Evidence map›Paper›PMID 35922533›Full record

ArticleScientific reports2022

Sulfated glycosaminoglycans inhibit transglutaminase 2 by stabilizing its closed conformation.

Claudia Damaris Müller, Gloria Ruiz-Gómez, Sophie Cazzonelli, Stephanie Möller, Robert Wodtke, Reik Löser, Joanna Freyse, Jan-Niklas Dürig, Jörg Rademann, Ute Hempel and 2 more

Erratum issuedOpen access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.5field-weighted citation impact, top 36% of its field
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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. The Role of Transglutaminase 2 in Cancer: An Update.International journal of molecular sciences · 2024
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 4 institutions in 1 country.

Claudia Damaris Müller *Institute of Physiological Chemistry, Medical Faculty Carl Gustav Carus, Technische Universität Dresden, Fetscherstraße 74, 01307, Dresden, Germany.
Gloria Ruiz-Gómez *Structural Bioinformatics, BIOTEC, Technische Universität Dresden, Tatzberg 47-51, 01307, Dresden, Germany.
Sophie CazzonelliInstitute of Physiological Chemistry, Medical Faculty Carl Gustav Carus, Technische Universität Dresden, Fetscherstraße 74, 01307, Dresden, Germany.
Stephanie MöllerBiomaterials Department, INNOVENT e.V., Prüssingstraße 27 B, 07745, Jena, Germany.
Robert WodtkeHelmholtz-Zentrum Dresden-Rossendorf, Institute of Radiopharmaceutical Cancer Research, Bautzner Landstrasse 400, 01328, Dresden, Germany.
Reik LöserHelmholtz-Zentrum Dresden-Rossendorf, Institute of Radiopharmaceutical Cancer Research, Bautzner Landstrasse 400, 01328, Dresden, Germany.
Joanna FreyseInstitute of Pharmacy, Freie Universität Berlin, Königin-Luise-Straße 2/4, 14195, Berlin, Germany.
Jan-Niklas DürigInstitute of Pharmacy, Freie Universität Berlin, Königin-Luise-Straße 2/4, 14195, Berlin, Germany.
Jörg RademannInstitute of Pharmacy, Freie Universität Berlin, Königin-Luise-Straße 2/4, 14195, Berlin, Germany.
Ute HempelInstitute of Physiological Chemistry, Medical Faculty Carl Gustav Carus, Technische Universität Dresden, Fetscherstraße 74, 01307, Dresden, Germany.
M Teresa PisabarroStructural Bioinformatics, BIOTEC, Technische Universität Dresden, Tatzberg 47-51, 01307, Dresden, Germany. maria_teresa.pisabarro@tu-dresden.de.
Sarah VogelInstitute of Physiological Chemistry, Medical Faculty Carl Gustav Carus, Technische Universität Dresden, Fetscherstraße 74, 01307, Dresden, Germany. sarah.vogel@tu-dresden.de.
TU Dresden · DEFreie Universität Berlin · DEHelmholtz-Zentrum Dresden-Rossendorf · DEInnovent · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transglutaminases (TGs) catalyze the covalent crosslinking of proteins via isopeptide bonds. The most prominent isoform, TG2, is associated with physiological processes such as extracellular matrix (ECM) stabilization and plays a crucial role in the pathogenesis of e.g. fibrotic diseases, cancer and celiac disease. Therefore, TG2 represents a pharmacological target of increasing relevance. The glycosaminoglycans (GAG) heparin (HE) and heparan sulfate (HS) constitute high-affinity interaction partners of TG2 in the ECM. Chemically modified GAG are promising molecules for pharmacological applications as their composition and chemical functionalization may be used to tackle the function of ECM molecular systems, which has been recently described for hyaluronan (HA) and chondroitin sulfate (CS). Herein, we investigate the recognition of GAG derivatives by TG2 using an enzyme-crosslinking activity assay in combination with in silico molecular modeling and docking techniques. The study reveals that GAG represent potent inhibitors of TG2 crosslinking activity and offers atom-detailed mechanistic insights.

Indexed as

GlycosaminoglycansProtein Glutamine gamma Glutamyltransferase 2Heparan SulfateTransglutaminasesA73025GlycosaminoglycansHeparan SulfateProtein Glutamine gamma Glutamyltransferase 2Transglutaminases

Identifiers

PMID35922533
PMCPMC9349199
OpenAlexW4289549981

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

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 Socratic graph.