ArticleProtein science : a publication of the Protein Society2016
Three reasons protein disorder analysis makes more sense in the light of collagen.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- A Survey of Predicted Protein-Protein Interactions Involving Disordered Regions in Humans.Journal of molecular biology · 2026Article
- Assessing variant effect predictors and disease mechanisms in intrinsically disordered proteins.PLoS computational biology · 2025Article
- Disentangling the complexity of low complexity proteins.Briefings in bioinformatics · 2020Review
- 'Why genes in pieces?'-revisited.Nucleic acids research · 2019Article
- Article
- Large-scale analysis of intrinsic disorder flavors and associated functions in the protein sequence universe.Protein science : a publication of the Protein Society · 2016Article
- Intrinsic disorder in spondins and some of their interacting partners.Intrinsically disordered proteins · 2016Article
- Intrinsic disorder in biomarkers of insulin resistance, hypoadiponectinemia, and endothelial dysfunction among the type 2 diabetic patients.Intrinsically disordered proteins · 2016Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
We have identified that the collagen helix has the potential to be disruptive to analyses of intrinsically disordered proteins. The collagen helix is an extended fibrous structure that is both promiscuous and repetitive. Whilst its sequence is predicted to be disordered, this type of protein structure is not typically considered as intrinsic disorder. Here, we show that collagen-encoding proteins skew the distribution of exon lengths in genes. We find that previous results, demonstrating that exons encoding disordered regions are more likely to be symmetric, are due to the abundance of the collagen helix. Other related results, showing increased levels of alternative splicing in disorder-encoding exons, still hold after considering collagen-containing proteins. Aside from analyses of exons, we find that the set of proteins that contain collagen significantly alters the amino acid composition of regions predicted as disordered. We conclude that research in this area should be conducted in the light of the collagen helix.
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Registered trials
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