beyond the CellPreprint

Perez, J. G., Stark, J. C., & Jewett, M. C. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a023853 · Cited by 200

Quo vadis? The challenges of recombinant protein folding and secretion in Pichia pastoris

Puxbaum, V., Mattanovich, D., & Gasser, B. (2015) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-015-6470-z · Cited by 178

Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation

Hurlburt, N. K., Seydoux, E., Wan, Y.-H., Edara, V. V., Stuart, A. B., Feng, J., Suthar, M. S., McGuire, A. T., Stamatatos, L., & Pancera, M. (2020) · Nature Communications · doi:10.1038/s41467-020-19231-9 · Cited by 162

Towards the next generation of biomedicines by site-selective conjugation

Hu, Q., Berti, F., & Adamo, R. (2016) · Chemical Society Reviews · doi:10.1039/c4cs00388h · Cited by 167

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

Advanced Plant-Based Glycan Engineering

Montero‐Morales, L., & Steinkellner, H. (2018) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2018.00081 · Cited by 135

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

Impact of Glycerol as Carbon Source onto Specific Sugar and Inducer Uptake Rates and Inclusion Body Productivity in E. coli BL21(DE3)

Kopp, J., Slouka, C., Ulonska, S., Kager, J., Fricke, J., Oliver Spadiut, A., & Herwig, C. (2017) · Bioengineering · doi:10.3390/bioengineering5010001 · Cited by 120

Glycan-Based Cell Targeting To Modulate Immune Responses

Johannssen, T., & Lepenies, B. (2016) · Trends in biotechnology · doi:10.1016/j.tibtech.2016.10.002 · Cited by 118

Affecting HEK293 Cell Growth and Production Performance by Modifying the Expression of Specific Genes

Abaandou, L., Quan, D. N., & Shiloach, J. (2021) · Cells · doi:10.3390/cells10071667 · Cited by 116

The ABCs of PTMs

Barber, K. W., & Rinehart, J. (2018) · Nature Chemical Biology · doi:10.1038/nchembio.2572 · Cited by 101

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 103

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 99

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 95

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 99

Glycan characterization of biopharmaceuticals: Updates and perspectives

Planinc, A., Bones, J., Dejaegher, B., Antwerpen, P. V., & Delporte, C. (2016) · Analytica Chimica Acta · doi:10.1016/j.aca.2016.03.049 · Cited by 91

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 82

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

Expression of eukaryotic membrane proteins in eukaryotic and prokaryotic hosts

Kesidis, A., Depping, P., Lodé, A., Vaitsopoulou, A., Bill, R. M., Goddard, A. D., & Rothnie, A. J. (2020) · Methods · doi:10.1016/j.ymeth.2020.06.006 · Cited by 85

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 86

Extended O-GlcNAc on HLA Class-I-Bound Peptides

Marino, F., Bern, M. W., Mommen, G. P. M., Leney, A. C., den Brink, J. A. M. V. G.-V., Bonvin, A. M. J. J., Becker, C. H., van Els, C. A. C. M., & Heck, A. J. R. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b06586 · Cited by 78

Bioconjugation – using selective chemistry to enhance the properties of proteins and peptides as therapeutics and carriers

Gunnoo, S. B., & Madder, A. (2016) · Organic & Biomolecular Chemistry · doi:10.1039/c6ob00808a · Cited by 79

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

Progress in the development of subunit vaccines for gastrointestinal nematodes of ruminants

Matthews, J. B., Geldhof, P., Tzelos, T., & Claerebout, E. (2016) · Parasite Immunology · doi:10.1111/pim.12391 · Cited by 67

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

Plant specific N-glycans do not have proven adverse effects in humans

Shaaltiel, Y., & Tekoah, Y. (2016) · Nature Biotechnology · doi:10.1038/nbt.3556 · Cited by 67

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

Glycosylation Shapes the Efficacy and Safety of Diverse Protein, Gene and Cell Therapies

Rocamora, F., Peralta, A. G., Shin, S., Sorrentino, J., Wu, M. Y. M., Toth, E. A., Fuerst, T. R., & Lewis, N. E. (2023) · Biotechnology Advances · doi:10.1016/j.biotechadv.2023.108206 · Cited by 67

