fibronectin

Further along the ribbon are three regions known as fibronectin domains.

Similar findings have also been described for fibronectin (Ginsberg et al, 1979).

Short fibronectin fibrils then begin to form between adjacent cells.

In addition, this protein binds with high affinity to fibronectin.

Fibronectin maps here also a polarized network together with other molecules.

There were no significant changes in fibronectin binding among any of the variants tested (see Table 2).

They are attracted to the site by fibronectin, growth factors, and substances such as kinins.

Fibronectin domains are found in a wide variety of extracellular proteins.

Silicone sheeting was associated with changing growth factor levels of only fibronectin.

Fibronectin is important for guiding cell attachment and migration during embryonic development.

Fibronectin is very abundant in the Reinke's space of newborn and infant.

Fibronectin also acts as a skeleton for the elastic tissue formation.

The molecule fibronectin has been found to play a role in radial intercalation.

Tenascin C has been shown to interact with fibronectin.

These variants are found in a subset of cellular fibronectin subunits.

A negative fetal fibronectin test gives a more than 95% likelihood of remaining undelivered for the next 2 weeks.

Fibronectin plays a crucial role in wound healing.

Fibronectin 1 acts as a potential biomarker for radioresistance.

Fibronectin and N-cadherin are key to epithelialization in the developing embryo.

The tenascins have anti-adhesive effects, as opposed to fibronectin which is adhesive.

In addition, it also regulates the splicing of fibronectin and CD45 genes.

Fibronectin has numerous functions that ensure the normal functioning of vertebrate organisms.

They are also known to interact with laminin, fibronectin, tenascin, and collagen.

Examples of these molecules include laminin, fibronectin, tenascin, and perlecan.