ArticlePloS one2011
Insights on the evolution of prolyl 3-hydroxylation sites from comparative analysis of chicken and Xenopus fibrillar collagens.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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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.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Preparation and Characterization of Hydroxylated Recombinant Collagen by Incorporating Proline and Hydroxyproline in Proline-DeficientBioengineering (Basel, Switzerland) · 2024Article
- White Isthmus Transcriptome Analysis Reveals the Mechanism of Translucent Eggshell Formation.Animals : an open access journal from MDPI · 2024Article
- Developmental Stage-dependent Regulation of Prolyl 3-Hydroxylation in Tendon Type I Collagen.The Journal of biological chemistry · 2016Article
- Ancient proteins resolve the evolutionary history of Darwin's South American ungulates.Nature · 2015Article
- Post-translationally abnormal collagens of prolyl 3-hydroxylase-2 null mice offer a pathobiological mechanism for the high myopia linked to human LEPREL1 mutations.The Journal of biological chemistry · 2015Article
- Evolutionary origins of C-terminal (GPP)n 3-hydroxyproline formation in vertebrate tendon collagen.PloS one · 2014Article
- Collagen prolyl 3-hydroxylation: a major role for a minor post-translational modification?Connective tissue research · 2013Review
- Peptidyl 3-hydroxyproline binding properties of type I collagen suggest a function in fibril supramolecular assembly.Biochemistry · 2012Article
- A role for prolyl 3-hydroxylase 2 in post-translational modification of fibril-forming collagens.The Journal of biological chemistry · 2011Article
- Type I and type V procollagen triple helix uses different subsets of the molecular ensemble for lysine posttranslational modifications in the rER.The Journal of biological chemistryArticle
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Recessive mutations that prevent 3-hydroxyproline formation in type I collagen have been shown to cause forms of osteogenesis imperfecta. In mammals, all A-clade collagen chains with a GPP sequence at the A1 site (P986), except α1(III), have 3Hyp at residue P986. Available avian, amphibian and reptilian type III collagen sequences from the genomic database (Ensembl) all differ in sequence motif from mammals at the A1 site. This suggests a potential evolutionary distinction in prolyl 3-hydroxylation between mammals and earlier vertebrates. Using peptide mass spectrometry, we confirmed that this 3Hyp site is fully occupied in α1(III) from an amphibian, Xenopus laevis, as it is in chicken. A thorough characterization of all predicted 3Hyp sites in collagen types I, II, III and V from chicken and xenopus revealed further differences in the pattern of occupancy of the A3 site (P707). In mammals only α2(I) and α2(V) chains had any 3Hyp at the A3 site, whereas in chicken all α-chains except α1(III) had A3 at least partially 3-hydroxylated. The A3 site was also partially 3-hydroxylated in xenopus α1(I). Minor differences in covalent cross-linking between chicken, xenopus and mammal type I and III collagens were also found as a potential index of evolving functional differences. The function of 3Hyp is still unknown but observed differences in site occupancy during vertebrate evolution are likely to give important clues.
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