11 research outputs found

    New Insights into Hydrosilylation of Unsaturated Carbon–Heteroatom (CO, CN) Bonds by Rhenium(V)–Dioxo Complexes

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    The hydrosilylation of unsaturated carbon–heteroatom (CO, CN) bonds catalyzed by high-valent rhenium­(V)–dioxo complex ReO<sub>2</sub>I­(PPh<sub>3</sub>)<sub>2</sub> (<b>1</b>) were studied computationally to determine the underlying mechanism. Our calculations revealed that the ionic outer-sphere pathway in which the organic substrate attacks the Si center in an η<sup>1</sup>-silane rhenium adduct to prompt the heterolytic cleavage of the Si–H bond is the most energetically favorable process for rhenium­(V)–dioxo complex <b>1</b> catalyzed hydrosilylation of imines. The activation energy of the turnover-limiting step was calculated to be 22.8 kcal/mol with phenylmethanimine. This value is energetically more favorable than the [2 + 2] addition pathway by as much as 10.0 kcal/mol. Moreover, the ionic outer-sphere pathway competes with the [2 + 2] addition mechanism for rhenium­(V)–dioxo complex <b>1</b> catalyzing the hydrosilylation of carbonyl compounds. Furthermore, the electron-donating group on the organic substrates would induce a better activity favoring the ionic outer-sphere mechanistic pathway. These findings highlight the unique features of high-valent transition-metal complexes as Lewis acids in activating the Si–H bond and catalyzing the reduction reactions

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    <p>Tumor necrosis factor receptor-associated factor 3 (TRAF3), an intracellular signal transducer, is identified as an important component of Toll-like receptors and RIG-I-like receptors induced type I interferon (IFN) signaling pathways. Previous studies have clarified TRAF3 function in mammals, but little is known about the role of TRAF3 in ducks. Here, we cloned and characterized the full-length duck TRAF3 (duTRAF3) gene and an alternatively spliced isoform of duTRAF3 (duTRAF3-S) lacking the fragment encoding amino acids 217–319, from duck embryo fibroblasts (DEFs). We found that duTRAF3 and duTRAF3-S played different roles in regulating IFN-β production in DEFs. duTRAF3 through its TRAF domain interacted with duMAVS or duTRIF, leading to the production of IFN-β. However, duTRAF3-S, containing the TRAF domain, was unable to bind duMAVS or duTRIF due to the intramolecular binding between the N- and C-terminal of duTRAF3-S that blocked the function of its TRAF domain. Further analysis identified that duTRAF3-S competed with duTRAF3 itself for binding to duTRAF3, perturbing duTRAF3 self-association, which impaired the assembly of duTRAF3-duMAVS/duTRIF complex, ultimately resulted in a reduced production of IFN-β. These findings suggest that duTRAF3 is an important regulator of duck innate immune signaling and reveal a novel mechanism for the negative regulation of IFN-β production via changing the formation of the homo-oligomerization of wild molecules, implying a novel regulatory role of truncated proteins.</p

    Representative DT imaging of the ROIs.

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    <p>(a) the trapezoid body, (b) superior olivary nucleus, (c) inferior colliculus, (d) medial geniculate body, (e) the auditory radiation, (f) the white matter of Heschl's gyrus, (square box) the selected ROI.</p

    Clinical and audiogram data of patients.

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    <p>Values are presented as mean±SD.</p><p>*Statistically significant difference.</p><p>CI, cochlear implantation; ABR, auditory brainstem response; CAP, categories of auditory performance.</p><p>Clinical and audiogram data of patients.</p

    Summary of MD values at the TB, SON, IC, MGB, AR and WHG in the SNHL and control groups.

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    <p>Values are presented as mean ± SD; MD values measured at the TB, SON, IC, MGB, AR and WHG of the SNHL group were compared with the control group.</p><p>Summary of MD values at the TB, SON, IC, MGB, AR and WHG in the SNHL and control groups.</p

    Summary of FA values at the TB, SON, IC, MGB, AR and WHG of the good/ poor outcome group of SNHL patients.

