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Abnormal collagen fibril structure in the gravis form (type I) of Ehlers-Danlos syndrome.

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TLDR
Altered abnormalities of fibrillogenesis are heterogeneous in origin; some might be due to primary defects in collagen whereas others may result from alterations of noncollagenous extracellular matrix components that influence collagen fibril formation.
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This article is published in Laboratory Investigation.The article was published on 1979-02-01 and is currently open access. It has received 150 citations till now. The article focuses on the topics: Fibrillogenesis & Ehlers–Danlos syndrome.

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Journal ArticleDOI

Ehlers‐Danlos syndromes: Revised nosology, Villefranche, 1997

TL;DR: This work proposes a revision of the classification of the Ehlers-Danlos syndromes based primarily on the cause of each type based on major and minor diagnostic criteria defined for each type and complemented whenever possible with laboratory findings.
Journal ArticleDOI

Mice that lack thrombospondin 2 display connective tissue abnormalities that are associated with disordered collagen fibrillogenesis, an increased vascular density, and a bleeding diathesis.

TL;DR: It seems likely that some of the diverse manifestations of this genetic disorder result from the ability of TSP2 to modulate the cell surface properties of mesenchymal cells, and thus, to affect cell functions such as adhesion and migration.
Journal ArticleDOI

A recessive form of the Ehlers-Danlos syndrome caused by tenascin-X deficiency.

TL;DR: This finding indicates that factors other than the collagens or collagen-processing enzymes can cause the Ehlers-Danlos syndrome and suggests a central role for tenascin-X in maintaining the integrity of collagenous matrix.
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Tenascin-X deficiency mimics Ehlers-Danlos syndrome in mice through alteration of collagen deposition.

TL;DR: A causative role for TNXB is confirmed in human Ehlers–Danlos syndrome and it is suggested that tenascin-X is an essential regulator of collagen deposition by dermal fibroblasts.
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