Evidence map›Paper›PMID 41358124›Full record

ArticleACS omega2025

Design of Glycosyltransferase Inhibitors: Targeting the Biosynthesis of Glycosaminoglycans by Phosphonate-Xyloside.

Daniel Willén, Hanna Malmquist, Pilar Blasco, Joachim Björklund, Roberto Mastio, Sophie Manner, Göran Widmalm, Emil Tykesson, Ulf Ellervik

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Article in ACS omega, 2025. 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

9 authors.

Daniel WillénDepartment of Chemistry, Centre for Analysis and Synthesis, Lund University, P.O. Box 124, Lund SE-221 00, Sweden.
Hanna MalmquistDepartment of Chemistry, Centre for Analysis and Synthesis, Lund University, P.O. Box 124, Lund SE-221 00, Sweden.
Pilar BlascoArrhenius Laboratory, Department of Organic Chemistry, Stockholm University, Stockholm SE-106 91, Sweden.ORCID https://orcid.org/0000-0001-6703-5417
Joachim BjörklundDepartment of Chemistry, Centre for Analysis and Synthesis, Lund University, P.O. Box 124, Lund SE-221 00, Sweden.
Roberto MastioDepartment of Chemistry, Centre for Analysis and Synthesis, Lund University, P.O. Box 124, Lund SE-221 00, Sweden.
Sophie MannerDepartment of Chemistry, Centre for Analysis and Synthesis, Lund University, P.O. Box 124, Lund SE-221 00, Sweden.
Göran WidmalmArrhenius Laboratory, Department of Organic Chemistry, Stockholm University, Stockholm SE-106 91, Sweden.ORCID https://orcid.org/0000-0001-8303-4481
Emil TykessonDepartment of Experimental Medical Science, Lund University, P.O. Box 117, Lund SE-221 00, Sweden.
Ulf EllervikDepartment of Chemistry, Centre for Analysis and Synthesis, Lund University, P.O. Box 124, Lund SE-221 00, Sweden.ORCID https://orcid.org/0000-0001-5287-0137

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-1,4-Galactosyltransferase 7 (β4GalT7) is a key enzyme in the biosynthesis of glycosaminoglycans (GAG) that transfers the first galactose unit to xylose in the linker region. Searching for new inhibitors of the GAG biosynthesis, we used saturation transfer difference (STD) nuclear magnetic resonance (NMR) spectroscopy to evaluate the binding interactions between β4GalT7 and several pentosides in the presence of UDP donors. These investigations verified the glycosylation specificity of β4GalT7 and revealed that the naphthalene and the uridine moieties were significant contributors to the binding of the acceptor and the donor, respectively, while the galactose part was less important. Based on these findings, we set out to investigate conjugates of UDP and naphthoxylosides to function as transition state analogues. These compounds were synthesized using a one-pot procedure and tested as inhibitors in a β4GalT7 assay. Interestingly, one truncated analogue, a bisphosphonate-xyloside construct, showed a significant inhibition (IC

Identifiers

PMID41358124
PMCPMC12676349

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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.