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    <p>Values are presented as mean±SD</p><p>*Statistically significant difference.</p><p>FA values measured at the TB, SON, IC, MGB, AR and WHG of the good outcome group of SNHL patients were compared with the poor group.</p><p>Summary of FA values at the TB, SON, IC, MGB, AR and WHG of the good/ poor outcome group of SNHL patients.</p

    Summary of FA values at the TB, SON, IC, MGB, AR and WHG in the SNHL and control groups.

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    <p>Values are presented as mean ± SD</p><p>*Statistically significant difference.</p><p>FA values measured at the TB, SON, IC, MGB, AR and WHG of the SNHL group were compared with the control group.</p><p>Summary of FA values at the TB, SON, IC, MGB, AR and WHG in the SNHL and control groups.</p

    De Novo Green Fluorescent Protein Chromophore-Based Probes for Capturing Latent Fingerprints Using a Portable System

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    Rapid visualization of latent fingerprints, preferably at their point of origin, is essential for effective crime scene evaluation. Here, we present a new class of green fluorescent protein chromophore-based fluorescent dyes (LFP-Yellow and LFP-Red) that can be used for real-time visualization of LFPs within 10 s. Compared with traditional chemical reagents for LFPs, these fluorescent dyes are completely water-soluble, exhibit low cytotoxicity, and are harmless to users. Level 1–3 details of the LFPs could be clearly revealed through “off–on” fluorescence signal readout. Additionally, the fluorescent dyes were constructed based on an imidazolinone core and so do not contain pyridine groups or metal ions, which ensures that the DNA is not contaminated during extraction and identification after the LFPs are treated with the dyes. Combined with our as-developed portable system for capturing LFPs, LFP-Yellow and LFP-Red enabled the rapid capture of LFPs. Therefore, these green fluorescent protein chromophore-based probes provide an approach for the rapid identification of individuals who were present at a crime scene

    De Novo Green Fluorescent Protein Chromophore-Based Probes for Capturing Latent Fingerprints Using a Portable System

    No full text
    Rapid visualization of latent fingerprints, preferably at their point of origin, is essential for effective crime scene evaluation. Here, we present a new class of green fluorescent protein chromophore-based fluorescent dyes (LFP-Yellow and LFP-Red) that can be used for real-time visualization of LFPs within 10 s. Compared with traditional chemical reagents for LFPs, these fluorescent dyes are completely water-soluble, exhibit low cytotoxicity, and are harmless to users. Level 1–3 details of the LFPs could be clearly revealed through “off–on” fluorescence signal readout. Additionally, the fluorescent dyes were constructed based on an imidazolinone core and so do not contain pyridine groups or metal ions, which ensures that the DNA is not contaminated during extraction and identification after the LFPs are treated with the dyes. Combined with our as-developed portable system for capturing LFPs, LFP-Yellow and LFP-Red enabled the rapid capture of LFPs. Therefore, these green fluorescent protein chromophore-based probes provide an approach for the rapid identification of individuals who were present at a crime scene

    De Novo Green Fluorescent Protein Chromophore-Based Probes for Capturing Latent Fingerprints Using a Portable System

    No full text
    Rapid visualization of latent fingerprints, preferably at their point of origin, is essential for effective crime scene evaluation. Here, we present a new class of green fluorescent protein chromophore-based fluorescent dyes (LFP-Yellow and LFP-Red) that can be used for real-time visualization of LFPs within 10 s. Compared with traditional chemical reagents for LFPs, these fluorescent dyes are completely water-soluble, exhibit low cytotoxicity, and are harmless to users. Level 1–3 details of the LFPs could be clearly revealed through “off–on” fluorescence signal readout. Additionally, the fluorescent dyes were constructed based on an imidazolinone core and so do not contain pyridine groups or metal ions, which ensures that the DNA is not contaminated during extraction and identification after the LFPs are treated with the dyes. Combined with our as-developed portable system for capturing LFPs, LFP-Yellow and LFP-Red enabled the rapid capture of LFPs. Therefore, these green fluorescent protein chromophore-based probes provide an approach for the rapid identification of individuals who were present at a crime scene
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