Evidence map›Paper›PMID 42603778›Full record

ArticleChemMedChem2026

Structural and Biophysical Characterization of C-Glycosylic 1,2-Thiodisaccharides Reveals Determinants of Selective Binding to Galectin-7 and Galectin-8N.

Anastasia S Tsagkarakou, Anastassia L Kantsadi, Vasiliki I Theodoridou, Nikolaos Veliotis, László Lázár, János József, László Juhász, George Kontopidis, Hakon Leffler, Ulf J Nilsson and 2 more

Abstract read
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In one paragraph

Article in ChemMedChem, 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

12 authors.

Anastasia S TsagkarakouDepartment of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece.ORCID https://orcid.org/0000-0003-1723-7840
Anastassia L KantsadiDepartment of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece.
Vasiliki I TheodoridouDepartment of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece.
Nikolaos VeliotisDepartment of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece.ORCID https://orcid.org/0009-0002-7812-7290
László LázárDepartment of Organic Chemistry, University of Debrecen, Debrecen, Hungary.
János JózsefDepartment of Organic Chemistry, University of Debrecen, Debrecen, Hungary.
László JuhászDepartment of Organic Chemistry, University of Debrecen, Debrecen, Hungary.ORCID https://orcid.org/0000-0002-7462-7944
George KontopidisDepartment of Biochemistry, Veterinary School, University of Thessaly, Karditsa, Greece.
Hakon LefflerDepartment of Laboratory Medicine, Lund University, Lund, Sweden.ORCID https://orcid.org/0000-0003-4482-8945
Ulf J NilssonDepartment of Chemistry, Lund University, Lund, Sweden.ORCID https://orcid.org/0000-0001-5815-9522
László SomsákDepartment of Organic Chemistry, University of Debrecen, Debrecen, Hungary.ORCID https://orcid.org/0000-0002-9103-9845
Demetres D LeonidasDepartment of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece.ORCID https://orcid.org/0000-0002-3874-2523

Funding

Hungarian National Research, Development and Innovation Office 2024-1.2.3-HU-RIZONT-2024-00005
6 · The paper itself

Abstract

Achieving isoform selectivity within the galectin family remains a central challenge in glycomimetic drug design due to the highly conserved architecture of their carbohydrate recognition domains. Here, we define the structural and thermodynamic basis of recognition of a series of C-glycosylic 1,2-thiodisaccharides targeting human galectin-7 and the N-terminal domain of galectin-8 (galectin-8N). Using an integrated approach combining fluorescence polarization, isothermal titration calorimetry, and high-resolution X-Ray crystallography, we establish a clear structure-activity relationship across the ligand series. Compound 17 emerges as the most potent galectin-8N ligand (K

Indexed as

DisaccharidesGalectinsBinding SitesCrystallography, X-RayHumansLigandsModels, MolecularMolecular StructureProtein BindingStructure-Activity RelationshipThermodynamicsDisaccharidesGalectinsLGALS7 protein, humanLGALS8 protein, humanLigands

Identifiers

PMID42603778
PMCPMC13477432

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.