Evidence map›Paper›PMID 29043680›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2018

Analysis of Protein Glycosylation in the ER.

Jennifer Schoberer, Yun-Ji Shin, Ulrike Vavra, Christiane Veit, Richard Strasser

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2018. 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
–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

21 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Circular RNA-based HPV16 therapeutic vaccine elicits potent and durable antitumor immunity.Journal of experimental & clinical cancer research : CR · 2026
    Article
  7. PeerJ · 2026
    Review
  8. Article
  9. Deciphering the determinants of recombinant protein expression across the human secretome.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. The Major Peanut Allergen Ara h 2 Produced inFrontiers in plant science · 2021
    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

5 authors.

Jennifer SchobererDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190, Vienna, Austria.
Yun-Ji ShinDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190, Vienna, Austria.
Ulrike VavraDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190, Vienna, Austria.
Christiane VeitDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190, Vienna, Austria.
Richard StrasserDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190, Vienna, Austria. richard.strasser@boku.ac.at.

Funding

Austrian Science Fund FWF P 28218Austrian Science Fund FWF T 655
6 · The paper itself

Abstract

Protein N-glycosylation is an essential posttranslational modification which is initiated in the endoplasmic reticulum. In plants, the N-glycans play a pivotal role for protein folding and quality control. Through the interaction of glycan processing and binding reactions mediated by ER-resident glycosidases and specific carbohydrate binding proteins, the N-glycans contribute to the adoption of a native protein conformation. Properly folded glycoproteins are released from these processes and allowed to continue their transit to the Golgi where further processing and maturation of N-glycans leads to the formation of more complex structures with different functions. Incompletely folded glycoproteins are removed from the ER by a highly conserved degradation process to prevent the accumulation or secretion of misfolded proteins and maintain ER homeostasis. Here, we describe methods to analyze the N-glycosylation status and the glycan-dependent ER-associated degradation process in plants.

Indexed as

Endoplasmic ReticulumEndoplasmic Reticulum-Associated DegradationGlycosylationPolysaccharidesProtein FoldingProteinsProtein TransportPolysaccharidesProteinsERADGlycoproteinN-glycosylationOligosaccharyltransferaseQuality control

Identifiers

PMID29043680
PMCPMC7039702

What OpenQuestion holds

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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.