In addition to binding PIP2, we show that NaD1 is also able to bind to a number of other phospholipids.
Members of the IRF family of transcription factors are known to bind to a number of consensus sites, as shown for the DNA-binding domain of IRF1 (Fig. 1B).
To understand how omega-3s curb inflammation, Jerrold Olefsky, an endocrinologist at the University of California, San Diego, and his colleagues trawled through the data on a family of proteins called G protein-coupled receptors, which can bind to a number of different fatty acids.
In mammals, ROR2 has been shown to bind to a number of canonical and non-canonical Wnts and mediate non-canonical Wnt signalling in cultured cells [10] [13].
GIT1 and 2 bind to a number of molecules, through which they affect actin remodeling, cell spreading, focal adhesion turnover [34], [35], [36], [37].
Additionally, EBNA3C has been reported to bind to a number of cell-cycle regulators, including cyclin A, SCFSKP2, pRb, Myc, p53 and MDM2 [33], [34], [35], [36], [37], [38], [38].
ChIP-qPCR analysis showed that RUNX1 was indeed bound to a number of tested p63 binding sites with the RUNX motif (Fig 4B; Supplementary Table S8B), indicating that RUNX1 can cooperate with p63 in epidermal cells.
We have discovered that microcystin binds to a number of these proteins in vivo and that the binding is strongly enhanced under high light and oxidative stress conditions.
p21 binds to a number of cyclin and Cdk complexes and inhibits the Cdk kinase activity, and hence cell progression is blocked.
Structures are available for NC bound to a number of different segments of the 5′ UTR, although it is not clear which of these is most biologically relevant for packaging.
IR-phosphorylated IRS5 binds to a number of SH2 domain-containing proteins, that are distinct from those associated with IRS1.
