fibrillogenesis


Also found in: Wikipedia.

fibrillogenesis

 [fi-bril″o-jen´ĕ-sis]
the formation and development of fibrils.

fi·bril·lo·gen·e·sis

(fī'bril-ō-jen'ĕ-sis),
The development of fine fibrils (as seen with the electron microscope) normally present in collagenous fibers of connective tissue.

fi·bril·lo·gen·e·sis

(fī'bril-ō-jen'ĕ-sis)
The development of fine fibrils (as seen with the electron microscope) normally present in collagenous fibers of connective tissue.
The development of fine fibrils (as seen with the electron microscope) normally present in collagenous fibers of connective tissue.

fibrillogenesis

the formation and development of fibrils.
References in periodicals archive ?
It is also known for influencing fibril formation for collagens type I and II, accelerating fibrillogenesis and binding to aggrecan, mediating the organization of cartilage matrix for its load bearing function.
Amyloid beta-protein fibrillogenesis Structure and biological activity of protofibrillar intermediates.
4c, d), suggesting that the fibrillogenesis process was taking place (see Discussion).
Teplow, "Structural and kinetic features of amyloid [beta]-protein fibrillogenesis," Amyloid, vol.
Following implantation, the RPC Pure-Collagen reacts with local tissue and fibrillogenesis is initiated to convert the collagen solution into a fiber matrix.
2007) COMP acts as a catalyst in collagen fibrillogenesis.
Small leucine-rich proteoglycans (SLRPs) are ECM proteoglycans required for collagen fibrillogenesis.
Results indicate cadmium binds to type I collagen with a higher affinity than calcium and alters collagen fibrillogenesis.
A network of thin collagen fibers oriented predominantly in the longitudinal direction with respect to the implant structures is detected in osteointegration zone osteoid, and large functionally active osteoblasts are localized secreting collagen and proteoglycans of bone matrix, as evidenced by pericellular fibrillogenesis near their surface (Figure 1, a) .
Owing to the interaction with type I and type II collagen fibrils and in vitro inhibition of fibrillogenesis, the encoded protein may play a role in the assembly of extracellular matrix.
8] Increased type V collagen production may affect normal collagen fibrillogenesis and alter the mechanical properties of the tissue, leading to improved endurance performance.
Fernandez-Velasco, "Thermodynamic and kinetic characterization of a germ line human A6 light-chain protein: the relation between unfolding and fibrillogenesis," Journal of Molecular Biology, vol.