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Mechanic, G.L., Katz, E.P., Henmi, M., Noyes, C. and Yamauchi, M. (1987) Locus of a histidine-based, stable trifunctional, helix to helix collagen cross-link: stereospecific structure of type I skin fibrils. Biochemistry, 26, 3500-3509.

has been cited by the following article:

• TITLE: Different architectures of collagen fibrils enforce different fibrillogenesis mechanisms

  AUTHORS: Mario Raspanti

  KEYWORDS: Fibrillogenesis; Microfibrils; Collagen Fibril Substructure

  JOURNAL NAME: Journal of Biomedical Science and Engineering, Vol.3 No.12, December 30, 2010

  ABSTRACT: According to current knowledge on collagen fibril-logenesis, collagen fibrils are formed by a cooperative process involving lateral fusion of small protofibrils. Almost all the experimental research, however, was carried out on tendon collagen, whose fibrils are characterized by approximately straight subfibrils. By contrast, in most tissues the collagen fibril sub-units follow a helical course in which geometrical constraints prevent lateral fusions, thereby implying a different mechanism where collagen fibrils grow by addition of individual microfibrils rather than by lateral fusion of pre-assembled subfibrils. The proc-ess at the origin of these fibrils may provide a simple, automatic explanation for the remarkable uniformity in fibrils size observed in most tissues without re-quiring the intervention of unknown mechanisms of diameter control. Other mechanisms of growth con-trol remain indispensable to terminate the fibril-logenesis process in tendons and ligaments.