Evidence map›Paper›PMID 18952191›Full record

ReviewThe international journal of biochemistry & cell biology2009

Role of unusual O-glycans in intercellular signaling.

Kelvin B Luther, Robert S Haltiwanger

Open access · greenAbstract readReview
In one paragraph

Review in The international journal of biochemistry & cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

30 citing papers in PubMed, 71 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Notch signaling pathway: architecture, disease, and therapeutics.Signal transduction and targeted therapy · 2022
    Review
  6. Review
  7. Frontiers in plant science · 2021
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Mannose metabolism: more than meets the eye.Biochemical and biophysical research communications · 2014
    Review
  16. Article
  17. Article
  18. Rescue of Notch signaling in cells incapable of GDP-L-fucose synthesis by gap junction transfer of GDP-L-fucose in Drosophila.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  19. Article
  20. Vertebrate protein glycosylation: diversity, synthesis and function.Nature reviews. Molecular cell biology · 2012
    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.

Kelvin B LutherDepartment of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, Stony Brook University, Stony Brook, NY 11794-5215, USA.
Robert S Haltiwanger
Stony Brook University · US

Funding

O-Glycosylation of Epidermal Growth Factor-like MotifsR01GM061126 · NIGMS · UNIVERSITY OF GEORGIA · PI HALTIWANGER, ROBERT S. · 2001 to 2021
$9.1M
Glycosylation of Thrombospondin Type 1 RepeatsR01CA123071 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI HALTIWANGER, ROBERT S. · 2007 to 2011
$1.7M
NCI NIH HHS CA12307101NCI NIH HHS R01 CA123071NIGMS NIH HHS GM061126NIGMS NIH HHS R01 GM061126
6 · The paper itself

Abstract

In the last two decades, our knowledge of the role of glycans in development and signal transduction has expanded enormously. While most work has focused on the importance of N-linked or mucin-type O-linked glycosylation, recent work has highlighted the importance of several more unusual forms of glycosylation that are the focus of this review. In particular, the ability of O-fucose glycans on the epidermal growth factor-like (EGF) repeats of Notch to modulate signaling places glycosylation alongside phosphorylation as a means to modulate protein-protein interactions and their resultant downstream signals. The recent discovery that O-glucose modification of Notch EGF repeats is also required for Notch function has further expanded the range of glycosylation events capable of modulating Notch signaling. The prominent role of Notch during development and in later cell-fate decisions underscores the importance of these modifications in human biology. The role of glycans in intercellular signaling events is only beginning to be understood and appears ready to expand into new areas with the discovery that thrombospondin type 1 repeats are also modified with O-fucose glycans. Finally, a rare form of glycosylation called C-mannosylation modifies tryptophans in some signaling competent molecules and may be a further layer of complexity in the field. We will review each of these areas focusing on the glycan structures produced, the consequence of their presence, and the enzymes responsible.

Indexed as

AnimalsCell CommunicationFucoseGlucoseGlycosylationHumansPolysaccharidesReceptors, NotchSignal TransductionFucoseGlucosePolysaccharidesReceptors, Notch

Identifiers

PMID18952191
PMCPMC2714165
OpenAlexW2092091529

What OpenQuestion holds

Textmetadata
LicenceTDM
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.