Evidence map›Paper›PMID 22634260›Full record

ReviewArchives of biochemistry and biophysics2012

IgG-Fc glycoengineering in non-mammalian expression hosts.

Andreas Loos, Herta Steinkellner

Abstract readReview
In one paragraph

Review in Archives of biochemistry and biophysics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Article
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  4. Review
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  6. Review
  7. FUT8 Alpha-(1,6)-Fucosyltransferase in Cancer.International journal of molecular sciences · 2021
    Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Expression and glycoengineering of functionally active heteromultimeric IgM in plants.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

2 authors.

Andreas LoosDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria. andreas.loos@boku.ac.at
Herta Steinkellner

Funding

Austrian Science Fund FWF L 575
6 · The paper itself

Abstract

The remarkable success of therapeutic applications of immunoglobulin G (IgG) in form of monoclonal antibodies and pooled immunoglobulin G preparations has directed attention to this class of glycoproteins. It is commonly appreciated that oligosaccharides attached to the Fc-region play a critical role in the biological activity of IgGs. Thus, glycosylation has been a focus of interest for many scientists and the biopharmaceutical industry and expression hosts have been engineered in order to optimize antibody products. In this review we focus on efforts towards a targeted manipulation of IgG-Fc N-glycans using non-mammalian expression hosts, i.e. yeast, insect cells and plants. Current achievements in generating human-like N-glycan structures will be presented and recent data on the molecular mechanisms that might explain how these potent drugs mediate in vivo activities will be discussed.

Indexed as

AnimalsAntibodies, MonoclonalCloning, MolecularGene ExpressionGlycosylationHumansImmunoglobulin Fc FragmentsImmunoglobulin GPlantsPolysaccharidesProtein EngineeringYeastsAntibodies, MonoclonalImmunoglobulin Fc FragmentsImmunoglobulin GPolysaccharides

Identifiers

PMID22634260
PMCPMC3442181

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.