Current Insights into Collagen Type I [PDF]
Polymers, 2021 Collagen type I (Col-I) is unique due to its high biocompatibility in human tissue. Despite its availability from various sources, Col-I naturally mimics the extracellular matrix (ECM) and generally makes up the larger protein component (90%) in vasculature, skin, tendon bone, and other tissue.
Ruth Naomi +2 more
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Nanomechanics of Type I Collagen [PDF]
Biophysical Journal, 2016 Type I collagen is the predominant collagen in mature tendons and ligaments, where it gives them their load-bearing mechanical properties. Fibrils of type I collagen are formed by the packing of polypeptide triple helices. Higher-order structures like fibril bundles and fibers are assembled from fibrils in the presence of other collagenous molecules ...
Sameer, Varma +2 more
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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
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Interaction of Biglycan with Type I Collagen [PDF]
Journal of Biological Chemistry, 1995 The small proteoglycan decorin is known to interact with type I collagen fibrils, thereby influencing the kinetics of fibril formation and the distance between adjacent collagen fibrils. The structurally related proteoglycan biglycan has been proposed not to bind to fibrillar collagens.
E, Schönherr +5 more
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Effect of Substrate Composition and Alignment on Corneal Cell Phenotype [PDF]
, 2011 Corneal blindness is a significant problem treated primarily by corneal transplants. Donor tissue supply is low, creating a growing need for an alternative.
Haskell, Richard C. +4 more
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Integrin α2β1 Expression Regulates Matrix Metalloproteinase-1-Dependent Bronchial Epithelial Repair in Pulmonary Tuberculosis. [PDF]
, 2018 Pulmonary tuberculosis (TB) is caused by inhalation of Mycobacterium tuberculosis, which damages the bronchial epithelial barrier to establish local infection.
Akif A. Khawaja +8 more
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Mineralization of Type I Collagen [PDF]
Biophysical Journal, 2003 It was previously found that the lateral spacing of the collagen molecules in wet mineralized tissues is exactly proportional to the inverse wet density. Several properties were investigated and the same type of relationship was observed each time. A possible explanation is offered.
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Structure-mechanics relationships of collagen fibrils in the Osteogenesis Imperfecta Mouse model [PDF]
, 2015 The collagen molecule, which is the building block of collagen fibrils, is a triple helix of two α1(I) chains and one α2(I) chain. However, in the severe mouse model of osteogenesis imperfecta (OIM), deletion of the COL1A2 gene results in the ...
Andriotis, OG +7 more
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Helical mutations in type I collagen that affect the processing of the amino-propeptide result in an Osteogenesis Imperfecta/Ehlers-Danlos Syndrome overlap syndrome [PDF]
, 2013 Background: Whereas mutations affecting the helical domain of type I procollagen classically cause Osteogenesis Imperfecta (OI), helical mutations near the amino (N)-proteinase cleavage site have been suggested to result in a mixed OI/Ehlers-Danlos ...
De Paepe, Anne +9 more
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Human collagen Krox up-regulates type I collagen expression in normal and scleroderma fibroblasts through interaction with Sp1 and Sp3 transcription factors. [PDF]
, 2007 Despite several investigations, the transcriptional mechanisms that regulate the expression of both type I collagen genes (COL1A1 and COL1A2) in either physiological or pathological situations, such as scleroderma, are not completely known.
Beauchef, Gallic +11 more
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