Evidence map›Paper›PMID 29492730›Full record

ArticleJournal of biomolecular NMR2018

Stable isotope labeling approaches for NMR characterization of glycoproteins using eukaryotic expression systems.

Saeko Yanaka, Hirokazu Yagi, Rina Yogo, Maho Yagi-Utsumi, Koichi Kato

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of biomolecular NMR, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
–field-weighted citation impact
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

30 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. 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
  5. Glycoprotein Preparation by Heterologous Expression.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  6. Automated Assignment ofJournal of the American Society for Mass Spectrometry · 2024
    Article
  7. Article
  8. Uniform [Journal of biomolecular NMR · 2024
    Article
  9. Synthesis ofOrganic & biomolecular chemistry · 2023
    Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
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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.

Saeko YanakaInstitute for Molecular Science and Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, 444-8787, Japan.
Hirokazu YagiGraduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya, 467-8603, Japan.
Rina YogoInstitute for Molecular Science and Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, 444-8787, Japan.
Maho Yagi-UtsumiInstitute for Molecular Science and Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, 444-8787, Japan.
Koichi KatoInstitute for Molecular Science and Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, 444-8787, Japan. kkatonmr@ims.ac.jp.

Funding

Japan Society for the Promotion of Science JP15K07935Japan Society for the Promotion of Science JP17H05893Japan Society for the Promotion of Science JP17H06414Japan Society for the Promotion of Science JP25102008
6 · The paper itself

Abstract

Glycoproteins are characterized by the heterogeneous and dynamic nature of their glycan moieties, which hamper crystallographic analysis. NMR spectroscopy provides potential advantages in dealing with such complicated systems, given that the target molecules can be isotopically labeled. Methods of metabolic isotope labeling in recombinant glycoproteins have been developed recently using a variety of eukaryotic production vehicles, including mammalian, yeast, insect, and plant cells, each of which has a distinct N-glycan diversification pathway. Yeast genetic engineering has enabled the overexpression of homogeneous high-mannose-type oligosaccharides with

Indexed as

Carbon IsotopesEukaryotic CellsGlycoproteinsImmunoglobulin Fc FragmentsIsotope LabelingNuclear Magnetic Resonance, BiomolecularProtein EngineeringRecombinant ProteinsCarbon-13Carbon IsotopesGlycoproteinsImmunoglobulin Fc FragmentsRecombinant ProteinsAntibodyEukaryotic expression systemGlycoproteinOligosaccharideSerumStable isotope labeling

Identifiers

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.