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Histone deacetylase-1 is known to interact with ATM and this interaction is enhanced by ionising radiation and inhibited by HDAC inhibition (Kim et al, 1999).
Together, these data demonstrate that CD98 interacts with Jurkat cells and this interaction is enhanced by the phosphorylation of CD98.
The results indicated that Stat6 interacts physically with PR and that this interaction is enhanced in a dose-dependent manner by progesterone.
HDAC3 is known to interact with TR2 (Franco et al. 2001) and this interaction is enhanced by the atRA-stimulated phosphorylation of TR2 at Thr-210 (Gupta et al. 2008).
Sirt1 interacts with WRN both in vitro and in vivo; this interaction is enhanced after DNA damage.
This interaction is enhanced by CKII-mediated phosphorylation of L1ICD.
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We found that, following PMA treatment of Dami cells, CIB1 protein expression increases, that CIB1 and Plk3 interact, and that this interaction was enhanced with prolonged PMA treatment, even though Plk3 protein expression decreased.
Mass spectrometry, immunoprecipitation and immunocytochemistry identified ubiquilin-2 as an interacting partner of C9ORF72, and this interaction was enhanced by proteasome inhibition, thus providing further evidence that the function of C9ORF72 is linked to protein degradation.
A biotin-labeled synthetic MMP1 promoter probe containing the putative NF-κB-binding sequence was able to interact with the nuclear lysate and this interaction was enhanced when cells were pretreated with TNF-α, which induced nuclear translocation of p65.
This interaction was enhanced significantly in the phosphomimetic mutant TR2 (210CP; Thr→Glu [38], [39]), but was abolished in the phosphorylation-negative mutant TR2 (210CN; Thr→Ala).
This interaction was enhanced by FGF-2 stimulation and repressed by U0126 (Supplementary Figure S3B).
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