Evidence map›Paper›PMID 32825463›Full record

ArticleInternational journal of molecular sciences2020

Differential Labeling of Glycoproteins with Alkynyl Fucose Analogs.

Chenyu Ma, Hideyuki Takeuchi, Huilin Hao, Chizuko Yonekawa, Kazuki Nakajima, Masamichi Nagae, Tetsuya Okajima, Robert S Haltiwanger, Yasuhiko Kizuka

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Review
  2. Article
  3. ProteinMolecules (Basel, Switzerland) · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Cells · 2021
    Article
  8. Chemical reporters to study mammalian O-glycosylation.Biochemical Society transactions · 2021
    Review
  9. 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

9 authors.

Chenyu MaDepartment of Molecular Biochemistry, Nagoya University Graduate School of Medicine, Showa-ku, Nagoya 466-8550, Japan.
Hideyuki TakeuchiDepartment of Molecular Biochemistry, Nagoya University Graduate School of Medicine, Showa-ku, Nagoya 466-8550, Japan.ORCID 0000-0002-2362-5850
Huilin HaoComplex Carbohydrate Research Center, Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.
Chizuko YonekawaCenter for Highly Advanced Integration of Nano and Life Sciences (G-CHAIN), Gifu University, Gifu 501-1193, Japan.
Kazuki NakajimaCenter for Research Promotion and Support, Fujita Health University, Toyoake 470-1192, Japan.
Masamichi NagaeDepartment of Molecular Immunology, Research Institute for Microbial Disease, Osaka University, Suita 565-0871, Japan.
Tetsuya OkajimaDepartment of Molecular Biochemistry, Nagoya University Graduate School of Medicine, Showa-ku, Nagoya 466-8550, Japan.ORCID 0000-0002-3677-648X
Robert S HaltiwangerComplex Carbohydrate Research Center, Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.ORCID 0000-0001-7439-9577
Yasuhiko KizukaCenter for Highly Advanced Integration of Nano and Life Sciences (G-CHAIN), Gifu University, Gifu 501-1193, Japan.ORCID 0000-0002-3181-9743

Funding

O-Glycosylation of Epidermal Growth Factor-like MotifsR01GM061126 · NIGMS · UNIVERSITY OF GEORGIA · PI HALTIWANGER, ROBERT S. · 2001 to 2021
$9.1M
Japan Agency for Medical Research and Development 16809274Japan Society for the Promotion of Science 16811705Japan Society for the Promotion of Science JP19H03176Japan Society for the Promotion of Science JP19H03416Japan Society for the Promotion of Science JP19KK0195Japan Society for the Promotion of Science JP20H03207NIGMS NIH HHS GM061126NIGMS NIH HHS R01 GM061126Takeda Science Foundation HTTakeda Science Foundation YKTokyo Biochemical Research Foundation YK
6 · The paper itself

Abstract

Fucosylated glycans critically regulate the physiological functions of proteins and cells. Alterations in levels of fucosylated glycans are associated with various diseases. For detection and functional modulation of fucosylated glycans, chemical biology approaches using fucose (Fuc) analogs are useful. However, little is known about how efficiently each unnatural Fuc analog is utilized by enzymes in the biosynthetic pathway of fucosylated glycans. We show here that three clickable Fuc analogs with similar but distinct structures labeled cellular glycans with different efficiency and protein specificity. For instance, 6-alkynyl (Alk)-Fuc modified

Indexed as

Binding SitesBiotinylationClick ChemistryFucoseFucosyltransferasesGlycoproteinsGlycosylationGuanosine DiphosphateHEK293 CellsHumansPolysaccharidesRecombinant ProteinsThrombospondin 13-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferaseFucoseFucosyltransferasesGlycoproteinsGuanosine Diphosphatepolypeptide fucosyltransferasePolysaccharidesRecombinant ProteinsThrombospondin 1thrombospondin-1, humanclick chemistryfucosefucosyltransferaseglycanglycan labelingglycosylationnotch

Identifiers

PMID32825463
PMCPMC7503990

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.