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But these experiments don't definitively prove that NS1 is the culprit, the human and pig immune systems might react differently to it.
We see what happens but these experiments do not probe how it happens.
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These materials include the bulk of the solid cellular material, the intracellular water and water-soluble cellular components, but, importantly for these experiments, do not include the starch-rich statoliths within the cells.
But there is a good reason why these experiments do not work.
Some labs have reported that at least one of the RS domains of SF2/ASF and U1-70K is required for interactions between these two proteins [13], [67], but these experiments did not demonstrate that the RS domains of both proteins were required for their interaction.
Previously, we found that RSSs are preferentially protected by a nucleosome (Baumann et al, 2003) but these experiments did not distinguish where the RSS lies with respect to the histone octamer.
Multi-site phosphorylation has been elegantly studied in the TGFβ signaling axis using protein semisynthesis previously (Huse et al., 2001; Wu et al., 2001), but these experiments did not require insect cell expression of an intein-fusion protein.
These experiments do not deserve taxpayers' money or statutory licences.
These experiments did not always work.
These experiments did not result in SiC or equilibrium assemblages.
These experiments did not, however, indicate which BMPs are involved.
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