In parallel to our clinical investigation (Thies et al, 2002a), we compared two different methodological approaches for HPA binding analyses, demonstrating that in the animal model both methods are warranted.
ChIP-SEQ and cDNA microarray analyses demonstrated that many binding sites for C/EBPδ, and the closely related C/EBPβ, exist throughout the mouse genome and control the upregulation or downregulation of many adjacent genes.
Functional analyses demonstrated that the intragenic AP-1 binding sites are fully responsible for the PMA-dependent enhancer activity of fragment 5103.
During the last decade, molecular analyses demonstrated that alternative splicing determines the binding properties, intracellular localization, enzymatic activity, protein stability and post-translational modifications of a large number of proteins [9].
Recently, in vitro protein interaction analyses demonstrated that the DSN1-NSL1 diser is a crucial binding partner for HP1, Ndc80C and KNL1C.
ChIP analyses demonstrated that Bmi1-deficiency did not greatly affect the binding of Zfp277 to the Ink4a/Arf locus in early passage Bmi1−/− MEFs (Figure 6A).
Further analyses demonstrated that miR-10b is controlled by the Twist binding site in its promoter region, and that induction of miR-10b expression by hyaluronan/CD44-activated c-Src in breast cancer cells is Twist dependent.
Our ICAT proteomic analysis identified the Myb-binding protein p160 as a protein whose expression is induced upon iron chelation, and further analyses demonstrated that p160 is a ubiquitination substrate of VHL.
These analyses demonstrated that genes associated with Wnt signaling pathway components and interacting proteins are prominent in binding regions within 50 Kb of a TSS associated with expressed genes from ECC-Limb shared Twist1 binding peaks.
