ArticleNature communications2025
Deciphering the folding code of collagens.
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 8 papers.
What it found
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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.
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Who cites it
8 citing papers in PubMed.
- Free energy of collagen-mimetic peptide dimerization and implications for fibrillization.Biophysical journal · 2026Article
- Targeting the immune-metabolic axis reverses orthodontics-induced systemic pathology.Signal transduction and targeted therapy · 2026Article
- Molecular foundations of collagen triple helical assembly: the central role of prolyl-4-hydroxylation.The Biochemical journal · 2026Review
- Biomarkers of pulmonary fibrosis in bronchoalveolar lavage fluid and saliva. Study methods and pathophysiological significance.Frontiers in medicine · 2026Review
- Determinants of Chain Selection and Staggering in Heterotrimeric Collagens: A Comprehensive Review of the Structural Data.International journal of molecular sciences · 2025Review
- Nanoscale Structural and Functional Impacts of Disease-Associated Collagen Mutations.bioRxiv : the preprint server for biology · 2025Article
- Collagen Biosynthesis and Its Molecular Ensemble: What Remains Unexplored.Biochemistry · 2025Review
- Decoding collagen's thermally induced unfolding and refolding pathways.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Collagen proteins contain a characteristic structural motif called a triple helix. During the self-assembly of this motif, three polypeptides form a folding nucleus at the C-termini and then propagate towards the N-termini like a zip-chain. While polypeptides from human collagens contain up to a 1000 amino acids, those found in bacteria can contain up to 6000 amino acids. Additionally, the collagen polypeptides are also frequently interrupted by non-helical sequences that disrupt folding and reduce stability. Given the length of polypeptides and the disruptive interruptions, compensating mechanisms that stabilize against local unfolding during propagation and offset the entropic cost of folding are not fully understood. Here, we show that the information for the correct folding of collagen triple helices is encoded in their sequence as interchain electrostatic interactions, which likely act as molecular clamps that prevent local unfolding. In the case of humans, disrupting these electrostatic interactions is associated with severe to lethal diseases.
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Registered trials
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