Results 11 to 20 of about 23,206 (306)
Collagen fibril formation [PDF]
Biochemical Journal, 1996 Collagen is most abundant in animal tissues as very long fibrils with a characteristic axial periodic structure. The fibrils provide the major biomechanical scaffold for cell attachment and anchorage of macromolecules, allowing the shape and form of tissues to be defined and maintained.
Karl E. Kadler +3 more
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Mechanical Properties of Collagen Fibrils [PDF]
Biophysical Journal, 2007 The formation of collagen fibers from staggered subfibrils still lacks a universally accepted model. Determining the mechanical properties of single collagen fibrils (diameter 50-200 nm) provides new insights into collagen structure. In this work, the reduced modulus of collagen was measured by nanoindentation using atomic force microscopy.
Patrick Mesquida +6 more
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Stabilization and anomalous hydration of collagen fibril under heating. [PDF]
PLoS ONE, 2013 BACKGROUND: Type I collagen is the most common protein among higher vertebrates. It forms the basis of fibrous connective tissues (tendon, chord, skin, bones) and ensures mechanical stability and strength of these tissues.
Sasun G Gevorkian +4 more
doaj +1 more source
Collagen Fibrils: Nanoscale Ropes [PDF]
Biophysical Journal, 2007 The formation of collagen fibrils from staggered repeats of individual molecules has become "accepted" wisdom. However, for over thirty years now, such a model has failed to resolve several structural and functional questions. In a novel approach, it was found, using atomic force microscopy, that tendon collagen fibrils are composed of subcomponents in
Michael A. Horton +4 more
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Inhibition of collagen fibril formation [PDF]
Fibrogenesis & Tissue Repair, 2012 The overall aim of presented study is to test the inhibition of the formation of collagen fibrils as the novel approach to reduce accumulation of pathological fibrotic deposits. The main hypothesis is that by interfering with the initial steps of the extracellular process of collagen fibril formation, it is possible to reduce the formation of fibrotic ...
Andrzej Steplewski, Andrzej Fertala
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Regional fibronectin and collagen fibril co-assembly directs cell proliferation and microtissue morphology. [PDF]
PLoS ONE, 2013 The extracellular matrix protein, fibronectin stimulates cells to self-assemble into three-dimensional multicellular structures by a mechanism that requires the cell-dependent conversion of soluble fibronectin molecules into insoluble fibrils ...
Carlos A Sevilla +2 more
doaj +1 more source
Frontiers in Bioengineering and Biotechnology, 2021 Porous mineralized collagen membranes efficiently promote bone regeneration. To generate them, we need to fabricate collagen membranes that are porous.
Zhenzhen Wu +4 more
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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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Decorin core protein (decoron) shape complements collagen fibril surface structure and mediates its binding. [PDF]
PLoS ONE, 2009 Decorin is the archetypal small leucine rich repeat proteoglycan of the vertebrate extracellular matrix (ECM). With its glycosaminoglycuronan chain, it is responsible for stabilizing inter-fibrillar organization. Type I collagen is the predominant member
Joseph P R O Orgel +4 more
doaj +1 more source
Quantification of collagen ultrastructure after penetrating keratoplasty - implications for corneal biomechanics. [PDF]
PLoS ONE, 2013 PURPOSE:To quantify long-term changes in stromal collagen ultrastructure following penetrating keratoplasty (PK), and evaluate their possible implications for corneal biomechanics.
Craig Boote +9 more
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