Distinct activation states of α5β1 integrin show differential binding to RGD and synergy domains of fibronectin
By Andrés J. García, J. Schwarzbauer, D. Boettiger. 2002
145 citations recorded by the source corpus.
Subfields: Cell Biology, Immunology and Allergy, Radiology, Nuclear Medicine and Imaging
View Paper: https://www.semanticscholar.org/paper/4fd1b7643983015d2a6e09564b58d41cd80d1692
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In Cell Biology
In Immunology and Allergy
Citations in the corpus
- Demonstration of catch bonds between an integrin and its ligand (2009, unknown): “In addition to the RGD-binding site at the A domain of the 1 subunit, the propeller of the 5 subunit may bind the synergy site at the FNIII9 domain to strengthen the FN–51 interaction (Garcia et al., 2002; Mould et al., 2003b; Friedland et al., 2009).”
- Adhesion signaling – crosstalk between integrins, Src and Rho (2009, background): “Instead, the particularly complex receptor-ligand interactions that are required for mechanocoupling through integrin α5β1 (Garcia et al., 2002), or the ability of integrin α5β1 to bind folded, ‘inactive’ fibronectin molecules promotes the turnover – and perhaps affects the clustering – of…”