Evidence map›Paper›PMID 11457982›Full record

ArticlePlant physiology2001

Influence of growth conditions and developmental stage on N-glycan heterogeneity of transgenic immunoglobulin G and endogenous proteins in tobacco leaves.

I J Elbers, G M Stoopen, H Bakker, L H Stevens, M Bardor, J W Molthoff, W J Jordi, D Bosch, A Lommen

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

21 citing papers in PubMed, 103 citations in OpenAlex.

  1. Article
  2. Review
  3. Glyco-Engineering of Plant-Based Expression Systems.Advances in biochemical engineering/biotechnology · 2021
    Article
  4. Article
  5. Molecular & cellular proteomics : MCP · 2018
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Comparative glycoproteomics: approaches and applications.Briefings in functional genomics & proteomics · 2009
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  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

9 authors at 2 institutions in 2 countries.

I J ElbersState Institute for Quality Control of Agricultural Products (RIKILT), P.O. Box 230, NL-6700 AE Wageningen, The Netherlands.
G M Stoopen
H Bakker
L H Stevens
M Bardor
J W Molthoff
W J Jordi
D Bosch
A Lommen
Ministry of Agriculture, Nature and Food Quality · NLUniversité de Rouen Normandie · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants are regarded as a promising system for the production of heterologous proteins. However, little is known about the influence of plant development and growth conditions on N-linked glycosylation. To investigate this, transgenic tobacco (Nicotiana tabacum cv Samsun NN) plants expressing a mouse immunoglobulin G antibody (MGR48) were grown in climate rooms under four different climate conditions, i.e. at 15 degrees C and 25 degrees C and at either low or high light conditions. N-glycans on plantibodies and soluble endogenous proteins were analyzed with matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry (MS). Antibodies isolated from young leaves have a relatively high amount of high- mannose glycans compared with antibodies from older leaves, which contain more terminal N-acetylglucosamine. Senescence was shown to affect the glycosylation profile of endogenous proteins. The relative amount of N-glycans without terminal N-acetylglucosamine increased with leaf age. Major differences were observed between glycan structures on endogenous proteins versus those on antibodies, probably to be attributed to their subcellular localization. The relatively high percentage of antibody N-glycan lacking both xylose and fucose is interesting.

Indexed as

Plants, ToxicAnimalsCarbohydrate SequenceCloning, MolecularEnvironmentGlycoproteinsGlycosylationImmunoglobulin GMiceMolecular Sequence DataNicotianaPlant LeavesPlants, Genetically ModifiedPolysaccharidesProtein ConformationRecombinant ProteinsGlycoproteinsImmunoglobulin GPolysaccharidesRecombinant Proteins

Identifiers

PMID11457982
PMCPMC116488
OpenAlexW2109842052

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.