Evidence map›Paper›PMID 23147167›Full record

ArticleBioengineered

Engineering of human-type O-glycosylation in Nicotiana benthamiana plants.

Richard Strasser

Abstract read
In one paragraph

Article in Bioengineered. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Glyco-Engineering of Plant-Based Expression Systems.Advances in biochemical engineering/biotechnology · 2021
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. 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

1 author.

Richard StrasserDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria. richard.strasser@boku.ac.at

Funding

Austrian Science Fund FWF TRP 242
6 · The paper itself

Abstract

Therapeutic properties of recombinant proteins are very often affected by the composition and heterogeneity of their glycans. Conventional expression systems for recombinant pharmaceutical proteins typically do not address this problem and produce a mixture of glycoforms that are neither identical to human glycans nor optimized for enhanced efficacy. In terms of glycosylation, plants offer certain advantages over mammalian cells as the N-glycosylation pathway of plants is comparably simple and a typical mammalian O-glycosylation pathway is not present at all. During the last ten years we have developed a plant-based expression platform for the generation of recombinant glycoproteins with defined N-glycans. Now we have extended our tool-box for glyco-engineering in the tobacco related species Nicotiana benthamiana toward the production of tailored mucin-type O-glycans on recombinant proteins.

Indexed as

GlycosylationHumansNicotianaPlants, Genetically ModifiedRecombinant ProteinsRecombinant Proteinserythropoietinglycoproteinglycosylationmolecular farmingposttranslational modificationrecombinant proteinsialic acid

Identifiers

PMID23147167
PMCPMC3728188

What OpenQuestion holds

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LicenceCC BY-NC
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.