Results 221 to 230 of about 395,166 (264)

Structure of equine type I and type II collagens

American Journal of Veterinary Research, 1994
Summary Collagen type I was purified from equine skin and flexor tendon, and type II collagen was purified from equine articular cartilage. The proteoglycans in these tissues were extracted, using guanidine hcl; the collagens were solubilized, using pepsin digestion, then were selectively precipitated with NaCl.
R J, Todhunter, J A, Wootton, G, Lust, R R, Minor   +3 more
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Targeting type I collagen for cancer treatment

International Journal of Cancer, 2022
AbstractCollagen is the most abundant protein in animals. Interactions between tumor cells and collagen influence every step of tumor development. Type I collagen is the main fibrillar collagen in the extracellular matrix and is frequently upregulated during tumorigenesis.
Run Shi, Zhe Zhang, Ankai Zhu, Xingxing Xiong, Jie Zhang, Jiang Xu, Man‐Sun Sy, Chaoyang Li   +7 more
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Collagen Type I: A Versatile Biomaterial

2018
Collagen type I is the most abundant matrix protein in the human body and is highly demanded in tissue engineering, regenerative medicine, and pharmaceutical applications. To meet the uprising demand in biomedical applications, collagen type I has been isolated from mammalians (bovine, porcine, goat and rat) and non-mammalians (fish, amphibian, and sea
Shiplu Roy, Chowdhury, Mohd Fauzi, Mh Busra, Yogeswaran, Lokanathan, Min Hwei, Ng, Jia Xian, Law, Ude Chinedu, Cletus, Ruszymah, Binti Haji Idrus   +6 more
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Intermolecular interactions in type I collagens

Journal of Molecular Recognition, 1992
AbstractX‐PLOR modelling of collagen dimers containing Gly‐Glu‐Arg in each chain has been carried out. The interaction between molecules when two Gly_Glu‐Arg are present on each chain is found to be substantially less than two times that obtained with one per chain, implying that relative tilting of two collagen molecules does not offset the ...
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Immunohistochemical study of type I collagen and type I pN-collagen in benign and malignant ovarian neoplasms

Cancer, 1995
Type I collagen is a major constituent of the interstitial connective tissue. Although ovarian carcinoma is known to induce the expression of type I collagen in the peritoneal cavity, the distribution and metabolic activity of this collagen in ovarian tumor tissue are not known.The distributions and staining intensities of different molecular forms of ...
G G, Zhu, L, Risteli, M, Mäkinen, J, Risteli, A, Kauppila, F, Stenbäck   +5 more
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Dual Effects of Type II Collagen on the Degradation of Type I Collagen by Tadpole Collagenase

Collagen and Related Research, 1981
Kinetic analysis of the degradation of mixtures of type I and type II collagens by tadpole collagenase was performed, using [14C]glycine-labeled type I collagen and [3H]acetylated type II collagen as substrates. The degradation rate of type I collagen was decreased in the initial stage of the reaction, then further slowed down giving a constant rate ...
H, Sunada, T, Hayashi, H, Hori, Y, Nagai
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Comparison of Axial Banding Patterns in Fibrils of Type V Collagen and Type I Collagen

Collagen and Related Research, 1987
Type V collagen and type I collagen were obtained from human placenta, essentially by salt fractionation. Precipitates were formed from mixed solutions of type V collagen and type I collagen in various ratios. They were incubated at 37 degrees C for 1 hour and negatively stained with 0.5% uranyl acetate (pH 4.4) at 37 degrees C.
E, Adachi, T, Hayashi
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Distribution of type I collagen in human kidney diseases in comparison with type III collagen

The Journal of Pathology, 1990
AbstractThe distribution of type I collagen in normal and diseased renal tissues was studied using immunofluorescence and immunoelectron microscopy, and was compared with that of type III collagen. In normal human kidneys, a monoclonal antibody against type I or type III collagen reacted with the renal interstitium, but not with the intra‐glomerular ...
K, Yoshioka, M, Tohda, T, Takemura, N, Akano, K, Matsubara, A, Ooshima, S, Maki   +6 more
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Synthetic Collagen Heterotrimers: Structural Mimics of Wild-Type and Mutant Collagen Type I

Journal of the American Chemical Society, 2008
Collagen type I is an AAB heterotrimer assembled from two alpha1 chains and one alpha2 chain. Missense mutations in either of these chains that substitute a glycine residue in the ubiquitous X-Y-Gly repeat with a bulky amino acid leads to osteogenesis imperfecta (OI) of varying severity. These mutations have been studied in the past using collagen-like
Varun, Gauba, Jeffrey D, Hartgerink
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Binding of type-I collagen to Chlamydia trachomatis

Microbial Pathogenesis, 1994
Denatured type-I collagen was found to bind to Chlamydia trachomatis elementary bodies (EBs) in a time-dependent and specific manner. Specificity was tested by having a large excess of other proteins present in the binding mixture. Only denatured type-I collagen efficiently competed for binding.
G, Fröman, K, Amin, A, Yacoub, P A, Mårdh   +3 more
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