Development of novel riboswitch for in vivo sensing and mornitoring of naringenin

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Novel Coenzyme B12 riboswitch-based sensor integrates with transcriptional repressor for signal inverting and amplify

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On-chip analysis of high producing strains for chemical production in microfluidic static droplet array

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Development of naringenin riboswitch-based biosensor for in vivo sensing

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Development of in vivo sensing biosensor based naringenin riboswitch

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Tuning of Riboswitch-Based Genetic Devices to Have Desired Dose-Reponse Curves

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Combating Label Distribution Shift for Active Domain Adaptation

We consider the problem of active domain adaptation (ADA) to unlabeled target data, of which subset is actively selected and labeled given a budget constraint. Inspired by recent analysis on a critical issue from label distribution mismatch between source and target in domain adaptation, we devise a method that addresses the issue for the first time in ADA. At its heart lies a novel sampling strategy, which seeks target data that best approximate the entire target distribution as well as being representative, diverse, and uncertain. The sampled target data are then used not only for supervised learning but also for matching label distributions of source and target domains, leading to remarkable performance improvement. On four public benchmarks, our method substantially outperforms existing methods in every adaptation scenario.1

Microfluidic static droplet array based on-chip screening for higher chemical producing strains

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SAMHD1 specifically restricts retroviruses through its RNase activity

Background Human SAMHD1 possesses dual enzymatic functions. It acts as both a dGTP-dependent triphosphohydrolase and as an exoribonuclease. The dNTPase function depletes the cellular dNTP pool, which is required for retroviral reverse transcription in differentiated myeloid cells and resting CD4+ T cells; thus this activity mainly plays a role in SAMHD1-mediated retroviral restriction. However, a recent study demonstrated that SAMHD1 directly targets HIV-1 genomic RNA via its RNase activity, and that this function (rather than dNTPase activity) is sufficient for HIV-1 restriction. While HIV-1 genomic RNA is a potent target for SAMHD1 during viral infection, the specificity of SAMHD1-mediated RNase activity during infection by other viruses is unclear. Results The results of the present study showed that SAMHD1 specifically degrades retroviral genomic RNA in monocyte-derived macrophage-like cells and in primary monocyte-derived macrophages. Consistent with this, SAMHD1 selectively restricted retroviral replication, but did not affect the replication of other common non-retro RNA genome viruses, suggesting that the RNase-mediated antiviral function of SAMHD1 is limited to retroviruses. In addition, neither inhibiting reverse transcription by treatment with several reverse transcriptase inhibitors nor infection with reverse transcriptase-defective HIV-1 altered RNA levels after viral challenge, indicating that the retrovirus-specific RNase function is not dependent on processes associated with retroviral reverse transcription. Conclusions The results presented herein suggest that the RNase activity of SAMHD1 is sufficient to control the replication of retroviruses, but not that of non-retro RNA viruses