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  1. No Access

    Article

    Optimization of humanized IgGs in glycoengineered Pichia pastoris

    As the fastest growing class of therapeutic proteins, monoclonal antibodies (mAbs) represent a major potential drug class1. Human antibodies are glycosylated in their native state and all clinically approved mAbs...

    Huijuan Li, Natarajan Sethuraman, Terrance A Stadheim, Dongxing Zha… in Nature Biotechnology (2006)

  2. No Access

    Article

    Use of high-performance anion exchange chromatography with pulsed amperometric detection for O-glycan determination in yeast

    O-glycosylation is a post-translational protein modification that occurs in all eukaryotes. Yeasts have received increasing attention as a host for therapeutic protein production because of their ability to se...

    Terrance A Stadheim, Huijuan Li, Warren Kett, Irina N Burnina… in Nature Protocols (2008)

  3. No Access

    Article

    Recombinant human lactoferrin expressed in glycoengineered Pichia pastoris: effect of terminal N-acetylneuraminic acid on in vitro secondary humoral immune response

    Traditional production of therapeutic glycoproteins relies on mammalian cell culture technology. Glycoproteins produced by mammalian cells invariably display N-glycan heterogeneity resulting in a mixture of gl...

    Byung-Kwon Choi, Jeffrey K. Actor, Sandra Rios, Marc d’Anjou… in Glycoconjugate Journal (2008)

  4. No Access

    Protocol

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

    The production of recombinant therapeutic glycoproteins is an active area of research and drug development. Typically, improvements in therapeutic glycoprotein efficacy have focused on engineering additional N...

    Bing Gong, Michael Cukan, Richard Fisher, Huijuan Li, Terrance A. Stadheim… in Glycomics (2009)

  5. No Access

    Article

    High-throughput screening and selection of yeast cell lines expressing monoclonal antibodies

    The methylotrophic yeast Pichia pastoris has recently been engineered to express therapeutic glycoproteins with uniform human N-glycans at high titers. In contrast to the current art where producing therapeutic p...

    Gavin C. Barnard, Angela R. Kull… in Journal of Industrial Microbiology & Biote… (2010)

  6. Article

    Open Access

    Generation of diploid Pichia pastoris strains by mating and their application for recombinant protein production

    Yeast mating provides an efficient means for strain and library construction. However, biotechnological applications of mating in the methylotrophic yeast Pichia pastoris have been hampered because of concerns ab...

    Ming-Tang Chen, Song Lin, Ishaan Shandil, Dewan Andrews… in Microbial Cell Factories (2012)

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  7. Article

    Erratum to: Improvement of N-glycan site occupancy of therapeutic glycoproteins produced in Pichia pastoris

    Byung-Kwon Choi, Shannon Warburton, He** Lin… in Applied Microbiology and Biotechnology (2012)

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  8. No Access

    Article

    Improvement of N-glycan site occupancy of therapeutic glycoproteins produced in Pichia pastoris

    Yeast is capable of performing posttranslational modifications, such as N- or O-glycosylation. It has been demonstrated that N-glycans play critical biological roles in therapeutic glycoproteins by modulating pha...

    Byung-Kwon Choi, Shannon Warburton, He** Lin… in Applied Microbiology and Biotechnology (2012)

  9. No Access

    Article

    The Impact of Glycosylation on the Pharmacokinetics of a TNFR2:Fc Fusion Protein Expressed in Glycoengineered Pichia Pastoris

    P. pastoris has previously been genetically engineered to generate strains that are capable of producing mammalian-like glycoforms. Our objective was to investigate the correlation bet...

    Liming Liu, Sujatha Gomathinayagam, Lora Hamuro… in Pharmaceutical Research (2013)

  10. No Access

    Article

    Elimination of diaminopeptidase activity in Pichia pastoris for therapeutic protein production

    Yeast are important production platforms for the generation of recombinant proteins. Nonetheless, their use has been restricted in the production of therapeutic proteins due to differences in their glycosylati...

    Daniel Hopkins, Sujatha Gomathinayagam… in Applied Microbiology and Biotechnology (2014)