Evidence map›Paper›PMID 25580689›Full record

ReviewMolecules (Basel, Switzerland)2015

The Lectin Frontier Database (LfDB), and data generation based on frontal affinity chromatography.

Jun Hirabayashi, Hiroaki Tateno, Toshihide Shikanai, Kiyoko F Aoki-Kinoshita, Hisashi Narimatsu

Abstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. The Historiography of Galactose and Its Recognition by Galectins.Advances in experimental medicine and biology · 2026
    Review
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  6. Extraction, purification, biological effects and applications of acrosin: a review.Frontiers in cellular and infection microbiology · 2025
    Review
  7. Article
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  15. Functions of Glycosylation and Related Web Resources for Its Prediction.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
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  17. Review
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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

5 authors.

Jun HirabayashiResearch Center for Stem Cell Engineering, National Institute of Advanced Industrial Science and Technology, Central-2, 1-1-1, Umezono, Tsukuba, Ibaraki 305-8568, Japan. jun-hirabayashi@aist.go.jp.
Hiroaki TatenoResearch Center for Stem Cell Engineering, National Institute of Advanced Industrial Science and Technology, Central-2, 1-1-1, Umezono, Tsukuba, Ibaraki 305-8568, Japan. h-tateno@aist.go.jp.
Toshihide ShikanaiResearch Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology, Central-2, 1-1-1, Umezono, Tsukuba, Ibaraki 305-8568, Japan. t.shikanai@aist.go.jp.
Kiyoko F Aoki-KinoshitaDepartment of Bioinformatics, Faculty of Engineering, Soka University, 1-236 Tangi-machi, Hachioji, Tokyo 192-8577, Japan. kkiyoko@soka.ac.jp.
Hisashi NarimatsuResearch Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology, Central-2, 1-1-1, Umezono, Tsukuba, Ibaraki 305-8568, Japan. h.narimatsu@aist.go.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lectins are a large group of carbohydrate-binding proteins, having been shown to comprise at least 48 protein scaffolds or protein family entries. They occur ubiquitously in living organisms-from humans to microorganisms, including viruses-and while their functions are yet to be fully elucidated, their main underlying actions are thought to mediate cell-cell and cell-glycoconjugate interactions, which play important roles in an extensive range of biological processes. The basic feature of each lectin's function resides in its specific sugar-binding properties. In this regard, it is beneficial for researchers to have access to fundamental information about the detailed oligosaccharide specificities of diverse lectins. In this review, the authors describe a publicly available lectin database named "Lectin frontier DataBase (LfDB)", which undertakes the continuous publication and updating of comprehensive data for lectin-standard oligosaccharide interactions in terms of dissociation constants (Kd's). For Kd determination, an advanced system of frontal affinity chromatography (FAC) is used, with which quantitative datasets of interactions between immobilized lectins and >100 fluorescently labeled standard glycans have been generated. The FAC system is unique in its clear principle, simple procedure and high sensitivity, with an increasing number (>67) of associated publications that attest to its reliability. Thus, LfDB, is expected to play an essential role in lectin research, not only in basic but also in applied fields of glycoscience.

Indexed as

Databases as TopicChromatography, AffinityHumansKineticsLectinsOligosaccharidesReceptors, Cell SurfaceLectinsOligosaccharidesReceptors, Cell Surfacesaccharide-binding proteins

Identifiers

PMID25580689
PMCPMC6272529

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.