Evidence map›Paper›PMID 21924891›Full record

ReviewCurrent opinion in structural biology2011

Fringe benefits: functional and structural impacts of O-glycosylation on the extracellular domain of Notch receptors.

Nadia A Rana, Robert S Haltiwanger

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
–field-weighted citation impact
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

84 citing papers in PubMed.

  1. Mining cancer genomes for copy number alterations identifies glycosylation enzymes as oncogenic drivers.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Deciphering the molecular drivers for cashmere/pashmina fiber production in goats: a comprehensive review.Mammalian genome : official journal of the International Mammalian Genome Society · 2025
    Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Biomolecular NMR assignments · 2023
    Article
  16. Article
  17. Retinal regeneration requires dynamic Notch signaling.Neural regeneration research · 2022
    Review
  18. Glycans that regulate Notch signaling in the intestine.Biochemical Society transactions · 2022
    Review
  19. Article
  20. Review

24 more citing papers are in PubMed but not listed here.

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.

Nadia A RanaDepartment of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, Stony Brook University, Stony Brook, NY 11794-5215, USA.
Robert S Haltiwanger

Funding

O-Glycosylation of Epidermal Growth Factor-like MotifsR01GM061126 · NIGMS · UNIVERSITY OF GEORGIA · PI HALTIWANGER, ROBERT S. · 2001 to 2021
$9.1M
VIRAL ONCOLOGYT32CA009176 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI HEARING, PATRICK · 1985 to 2012
$5.2M
NCI NIH HHS NCI T32 CA009176NCI NIH HHS T32 CA009176NIGMS NIH HHS GM061126NIGMS NIH HHS R01 GM061126
6 · The paper itself

Abstract

The Notch family of receptors plays essential roles in many phases of development, and dysregulation of Notch activity is increasingly recognized as a player in many diseases. O-Glycosylation of the Notch extracellular domain is essential for Notch activity, and tissue-specific alterations in the glycan structures are known to regulate activity. Here we review recent advances in identification and characterization of the enzymes responsible for glycosylating Notch and molecular mechanisms for how these O-glycans affect Notch activity.

Indexed as

AnimalsDrosophilaDrosophila ProteinsFucoseFucosyltransferasesGlucoseGlucosyltransferasesGlycosylationMammalsMiceN-AcetylglucosaminyltransferasesPolysaccharidesProtein BindingProtein Structure, TertiaryReceptors, NotchSignal TransductionDrosophila Proteinsfng protein, DrosophilaFucoseFucosyltransferasesGlucoseGlucosyltransferasesN-AcetylglucosaminyltransferasesN protein, DrosophilaPofut1 protein, mousePolysaccharidesReceptors, NotchRumi protein, Drosophila

Identifiers

PMID21924891
PMCPMC3195399

What OpenQuestion holds

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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.