Evidence map›Paper›PMID 41835542›Full record

ArticleACS omega2026

Inhibition of Dermatan Sulfate Epimerase 1 by Substituted Glucuronic Acids.

Roberto Mastio, Isolde Zuleta Sjögren, John Dahlquist, Anders Sundin, Gunilla Westergren-Thorsson, Sophie Manner, Emil Tykesson, Anders Malmström, Ulf Ellervik

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In one paragraph

Article in ACS omega, 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

9 authors.

Roberto MastioLund University, Department of Chemistry, Centre for Analysis and Synthesis, P.O. Box 124, Lund SE-221 00, Sweden.
Isolde Zuleta SjögrenLund University, Department of Chemistry, Centre for Analysis and Synthesis, P.O. Box 124, Lund SE-221 00, Sweden.ORCID https://orcid.org/0009-0007-5193-5438
John DahlquistLund University, Department of Chemistry, Centre for Analysis and Synthesis, P.O. Box 124, Lund SE-221 00, Sweden.
Anders SundinLund University, Department of Chemistry, Centre for Analysis and Synthesis, P.O. Box 124, Lund SE-221 00, Sweden.ORCID https://orcid.org/0000-0001-6615-2419
Gunilla Westergren-ThorssonLund University, Department of Experimental Medical Science, P.O. Box 117, Lund SE-221 00, Sweden.
Sophie MannerLund University, Department of Chemistry, Centre for Analysis and Synthesis, P.O. Box 124, Lund SE-221 00, Sweden.ORCID https://orcid.org/0000-0002-3492-5066
Emil TykessonLund University, Department of Experimental Medical Science, P.O. Box 117, Lund SE-221 00, Sweden.ORCID https://orcid.org/0000-0002-0511-9831
Anders MalmströmLund University, Department of Experimental Medical Science, P.O. Box 117, Lund SE-221 00, Sweden.
Ulf EllervikLund University, Department of Chemistry, Centre for Analysis and Synthesis, 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

Dermatan sulfate epimerase 1 (DS-epi1) is a key enzyme in the biosynthesis of the glycosaminoglycan chondroitin sulfate/dermatan sulfate, catalyzing the conversion of glucuronic acid to iduronic acid at the polymer level. Chondroitin sulfate/dermatan sulfate chains are found on at least 32 proteoglycans, many of which are implicated in human diseases and syndromes, as well as in both malignant and normal cell development. DS-epi1 therefore represents a promising target for drug development, and recent structural studies have provided insights into its active site and catalytic mechanism. Here, we report the synthesis and biological evaluation of inhibitors based on 1,4-disubstituted glucuronic acids. These compounds were synthesized from glucose through a divergent approach, yielding 19 derivatives that were tested in a functional assay. To explore the importance of the carboxylic acid moiety, we also tested the methyl ester analog and the analogous xylose derivative. The most potent compound exhibited an IC

Identifiers

PMID41835542
PMCPMC12980235

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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.