@article{83666,
  keywords = {Animals, Models, Molecular, Protein Conformation, Protein Structure, Tertiary, Humans, Rats, signal transduction, Binding Sites, Models, Biological, Dimerization, Macromolecular Substances, Protein Folding, Actins, Cytoskeleton, Fibronectins, Extracellular Matrix, Integrins, Cell Adhesion, CHO Cells, Cricetinae, Integrin alpha5beta1},
  author = {Yong Mao and Jean Schwarzbauer},
  title = {Fibronectin fibrillogenesis, a cell-mediated matrix assembly process.},
  abstract = {<p>The extracellular matrix provides a framework for cell adhesion, supports cell movement, and serves to compartmentalize tissues into functional units. Fibronectin is a core component of many extracellular matrices where it regulates a variety of cell activities through direct interactions with cell surface integrin receptors. Fibronectin is synthesized by many adherent cells which then assemble it into a fibrillar network. The assembly process is integrin-dependent and fibronectin-integrin interactions initiate a step-wise process involving conformational activation of fibronectin outside and organization of the actin cytoskeleton inside. During assembly, fibronectin undergoes conformational changes that expose fibronectin-binding sites and promote intermolecular interactions needed for fibril formation. In this review, the main steps of fibronectin assembly are described and recent studies on fibronectin conformational changes are discussed.</p>
},
  year = {2005},
  journal = {Matrix Biol},
  volume = {24},
  pages = {389-99},
  month = {09/2005},
  issn = {0945-053X},
  doi = {10.1016/j.matbio.2005.06.008},
  language = {eng},
}