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
doaj +1 more source
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
doaj +1 more source
Non-equilibrium Growth and Twist of Cross-Linked Collagen Fibrils [PDF]
, 2020 The lysyl oxidase (LOX) enzyme that catalyses cross-link formation during the assembly of collagen fibrils in vivo is too large to diffuse within assembled fibrils, and so is incompatible with a fully equilibrium mechanism for fibril formation. We propose that enzymatic cross-links are formed at the fibril surface during the growth of collagen fibrils;
arxiv +1 more source
Live Imaging of Type I Collagen Assembly Dynamics in Osteoblasts Stably Expressing GFP and mCherry-Tagged Collagen Constructs [PDF]
, 2018 Type I collagen is the most abundant extracellular matrix protein in bone and other connective tissues and plays key roles in normal and pathological bone formation as well as in connective tissue disorders and fibrosis.
Bonewald, Lynda F. +9 more
core +1 more source
Determinants of Collagen Fibril Structure
Biophysical Journal, 1986 Fillers, and C. Cohen. 1980. Motions of tropomyosin. Biophys. J. 32:485-502. 3. Phillips, G. N., Jr., and D. Boylan. 1984. Large scale fluctuations of tropomyosin in the crystal. Trans. Amer. Cryst. Assoc. 20:163166. 4. Petsko, G. A., and D. Ringe. 1984. Fluctuations in protein structure form x-ray diffraction. Annu. Rev. Biophys. Bioeng. 13:331-371. 5.
Eric F. Eikenberry, Barbara Brodsky
openaire +3 more sources
Collagens - structure, function and biosynthesis. [PDF]
, 2003 The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions.
Aigner, T, Gelse, K, Poschl, E
core +1 more source
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
doaj +1 more source
Advanced-Glycation Endproducts: How cross-linking properties affect the collagen fibril behavior [PDF]
arXiv, 2023 Advanced-Glycation-Endproducts (AGEs) are known to be a major cause of impaired tissue material properties. In collagen fibrils, the main building component of human tissue, these AGEs appear as fibrillar cross-links. When AGEs accumulate in collagen fibrils, a process often caused by diabetes and aging, the mechanical properties of the collagen fibril
arxiv
Multiscale approach including microfibril scale to assess elastic constants of cortical bone based on neural network computation and homogenization method [PDF]
, 2013 The complexity and heterogeneity of bone tissue require a multiscale modelling to understand its mechanical behaviour and its remodelling mechanisms.
Alexander +106 more
core +6 more sources
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
doaj +1 more source