Frankel:ECM Proteins: Difference between revisions
No edit summary |
No edit summary |
||
| (11 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
{{Frankel}} | {{Frankel}} | ||
<br> | |||
<br> | |||
< | ''<font align="center" font color=#ffffff font size=8>_________ </font>'''''<font color=#000000 font size=8>ECM Proteins</font>''' | ||
< | <br> | ||
{| cellspacing="3px" | |||
<div> | |||
| align="justify" width=400px style="border: 2px solid #000033; background-color:#ffffff; padding:1em;" class="plainlinks" valign="top"| | |||
''<font align="center" font color=#ffffff font size=8>_______ </font>'''''<font color=#000000 font size=3>Fibronectin</font>''' | |||
<br> | |||
< | |||
[[Image:FN.png|500px]] | [[Image:FN.png|500px]] | ||
</div> | </div> | ||
| rowspan="2" width= | | align="center" rowspan="2" width=30px style="border: 2px solid #000033; background-color:#ffffff; padding:1em;" valign="top"| | ||
<br> | |||
[[Image:FNselec.png| | <br> | ||
[[Image:FNselec.png|235px]] | |||
<br> | |||
<br> | |||
[[Image:FNseleczoom.png|235px]] | |||
<br> | |||
<br> | |||
[[Image:FN_complexes.jpg|235px]] | |||
<br> | |||
<br> | |||
[[Image:FN_adsorbed.jpg|235px]] | |||
{|width="*" | {|width="*" | ||
| | | | ||
{| style="width: 728px; text-align:center;font-size:12px;font-variant: small-caps;width: 18px; " align=" | {| style="width: 728px; text-align:center;font-size:12px;font-variant: small-caps;width: 18px; " align="justify" | ||
|- | |- | ||
| Line 39: | Line 47: | ||
|} | |} | ||
|- | |- | ||
| style="border: 2px solid #000000; background-color:#FFFFFF; padding:1em;" valign="top"| | | align="justify" width=21px style="border: 2px solid #000000; background-color:#FFFFFF; padding:1em;" valign="top"| | ||
[[Image:FNint.png|500px]] | [[Image:FNint.png|500px]] | ||
| Line 51: | Line 58: | ||
'''<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. | '''<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. | ||
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. | 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. | ||
Atomic force microscopy images can be appreciated, these illustrations depict how fibronectin molecules are almost exclusively absorbed on the DPPC domains. | |||
Latest revision as of 18:14, 9 January 2013
<owwmenu align="center" font="helvetica" bold="1" color="white" bgcolor="black" hovercolor="black" bghovercolor="orange" topfontsize="10" fontSize="10" image="Danbanner-bio-machines.jpg" >
Home=Frankel
Members=#,Principal Investigator=Frankel:Lab_Members, PhD students=Frankel:Lab_Members, Alumni=Frankel:Lab_Members
Contact=Frankel:Contact
Collaborators=Frankel:Collaborators
Publications=Frankel:Publications
Lab=Frankel:Research
Research=#,Force Spectroscopy=Frankel:Force Spectroscopy,HIV/Virus=Frankel:HIV/Virus,ECM Proteins=Frankel:ECM Proteins,Cyberplasm=Frankel:Cyberplasm,Cancer=Frankel:Cancer
_________ ECM Proteins
|
_______ Fibronectin
|
| |
|
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. 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. Atomic force microscopy images can be appreciated, these illustrations depict how fibronectin molecules are almost exclusively absorbed on the DPPC domains. |
