Evidence map›Paper›PMID 41969275›Full record

ArticleChembiochem : a European journal of chemical biology2026

β-Mannosyl Triazoles as Mimics of Galactosyl Galectin-3 and Galectin-9 N-Terminal Domain Inhibitors.

Fredrik Sjövall, Ulf J Nilsson

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical 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.

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0citing papers in PubMed
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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

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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

2 authors.

Fredrik SjövallDepartment of Chemistry, Lund University, Lund, Sweden.
Ulf J NilssonDepartment of Chemistry, Lund University, Lund, Sweden.ORCID 0000-0001-5815-9522

Funding

Galecto Biotech ABKungliga Fysiografiska Sällskapet i LundVetenskapsrådet 2025-04985
6 · The paper itself

Abstract

Mannosyl β-C-1 amidotriazoles have previously been reported to have higher selectivity for galectin-9N (N-terminal domain) than the corresponding galactoside C3 amidotriazoles have, which were more selective for galectin-3. This study further investigated this by synthesis of mono- and bis-aryltriazolyl mannoside analogues to known high-affinity galectin-3 galactosyl-derived inhibitors. Following synthesis, affinity measurements using competititve fluorescence polarization assays were performed which indicated low affinity of the bis-aryltriazolyl mannosyls, while the mono-aryltriazolyl mannosyls analogs possessed improved affinity, albeit with lower and selectivity. From conformational calculations it was implied that the weak-binding bis-aryltriazolyl mannosyl analogues do not find the same conformation and binding pose as the parent galactoside compounds.

Indexed as

Galectin 3GalectinsMannosidesTriazolesBlood ProteinsGalactosidesHumansProtein DomainsBlood ProteinsGalactosidesGalectin 3GalectinsLGALS3 protein, humanLGALS9 protein, humanMannosidesTriazolesgalectinglycomimeticmannosylTriazole

Identifiers

PMID41969275
PMCPMC13072086

What OpenQuestion holds

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LicenceCC BY
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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.