Evidence map›Paper›PMID 24105266›Full record

ArticleJournal of cell science2013

Glycosylation of closely spaced acceptor sites in human glycoproteins.

Shiteshu Shrimal, Reid Gilmore

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed, 61 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. N-glycan-dependent protein maturation and quality control in the ER.Nature reviews. Molecular cell biology · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Site-to-site cross-talk in OST-B glycosylation of hCEACAM1-IgV.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Oligosaccharyltransferase: A Gatekeeper of Health and Tumor Progression.International journal of molecular sciences · 2019
    Review
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, Worcester, MA 01605, USA.
Reid Gilmore
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 GM43768NIGMS NIH HHS R01 GM043768
6 · The paper itself

Abstract

Asparagine-linked glycosylation of proteins by the oligosaccharyltransferase (OST) occurs when acceptor sites or sequons (N-x≠P-T/S) on nascent polypeptides enter the lumen of the rough endoplasmic reticulum. Metazoan organisms assemble two isoforms of the OST that have different catalytic subunits (STT3A or STT3B) and partially non-overlapping cellular roles. Potential glycosylation sites move past the STT3A complex, which is associated with the translocation channel, at the protein synthesis elongation rate. Here, we investigated whether close spacing between acceptor sites in a nascent protein promotes site skipping by the STT3A complex. Biosynthetic analysis of four human glycoproteins revealed that closely spaced sites are efficiently glycosylated by an STT3B-independent process unless the sequons contain non-optimal sequence features, including extreme close spacing between sequons (e.g. NxTNxT) or the presence of paired NxS sequons (e.g. NxSANxS). Many, but not all, glycosylation sites that are skipped by the STT3A complex can be glycosylated by the STT3B complex. Analysis of a murine glycoprotein database revealed that closely spaced sequons are surprisingly common, and are enriched for paired NxT sites when the gap between sequons is less than three residues.

Indexed as

Protein Processing, Post-TranslationalAmino Acid MotifsAnimalsEndoplasmic ReticulumGene ExpressionGlycoproteinsGlycosylationHaptoglobinsHeLa CellsHemopexinHexosyltransferasesHumansMembrane ProteinsMiceMolecular Sequence DataGlycoproteinsHaptoglobinsHemopexinHexosyltransferasesHP protein, humanMembrane ProteinsSTT3A protein, humanSTT3B protein, humanAsparagine-linked glycosylationEndoplasmic reticulumOligosaccharyltransferase

Identifiers

PMID24105266
PMCPMC3843140
OpenAlexW2019894781

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.