Evidence map›Paper›PMID 34978013›Full record

ArticleJournal of biomolecular NMR2022

Glutamine-free mammalian expression of recombinant glycoproteins with uniform isotope labeling: an application for NMR analysis of pharmaceutically relevant Fc glycoforms of human immunoglobulin G1.

Saeko Yanaka, Hirokazu Yagi, Rina Yogo, Masayoshi Onitsuka, Koichi Kato

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of biomolecular NMR, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Exploring glycoform-dependent dynamic modulations in human immunoglobulin G via computational and experimental approaches.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Glycoprotein Preparation by Heterologous Expression.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  7. Automated Assignment ofJournal of the American Society for Mass Spectrometry · 2024
    Article
  8. Article
  9. A comprehensive assessment of selective amino acidJournal of biomolecular NMR · 2024
    Article
  10. Uniform [Journal of biomolecular NMR · 2024
    Article
  11. A consensus structural motif for the capsular polysaccharide ofProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Saeko YanakaExploratory Research Center on Life and Living Systems (ExCELLS) and Institute for Molecular Science (IMS), National Institutes of Natural Sciences, Okazaki, 444-8787, Japan.ORCID http://orcid.org/0000-0002-3513-5701
Hirokazu YagiGraduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, 467-8603, Japan.ORCID http://orcid.org/0000-0001-9296-0225
Rina YogoExploratory Research Center on Life and Living Systems (ExCELLS) and Institute for Molecular Science (IMS), National Institutes of Natural Sciences, Okazaki, 444-8787, Japan.ORCID http://orcid.org/0000-0002-1595-0194
Masayoshi OnitsukaGraduate School of Technology, Industrial and Social Sciences, Tokushima University, Tokushima, 770-8513, Japan.ORCID http://orcid.org/0000-0003-4220-1401
Koichi KatoExploratory Research Center on Life and Living Systems (ExCELLS) and Institute for Molecular Science (IMS), National Institutes of Natural Sciences, Okazaki, 444-8787, Japan. kkatonmr@ims.ac.jp.ORCID http://orcid.org/0000-0001-7187-9612
National Institutes of Natural Sciences · JPNagoya City University · JPTokushima University · JP

Funding

Japan Agency for Medical Research and Development JP20ae0101062Japan Agency for Medical Research and Development JP21ae0121013h0301Ministry of Education, Culture, Sports, Science and Technology JP19H01017Ministry of Education, Culture, Sports, Science and Technology JP19J15602Ministry of Education, Culture, Sports, Science and Technology JP20K15981
6 · The paper itself

Abstract

Mammalian cells are widely used for producing recombinant glycoproteins of pharmaceutical interest. However, a major drawback of using mammalian cells is the high production costs associated with uniformly isotope-labeled glycoproteins due to the large quantity of labeled L-glutamine required for their growth. To address this problem, we developed a cost-saving method for uniform isotope labeling by cultivating the mammalian cells under glutamine-free conditions, which was achieved by co-expression of glutamine synthase. We demonstrate the utility of this approach using fucosylated and non-fucosylated Fc glycoforms of human immunoglobulin G1.

Indexed as

GlutamineGlycoproteinsAnimalsHumansImmunoglobulinsIsotope LabelingMammalsNuclear Magnetic Resonance, BiomolecularRecombinant ProteinsGlutamineGlycoproteinsImmunoglobulinsRecombinant ProteinsFucoseGlutamine synthaseGlycoproteinMammalian expression systemMetabolic isotope labelingTherapeutic antibody

Identifiers

PMID34978013
OpenAlexW4205616229

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.