Evidence map›Paper›PMID 26175280›Full record

ReviewExpert opinion on biological therapy2015

Using glyco-engineering to produce therapeutic proteins.

Martina Dicker, Richard Strasser

Abstract readReview
In one paragraph

Review in Expert opinion on biological therapy, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
8.5field-weighted citation impact, top 2% 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

34 citing papers in PubMed, 79 citations in OpenAlex.

  1. Recombinant Protein Drugs: A 2025 Update.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
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  10. Review
  11. Review
  12. Article
  13. Process- and Product-Related Foulants in Virus Filtration.Bioengineering (Basel, Switzerland) · 2022
    Review
  14. Review
  15. Article
  16. Article
  17. Impact of Protein Glycosylation on the Design of Viral Vaccines.Advances in biochemical engineering/biotechnology · 2021
    Review
  18. Impact of SpecificFrontiers in plant science · 2021
    Article
  19. Article
  20. Cell-free systems for accelerating glycoprotein expression and biomanufacturing.Journal of industrial microbiology & biotechnology · 2020
    Review
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 at 2 institutions in 2 countries.

Martina Dickera 1 University of Natural Resources and Life Sciences , Department of Applied Genetics and Cell Biology , Muthgasse 18, Vienna, Austria.
Richard Strasserb 2 University of Natural Resources and Life Sciences, Department of Applied Genetics and Cell Biology , Muthgasse 18, Vienna, Austria +43 1 47654 6705 ; +43 1 47654 6392 ; richard.strasser@boku.ac.at.
BOKU University · ATWeatherford College · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

introductionGlycans are increasingly important in the development of new biopharmaceuticals with optimized efficacy, half-life, and antigenicity. Current expression platforms for recombinant glycoprotein therapeutics typically do not produce homogeneous glycans and frequently display non-human glycans which may cause unwanted side effects. To circumvent these issues, glyco-engineering has been applied to different expression systems including mammalian cells, insect cells, yeast, and plants. AREAS COVERED: This review summarizes recent developments in glyco-engineering focusing mainly on in vivo expression systems for recombinant proteins. The highlighted strategies aim at producing glycoproteins with homogeneous N- and O-linked glycans of defined composition. EXPERT OPINION: Glyco-engineering of expression platforms is increasingly recognized as an important strategy to improve biopharmaceuticals. A better understanding and control of the factors leading to glycan heterogeneity will allow simplified production of recombinant glycoprotein therapeutics with less variation in terms of glycosylation. Further technological advances will have a major impact on manufacturing processes and may provide a completely new class of glycoprotein therapeutics with customized functions.

Indexed as

Antibodies, MonoclonalGlycoproteinsGlycosylationHalf-LifeHumansPolysaccharidesProtein EngineeringRecombinant ProteinsAntibodies, MonoclonalGlycoproteinsPolysaccharidesRecombinant ProteinsbiopharmaceuticalsglycosyltransferasesN-glycosylationO-glycosylationrecombinant glycoprotein

Identifiers

PMID26175280
PMCPMC7100909
OpenAlexW1664984642

What OpenQuestion holds

Textmetadata
LicenceTDM
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.