The authors observed epigenetic modifications in a number of genes, with alterations observed in CpG methylation (PPARγ, PPARα and TGF-β 1), histone H3 acetylation (PPARγ and TGF-β 1) and other chromatin modifications (PPARγ).
In addition, the generality of the solid-phase synthetic methodology should facilitate the construction of other sulfopeptide and sulfoprotein libraries to interrogate the importance of Tyr sulfate modifications in a number of diverse systems, including chemokine-chemokine receptor interactions (e.g. CCR5/RANTES), decoy receptors, and complement proteins, in the future.
The wide range of simultaneous changes in O-GlcNAc modification in a number of proteins under different experimental conditions as previously observed by Wang et al [ 15] and in a recent report by Gu et al [ 16], could not be explained by changes in the expression and/or the activity of O-GlcNAc cycling enzymes.
The problem is especially demanding because of the almost symmetric structure of the tailcone, which in its initial configuration (prior to modification) results in a number of very weakly excited responses to certain excitations, so the corresponding terms in the full 6×6 receptance matrix are very difficult to obtain.
Our pathway ontology analysis revealed that the differentially expressed genes that were regulated by changes of H3K9Ac and/or H3K9Me2 modifications were involved in a number of cellular pathways.
Epigenomic features, such as DNA methylation and histone modifications, are involved in a number of key cellular processes ranging from the regulation of gene expression (Li and Reinberg 2011), to splicing (Shukla et al. 2011) and the repression of transposable elements (Miura et al. 2001).
During knowledge acquisition, given a case x that requires an NRDR knowledge base to be modified, the modification can occur in a number of places.
Protein glycosylation, as an important post-translational modification, is implicated in a number of ailments.
Although hydrophobic modifications can be designed in a number of ways, including point mutations of individual amino acids or acyl modification, end-tagging by hydrophobic oligoamino acid stretches constitutes an attractive alternative.
Recent research has shown that the diabetes environment fosters epigenetic modifications of a number of genes implicated in the pathogenesis of diabetic retinopathy, and enzymes responsible for bringing in the epigenetic changes are altered.
Although such hydrophobic modifications can be achieved in a number of ways, end-tagging by hydrophobic amino acid stretches is one of the easier ones since it requires no post-synthesis modification, since it allows the primary AMP sequence to be retained, as well as maximized interaction between the hydrophobic tag and the phospholipid membrane.
