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This broad specificity against distinct branching modifications represents a great advantage for biotechnological processing of complex and branched polysaccharides [ 26].
Identification of specific binding proteins for all of these novel modifications represents a future research direction that is required to reveal their biological functions.
Although it may be coincidental, acetylation has recently been identified as a mechanism regulating tau turnover (32), implying that complex interplay between different post-translational modifications represents a common mechanism neurons uses to fine-tune major classes of molecular processes.
Given the identification of mutations in genes encoding proteins involved in mt-tRNA modification as a cause of mitochondrial disease (e.g., PUS1 [Bykhovskaya et al., 2004], TRMU [Zeharia et al., 2009], MTO1 [Ghezzi et al., 2012], MTFMT [Tucker et al., 2011], the disruption of these post-transcriptional modifications represents a major consideration for potential disease mechanisms.
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Each additional modification and each new combination of modifications represents an additional protein species of that single protein.
The ability to create fully reversible genetic modifications represents an important step toward clinical applications of hESCs.
The correlation between the physico-chemical properties and chemical modifications represents an essential step toward the de novo design of quadruplex forming oligonucleotides for biomedical applications.
Therefore, the identification and characterization of genes that are translationally affected by these modifications represents an interesting future research direction to explore.
In addition, numerous epigenetic modifications represent a potential goal of novel therapeutic strategies and treatment design.
Thus, balanced and proportionate modifications represent a win-win situation for everyone.
These experiments prompt questions concerning the extent to which histone modifications represent a cause or a consequence of pluripotency.
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