Evidence map›Paper›PMID 26971576›Full record

ArticleScientific reports2016

Atomic visualization of a flipped-back conformation of bisected glycans bound to specific lectins.

Masamichi Nagae, Mayumi Kanagawa, Kana Morita-Matsumoto, Shinya Hanashima, Yasuhiko Kizuka, Naoyuki Taniguchi, Yoshiki Yamaguchi

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.1field-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

26 citing papers in PubMed, 54 citations in OpenAlex.

  1. Bisecting βGlcNAc: MA'AT analysis ofThe Journal of biological chemistry · 2026
    Article
  2. Review
  3. Oxr1 and Ncoa7 regulate V-ATPase to achieve optimal pH for glycosylation within the Golgi apparatus and trans-Golgi network.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. BisectingACS chemical biology · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Systematic synthesis of bisectedChemical science · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Peptide Sequence Mapping around Bisecting GlcNAc-BearingInternational journal of molecular sciences · 2021
    Article
  14. Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021
    Review
  15. Recent Advances in the Chemical Biology ofMolecules (Basel, Switzerland) · 2021
    Review
  16. Review
  17. 3D Structure and Function of Glycosyltransferases Involved inInternational journal of molecular sciences · 2020
    Review
  18. Review
  19. Article
  20. 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

7 authors at 2 institutions in 1 country.

Masamichi NagaeStructural Glycobiology Team, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Mayumi KanagawaStructural Glycobiology Team, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Kana Morita-MatsumotoStructural Glycobiology Team, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Shinya HanashimaDepartment of Chemistry, Osaka University, Machikaneyama, Toyonaka, Osaka 560-0043, Japan.
Yasuhiko KizukaDisease Glycomics Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, RIKEN Global Research Cluster, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Naoyuki TaniguchiDisease Glycomics Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, RIKEN Global Research Cluster, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Yoshiki YamaguchiStructural Glycobiology Team, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
RIKEN · JPOsaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycans normally exist as a dynamic equilibrium of several conformations. A fundamental question concerns how such molecules bind lectins despite disadvantageous entropic loss upon binding. Bisected glycan, a glycan possessing bisecting N-acetylglucosamine (GlcNAc), is potentially a good model for investigating conformational dynamics and glycan-lectin interactions, owing to the unique ability of this sugar residue to alter conformer populations and thus modulate the biological activities. Here we analyzed bisected glycan in complex with two unrelated lectins, Calsepa and PHA-E. The crystal structures of the two complexes show a conspicuous flipped back glycan structure (designated 'back-fold' conformation), and solution NMR analysis also provides evidence of 'back-fold' glycan structure. Indeed, statistical conformational analysis of available bisected and non-bisected glycan structures suggests that bisecting GlcNAc restricts the conformations of branched structures. Restriction of glycan flexibility by certain sugar residues may be more common than previously thought and impinges on the mechanism of glycoform-dependent biological functions.

Indexed as

Carbohydrate ConformationProtein DomainsAcetylglucosamineAnimalsBinding, CompetitiveBrainCarbohydrate SequenceCell MembraneCrystallography, X-RayElectrophoresis, Polyacrylamide GelMagnetic Resonance SpectroscopyMaleMice, KnockoutModels, MolecularN-AcetylglucosaminyltransferasesPhytohemagglutininsAcetylglucosaminebeta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferaseerythroagglutinating phytohemagglutininN-AcetylglucosaminyltransferasesPhytohemagglutininsPlant LectinsPolysaccharides

Identifiers

PMID26971576
PMCPMC4789653
OpenAlexW2300581299

What OpenQuestion holds

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LicenceCC BY
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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.