Evidence map›Paper›PMID 40166736›Full record

ArticleBBA advances2025

Tools for structural lectinomics: From structures to lectomes.

Frédérique Lisacek, Boris Schnider, Anne Imberty

Abstract read
In one paragraph

Article in BBA advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Article
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

3 authors.

Frédérique LisacekSIB Swiss Institute of Bioinformatics CH-1227 Geneva, Switzerland.
Boris SchniderSIB Swiss Institute of Bioinformatics CH-1227 Geneva, Switzerland.
Anne ImbertyUniv. Grenoble Alpes, CNRS, CERMAV 38000 Grenoble, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lectins are ubiquitous proteins that interact with glycans in a variety of molecular processes and as such, also play a role in diseases, whether infectious, chronic or cancer-related. The systematic study of lectins is therefore essential, in particular for understanding cell-cell communication. Accumulated protein three-dimensional structural data in the past decades boosted advance in AI-based prediction and opened up new options to characterise lectins that are known to often be multimeric and multivalent. This article reviews the methods to obtain structures of lectins, the current data available for lectin 3D structures and their interactions, how this knowledge is used to classify these proteins and shows that the combination of an array of bioinformatics tools should make the prediction of binding specificity possible in a near future.

Indexed as

AIBioinformaticsCarbohydrate-bindingLectinModellingPrediction methodStructural biology

Identifiers

PMID40166736
PMCPMC11957679

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.