Custom made inclusion bodies: impact of classical process parameters and physiological parameters on inclusion body quality attributes

Slouka, C., Kopp, J., Hutwimmer, S., Strahammer, M., Strohmer, D., Eitenberger, E., Schwaighofer, A., & Herwig, C. (2018) · Microbial Cell Factories · doi:10.1186/s12934-018-0997-5 · Cited by 63

Stable mammalian producer cell lines for structural biology

Büssow, K. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.03.002 · Cited by 60

Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: an update for 2013–2014

Harvey, D. J. (2018) · Mass Spectrometry Reviews · doi:10.1002/mas.21530 · Cited by 61

Plant glyco-biotechnology on the way to synthetic biology

Loos, A., & Steinkellner, H. (2014) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00523 · Cited by 56

Hijacking bacterial glycosylation for the production of glycoconjugates, from vaccines to humanised glycoproteins

Cuccui, J., & Wren, B. W. (2014) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.12321 · Cited by 55

Engineering orthogonal human O-linked glycoprotein biosynthesis in bacteria

Natarajan, A., Jaroentomeechai, T., Cabrera-Sánchez, M., Mohammed, J. C., Cox, E. C., Young, O., Shajahan, A., Vilkhovoy, M., Vadhin, S., Varner, J. D., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0595-9 · Cited by 53

Using GlycoDelete to produce proteins lacking plant-specific N-glycan modification in seeds

Piron, R., Santens, F., Paepe, A. D., Depicker, A., & Callewaert, N. (2015) · Nature Biotechnology · doi:10.1038/nbt.3359 · Cited by 49

Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies

Le, N. P. L., Bowden, T. A., Struwe, W. B., & Crispin, M. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.04.016 · Cited by 48

Reexamining opportunities for therapeutic protein production in eukaryotic microorganisms

Matthews, C. B., Wright, C. M., Kuo, A., Colant, N., Westoby, M., & Love, J. C. (2017) · Biotechnology and Bioengineering · doi:10.1002/bit.26378 · Cited by 47

Systems glycobiology for glycoengineering

Spahn, P. N., & Lewis, N. E. (2014) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2014.08.004 · Cited by 46

On the glycosylation aspects of biosimilarity

Hajba, L., Szekrényes, Á., Borza, B., & Guttman, A. (2018) · Drug Discovery Today · doi:10.1016/j.drudis.2018.01.009 · Cited by 47

Plant glycoengineering for designing next-generation vaccines and therapeutic proteins

Strasser, R. (2023) · Biotechnology Advances · doi:10.1016/j.biotechadv.2023.108197 · Cited by 43

Structure and Assembly Mechanism of the Signaling Complex Mediated by Human CSF-1

Félix, J., Munck, S. D., Verstraete, K., Meuris, L., Callewaert, N., Elegheert, J., & Savvides, S. N. (2015) · Structure · doi:10.1016/j.str.2015.06.019 · Cited by 45

N-Glycosylation Fingerprinting of Viral Glycoproteins by xCGE-LIF

Hennig, R., Rapp, E., Kottler, R., Cajic, S., Borowiak, M., & Reichl, U. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2874-3_8 · Cited by 42

Modulating antibody effector functions by Fc glycoengineering

García-Alija, M., Moer, B. V., Sastre, D. E., Azzam, T., Du, J. J., Trastoy, B., Callewaert, N., Sundberg, E. J., & Guerin, M. E. (2023) · Biotechnology Advances · doi:10.1016/j.biotechadv.2023.108201 · Cited by 43

High-throughput profiling of nucleotides and nucleotide sugars to evaluate their impact on antibody N-glycosylation

Villiger, T. K., Steinhoff, R., Ivarsson, M., Solacroup, T., Stettler, M., Broly, H., Krismer, J., Pabst, M., Zenobi, R., Morbidelli, M., et al. (2016) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2016.04.039 · Cited by 41

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

Genetic disruption of multiple α1,2-mannosidases generates mammalian cells producing recombinant proteins with high-mannose–type N-glycans

