Evidence map›Paper›PMID 41917414›Full record

ReviewAdvances in experimental medicine and biology2026

Carbohydrate-Binding Mechanism and Therapeutic Potential of Lectin Mimics.

Yu Nakagawa

Abstract readReview
PubMed Publisher
In one paragraph

Review in Advances in experimental medicine and biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

1 author.

Yu NakagawaInstitute for Glyco-core Research (iGCORE), Nagoya University, Nagoya, Japan. yu@agr.nagoya-u.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lectins exhibit antiviral and antimicrobial activities by binding to glycans of pathogenic species. However, their therapeutic application is impeded by high manufacturing costs, low chemical stability, hemagglutination, cytotoxicity, and the potential risk of initiating an unfavorable immune response. These disadvantages have stimulated considerable efforts to develop small molecules with carbohydrate-binding properties (lectin mimics) that are readily preparable, chemically stable, and easily tunable, as alternatives to lectins. This review outlines the representative design concepts and carbohydrate-binding properties of lectin mimics and discusses their therapeutic potential in the treatment of infectious diseases. In addition to synthetic lectin mimics, naturally occurring lectin mimics, pradimicins, are also highlighted, and the molecular basis of carbohydrate recognition and their therapeutic potential are presented.

Indexed as

Anti-Infective AgentsCarbohydratesLectinsMolecular MimicryAnimalsAntiviral AgentsHumansAnti-Infective AgentsAntiviral AgentsCarbohydratesLectinsAnti-infective drugCarbohydrate recognitionLectin mimicMolecular designNatural product

Identifiers

PMID41917414

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.