ArticleMethods in molecular biology (Clifton, N.J.)2026
Atomic Force Microscopy Investigations of Collagen: From Single Molecules to Fibrils.
Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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
1 citing paper in PubMed.
- On-glass Interference Confocal Reflectance Microscopy for Collagen Fibril Diameter Measurement.Proceedings of SPIE--the International Society for Optical Engineering · 2026Article
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Authors and funding
3 authors.
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Abstract
Collagen is a key component of the extracellular matrix, providing structural support and influencing cellular behavior through its physical properties. Understanding its mechanical properties is essential for elucidating its role in tissue integrity and pathology. Collagen forms complex hierarchical structures, ranging from individual proteins to higher-order fibrils, fibers, and networks, each contributing to the mechanical stability of tissues. In this methods chapter, we outline the use of atomic force microscopy (AFM) to investigate collagen's structural properties across multiple hierarchical levels, from single molecules to fibrils. We describe the preparation of collagen samples for AFM analysis of collagen in three forms: proteins, reconstituted fibrils, and tendon-derived fibrils from rat tails. Additionally, we describe a MATLAB-based image analysis method for quantitatively assessing mechanical properties of individual collagen proteins.
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Registered trials
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