Exact(3)
It could be suggested that both mutants do not effectively activate processes leading to recovery of energy from PHAs.
Interestingly, both mutants do not support autophagosome formation.
Whilst the Tdp1 H493R (SCand) and H263A mutants retain the ability to bind an AP site-containing DNA, both mutants do not reveal endonuclease activity, further suggesting the specificity of the AP cleavage activity.
Similar(57)
Interestingly, the expression of two genes (At1g75830, At4g29100), which had similar expression patterns in both mutants, did not change significantly in lif2 lif2.
However, both mutants did not accumulate viral DNA in newly emerged leaves of inoculated N. benthamiana and Arabidopsis, and the inoculated plants were asymptomatic.
Further in vitro invasion assay using BEAS-2B and NIH3T3 cells stably transfected with overexpression constructs for full length wild-type AQP5 (and5) and its two mutants, N185D which blocks membrane trafficking and S156A which blocks phosphorylation on Ser156, showed that AQP5 induced cell invasions while both mutants did not.
As the learning deficits of both mutants did not add up to a stronger impairment in double mutants, it is likely that both proteins converge, at least partially, into a common regulatory pathway.
Both mutants did not show the additional peaks of the UbretraCT conformation, but revealed a spectrum with 69 resonances (Thr9, Glu24 and Ala46 were exchange-broadened as compared to Ub) resembling the major conformation of phosphoUb (Supplementary Fig S12B).
While IR-B and IR-B fused to the super cyan fluorescent protein (SCFP) (IR-B-SCFP) could be activated after 10 min by recombinant human insulin (rhIns), both mutants did not show any activation signal.
Both bar allele mutants do not express Ubiad1 and are fully rescued by Ubiad1 mRNA expression.
Both CDK9 S175andnd CDK9 S175D mutants do not bind to Brd4 [30], suggesting that phosphorylation of Ser 175 might be important for the binding of CDK9/cyclin to to Brd4.
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