Evidence map›Paper›PMID 18607003›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Ribophorin I regulates substrate delivery to the oligosaccharyltransferase core.

Cornelia M Wilson, Quentin Roebuck, Stephen High

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.5field-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

39 citing papers in PubMed, 68 citations in OpenAlex.

  1. Unraveling the Glycosylation Machinery ofInternational journal of molecular sciences · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Dysregulation of N-glycosylation byInternational journal of biological sciences · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Platelets and Defective N-Glycosylation.International journal of molecular sciences · 2020
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Analysis of substrate specificity ofThe Journal of biological chemistry · 2017
    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

3 authors at 1 institution in 1 country.

Cornelia M WilsonFaculty of Life Sciences, University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, United Kingdom.
Quentin Roebuck
Stephen High
University of Manchester · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E01979X/1
6 · The paper itself

Abstract

Protein N-glycosylation is widespread among biological systems, and the fundamental process of transferring a lipid-linked glycan to suitable asparagine residues of newly synthesized proteins occurs in both prokaryotes and eukaryotes. The core reaction is mediated by Stt3p family members, and in many organisms this component alone is sufficient to constitute the so called oligosaccharyltransferase (OST). However, eukaryotes typically have a more elaborate OST with several additional subunits of poorly defined function. In the mammalian OST complex one such subunit, ribophorin I, is proposed to facilitate the N-glycosylation of certain precursors during their biogenesis at the endoplasmic reticulum. Here, we use cell culture models to show that ribophorin I depletion results in substrate-specific defects in N-glycosylation, clearly establishing a defined physiological role for ribophorin I. To address the molecular mechanism of ribophorin I function, a cross-linking approach was used to explore the environment of nascent glycoproteins during the N-glycosylation reaction. We show for the first time that ribophorin I can regulate the delivery of precursor proteins to the OST complex by capturing substrates and presenting them to the catalytic core.

Indexed as

Biological TransportCatalytic DomainCell LineGlycoproteinsGlycosylationHexosyltransferasesHumansMembrane ProteinsRNA, Small Interferingdolichyl-diphosphooligosaccharide - protein glycotransferaseGlycoproteinsHexosyltransferasesMembrane ProteinsribophorinRNA, Small Interfering

Identifiers

PMID18607003
PMCPMC2443820
OpenAlexW2068288504

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.