Evidence map›Paper›PMID 30312397›Full record

ReviewGlycobiology2019

Oligosaccharyltransferase structures provide novel insight into the mechanism of asparagine-linked glycosylation in prokaryotic and eukaryotic cells.

Shiteshu Shrimal, Reid Gilmore

Open access · bronzeAbstract readReview
In one paragraph

Review in Glycobiology, 2019. 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
2.7field-weighted citation impact, top 9% 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, 59 citations in OpenAlex.

  1. Article
  2. Systematic optimization ofEngineering microbiology · 2026
    Review
  3. Unraveling the Glycosylation Machinery ofInternational journal of molecular sciences · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. N-glycan-dependent protein maturation and quality control in the ER.Nature reviews. Molecular cell biology · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Analysis of Protein Glycosylation in the ER.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  17. Review
  18. Article
  19. Review
  20. An oligosaccharyltransferase fromFrontiers in plant science · 2023
    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

2 authors at 1 institution in 1 country.

Shiteshu ShrimalDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA, USA.
Reid GilmoreDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA, USA.
University of Massachusetts Chan Medical School · US

Funding

ASSEMBLY AND TRANSFER OF N-LINKED OLIGOSACCHARIDESR01GM043768 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI GILMORE, JAMES REID · 1990 to 2018
$6.9M
NIGMS NIH HHS R01 GM043768
6 · The paper itself

Abstract

Asparagine-linked (N-linked) glycosylation is one of the most common protein modification reactions in eukaryotic cells, occurring upon the majority of proteins that enter the secretory pathway. X-ray crystal structures of the single subunit OSTs from eubacterial and archaebacterial organisms revealed the location of donor and acceptor substrate binding sites and provided the basis for a catalytic mechanism. Cryoelectron microscopy structures of the octameric yeast OST provided substantial insight into the organization and assembly of the multisubunit oligosaccharyltransferases. Furthermore, the cryoelectron microscopy structure of a complex consisting of a mammalian OST complex, the protein translocation channel and a translating ribosome revealed new insight into the mechanism of cotranslational glycosylation.

Indexed as

AsparagineCryoelectron MicroscopyCrystallography, X-RayEukaryotic CellsGlycosylationHexosyltransferasesHumansMembrane ProteinsModels, MolecularProkaryotic CellsProtein ConformationAsparaginedolichyl-diphosphooligosaccharide - protein glycotransferaseHexosyltransferasesMembrane Proteinscotranslational glycosylationlipid-linked oligosaccharideN-glycosylationoligosaccharyltransferaseOST structure

Identifiers

PMID30312397
PMCPMC6499010
OpenAlexW2896738812

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.