ArticleNature communications2025
Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1.
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.
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Who cites it
12 citing papers in PubMed.
- Crystal structure of a β1,3-Glucosyltransferase reveals an unusual substrate recognition by a two-domain GT-A fold glycosyltransferase.The Journal of biological chemistry · 2026Article
- Effect of Letrozole Administration on Reproductive Performance and Plasma Metabolites of Ewes During Estrus Synchronization Treatment.Life (Basel, Switzerland) · 2026Article
- Salvianolic Acid B Inhibited LH2 Expression to Reduce Collagen Synthesis in Pulmonary Fibrosis.Journal of cellular and molecular medicine · 2026Article
- High-Fiber Diet Supplemented with N-Carbamylglutamate Modulates Uterine Microbiota, Metabolites, and Transcriptome to Improve Reproductive Efficiency in Sows.Antioxidants (Basel, Switzerland) · 2026Article
- Gene Polymorphisms Associated with Osteoarthritis: Potential Implications for Nutrigenetics and Precision Nutrition.Nutrients · 2026Review
- Succinate supplementation ameliorates musculoskeletal defects caused by PLOD3 mutations in a BCARD syndrome model.Genome medicine · 2026Article
- Magnesium Deficiency Accelerates Gut Aging and Increases Susceptibility to Colitis.Aging cell · 2026Article
- Molecular basis of collagen galactosylation by GLT25D1.Nature communications · 2026Article
- Enzymatic craftsmanship in collagen glycosylation.Nature communications · 2025Article
- Impact of Genetic Variants Associated with Neurodevelopmental Disorders on the WAVE Regulatory Complex.Journal of chemical information and modeling · 2025Article
- The Crystal Structure ofBiochemistry · 2025Article
- Cloning, expression, and characterization of collagen galactosyltransferases from human, sponge, and sea walnut.Protein expression and purification · 2025Article
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Authors and funding
12 authors.
Funding
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
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