Jin, Z., Kitajima, T., Dong, W., Huang, Y., Ren, W.-W., Guan, F., Chiba, Y., Gao, X., & Fujita, M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.813030 · Cited by 40

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

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 42

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 41

Immobilized enzyme cascade for targeted glycosylation

Makrydaki, E., Donini, R., Krueger, A., Royle, K. E., Moya‐Ramírez, I., Kuntz, D. A., Rose, D. R., Haslam, S. M., Polizzi, K. M., & Kontoravdi, C. (2024) · Nature Chemical Biology · doi:10.1038/s41589-023-01539-4 · Cited by 38

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

Exposing the molecular heterogeneity of glycosylated biotherapeutics

Schachner, L. F., Mullen, C., Phung, W., Hinkle, J. D., Beardsley, M. I., Bentley, T., Day, P., Tsai, C., Sukumaran, S., Baginski, T., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47693-8 · Cited by 36

Biomanufacturing of protective antibodies and other therapeutics in edible plant tissues for oral applications

Juárez, P., Virdi, V., Depicker, A., & Orzáez, D. (2016) · Plant Biotechnology Journal · doi:10.1111/pbi.12541 · Cited by 37

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

Glycosylation profiles determine extravasation and disease-targeting properties of armed antibodies

Venetz, D., Hess, C., Lin, C., Aebi, M., & Neri, D. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1416694112 · Cited by 33

Expression of Lectins in Heterologous Systems

Martínez-Alarcón, D., Blanco‐Labra, A., & García-Gasca, T. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020616 · Cited by 33

Glycoprotein Semisynthesis by Chemical Insertion of Glycosyl Asparagine Using a Bifunctional Thioacid-Mediated Strategy

Nomura, K., Maki, Y., Okamoto, R., Satoh, A., & Kajihara, Y. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c02601 · Cited by 33

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

Glycosylation of Recombinant Anticancer Therapeutics in Different Expression Systems with Emerging Technologies

Nadeem, T., Khan, M. A., Ijaz, B., Ahmed, N., Rahman, Z. U., Latif, M. S., Ali, Q., & Rana, M. A. (2018) · Cancer Research · doi:10.1158/0008-5472.can-18-0032 · Cited by 32

Magnetophoretic Conductors and Diodes in a 3D Magnetic Field

Abedini‐Nassab, R., Joh, D. Y., Triggiano, M. A., Baker, C. D., Chilkoti, A., Murdoch, D. M., & Yellen, B. B. (2015) · Advanced Functional Materials · doi:10.1002/adfm.201503898 · Cited by 30

Are glycan biosensors an alternative to glycan microarrays?

Hushegyi, A., & Tkáč, J. (2014) · Analytical Methods · doi:10.1039/c4ay00692e · Cited by 28

Simply better glycoproteins

Lepenies, B., & Seeberger, P. H. (2014) · Nature Biotechnology · doi:10.1038/nbt.2893 · Cited by 27

Modular Integrated Secretory System Engineering in Pichia pastoris To Enhance G-Protein Coupled Receptor Expression

Claes, K., Vandewalle, K., Laukens, B., Laeremans, T., Vosters, O., Langer, I., Parmentier, M., Steyaert, J., & Callewaert, N. (2016) · ACS Synthetic Biology · doi:10.1021/acssynbio.6b00032 · Cited by 27

Inclusion Body Bead Size in E. coli Controlled by Physiological Feeding

Kopp, J., Slouka, C., Strohmer, D., Kager, J., Oliver Spadiut, A., & Herwig, C. (2018) · Microorganisms · doi:10.3390/microorganisms6040116 · Cited by 26

Modulating carbohydrate–protein interactions through glycoengineering of monoclonal antibodies to impact cancer physiology

Chiang, A. W. T., Li, S., Spahn, P. N., Richelle, A., Kuo, C., Samoudi, M., & Lewis, N. E. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.08.008 · Cited by 25

Production of recombinant human acid α-glucosidase with high-mannose glycans in gnt1 rice for the treatment of Pompe disease

