Evidence map›Paper›PMID 28430973›Full record

ReviewGlycobiology2017

Biological functions of fucose in mammals.

Michael Schneider, Esam Al-Shareffi, Robert S Haltiwanger

Open access · bronzeAbstract readReview
In one paragraph

Review in Glycobiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 214 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
214citing papers in PubMed, 1 pooled it
12.3field-weighted citation impact, top 1% 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

214 citing papers in PubMed, 1 synthesis or guideline pooled it, 424 citations in OpenAlex.

  1. Pooled it
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  15. 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
  16. Article
  17. Article
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  19. Article
  20. PredictiveACS omega · 2026
    Article

154 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

3 authors at 2 institutions in 1 country.

Michael SchneiderDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794, USA.
Esam Al-ShareffiDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794, USA.
Robert S HaltiwangerDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794, USA.
Stony Brook University · USUniversity of Georgia · US

Funding

O-Glycosylation of Epidermal Growth Factor-like MotifsR01GM061126 · NIGMS · UNIVERSITY OF GEORGIA · PI HALTIWANGER, ROBERT S. · 2001 to 2021
$9.1M
NIGMS NIH HHS R01 GM061126
6 · The paper itself

Abstract

Fucose is a 6-deoxy hexose in the l-configuration found in a large variety of different organisms. In mammals, fucose is incorporated into N-glycans, O-glycans and glycolipids by 13 fucosyltransferases, all of which utilize the nucleotide-charged form, GDP-fucose, to modify targets. Three of the fucosyltransferases, FUT8, FUT12/POFUT1 and FUT13/POFUT2, are essential for proper development in mice. Fucose modifications have also been implicated in many other biological functions including immunity and cancer. Congenital mutations of a Golgi apparatus localized GDP-fucose transporter causes leukocyte adhesion deficiency type II, which results in severe developmental and immune deficiencies, highlighting the important role fucose plays in these processes. Additionally, changes in levels of fucosylated proteins have proven as useful tools for determining cancer diagnosis and prognosis. Chemically modified fucose analogs can be used to alter many of these fucose dependent processes or as tools to better understand them. In this review, we summarize the known roles of fucose in mammalian physiology and pathophysiology. Additionally, we discuss recent therapeutic advances for cancer and other diseases that are a direct result of our improved understanding of the role that fucose plays in these systems.

Indexed as

Protein Processing, Post-TranslationalAnimalsFucoseFucosyltransferasesHumansImmune System DiseasesMetabolic DiseasesMutationNeoplasmsFucoseFucosyltransferasescancerdevelopmentfucosefucosyltransferaseimmunology

Identifiers

PMID28430973
PMCPMC5458543
OpenAlexW2606454401

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.