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| {{Frankel}}
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| <startFeed/>
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| <center>
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| <div style="padding: 10px; width: 800px; border: 5px solid white;">
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| '''<font color=#000000 font size=8>ECM Proteins</font>'''
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| {| cellspacing="5px"
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| | width="30%" align="center" style="border: 2px solid #000033; background-color:#FFFFFF; padding:1em;" class="plainlinks"|
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| <div style="float:left;margin-left:0.3em;margin-right:0.7em">
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| '''<font color=#FFFFFF font size=8>HIV-gp160</font>'''
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| [[Image:FN.png|500px]]
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| </div>
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| | rowspan="2" width="70%" style="border: 2px solid #000033; background-color:#ffffff; padding:1em;" valign="top"|
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| [[Image:FNselec.png|300px]]
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| [[Image:FNseleczoom.png|300px]]
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| {|width="*"
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| {| style="width: 728px; text-align:center;font-size:12px;font-variant: small-caps;width: 18px; " align="center"
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| |}
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| <br />
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| <br />
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| |----
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| |}
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| |-
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| | style="border: 2px solid #000000; background-color:#FFFFFF; padding:1em;" valign="top"|
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| [[Image:FNint.png|500px]]
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| ----
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| '''<font color=#000000 font size=3> One of the major components of the extracellular matrix (ECM) is fibronectin, this dimeric glycoprotein is involved in numerous cell processes and has important functions in vertebrate development.
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| Fibronectin in the extracellular matrix interacts with the transmembrane integrins in a highly specific manner. The ECM ligand protein contains a tripeptide recognition site, Arg-Gly-Asp (RGD), responsible for the affinity of the cell surface receptors with its ligand.
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| Atomic force microscopy images can be appreciated, these illustrations depict how fibronectin molecules are almost exclusively absorbed on the DPPC domains. </font>'''
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