ArticleProceedings of the National Academy of Sciences of the United States of America2006
Microfibrillar structure of type I collagen in situ.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 321 papers.
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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.
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Who cites it
321 citing papers in PubMed, 928 citations in OpenAlex.
- Free energy of collagen-mimetic peptide dimerization and implications for fibrillization.Biophysical journal · 2026Article
- Collagen Scaffolds in Veterinary Medicine: Safety, Sustainability, and Clinical Accessibility of Mammalian- and Marine-Derived Sources-A Scoping Review.Animals : an open access journal from MDPI · 2026Review
- Nonuniform Curvature and Bending Rigidity of Adsorbed Collagen Molecules in Aqueous Solution.Biomacromolecules · 2026Article
- Combination of 3D and 2D Small and Wide Angle X-Ray Scattering Imaging Reveals Diminished Bone Quality in the Superior Human Femoral Neck Cortex.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Sites of non-enzymatic crosslinks pentosidine and glucosepane in collagen I of human cortical bone.Bone · 2026Article
- Unwinding the Neurovascular Unit: The Vascular Extracellular Matrix and Mechanochemical Collagen Functionalization in Vascular Dementia.International journal of molecular sciences · 2026Review
- Introducing non-enzymatic crosslinks into atomistic simulations of collagen fibrils.Bioinformatics (Oxford, England) · 2026Article
- Integrating serial block-face SEM with voxel-based finite element analysis for high-fidelity micromechanical modelling of anisotropic soft tissues: application to human dermis.Biomechanics and modeling in mechanobiology · 2026Article
- Biomimetic mineralization of electrospun elastin-like recombinamer nanofibers.Scientific reports · 2026Article
- Real-time visualization of collagen assembly uncovers metastable properties in hierarchical organization.Nature communications · 2026Article
- Cross-linking of collagen fibrils leads to preferential gap zone mineralization in vitro.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Supramolecular Assembly of Collagen-Mimetic Peptide D-Periodic Fibrils and Nanoassemblies.Biomacromolecules · 2026Article
- Collagen organisation in the fibrous joint capsules in the digits of the human hand.Journal of anatomy · 2026Review
- Analysis of Multi-Component Echo Decay in Achilles Tendon by NMR Spectroscopy.NMR in biomedicine · 2026Article
- Electron and focused ion beam microscopy of fossilized Albertosaurus sarcophagus (Dinosauria: Theropoda) bone reveals nano to microscale features.Scientific reports · 2026Article
- Coarse-grained Martini 3 model for collagen fibrils.Biophysical journal · 2026Article
- How Hydration Weakens Collagen: A Mesoscale Energy Decomposition of Type I and Type II Fibrils.Computational and structural biotechnology journal · 2026Article
- Collagen Mechanics.Sub-cellular biochemistry · 2026Review
- Atomic Force Microscopy Investigations of Collagen: From Single Molecules to Fibrils.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Construction of an In Silico Model to Study the Molecular Functions of Type I Collagen.Methods in molecular biology (Clifton, N.J.) · 2026Article
261 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
The fibrous collagens are ubiquitous in animals and form the structural basis of all mammalian connective tissues, including those of the heart, vasculature, skin, cornea, bones, and tendons. However, in comparison with what is known of their production, turnover and physiological structure, very little is understood regarding the three-dimensional arrangement of collagen molecules in naturally occurring fibrils. This knowledge may provide insight into key biological processes such as fibrillo-genesis and tissue remodeling and into diseases such as heart disease and cancer. Here we present a crystallographic determination of the collagen type I supermolecular structure, where the molecular conformation of each collagen segment found within the naturally occurring crystallographic unit cell has been defined (P1, a approximately 40.0 A, b approximately 27.0 A, c approximately 678 A, alpha approximately 89.2 degrees , beta approximately 94.6 degrees , gamma approximately 105.6 degrees ; reflections: 414, overlapping, 232, and nonoverlapping, 182; resolution, 5.16 A axial and 11.1 A equatorial). This structure shows that the molecular packing topology of the collagen molecule is such that packing neighbors are arranged to form a supertwisted (discontinuous) right-handed microfibril that interdigitates with neighboring microfibrils. This interdigitation establishes the crystallographic superlattice, which is formed of quasihexagonally packed collagen molecules. In addition, the molecular packing structure of collagen shown here provides information concerning the potential modes of action of two prominent molecules involved in human health and disease: decorin and the Matrix Metallo-Proteinase (MMP) collagenase.
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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.