Evidence map›Paper›PMID 40240392›Full record

ArticleNature communications2025

Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1.

Matteo De Marco, Sristi Raj Rai, Luigi Scietti, Daiana Mattoteia, Stefano Liberi, Elisabetta Moroni, Alberta Pinnola, Alice Vetrano, Claudio Iacobucci, Carlo Santambrogio and 2 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
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  5. Review
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  7. Article
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  9. Article
  10. Article
  11. The Crystal Structure ofBiochemistry · 2025
    Article
  12. Article
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.

Matteo De Marco *The Armenise-Harvard Laboratory of Structural Biology, Dept. Biology and Biotechnology, University of Pavia, Via Ferrata 9A, 27100, Pavia, Italy.ORCID http://orcid.org/0000-0002-6637-0683
Sristi Raj Rai *The Armenise-Harvard Laboratory of Structural Biology, Dept. Biology and Biotechnology, University of Pavia, Via Ferrata 9A, 27100, Pavia, Italy.
Luigi Scietti *The Armenise-Harvard Laboratory of Structural Biology, Dept. Biology and Biotechnology, University of Pavia, Via Ferrata 9A, 27100, Pavia, Italy.
Daiana MattoteiaThe Armenise-Harvard Laboratory of Structural Biology, Dept. Biology and Biotechnology, University of Pavia, Via Ferrata 9A, 27100, Pavia, Italy.ORCID http://orcid.org/0000-0003-1089-0126
Stefano LiberiThe Armenise-Harvard Laboratory of Structural Biology, Dept. Biology and Biotechnology, University of Pavia, Via Ferrata 9A, 27100, Pavia, Italy.
Elisabetta MoroniSCITEC-CNR, via Mario Bianco 9, I-20131, Milano, Italy.ORCID http://orcid.org/0000-0002-7705-7457
Alberta PinnolaBioPhotoLab, Dept. Biology and Biotechnology, University of Pavia, Via Ferrata 9A, 27100, Pavia, Italy.ORCID http://orcid.org/0000-0001-8373-7638
Alice VetranoDepartment of Physical and Chemical Sciences, University of L'Aquila, 67100, L'Aquila, Italy.ORCID http://orcid.org/0000-0002-9844-5942
Claudio IacobucciDepartment of Physical and Chemical Sciences, University of L'Aquila, 67100, L'Aquila, Italy.
Carlo SantambrogioDepartment of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126, Milan, Italy.ORCID http://orcid.org/0000-0003-3986-6971
Giorgio ColomboDepartment of Chemistry, University of Pavia, Via Taramelli 12, Pavia, Italy.ORCID http://orcid.org/0000-0002-1318-668X
Federico FornerisThe Armenise-Harvard Laboratory of Structural Biology, Dept. Biology and Biotechnology, University of Pavia, Via Ferrata 9A, 27100, Pavia, Italy. federico.forneris@unipv.it.ORCID http://orcid.org/0000-0002-7818-1804

Funding

Associazione Italiana per la Ricerca sul Cancro (Italian Association for Cancer Research) MFAG 20075, BRIDGE 27004Ehlers-Danlos Society (EDS) Rarer Types EDS Grant 2022Giovanni Armenise-Harvard Foundation CDA 2013Ministero della Salute (Ministry of Health, Italy) Piano Operativo Salute, IMMUNO-HUBMinistero dell'Istruzione, dell'Università e della Ricerca (Ministry of Education, University and Research) NextGeneration-EU PNRR MUR M4C2 PE00000007 INF-ACTMinistero dell'Istruzione, dell'Università e della Ricerca (Ministry of Education, University and Research) PRIN PNRR 2022 P20224WAMERegione Lombardia (Region of Lombardy) regional law n° 9/2020, resolution n° 3776/2020
6 · The paper itself

Abstract

During collagen biosynthesis, lysine residues undergo extensive post-translational modifications through the alternate action of two distinct metal ion-dependent enzyme families (i.e., LH/PLODs and GLT25D/COLGALT), ultimately producing the highly conserved α-(1,2)-glucosyl-β-(1,O)-galactosyl-5-hydroxylysine pattern. Malfunctions in these enzymes are linked to developmental pathologies and extracellular matrix alterations associated to enhanced aggressiveness of solid tumors. Here, we characterized human GLT25D1/COLGALT1, revealing an elongated head-to-head homodimeric assembly. Each monomer encompasses two domains (named GT1 and GT2), both unexpectedly capable of binding metal ion cofactors and UDP-α-galactose donor substrates, resulting in four candidate catalytic sites per dimer. We identify the catalytic site in GT2, featuring an unusual Glu-Asp-Asp motif critical for Mn

Indexed as

CollagenGalactosyltransferasesHydroxylysineCalciumCatalytic DomainHumansManganeseModels, MolecularProtein MultimerizationSubstrate SpecificityCalciumCollagenGalactosyltransferasesHydroxylysineManganese

Identifiers

PMID40240392
PMCPMC12003778

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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.