Evidence map›Paper›PMID 24145658›Full record

ArticleScientific reports2013

A gene responsible for prolyl-hydroxylation of moss-produced recombinant human erythropoietin.

Juliana Parsons, Friedrich Altmann, Manuela Graf, Johannes Stadlmann, Ralf Reski, Eva L Decker

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
5.9field-weighted citation impact, top 4% 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

28 citing papers in PubMed, 60 citations in OpenAlex.

  1. Recombinant Protein Drugs: A 2025 Update.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026
    Review
  2. Article
  3. Differential prolyl hydroxylation by six Physcomitrella prolyl-4 hydroxylases.Computational and structural biotechnology journal · 2024
    Article
  4. Plant-made pharmaceuticals.Plant biotechnology (Tokyo, Japan) · 2024
    Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Unexpected Arabinosylation after Humanization of Plant ProteinFrontiers in bioengineering and biotechnology · 2022
    Article
  10. Review
  11. Glycosylation of Plant-Produced Immunoglobulins.Experientia supplementum (2012) · 2021
    Article
  12. Prolyl Hydroxylase Paralogs inFrontiers in plant science · 2021
    Article
  13. Review
  14. Stable Protein Sialylation in Physcomitrella.Frontiers in plant science · 2020
    Article
  15. Review
  16. Advanced Plant-Based Glycan Engineering.Frontiers in bioengineering and biotechnology · 2018
    Review
  17. Article
  18. Article
  19. Review
  20. 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

6 authors at 2 institutions in 2 countries.

Juliana ParsonsPlant Biotechnology, Faculty of Biology, University of Freiburg, Schaenzlestr. 1, 79104 Freiburg, Germany.
Friedrich Altmann
Manuela Graf
Johannes Stadlmann
Ralf Reski
Eva L Decker
University of Freiburg · DEBOKU University · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recombinant production of pharmaceutical proteins is crucial, not only for personalized medicine. While most biopharmaceuticals are currently produced in mammalian cell culture, plant-made pharmaceuticals gain momentum. Post-translational modifications in plants are similar to those in humans, however, existing differences may affect quality, safety and efficacy of the products. A frequent modification in higher eukaryotes is prolyl-4-hydroxylase (P4H)-catalysed prolyl-hydroxylation. P4H sequence recognition sites on target proteins differ between humans and plants leading to non-human posttranslational modifications of recombinant human proteins produced in plants. The resulting hydroxyprolines display the anchor for plant-specific O-glycosylation, which bears immunogenic potential for patients. Here we describe the identification of a plant gene responsible for non-human prolyl-hydroxylation of human erythropoietin (hEPO) recombinantly produced in plant (moss) bioreactors. Targeted ablation of this gene abolished undesired prolyl-hydroxylation of hEPO and thus paves the way for plant-made pharmaceuticals humanized via glyco-engineering in moss bioreactors.

Indexed as

Protein Processing, Post-TranslationalBryopsidaEpoetin AlfaErythropoietinGene ExpressionHumansHydroxylationIntracellular SpaceMass SpectrometryProcollagen-Proline DioxygenaseProtein TransportRecombinant ProteinsEpoetin AlfaErythropoietinProcollagen-Proline DioxygenaseRecombinant Proteins

Identifiers

PMID24145658
PMCPMC3804855
OpenAlexW1977227569

What OpenQuestion holds

Textmetadata
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.