Sentence examples for substantial phosphorylation of from inspiring English sources

Substantial phosphorylation of mtPykA within a few minutes of reaction indicated that mtPykA was promptly phosphorylated by the kinase (Fig. 4B).

On the other hand, substantial phosphorylation of Chk1 at Ser-345 and Cdc25C at Ser-216 was observed in BxPC-3 cells treated with curcumin.

During the optimization of the fixed cell-based enzyme-linked immunosorbent assay for ERK activation, we established the optimal cell density for a 10 min EGF treatment, which is known to result in substantial phosphorylation of ERK1/2.

Consistent with this, there was substantial phosphorylation of Ser in a human α2β2γ1 complex, and slight phosphorylation of Ser in a human α1β2γ1 complex, when they were incubated with MgATP alone; these effects were completely abolished by D157A mutations that rendered the complexes inactive, although Ser could still be phosphorylated by Akt in the inactive complex.

Figure 3 shows, in addition to substantial decreased phosphorylation of Ser46, a target of TP53INP1/2, Ser15 and Ser392, targets of MDM2 and casein kinase II [13,33,53], which indicated an unstable and dysfunctional p53 response in contributing to B-SWCNT malignant phenotype and enhanced cancer signaling (Table 3, network 7).

At 200 nM, a concentration known to block the activity of ADAM17 (34), we observed a substantial decrease in phosphorylation of ERK1/2 (P < 0.05; Fig.  4C).

The expression of OTCΔ in COS-7 cells had a substantial effect on the phosphorylation of JNK1 and 2 (Fig 3A).

Incubation of cells for 30 min with ouabain caused substantial increases in the phosphorylation of fNKCC1 (4-fold) and fNKCC2A (2–3 fold), and a smaller increase in that of endogenous HEK-293 NKCC as detected by phospho-specific antibodies R5 and NKCC-P (Figure 2C, Table 1).

However, treatment with D1870 but not with BIX resulted in a substantial decrease in the phosphorylation of ERM proteins, the phosphorylation of ezrin and/or radixin being the most affected.

In addition to the impairment of insulin signaling, the brain/neuron-specific insulin-receptor KO mice exhibited a substantial increase in the phosphorylation of the microtubule-associated protein tau, a hallmark of neurodegenerative diseases [ 79].

In keeping with this concept, we found that transfection of STAT1C into EC1 and EC109 cells resulted in a substantial decrease in the phosphorylation of NF-κB p65, a marker of NF-κB activation [ 19].