Evidence map›Paper›PMID 23553222›Full record

ArticlePlant molecular biology2013

Plant species and organ influence the structure and subcellular localization of recombinant glycoproteins.

Elsa Arcalis, Johannes Stadlmann, Thomas Rademacher, Sylvain Marcel, Markus Sack, Friedrich Altmann, Eva Stoger

Abstract read
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In one paragraph

Article in Plant molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

23 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Cell Biology Methods to Study Recombinant Proteins in Seeds.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  7. Glyco-Engineering of Plant-Based Expression Systems.Advances in biochemical engineering/biotechnology · 2021
    Article
  8. Plant Platforms for Efficient Heterologous Protein Production.Biotechnology and bioprocess engineering : BBE · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Edible plants for oral delivery of biopharmaceuticals.British journal of clinical pharmacology · 2017
    Review
  14. Review
  15. Site-targeted mutagenesis for stabilization of recombinant monoclonal antibody expressed in tobacco (Nicotiana tabacum) plants.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

7 authors at 4 institutions in 3 countries.

Elsa ArcalisDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Johannes Stadlmann
Thomas Rademacher
Sylvain Marcel
Markus Sack
Friedrich Altmann
Eva Stoger
BOKU University · ATCaliber Imaging and Diagnostics (United States) · USFraunhofer Institute for Molecular Biology and Applied Ecology · DERWTH Aachen University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many plant-based systems have been developed as bioreactors to produce recombinant proteins. The choice of system for large-scale production depends on its intrinsic expression efficiency and its propensity for scale-up, post-harvest storage and downstream processing. Factors that must be considered include the anticipated production scale, the value and intended use of the product, the geographical production area, the proximity of processing facilities, intellectual property, safety and economics. It is also necessary to consider whether different species and organs affect the subcellular trafficking, structure and qualitative properties of recombinant proteins. In this article we discuss the subcellular localization and N-glycosylation of two commercially-relevant recombinant glycoproteins (Aspergillus niger phytase and anti-HIV antibody 2G12) produced in different plant species and organs. We augment existing data with novel results based on the expression of the same recombinant proteins in Arabidopsis and tobacco seeds, focusing on similarities and subtle differences in N-glycosylation that often reflect the subcellular trafficking route and final destination, as well as differences generated by unique enzyme activities in different species and tissues. We discuss the potential consequences of such modifications on the stability and activity of the recombinant glycoproteins.

Indexed as

6-PhytaseAntibodies, MonoclonalArabidopsisAspergillus nigerBroadly Neutralizing AntibodiesFungal ProteinsGlycoproteinsGlycosylationHIV AntibodiesNicotianaPlant LeavesPlants, Genetically ModifiedPolysaccharidesProtein StabilityProtein TransportRecombinant Proteins2G12 monoclonal antibody6-PhytaseAntibodies, MonoclonalBroadly Neutralizing AntibodiesFungal ProteinsGlycoproteinsHIV AntibodiesPolysaccharidesRecombinant Proteins

Identifiers

PMID23553222
OpenAlexW2087987845

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.