ReviewBiomolecules2017
Revealing Accessibility of Cryptic Protein Binding Sites within the Functional Collagen Fibril.
Review in Biomolecules, 2017. 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.
- Formins and Arp2/3 Reciprocally Regulate Contact Guidance on Aligned Collagen Fibrils.Cellular and molecular bioengineering · 2025Article
- 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
- Regulation of Joint Tissues and Joint Function: Is There Potential for Lessons to Be Learned Regarding Regulatory Control from Joint Hypermobility Syndromes?International journal of molecular sciences · 2025Review
- 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
- The interplay of collagen, macrophages, and microcalcification in atherosclerotic plaque cap rupture mechanics.Basic research in cardiology · 2024Review
- 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
- Regenerative Approaches for the Treatment of Large Bone Defects.Tissue engineering. Part B, Reviews · 2021Review
- Targeting mechanosensitive MDM4 promotes lung fibrosis resolution in aged mice.The Journal of experimental medicine · 2021Article
- β-Ionone Attenuates Dexamethasone-Induced Suppression of Collagen and Hyaluronic Acid Synthesis in Human Dermal Fibroblasts.Biomolecules · 2021Article
- Ultrastructural Location and Interactions of the Immunoglobulin Receptor Binding Sequence within Fibrillar Type I Collagen.International journal of molecular sciences · 2020Article
- Cellular and extracellular matrix of bone, with principles of synthesis and dependency of mineral deposition on cell membrane transport.American journal of physiology. Cell physiology · 2020Review
- Tumour Initiation: a Discussion on Evidence for a "Load-Trigger" Mechanism.Cell biochemistry and biophysics · 2019Review
- Article
- 3D collagen architecture regulates cell adhesion through degradability, thereby controlling metabolic and oxidative stress.Integrative biology : quantitative biosciences from nano to macro · 2019Article
- Contribution of biomimetic collagen-ligand interaction to intrafibrillar mineralization.Science advances · 2019Article
- Cryptic binding sites become accessible through surface reconstruction of the type I collagen fibril.Scientific reports · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Fibrillar collagens are the most abundant proteins in the extracellular matrix. Not only do they provide structural integrity to all of the connective tissues in the human body, but also their interactions with multiple cell receptors and other matrix molecules are essential to cell functions, such as growth, repair, and cell adhesion. Although specific binding sequences of several receptors have been determined along the collagen monomer, processes by which collagen binding partners recognize their binding sites in the collagen fibril, and the critical driving interactions, are poorly understood. The complex molecular assembly of bundled triple helices within the collagen fibril makes essential ligand binding sites cryptic or hidden from the molecular surface. Yet, critical biological processes that require collagen ligands to have access to interaction sites still occur. In this contribution, we will discuss the molecular packing of the collagen I fibril from the perspective of how collagen ligands access their known binding regions within the fibril, and we will present our analysis of binding site accessibility from the fibril surface. Understanding the basis of these interactions at the atomic level sets the stage for developing drug targets against debilitating collagen diseases and using collagen as drug delivery systems and new biomaterials.
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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 OpenQuestion graph.