Results 261 to 270 of about 646,289 (312)

Glycosylation of Type I Collagen

2019
Fibrillar type I collagen is the most abundant structural protein in most tissues and organs. One of the unique and functionally important characteristics of collagen is sequential posttranslational modifications of lysine (Lys) residues. In the endoplasmic reticulum, hydroxylation of specific Lys occurs producing 5-hydroxylysine (Hyl).
Mitsuo, Yamauchi, Marnisa, Sricholpech, Masahiko, Terajima, Kenneth B, Tomer, Irina, Perdivara   +4 more
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Hydroperoxide formation in model collagens and collagen type I

International Journal of Cosmetic Science, 2002
SynopsisProtein hydroperoxides represent a relatively new concept in understanding biological oxidation chemistry. Here, we show with post‐column‐chemiluminescence that this sometimes remarkably stable and yet reactive species can be formed in collagen models and collagen type I when submitted to oxidative stress as exemplified by the Fenton reaction ...
S A, Madison, J E B, McCallum, R U, Rojas Wahl   +2 more
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In vitro Formation of Hybrid Fibrils of Type v Collagen and Type I Collagen Limited Growth of Type I Collagen Into Thick Fibrils by Type V Collagen

Connective Tissue Research, 1986
Type V collagen and type I collagen were obtained from human placentas by pepsin treatment, followed by salt fractionation. The precipitates formed at 37 degrees C from a mixed solution of type V collagen and type I collagen, reacted with antibodies to either type V collagen or type I collagen.
E, Adachi, T, Hayashi
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Improvement of the Material Property of Shark Type I Collagen by Composing with Pig Type I Collagen

Journal of Agricultural and Food Chemistry, 2000
Fibril reconstruction process, that is, the nucleation and growth of mixed type I collagen fibril of shark and pig, progressed faster than that of the individual collagen species of shark or pig. The reconstructed mixed collagen fibril had a greater resistance to return to the solution or to melt into gelatin in comparison with the counterpart ...
Y, Nomura, S, Toki, Y, Ishii, K, Shirai
openaire   +2 more sources

Characteristics of cellular immune responses to collagen type I or collagen type II

Cellular Immunology, 1986
We have examined the murine cell-mediated immune (CMI) response to collagens type I (CI) and type II (CII) as measured by in vivo delayed-type hypersensitivity responses. We have verified the histopathology and kinetics of the cell-mediated immune responses. Predominant cell-mediated responses were obtained 7, 10, or 14 days following immunization.
L, Butler, B, Simmons, J, Zimmermann, P, DeRiso, K, Phadke   +4 more
openaire   +2 more sources

Dermal collagen fibrils are hybrids of type I and type III collagen molecules

Journal of Structural Biology, 1990
It has been suggested that dermal collagen fibrils with 67-nm periodicity consist of hybrids of type I and type III collagens. This is based on the assumption that all these banded fibrils are coated with type III collagen regardless of their diameter. However, conclusive evidence for this form of hybridization is lacking.
R, Fleischmajer, E D, MacDonald, J S, Perlish, R E, Burgeson, L W, Fisher   +4 more
openaire   +2 more sources

Type I Collagen and Collagen Mimetics as Angiogenesis Promoting Superpolymers

Current Pharmaceutical Design, 2007
Angiogenesis, the development of blood vessels from the pre-existing vasculature, is a key component of embryogenesis and tissue regeneration. Angiogenesis also drives pathologies such as tumor growth and metastasis, and hemangioma development in newborns.
T, Twardowski, A, Fertala, J P R O, Orgel, J D, San Antonio   +3 more
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Type I and Type III Collagens in Cutaneous Mucinosis

The American Journal of Dermatopathology, 1998
Cutaneous mucinoses are a heterogeneous group of diseases characterized by the focal or diffuse dermal deposition of glycosaminoglycans. The histopathologic examination of many cutaneous mucinoses reveals that the collagen fibers are fragmented. We wanted to characterize the type I (COL1) and type III (COL3) collagen distribution in skin biopsy ...
M F, Alves, A L, Filgueira, D E, Lorena, L C, Porto   +3 more
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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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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
openaire   +2 more sources