ArticleProceedings of the National Academy of Sciences of the United States of America2025
Poly(ADP-ribose) binding sites on collagen I fibrils for nucleating intrafibrillar bone mineral.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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.
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
5 citing papers in PubMed.
- Osteoblast-derived CAR3 synergizing with collagen and bone sialoprotein enhances bone formation.International journal of oral science · 2026Article
- Poly(ADP-ribose) (PAR) exhibits ion-dependent structural properties distinct from RNA.Nucleic acids research · 2026Article
- The Role of Confinement in Biomineralization.Chemical reviews · 2025Review
- Taking a closer look at matrix vesicle biogenesis.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2025Review
- Ultrastructural Aspects of Physiological Mineralization: A Comparative Study in Different Hard Tissues.Biomolecules · 2025Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Bone calcification is essential for vertebrate life. The mechanism by which mineral ions are transported into collagen fibrils to induce intrafibrillar mineral formation requires a calcium binding biopolymer that also has highly selective binding to the collagen fibril hole zones where intrafibrillar calcification begins, over other bone extracellular matrix components. Poly(ADP-ribose) (PAR) has been shown to be a candidate biopolymer for this process and we show here that PAR has high affinity, highly conserved binding sites in the collagen type I C-terminal telopeptides. The identification of these PAR-collagen binding sites gives insights into the chemical mechanisms underlying bone calcification and possible mechanisms behind pathologies where there is dysfunctional bone calcification.
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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 Socratic graph.