Evidence map›Paper›PMID 30484247›Full record

ReviewAdvances in experimental medicine and biology

Biophysical Analyses for Probing Glycan-Protein Interactions.

Masamichi Nagae, Yoshiki Yamaguchi

Abstract readReview
In one paragraph

Review in Advances in experimental medicine and biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. 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

2 authors.

Masamichi NagaeGraduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.
Yoshiki YamaguchiSynthetic Cellular Chemistry Laboratory, RIKEN Cluster for Pioneering Research, Wako, Saitama, Japan. yyoshiki@riken.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycan-protein interactions occur at many physiological events, and the analyses are of considerable importance for understanding glycan-dependent mechanisms. Biophysical approaches including 3D structural analysis are essential for revealing glycan-protein interactions at the atomic level. The inherent diversity of glycans suits them to function as identification tags, e.g., distinguish self from the nonself components of pathogens. However, the complexity of glycans and poor affinities for interaction partners limit the usefulness of conventional analyses. To cope with such troublesome glycans, a logical sequence of biophysical analyses need to be developed. In this chapter, we introduce a workflow of glycan-protein interaction analysis consisting of six steps: preparation of lectin and glycan, screening of glycan ligand, determination of binding epitope, quantitative interaction analysis, 3D structural analysis, and molecular dynamics simulation. Our increasing knowledge and understanding of lectin-glycan interactions will hopefully lead to the design of glyco-based medicines and vaccines.

Indexed as

LectinsMolecular Dynamics SimulationPolysaccharidesProtein BindingProteinsLectinsPolysaccharidesProteinsFrontal affinity chromatographyGlycan microarrayIsothermal titration calorimetryMolecular dynamics simulationNuclear magnetic resonanceSurface plasmon resonanceX-ray crystallography

Identifiers

PMID30484247
PMCPMC7153041

What OpenQuestion holds

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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.