Advanced glycation end-products reduce collagen molecular sliding to affect collagen fibril damage mechanisms but not stiffness. [PDF]
PLoS ONE, 2014 Advanced glycation end-products (AGE) contribute to age-related connective tissue damage and functional deficit. The documented association between AGE formation on collagens and the correlated progressive stiffening of tissues has widely been presumed ...
Gion Fessel +7 more
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Thermal Destabilization of Collagen Matrix Hierarchical Structure by Freeze/Thaw. [PDF]
PLoS ONE, 2016 This study aims to characterize and understand the effects of freezing on collagen structures and functionality. Specifically, thermodynamic destabilization of collagen at molecular- and fibril-levels by combination of low temperatures and freezing were ...
Altug Ozcelikkale, Bumsoo Han
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PLoS ONE, 2020 Opticin is a class III member of the extracellular matrix small leucine-rich repeat protein/proteoglycan (SLRP) family found in vitreous humour and cartilage.
Uwe Hansen +3 more
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Revealing Accessibility of Cryptic Protein Binding Sites within the Functional Collagen Fibril
Biomolecules, 2017 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 ...
Cody L. Hoop +4 more
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Marine Polysaccharide-Collagen Coatings on Ti6Al4V Alloy Formed by Self-Assembly
Micromachines, 2019 Polysaccharides of marine origin are gaining interest as biomaterial components. Bacteria derived from deep-sea hydrothermal vents can produce sulfated exopolysaccharides (EPS), which can influence cell behavior.
Karl Norris +10 more
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Journal of Tissue Engineering, 2022 Tendon is predominantly composed of aligned type I collagen, but additional isoforms are known to influence fibril architecture and maturation, which contribute to the tendon’s overall biomechanical performance. The role of the less well-studied collagen
Adam J Janvier +5 more
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The collαgen III fibril has a "flexi-rod" structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles. [PDF]
PLoS ONE, 2017 Collagen III is critical to the integrity of blood vessels and distensible organs, and in hemostasis. Examination of the human collagen III interactome reveals a nearly identical structural arrangement and charge distribution pattern as for collagen I ...
J Des Parkin +7 more
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Collagen type XIV is proportionally lower in the lung tissue of patients with IPF
Scientific Reports, 2023 Abnormal deposition of extracellular matrix (ECM) in lung tissue is a characteristic of idiopathic pulmonary fibrosis (IPF). Increased collagen deposition is also accompanied by altered collagen organization.
Mehmet Nizamoglu +10 more
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Measurement of Elastic Modulus of Collagen Type I Single Fiber. [PDF]
PLoS ONE, 2016 Collagen fibers are the main components of the extra cellular matrix and the primary contributors to the mechanical properties of tissues. Here we report a novel approach to measure the longitudinal component of the elastic moduli of biological fibers ...
Pavel Dutov +4 more
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New imaging tools reveal live cellular collagen secretion, fibril dynamics and network organisation
Scientific ReportsAlthough light microscopy has been used to examine the early trafficking of collagen within the cell, much of our understanding of the detailed organisation of cell deposited collagen is from static electron microscopy studies. To understand the dynamics
Olivia Kent +8 more
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