Results 1 to 10 of about 70 (69)

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, Pauzi Muhd Ridzuan, Hasnah Bahari   +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, Joseph P R O, Orgel, Jay D, Schieber   +2 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, P, Witsch-Prehm, B, Harrach, H, Robenek, J, Rauterberg, H, Kresse   +5 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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Thermal (In)Stability of Type I Collagen Fibrils [PDF]

Physical Review Letters, 2009
We measured Young's modulus at temperatures ranging from 20 to 100 ^{\circ}$C for a collagen fibril taken from rat's tendon. The hydration change under heating and the damping decrement were measured as well. At physiological temperatures $25-45^{\circ}$C Young's modulus decreases, which can be interpreted as instability of collagen.
Gevorkian, S. G., Allahverdyan, A. E., Gevorgyan, D. S., Simonian, A. L.   +3 more
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Chondrocyte Migration to Fibronectin, Type I Collagen, and Type II Collagen.

Cell Structure and Function, 1997
It is well known that cellular interactions, such as cell adhesion, migration, invasion, between cells and the extracellular matrix are mediated by the integrin family of cell surface receptors. Chondrocytes are surrounded by an abundant extracellular matrix, but there is less information on the cellular receptors which interact with this matrix.
Shimizu, Mitsuo, Minakuchi, Kazunobu, Kaji, Satomi, Koga, Junichi   +3 more
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Coating of titanium implants with type‐I collagen [PDF]

Journal of Orthopaedic Research, 2004
AbstractPurpose: Type‐I collagen, the major structural protein in bone, has beneficial properties regarding bone regeneration. Little is known about the potential effects of collagen coating on orthopedic implants.Methods: 3 to 6 μg/cm2 of lyophilized type‐I collagen was absorbed on titanium rods.
Rammelt, Stefan, Schulze, Eva, Bernhardt, Ricardo, Hanisch, Uwe, Scharnweber, Dieter, Worch, Hartmut, Zwipp, Hans, Biewener, Achim   +7 more
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Microfibrillar structure of type I collagen in situ [PDF]

Proceedings of the National Academy of Sciences, 2006
The fibrous collagens are ubiquitous in animals and form the structural basis of all mammalian connective tissues, including those of the heart, vasculature, skin, cornea, bones, and tendons. However, in comparison with what is known of their production, turnover and physiological structure, very little is understood regarding the three ...
Orgel, J P R O, Irving, T C, Miller, A, Wess, Tim J   +3 more
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Collagen Type I, Collagen Type III, and Versican in Vocal Fold Lamina Propria [PDF]

Archives of Otolaryngology–Head & Neck Surgery, 2011
To analyze the distributions of collagen type I, collagen type III, and versican in the lamina propria of the human vocal fold.Cross-sectional analysis of cadaveric vocal folds of adult human larynges.Academic tertiary referral center.Larynges harvested at autopsy from 10 adult men and 10 adult women.Immunohistochemical reactions were performed using ...
Rogerio B, Bühler, Luiz U, Sennes, Domingos H, Tsuji, Thais, Mauad, Luiz, Ferraz da Silva, Paulo N, Saldiva   +5 more
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Collagen cross‐links: location of pyridinoline in type I collagen

FEBS Letters, 1985
Collagen from bone, dentine and tendon (type I), all of which contain the pyridinoline cross‐link at varying levels, were each digested with CNBr. The resulting peptide mixtures were resolved by gel filtration on A 1.5m agarose and assayed for pyridinoline. The polymeric cross‐linked peptide complex, polyαlCB6 [(1980) Biochem. J.
Light, Nicholas, Bailey, Allen J.
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