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Sp1 is a widely studied transcription factor that can bind to and act through the GC boxes.
A high-efficacy medicine is defined as a compound that can bind to and act on receptors at low concentrations.
These soluble receptors are free-floating in the serum and can bind to and act as natural TNF- α antagonists.
Exogenous Gremlin may bind to and act directly on endothelial cells to modulate angiogenesis including endothelial cell migration [ 45, 46].
Moreover, while the mutant forms of Rab1 and Rab35 were poor substrates for certain GAP proteins, a GAP protein called RUTBC3 could bind to and act upon mutant Rab5 protein, similar to previous reports from other groups (see, e.g., Pan et al., 2006).
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In this case, when the level of K is increased, initially it binds to P and forms KP that acts as a phosphatase and R remains close to zero.
Sp1 is the prototype of a family of zinc finger (Cys2/Hys2) DNA binding transcription factors that binds to and acts through G-rich elements such as GC-box.
NPC1 and NPC2 each bind to cholesterol and act in tandem in late endosomes and/or lysosomes to mediate the egress of unesterified cholesterol derived from endocytosed lipoproteins (Fig. 3) (Vance, 2010; Wang et al., 2010).
There are also AA proteins that assist in cellulose breakdown through direct or indirect enzyme activity [ 21], and CBMs that bind to cellulose and act to concentrate enzyme activities.
HDAC family members bind to Runx2 and act as transcription co-repressors in skeletal development [6], [32], [33].
The p27 could also bind to CDKs and act as CDKI as p21.
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