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TIMPs bind to active matrix metalloproteinases and, amongst other effects, inhibit their proteolytic activity of the extracellular matrix.
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The β- and γ- subunits bind to active Arf1-GTP, γCOP also binds to p23.
Secreted Maspin could bind to extracellular matrix components.
As a non-structural component of extracellular matrices, SPARC can bind to extracellular matrix components such as collagens, laminin, fibronectin, and vitronectin [1] and mediate cell-matrix interactions.
These integrins can also bind to extracellular matrix components such as serum, fibrinogen and fibronectin.
These probes bind to the active form of a protease and become permanently bound to the active site nucleophile.
When a cell moves, cell-matrix receptors, such as integrins, become engaged and bind to the extracellular matrix.
This occurs when an inhibitor does not bind to the active site but does bind to a different part of the enzyme and changes the active site shape.
Suicide substrates act as modified substrates for the target enzymes and bind to the active site.
Oto expressed alone does not bind to the HA matrix (Fig. 5a).
LARGE-dependent modification enables α-dystroglycan (α-DG) to bind to its extracellular matrix ligands.
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