Evidence map›Paper›PMID 28192664›Full record

ArticleACS chemical biology2017

NMR and Molecular Recognition of N-Glycans: Remote Modifications of the Saccharide Chain Modulate Binding Features.

Ana Gimeno, Niels-Christian Reichardt, F Javier Cañada, Lukas Perkams, Carlo Unverzagt, Jesús Jiménez-Barbero, Ana Ardá

Abstract read
In one paragraph

Article in ACS chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Conformationally Constrained Sialyl Analogues as New Potential Binders of h-CD22.Chembiochem : a European journal of chemical biology · 2022
    Article
  4. Article
  5. Article
  6. Automated Glycan Assembly ofAngewandte Chemie (International ed. in English) · 2021
    Article
  7. Recent Advances in the Chemical Biology ofMolecules (Basel, Switzerland) · 2021
    Review
  8. Article
  9. Review
  10. Article
  11. Glycan structures and their interactions with proteins. A NMR view.Current opinion in structural biology · 2020
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. 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.

Ana GimenoMolecular Recognition & Host-Pathogen Interactions Unit, CIC bioGUNE , Bizkaia Technology Park, Building 801A, 48170 Derio, Spain.
Niels-Christian ReichardtGlycotechnology Laboratory, CIC biomaGUNE , Paseo Miramón 182, 20014 San Sebastián, Spain.
F Javier CañadaChemical and Physical Biology, CIB-CSIC , Ramiro de Maeztu 9, 28040 Madrid, Spain.
Lukas PerkamsBioorganic Chemistry, Gebäude NWI, Universität Bayreuth , 95440 Bayreuth, Germany.
Carlo UnverzagtBioorganic Chemistry, Gebäude NWI, Universität Bayreuth , 95440 Bayreuth, Germany.
Jesús Jiménez-BarberoMolecular Recognition & Host-Pathogen Interactions Unit, CIC bioGUNE , Bizkaia Technology Park, Building 801A, 48170 Derio, Spain.ORCID 0000-0001-5421-8513
Ana ArdáMolecular Recognition & Host-Pathogen Interactions Unit, CIC bioGUNE , Bizkaia Technology Park, Building 801A, 48170 Derio, Spain.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycans play a key role as recognition elements in the communication of cells and other organisms. Thus, the analysis of carbohydrate-protein interactions has gained significant importance. In particular, nuclear magnetic resonance (NMR) techniques are considered powerful tools to detect relevant features in the interaction between sugars and their natural receptors. Here, we present the results obtained in the study on the molecular recognition of different mannose-containing glycans by Pisum sativum agglutinin. NMR experiments supported by Corcema-ST analysis, isothermal titration calorimetry (ITC) experiments, and molecular dynamics (MD) protocols have been successfully applied to unmask important binding features and especially to determine how a remote branching substituent significantly alters the binding mode of the sugar entity. These results highlight the key influence of common structural modifications in natural glycans on molecular recognition processes and underscore their importance for the development of biomedical applications.

Indexed as

Binding SitesCalorimetryCarbohydrate ConformationMagnetic Resonance SpectroscopyOligosaccharidesPolysaccharidesX-Ray DiffractionOligosaccharidesPolysaccharides

Identifiers

PMID28192664
PMCPMC5435455

What OpenQuestion holds

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Registered trials

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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.