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Journal ArticleDOI

Collagen fibril assembly by corneal fibroblasts in three-dimensional collagen gel cultures: small-diameter heterotypic fibrils are deposited in the absence of keratan sulfate proteoglycan.

TLDR
The assembly and deposition of small-diameter fibrils with a collagen composition and structure identical to that seen in the corneal stroma in the absence of proteoglycans typical of the secondary cornean stroma imply that although proteoglycan-collagen interactions may function in the establishment of interfibrillar spacing and lamellar organization, collagen-Collagen interactions are the major parameter in the regulation of fibril diameter.
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This article is published in Experimental Cell Research.The article was published on 1992-09-01. It has received 47 citations till now. The article focuses on the topics: Lumican & Collagen, type I, alpha 1.

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Citations
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Journal ArticleDOI

Type V collagen: molecular structure and fibrillar organization of the chicken alpha 1(V) NH2-terminal domain, a putative regulator of corneal fibrillogenesis.

TL;DR: In this paper, the NH2-terminal domain of the alpha 1(V) protein was used to identify potential propeptidase cleavage sites in the corneal stroma.
Journal ArticleDOI

Collagen fibrillogenesis in situ: Fibril segments undergo post‐depositional modifications resulting in linear and lateral growth during matrix development

TL;DR: The hypothesis that a decrease in fibril‐associated decorin is necessary for fibrils growth associated with tissue maturation is supported by the morphological data.
Journal ArticleDOI

Keratocan-deficient Mice Display Alterations in Corneal Structure

TL;DR: Ablation of the Kera gene resulted in subtle structural alterations of collagenous matrix and did not perturb the expression of other SLRPs in cornea, showing that keratocan plays a unique role in maintaining the appropriate corneal shape to ensure normal vision.
Journal ArticleDOI

Prelude to corneal tissue engineering – Gaining control of collagen organization

TL;DR: Tissue engineering efforts, which have been focused on producing the fundamental functional component of a cornea (organized alternating arrays of collagen or "lamellae"), may have already provided valuable new insights and tools relevant to development, growth, remodeling and pathologies associated with connective tissue in general.
Journal ArticleDOI

Morphologic characterization of organized extracellular matrix deposition by ascorbic acid-stimulated human corneal fibroblasts.

TL;DR: Human keratocytes, cultured in a stable vitamin C derivative, are capable of assembling extracellular matrix, which comprises parallel arrays of ECM fibrils, which are morphologically similar to the developing mammalian stroma.
References
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Journal ArticleDOI

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article

Cleavage of structural proteins during the assemble of the head of bacterio-phage T4

U. K. Laemmli
- 01 Jan 1970 - 
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
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Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon.

TL;DR: The small dermatan sulphate proteoglycan of bovine tendon demonstrated a unique ability to inhibit fibrillogenesis of both type I and type II collagen from bovines tendon and cartilage respectively in an assay performed in vitro, suggesting that interactions between collagen and proteoglycans may be quite specific both for the type of proteogly can and its tissue of origin.
Journal ArticleDOI

Collagen fibrillogenesis in vitro: interaction of types I and V collagen regulates fibril diameter.

TL;DR: Electron microscopy using collagen type-specific monoclonal antibodies demonstrated that the fibrils formed were heterotypic, containing both collagen types I and V, indicating that the interaction of type V with type I collagen is at least partially responsible for the regulation of collagen fibril formation.
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