Evidence map›Paper›PMID 37399117›Full record

ReviewGlycobiology2023

Structural and mechanistic studies of the N-glycosylation machinery: from lipid-linked oligosaccharide biosynthesis to glycan transfer.

Ana S Ramírez, Kaspar P Locher

Open access · hybridAbstract readReview
In one paragraph

Review in Glycobiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

16 citing papers in PubMed, 22 citations in OpenAlex.

  1. Unraveling the Glycosylation Machinery ofInternational journal of molecular sciences · 2026
    Article
  2. Article
  3. Review
  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. Functions ofJournal of fungi (Basel, Switzerland) · 2025
    Review
  11. Article
  12. The Intersection of Glycosylation and Ferroptosis in Cancer.Antioxidants (Basel, Switzerland) · 2025
    Review
  13. Review
  14. O-antigen polysaccharides inMicrobiology and molecular biology reviews : MMBR · 2025
    Review
  15. Review
  16. 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.

Ana S RamírezInstitute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule (ETH), Zürich 8093, Switzerland.ORCID 0000-0002-1619-0721
Kaspar P LocherInstitute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule (ETH), Zürich 8093, Switzerland.ORCID 0000-0002-8207-2889
ETH Zurich · CH

Funding

ETH Zurich 27-16-2National Science Foundation 310030_196862
6 · The paper itself

Abstract

N-linked protein glycosylation is a post-translational modification that exists in all domains of life. It involves two consecutive steps: (i) biosynthesis of a lipid-linked oligosaccharide (LLO), and (ii) glycan transfer from the LLO to asparagine residues in secretory proteins, which is catalyzed by the integral membrane enzyme oligosaccharyltransferase (OST). In the last decade, structural and functional studies of the N-glycosylation machinery have increased our mechanistic understanding of the pathway. The structures of bacterial and eukaryotic glycosyltransferases involved in LLO elongation provided an insight into the mechanism of LLO biosynthesis, whereas structures of OST enzymes revealed the molecular basis of sequon recognition and catalysis. In this review, we will discuss approaches used and insight obtained from these studies with a special emphasis on the design and preparation of substrate analogs.

Indexed as

HexosyltransferasesGlycosylationGlycosyltransferasesLipopolysaccharidesPolysaccharidesGlycosyltransferasesHexosyltransferaseslipid-linked oligosaccharidesLipopolysaccharidesPolysaccharidesglycosyltransferaselipid-linked oligosaccharideN-glycosylationoligosaccharyltransferasestructure

Identifiers

PMID37399117
PMCPMC10859629
OpenAlexW4383058370

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.