Evidence map›Paper›PMID 42681151›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

Recombinant Production and Characterization of Human Enzymes Responsible for Collagen Lysine Post-translational Modifications.

Daiana Mattoteia, Matteo De Marco, Sristi Raj Rai, Silvia Faravelli, Luigi Scietti, Federico Forneris

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Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Daiana Mattoteia *Department of Biology and Biotechnology, The Armenise-Harvard Laboratory of Structural Biology, University of Pavia, Pavia, Italy.
Matteo De Marco *Department of Biology and Biotechnology, The Armenise-Harvard Laboratory of Structural Biology, University of Pavia, Pavia, Italy.
Sristi Raj RaiDepartment of Biology and Biotechnology, The Armenise-Harvard Laboratory of Structural Biology, University of Pavia, Pavia, Italy.
Silvia FaravelliDepartment of Biology and Biotechnology, The Armenise-Harvard Laboratory of Structural Biology, University of Pavia, Pavia, Italy.
Luigi SciettiDepartment of Biology and Biotechnology, The Armenise-Harvard Laboratory of Structural Biology, University of Pavia, Pavia, Italy.
Federico FornerisDepartment of Biology and Biotechnology, The Armenise-Harvard Laboratory of Structural Biology, University of Pavia, Pavia, Italy. federico.forneris@unipv.it.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biosynthesis of collagen molecules, as well as collagenous segments of non-collagen proteins, requires extensive post-translational modifications (PTMs) that confer specific functional and structural properties to tissues and organs. Within collagen polypeptide sequences, lysine residues are subject to a series of PTMs, resulting in hydroxylation and subsequent O-linked glycosylation of their side chains. These modifications are catalyzed by two distinct metalloenzyme families, named LH/PLOD and GLT25D/COLGALT, which alternatively process modified lysine side chains yielding 5-hydroxylysine (LH/PLOD), β-(1,O)-galactosyl-5-hydroxylysine (GLT25D/COLGALT), and α-(1,2)-glucosyl-β-(1,O)-galactosyl-5-hydroxylysine (LH/PLOD). In this chapter, we illustrate strategies to recombinantly produce human full-length LH3/PLOD3 as well as GLT25D1/COLGALT1, verify the quality of these recombinant preparations, and perform direct and indirect assays to evaluate their enzymatic activities in vitro on synthetic collagen peptides and gelatin.

Indexed as

CollagenLysineProtein Processing, Post-TranslationalGalactosyltransferasesGlycosylationHumansHydroxylysineProcollagen-Lysine, 2-Oxoglutarate 5-DioxygenaseRecombinant ProteinsCollagenGalactosyltransferasesHydroxylysineLysinePLOD3 protein, humanProcollagen-Lysine, 2-Oxoglutarate 5-DioxygenaseRecombinant ProteinsEnzymatic activity assaysEnzymeGalactosyltransferaseGLT25D/COLGALTGlucosyltransferaseLH/PLODLysyl hydroxylasePost-translational modificationsProtein characterizationRecombinant protein production

Identifiers

PMID42681151

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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.