Jung, J., Huy, N.-X., Kim, H.-B., Kim, N.-S., Giap, V., & Yang, M. (2017) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2017.03.033 · Cited by 25

Glycoengineering of HEK293 cells to produce high-mannose-type N-glycan structures

Ren, W., Jin, Z., Dong, W., Kitajima, T., Gao, X., & Fujita, M. (2019) · The Journal of Biochemistry · doi:10.1093/jb/mvz032 · Cited by 24

Membrane traffic related to endosome dynamics and protein secretion in filamentous fungi

Higuchi, Y. (2021) · Bioscience Biotechnology and Biochemistry · doi:10.1093/bbb/zbab004 · Cited by 23

Recent advances in engineering yeast for pharmaceutical protein production

Fidan, Ö., & Zhan, J. (2015) · RSC Advances · doi:10.1039/c5ra13003d · Cited by 26

Inactivation of N-Acetylglucosaminyltransferase I and α1,3-Fucosyltransferase Genes in Nicotiana tabacum BY-2 Cells Results in Glycoproteins With Highly Homogeneous, High-Mannose N-Glycans

Herman, X., Far, J., Courtoy, A., Bouhon, L., Quinton, L., Pauw, E. D., Chaumont, F., & Navarre, C. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.634023 · Cited by 22

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

Post-translational and transcriptional dynamics – regulating extracellular vesicle biology

Claridge, B., Kastaniegaard, K., Stensballe, A., & Greening, D. W. (2018) · Expert Review of Proteomics · doi:10.1080/14789450.2019.1551135 · Cited by 21

New Mammalian Expression Systems

Zhu, J., & Hatton, D. (2017) · Advances in biochemical engineering, biotechnology · doi:10.1007/10_2016_55 · Cited by 22

The sweet branch of metabolic engineering: cherry-picking the low-hanging sugary fruits

Chen, R. (2015) · Microbial Cell Factories · doi:10.1186/s12934-015-0389-z · Cited by 20

Optimized expression of the Starmerella bombicola lactone esterase in Pichia pastoris through temperature adaptation, codon-optimization and co-expression with HAC1

Waele, S. D., Vandenberghe, I. H. M., Laukens, B., Planckaert, S., Verweire, S., Bogaert, I. V., Soetaert, W., Devreese, B. V., & Ciesielska, K. (2017) · Protein Expression and Purification · doi:10.1016/j.pep.2017.10.016 · Cited by 20

Quantitative glycomics using liquid phase separations coupled to mass spectrometry

Smith, J., Mittermayr, S., Váradi, C., & Bones, J. (2017) · The Analyst · doi:10.1039/c6an02715f · Cited by 19

Monitoring and control strategies for inclusion body production in E. coli based on glycerol consumption

Slouka, C., Kopp, J., Strohmer, D., Kager, J., Oliver Spadiut, A., & Herwig, C. (2019) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2019.03.014 · Cited by 19

An Engineered Pathway for Production of Terminally Sialylated N-glycoproteins in the Periplasm of Escherichia coli

Zhu, J., Ruan, Y., Fu, X., Zhang, L.-C., Ge, G.-S., Wall, J., Zou, T., Zheng, Y., Ding, N., & Hu, X.-J. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.00313 · Cited by 19

Cellular and Molecular Engineering of Glycan Sialylation in Heterologous Systems

Hombu, R., Neelamegham, S., & Park, S. (2021) · Molecules · doi:10.3390/molecules26195950 · 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

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Hasan, M., Khakzad, H., Happonen, L., Sundin, A., Unge, J., Müeller, U., Malmström, J. A., Westergren‐Thorsson, G., Malmström, L., Ellervik, U., et al. (2020) · Chemical Science · doi:10.1039/d0sc05971d · Cited by 17

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van Schie, L., Breedam, W. V., Roels, C., Schepens, B., Frank, M., Mehdipour, A. R., Laukens, B., Nerinckx, W., Santens, F., Devos, S., et al. (2023) · mAbs · doi:10.1080/19420862.2023.2210709 · Cited by 12

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(2014) · Science-Business eXchange · doi:10.1038/scibx.2014.598