Little, William C <br/><br/>
Assay to mechanically tune and optically probe fibrillar fibronectin conformations from fully relaxed to breakage.  [electronic resource] 

 -  Matrix biology : journal of the International Society for Matrix Biology  Jun 2008 
 - 451-61 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0945-053X 
<br/><br/><label>Standard No.: </label>10.1016/j.matbio.2008.02.003  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Animals<br/>Elasticity<br/>Endothelial Cells--cytology<br/>Extracellular Matrix--chemistry<br/>Fibroblasts--cytology<br/>Fibronectins--chemistry<br/>Fluorescence Resonance Energy Transfer--methods<br/>Fluorescent Dyes--chemistry<br/>Humans<br/>Mechanotransduction, Cellular--physiology<br/>Mice<br/>Microscopy, Atomic Force<br/>Microscopy, Fluorescence<br/>NIH 3T3 Cells<br/>Peptide Fragments--chemistry<br/>Protein Conformation<br/>Protein Denaturation<br/>Protein Folding<br/>Protein Structure, Quaternary<br/>Protein Structure, Secondary<br/>Silicones--chemistry<br/>Stress, Mechanical<br/>Tensile Strength