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Here we present several lines of evidence that accumulation of cytoplasmic PML also represents a mechanism of cellular resistance to viral infection, and what was formerly interpreted as the relocation of nuclear PML is at least partially indicative of a bona fide cytoplasmic PML isoform (or isoforms) that lack a nuclear localization sequence collectively called cPMLΔ5&6.
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EMT was characterized by significant downregulation of E-cadherin, relocation and nuclear accumulation of β-catenin as well as significant upregulation of ZEB1 and vimentin.
Together these results suggested that doxorubicin causes nuclear relocation of FOXO3a in the drug sensitive breast cancer cells, and confirmed our previous data that FOXO3a expression is predominantly nuclear in the resistant cells.
By inducing RNA-chromatin binding a number of RNA-dependent activities can be dissected: (i) The RNA-induced compaction or decondensation of chromatin, (ii) identification of RNA-interacting chromatin modifiers that set epigenetic signals such as posttranslational histone modifications, and (iii) nuclear relocation of a genomic locus targeted by the tethered RNA.
In contrast, mutation at Thr-469 did not impair NIK-mediated nuclear relocation of rpL10 or tolerance against geminivirus.
Furthermore, mutations at Thr-474 and Thr-469 residues antagonistically affected NIK-mediated nuclear relocation of the downstream effector rpL10.
The observations suggest that nuclear relocation of WOX1, JNK1 and transcription factors is a p53-independent event.
Both Toll and Imd pathways affect the production of AMPs through the nuclear relocation of dorsal, dif and relish, which can act as transcriptional regulators.
The nuclear relocation of FOXO3a(A3):ER in response to 4-OHT induction in the MDA-MB-231-FOXO3a MDA-MB-231-FOXO3a MDA-MB-231-FOXO3a MDA-MB-231-FOXO3aing of the estrogen receptor (ER) (Fig. 11A3.
Although T469A did not enhance translocation of rpL10 to the nucleus as would be expected from its increased in vitro substrate phosphorylation activity when compared with wild type NIK1, these results showed that mutation at Thr-469 did not impair NIK-mediated nuclear relocation of rpL10, confirming in vivo that the Thr-469 and Thr-474 phosphorylation sites play distinct roles in NIK activation.
We therefore tested whether silencing of NbNAG similarly induced nuclear relocation of bZIP28 from the ER membrane.
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