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One of the variants induced a frame-shift mutation that could lead to nonsense-mediated mRNA decay, a ubiquitous cellular mechanism that eliminates mRNA containing a premature termination codon.
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The observation that these variants induce a similar effect to chloranil and that chloranil acts via the production of ROS suggest strongly that chloranil variants increase ROS production as well leading to the activation of metalloproteinases.
Each protein variant is composed of one or more exons, each of which corresponds to a contiguous stretch of nucleotides within U. Therefore each protein variant i∈{1,…, n}, where n is the total number of variants, induces a subset S i of U, and the union of all S i ∈{1,…, n }= U. Our goal was to find the minimum number of sets within { S1,…, S n } that maximally cover U.
Hence, the MICA-129Met variant induced a stronger down-regulation of NKG2D than the MICA-129Val variant.
Importantly, the MICA-129Met variant induced a stronger down-regulation of NKG2D on NK cells and even more on CD8+ T cells than the MICA-129Val isoform.
On the other site, the MICA-129Met variant induced a faster and stronger down-regulation of NKG2D on NK and cytotoxic T cells than the MICA-129Val isoform.
Investigation of the structural consequences for the aortic wall of an heterozygous in-frame deletion in the C-terminal region of MYH11 suggested that this variant induced a conformation change consistent with previously described heterozygous variants in the coiled-coil domain of other myosin-II heavy chains.
We find that the more fusogenic variants induce an unaligned lipid phase component and a large degree of phase separation as observed in 31P 2D spectra.
Our mini-gene splicing assay results revealed that the variant induced an in-frame inclusion of 87 bp of intron 20, which also is in agreement with the sequence reported in the original publication.
Taken together, these results suggest that A30P and E46K, as opposed to either Wt α-Syn or the A53T variant, induce a pro-inflammatory response in glia.
The Pro143Ala variant induces a transformation of the shape of helix α1 compared to HTRA2 (1LCY) (Fig. 3a, red circle indicates the helix α1).
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