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The most widely studied epigenetic modification in humans is cytosine methylation at CpG dinucleotides.
DNA methylation, an important type of epigenetic modification in humans, participates in crucial cellular processes, such as embryonic development, X-inactivation, genomic imprinting and chromosome stability.
While protein phosphorylation constitutes the most abundant modification in eukaryotes, the ∼500 kinases that establish this modification in humans display moderate substrate site specificities, typically governed by ∼9 residues flanking the phosphorylatable amino acid.
Currently, the most widely studied epigenetic modification in humans is DNA methylation, which occurs almost exclusively in the context of CpG dinucleotides that control the transcriptional activity of genes [ 21].
The mechanism of action and the regulation of the ASPP family members in tumour cells is summarised in Figure 2. DNA methylation is the main epigenetic modification in humans, and changes in the methylation status of genes play an important role in tumorigenesis.
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As well, the differentiation capacity of the progenitor cells treated with nanoparticles did not change relative to untreated progenitor cells, indicating that nanoparticles are safe and minimally disruptive delivery vectors for PNAs and DNAs to mediate gene modification in human primary cells.
Phosphorylation of T676 in Mps1 provides the first specific post-translational modification in human cells as a cause for this.
To our knowledge, phosphorylation of T676 on Mps1 is the first post-translational modification in human cells of which the absence causes checkpoint weakening and CIN without affecting cell viability.
Interestingly, Zhong et al [37] recently used expression profiling to analyze novel targets for epigenetic modification in human lung cancer and revealed that silencing by histone deacetylation was nearly as common as silencing by DNA methylation in a panel of nine genes.
B[a]P is known to induce histone modification in human cancer cells [ 20, 21].
The most reactive sites for modification in human albumin are K190 and K351.
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