ArticleScientific reports2018
Cryptic binding sites become accessible through surface reconstruction of the type I collagen fibril.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Upregulated CCN1 from pleural mesothelial cells alters collagen I conformation and drives fibrosis via ITGB1/MAPK signaling.Cellular & molecular biology letters · 2026Article
- Nanoscale Structural and Functional Impacts of Disease-Associated Collagen Mutations.bioRxiv : the preprint server for biology · 2025Article
- Poly(ADP-ribose) binding sites on collagen I fibrils for nucleating intrafibrillar bone mineral.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Characterization of Composite Agarose-Collagen Hydrogels for Chondrocyte Culture.Annals of biomedical engineering · 2025Article
- Physiological mechanical forces accelerate the degradation of bovine lung collagen fibers by bacterial collagenase.Scientific reports · 2024Article
- Real-time single-molecule observation of incipient collagen fibrillogenesis and remodeling.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- A practical guide to machine-learning scoring for structure-based virtual screening.Nature protocols · 2023Review
- Probing the effect of glycosaminoglycan depletion on integrin interactions with collagen I fibrils in the native extracellular matrix environment.Protein science : a publication of the Protein Society · 2023Article
- The mechanical cell - the role of force dependencies in synchronising protein interaction networks.Journal of cell science · 2022Review
- Adhesion force microscopy is sensitive to the charge distribution at the surface of single collagen fibrils.Nanoscale advances · 2022Article
- Key Roles of RGD-Recognizing Integrins During Cardiac Development, on Cardiac Cells, and After Myocardial Infarction.Journal of cardiovascular translational research · 2022Review
- Possible Treatment of Myocardial Infarct Based on Tissue Engineering Using a Cellularized Solid Collagen Scaffold Functionalized with Arg-Glyc-Asp (RGD) Peptide.International journal of molecular sciences · 2021Review
- Contrasting Local and Macroscopic Effects of Collagen Hydroxylation.International journal of molecular sciences · 2021Article
- Review
- Increased Collagen Turnover Impairs Tendon Microstructure and Stability in Integrin α2β1-Deficient Mice.International journal of molecular sciences · 2020Article
- Structural studies of the MMP-3 interaction with triple-helical collagen introduce new roles for the enzyme in tissue remodelling.Scientific reports · 2019Article
- Role of prolyl hydroxylation in the molecular interactions of collagens.Essays in biochemistry · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
Collagen fibril interactions with cells and macromolecules in the extracellular matrix drive numerous cellular functions. Binding motifs for dozens of collagen-binding proteins have been determined on fully exposed collagen triple helical monomers. However, when the monomers are assembled into the functional collagen fibril, many binding motifs become inaccessible, and yet critical cellular processes occur. Here, we have developed an early stage atomic model of the smallest repeating unit of the type I collagen fibril at the fibril surface that provides a novel framework to address questions about these functionally necessary yet seemingly obstructed interactions. We use an integrative approach by combining molecular dynamics (MD) simulations with atomic force microscopy (AFM) experiments and show that reconstruction of the collagen monomers within the complex fibril play a critical role in collagen interactions. In particular, the fibril surface shows three major conformational changes, which allow cryptic binding sites, including an integrin motif involved in platelet aggregation, to be exposed. The observed dynamics and reconstruction of the fibril surface promote its role as a "smart fibril" to keep certain binding sites cryptic, and to allow accessibility of recognition domains when appropriate.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.