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Li, Jun

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Li, Jun

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2013 - 20142

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Author's Publications: search.filters.isAuthorOfPublication.7db73928-0cc6-4433-a2d6-3993d2bd9d76

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    Towards construction of synthetic ribosomes and a self-replicating system
    (2014-06-06) Li, Jun; Church, George McDonald; Szostak, Jack William; Munger, Karl; Buratowski, Steven; Khalil, Ahmad
    In 2006, the Church Group, using biochemical approaches, hypothesized that ∼ 151 biomolecular components from Escherichia coli and its bacteriophages may be sufficient to enable rapid and accurate self–replication in vitro. However, efforts to construct such a system are precluded by our inability to sufficiently co–regenerate these 151 biomolecular components (or the components of ribosome — the key player of protein translation) and the inability to assemble E. coli ribosomes under conditions that are compatible with in vitro transcription and translation and also the lacking of evidence that functionally active ribosomes can be reconstituted from in vitro synthesized proteins and RNAs.
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    Evidence for a Common Mechanism of SIRT1 Regulation by Allosteric Activators
    (American Association for the Advancement of Science (AAAS), 2013) Hubbard, B. P.; Gomes, A. P.; Dai, H.; Li, Jun; Case, A. W.; Considine, T.; Riera, T. V.; Lee, J. E.; E, S. Y.; Lamming, D. W.; Pentelute, Brad Lether; Schuman, E. R.; Stevens, L. A.; Ling, A. J. Y.; Armour, S. M.; Michan, S.; Zhao, H.; Jiang, Y.; Sweitzer, S. M.; Blum, C. A.; Disch, J. S.; Ng, P. Y.; Howitz, K. T.; Rolo, A. P.; Hamuro, Y.; Moss, J.; Perni, R. B.; Ellis, J. L.; Vlasuk, G. P.; Sinclair, David
    A molecule that treats multiple age-related diseases would have a major impact on global health and economics. The SIRT1 deacetylase has drawn attention in this regard as a target for drug design. Yet controversy exists around the mechanism of sirtuin-activating compounds (STACs). We found that specific hydrophobic motifs found in SIRT1 substrates such as PGC-1α and FOXO3a facilitate SIRT1 activation by STACs. A single amino acid in SIRT1, Glu230, located in a structured N-terminal domain, was critical for activation by all previously reported STAC scaffolds and a new class of chemically distinct activators. In primary cells reconstituted with activation-defective SIRT1, the metabolic effects of STACs were blocked. Thus, SIRT1 can be directly activated through an allosteric mechanism common to chemically diverse STACs.