ReviewmAbs
Biochemical and biophysical characterization of humanized IgG1 produced in Pichia pastoris.
Review in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
13 citing papers in PubMed, 33 citations in OpenAlex.
- Analytical Physicochemical and Functional Studies to Compare AryoTrust, a Follow-On Biologics, with the Originator Trastuzumab (Herceptin).Pharmaceutics · 2026Article
- Recent Advances Toward Engineering Glycoproteins Using Modified Yeast Display Platforms.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Fermentation, Purification, and Tumor Inhibition of a Disulfide-Stabilized Diabody Against Fibroblast Growth Factor-2.Frontiers in oncology · 2021Article
- Recent progress in the molecular imaging of therapeutic monoclonal antibodies.Journal of pharmaceutical analysis · 2020Review
- A Simple Strategy to Eliminate Hexosylation Bias in the Relative Quantification of N-Glycosylation in Biopharmaceuticals.Angewandte Chemie (International ed. in English) · 2020Article
- Immunogenicity Risk Assessment for an Engineered Human Cytokine Analogue Expressed in Different Cell Substrates.The AAPS journal · 2020Review
- Glycosylation engineering of therapeutic IgG antibodies: challenges for the safety, functionality and efficacy.Protein & cell · 2018Review
- Characterization and high-yield production of non-Engineering in life sciences · 2017Article
- Engineering yeast for producing human glycoproteins: where are we now?Future microbiology · 2015Article
- High-throughput biophysical analysis and data visualization of conformational stability of an IgG1 monoclonal antibody after deglycosylation.Journal of pharmaceutical sciences · 2013Article
- Investigating the physiological response of Pichia (Komagataella) pastoris GS115 to the heterologous expression of misfolded proteins using chemostat cultures.Applied microbiology and biotechnology · 2013Article
- Reconstruction and visualization of carbohydrate, N-glycosylation pathways in Pichia pastoris CBS7435 using computational and system biology approaches.Systems and synthetic biology · 2013Article
- Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The first full length IgG produced in Pichia pastoris was reported in late 1980. However, use of a wild-type Pichia expression system to produce IgGs with human-like N-linked glycans was not possible until recently. Advances in glycoengineering have enabled organisms such as Pichia to mimic human N-glycan biosynthesis and produce IgGs with human glycans on an industrial scale. Since there are only a few reports of the analytical characterization of Pichia-produced IgG, we summarize the results known in this field, and provide additional characterization data generated in our laboratories. The data suggest that Pichia-produced IgG has the same stability as that produced in Chinese hamster ovary (CHO) cells. It has similar aggregation profiles, charge variant distribution and oxidation levels as those for a CHO IgG. It contains human N-linked glycans and O-linked single mannose. Because of the comparable biophysical and biochemical characteristics, glycoengineered Pichia pastoris is an attractive expression system for therapeutic IgG productions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.