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A mechanism by which Akt might regulate activation of SREBPs has been suggested by the recent work of Sundqvist and colleagues [ 101], who demonstrated that degradation of SREBP is regulated by phosphorylation of Thr426 and Ser430.
The C2 and C1 domains of ForA and ForE, respectively, might regulate activation or targeting of the molecule through interaction with specific lipids [ 29, 30], while the FHA domain of ForJ might be involved in interactions with components of the cell nucleus [ 31].
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Further, the MECP2 and LEDGF/P75 complex might also regulate activation of other stress survival genes like those of chaperones.
We have previously demonstrated that perturbation of the AIE (autoinhibitory element) in the FMN-binding subdomain can also lead to eNOS activation with a basal level of calcium, implying that the AIE might regulate eNOS activation through modulating phosphorylation at Thr and Ser.
A C-terminal fragment of BRCA1, which is fused to the GAL4 DNA-binding domain, activates transcription of reporter genes, suggesting that BRCA1 might regulate transcriptional activation [ 11*, 12*, 13*].
We applied smRNA-seq analyses to endothelial lineage cells for identifying miRNAs that might regulate the activation of the angiogenesis-related phenotypes of EPCs.
Although the role of CD36 receptor in mediating oxLDL uptake and PPARγ activation in macrophages is recognized, the cellular events by which GHS-R1a activation might regulate PPARγ activity and downstream gene expression remain unknown.
We hypothesized that PLCγ2 might regulate T cell activation by affecting DC maturation or function.
It was speculated that HS1 might regulate the differential activation of distal versus proximal VH families [9]; therefore, we analyzed the rearrangement efficiencies of the proximal VH7183 family (Fig. 3C), the distal VHJ558 familiy (Fig. 3D), and the distal most VH segment VHJ558.55 (Fig. 3E).
Since the coding region contains the trypsin-like serine protease domain required for the function of granzyme B in cell killing, the alternative splicing demonstrated here might regulate the structure and activation capacity of the molecule as a function of T cell activation.
We have previously found that deletions from the AIE (Δ594 604, Δ605 612 and Δ626 634) can also lead to eNOS activation at the lower level of calcium [ 19], implicating that the AIE might regulate Ca2+/CaM-dependent eNOS activation through modulating phosphorylation at Thr and Ser.
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