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Comment
. 2000 Jun;105(11):1507-9.
doi: 10.1172/JCI10119.

Fibronectin peptides in cell migration and wound repair

Affiliations
Comment

Fibronectin peptides in cell migration and wound repair

K M Yamada. J Clin Invest. 2000 Jun.
No abstract available

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Figures

Figure 1
Figure 1
The fibronectin molecule consists of repeating globular domains with specific cell-binding sites for interactions with integrins. Four of the fibronectin peptide sites (abbreviated using the single-letter code for amino acids) that can interact with specific integrins are shown extending down toward the integrins. Integrins contain one α and one β subunit, which span the plasma membrane and terminate in short cytoplasmic domains that are thought to mediate intracellular signaling.
Figure 2
Figure 2
Synthetic fibronectin peptides such as PHSRN could function in at least three different ways: (a) by providing binding sites for specific integrins, e.g., using peptides covalently attached to a synthetic matrix; (b) by competing for the binding of native fibronectin by integrins; or (c) by directly activating an integrin.

Comment on

References

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