linkedin post 2017-08-17 04:57:13

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HIDDEN SUB-CODE. "Transcription Factors which can modulate the expression levels of genes. This new research suggests that there is a sub-code buried within the same stretches of DNA that make proteins, one that specifies TF binding and thus at least partially controls gene expression." http://www.geek.com/science/scientists-discover-a-second-genetic-code-except-not-really-1579496/ View in LinkedIn
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linkedin post 2017-08-17 04:48:52

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ANTISENSE. “Compared with coding transcripts, most antisense lncRNAs are expressed at 10-fold lower levels on average, and their expression in different tissues and cell types has generally been found to be more cell type specific. A biological role of antisense lncRNAs, despite this low expression, could still be rationalized due to the fact that there are two copies of DNA for any given gene in a cell; consequently, just two antisense lncRNA molecules are sufficient to interact with the two gene copies and elicit regulatory effects.” (IncRNA = long non coding RNA). http://www.mdpi.com/1422-0067/16/2/3251/htm View in LinkedIn
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linkedin post 2017-08-20 05:38:46

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SO ENDS this first weekend of postings about the most common protein fold on planet earth. No surprises that such an innovation came from viruses, which are so quickly evolving and numerous, that they have generated vast varieties of genetic and structural molecules that have been incorporated into all life forms. And there are still those who believe that viruses are not alive, and simply cannot recognize an alternative and innovative life format. View in LinkedIn
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linkedin post 2017-08-20 05:34:33

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CHAINMAIL AND CEMENT. "In HK97 itself, the intersubunit contacts are reinforced by a post-assembly covalent linkage—an isopeptide bond between adjacent gp5 subunits, so positioned that the entire capsid is topologically interlinked in a ‘chainmail’ arrangement. In other cases, such as bacteriophage λ, the non-covalent interactions between the subunits are reinforced by an additional ‘cement’ protein, which binds on the outer surface of the capsid at positions close to those of the isopeptide bonds in HK97." https://elifesciences.org/content/2/e01299 View in LinkedIn
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