Evidence map›Paper›PMID 27040397›Full record

ReviewJournal of molecular biology2016

What Have We Learned from Glycosyltransferase Knockouts in Mice?

Pamela Stanley

Open access · greenAbstract readReview
In one paragraph

Review in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

48 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. FUT1- and GAL3ST2-mediated cellular glycan remodeling broadly restricts sialic acid-dependent viral infections.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. NMR of Gangliosides.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  4. Review
  5. Review
  6. Article
  7. Dysregulation of N-glycosylation byInternational journal of biological sciences · 2025
    Article
  8. Glycosylation in Cancer.Handbook of experimental pharmacology · 2025
    Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. What is the Sugar Code?Chembiochem : a European journal of chemical biology · 2022
    Review
  20. 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

1 author at 1 institution in 1 country.

Pamela StanleyDepartment of Cell Biology, Albert Einstein College of Medicine, New York, NY 10461, USA. Electronic address: pamela.stanley@einstein.yu.edu.
Albert Einstein College of Medicine · US

Funding

Roles of Glycoslyation in Notch SignalingR01GM106417 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI STANLEY, PAMELA M · 2013 to 2021
$3.8M
Lectin Resistant Tumor Cells and Functional GlycomicsR01GM105399 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI STANLEY, PAMELA M · 2013 to 2022
$3.6M
NIGMS NIH HHS R01 GM105399NIGMS NIH HHS R01 GM106417
6 · The paper itself

Abstract

There are five major classes of glycan including N- and O-glycans, glycosaminoglycans, glycosphingolipids, and glycophosphatidylinositol anchors, all expressed at the molecular frontier of each mammalian cell. Numerous biological consequences of altering the expression of mammalian glycans are understood at a mechanistic level, but many more remain to be characterized. Mouse mutants with deleted, defective, or misexpressed genes that encode activities necessary for glycosylation have led the way to identifying key functions of glycans in biology. However, with the advent of exome sequencing, humans with mutations in genes involved in glycosylation are also revealing specific requirements for glycans in mammalian development. The aim of this review is to summarize glycosylation genes that are necessary for mouse embryonic development, pathway-specific glycosylation genes whose deletion leads to postnatal morbidity, and glycosylation genes for which effects are mild, but perturbation of the organism may reveal functional consequences. General strategies for generating and interpreting the phenotype of mice with glycosylation defects are discussed in relation to human congenital disorders of glycosylation (CDG).

Indexed as

AnimalsGlycosylationGlycosyltransferasesHumansMiceMice, KnockoutMutationPolysaccharidesGlycosyltransferasesPolysaccharidesglycosidaseglycosylationglycosyltransferasemouse mutantsnucleotide sugar

Identifiers

PMID27040397
PMCPMC5532804
OpenAlexW2325864027

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.