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Chemical diversity was generated by in vitro chemoenzymatic and in vivo whole cell biocatalytic syntheses using either a B. bassiana mutant or an E. coli strain expressing the bbBeas gene [126].
We showed that LHP1 binding can be associated with a silent (i.e. in lif2 mutant) or an active (i.e. in WT) transcriptional status of FLC locus suggesting that LIF2 and most probably other components can modulate LHP1 activity.
Briefly 1×107 mouse MPCs expressing either EWS-FLI-1, EWS-FLI-1 R340N mutant or an empty pMSCV vector, were cross-linked with 1% folmaldehyde for 10 min. After addition of 0.125 M glycine and washing in cold PBS, cells were lysed and the chromatin fraction was sheared to roughly 700bp fragments by sonication.
Each allele, under the control of an arabinose-inducible araBAD promoter, was inserted in single copy into a neutral site of the chromosome of a lasR, rhlR mutant or an rpoS mutant, respectively.
RT-PCR and sequencing of the PCR fragments showed two introns in the tih gene; the first is spliced correctly in both the wild type and the fus mutant strain, whereas the second intron is either not spliced at all in the mutant, or an incorrect 5′ splice site is used leading to a shorter transcript.
Consistent with our hypothesis, prior phosphorylation of the WT complex by Akt reduced subsequent activation and Thr phosphorylation by LKB1, but this effect was completely abolished by either an S487A mutant or an AAA mutant, even though the latter was still phosphorylated on Ser by Akt.
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Remember all those sci-fi movies where the heroes were stuck in a terrible world where everybody but them was a mutant or a pod person or a hologram and their only hope was to reach a legendary and possibly mythical refuge?
In contrast, none of the human PP6Rs were capable of restoring normal eIF2α phosphorylation levels in either a quadruple sap mutant or a sap185 sap190 double mutant strain.
To investigate the virulence of the double mutant, SCID mice were injected intravenously with 105 CFU of either wild-type M. tuberculosis (strain H37Rv), a ΔsecA2 mutant, or a double mutant strain ΔsecA2ΔlysA.
Similarly, in several instances agonist-induced internalization of a given GPCR has been shown to promote internalization of either a disabled mutant or a different GPCR altogether [7], [8], [9], [10], [11].
In the current study, we found that PFO production by CPJV501 could be restored by coincubating CPJV501 with either a strain 13 pfoA-null mutant or a C. perfringens type C CN3685 pfoA-null mutant, both of which retain an intact agr locus (Fig. 6A and 6B).
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Justyna Jupowicz-Kozak
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