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This result suggests that DNA damage-induced posttranslational modifications might regulate the interaction of Che-1 with p53.
Alternatively, both post-translational modifications might regulate distinct set of NF-κB-dependent genes and thus not influence each other.
To assess whether these modifications might regulate Che-1 dissociation from p53, we performed co-immunoprecipitation assays using p53-null EJ cells overexpressing p53 WT or a p53 mutant lacking only serine 46 (S46a), a phosphorylation target involved in apoptosis induction.
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This study also suggests that palmitoylation modifies proteins downstream of BMPR and upstream of p38 MAPK and this modification might regulate other cellular events that involve this pathway.
Since S-nitrosation has been reported to facilitate protein-protein interactions [9], we speculated that NO-mediated specific molecular modification of Pias3 (or Trim32) might regulate its interaction with Trim32 (or Pias3).
Post-translational modifications as phosphorylation and mono-ubiquitination might regulate Eps15 functioning, but molecular details of these processes are still unknown.
We thus have to assume that certain posttranslational modifications or interactions with some auxiliary/associated proteins might regulate the function of these ion channels in a dramatic manner.
Besides, according to the subcellular localization of Linc00974, we suspected that Linc00974 might regulate KRT19 through posttranscriptional modification.
Presence in multiple copies, functional crosstalk, differential binding affinity, and posttranslational modifications are some of the key factors that might regulate the biological functions of Alba family proteins.
These data suggested that Mageb3 might regulate the recruitment of the Polycomb complex onto Xi and subsequent H3K27me3 modification through Pcgf3.
Moreover, atypical antipsychotics might regulate the transcription and function of genes that are related to histone post-transcriptional modifications [ 62].
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