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Finally, plasmodial histone deacetylase has been proposed as a promising target for anti-malarial therapy due to its key role in regulating gene transcription, and it has been shown that histone deacetylase inhibitors are potent inhibitors of the growth of P. falciparum [53].
Recently it has been shown that histone variant H2A.Z is preferentially incorporated into transcription factor binding sites [67].
Previously, it has been shown that histone H3K27 trimethylation can silence the expression of miR-22 independent of promoter methylation.
Through the use of computational measures, it has been shown that histone modifications are indeed predictive of gene expression levels.
On the role of epigenetic modifications in reprogramming, it has been shown that histone deacetylation impedes reprogramming and that inhibition of histone deacetylase enzymes can enhance iPSC generation [ 30, 92, 93].
It has been shown that histone acetylation influences chromatin structure and organization that play a role in protein DNA interactions and regulate expression of POLR3-transcribed genes (Lee et al., 1993; Boyd et al., 2000; Noma et al., 2006).
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It has been shown that histones are depleted from active promoters by transcription-coupled machinery [2] [5].
Although these model experiments conveniently used heparin, it has been shown that histones H1, H2A and H2B also have a high binding affinity for heparan sulphate[14], [15], [16].
Notably, several decades earlier, it had already been shown that histones, in particular H3 and H4, possess bactericidal activity, thereby providing at least a partial explanation for the release of histones during NETosis.
Several decades ago, it was shown that histone proteins can be ADP-ribosylated.
Moreover, in some specific case it was shown that histone methylation is extremely stable: for instance, on nuclear somatic transfer into oocytes, H3K9me3 in the donor nucleus is not erased over several days (Santos et al, 2003).
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