67 research outputs found

    Tertiary Amine-Triggered Cascade S<sub>N</sub>2/Cycloaddition: An Efficient Construction of Complex Azaheterocycles under Mild Conditions

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    In this paper, an amine-triggered cascade S<sub>N</sub>2/cycloaddtion sequence between 2-(acetoxymethyl)buta-2,3-dienoate <b>1</b> and various π-system functionalized tosylamides <b>3</b> has been reported, which provides a facile method for stereoselective construction of structurally diverse azaheterocycles

    Tertiary Amine-Triggered Cascade S<sub>N</sub>2/Cycloaddition: An Efficient Construction of Complex Azaheterocycles under Mild Conditions

    No full text
    In this paper, an amine-triggered cascade S<sub>N</sub>2/cycloaddtion sequence between 2-(acetoxymethyl)buta-2,3-dienoate <b>1</b> and various π-system functionalized tosylamides <b>3</b> has been reported, which provides a facile method for stereoselective construction of structurally diverse azaheterocycles

    α‑Imino Gold Carbenes from 1,2,4-Oxadiazoles: Atom-Economical Access to Fully Substituted 4‑Aminoimidazoles

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    A novel and atom-economical synthesis of fully substituted 4-aminoimidazoles via gold-catalyzed selective [3 + 2] annulation of 1,2,4-oxadiazoles with ynamides is reported. This protocol represents a new strategy to access α-imino gold carbenes, which corresponds to an unprecedented intermolecular transfer of <i>N</i>-acylimino nitrenes to ynamides. Moreover, the reaction proceeds with 100% atom economy, exhibits good functional group tolerance, and can be conducted in gram scale

    α‑Imino Gold Carbenes from 1,2,4-Oxadiazoles: Atom-Economical Access to Fully Substituted 4‑Aminoimidazoles

    No full text
    A novel and atom-economical synthesis of fully substituted 4-aminoimidazoles via gold-catalyzed selective [3 + 2] annulation of 1,2,4-oxadiazoles with ynamides is reported. This protocol represents a new strategy to access α-imino gold carbenes, which corresponds to an unprecedented intermolecular transfer of <i>N</i>-acylimino nitrenes to ynamides. Moreover, the reaction proceeds with 100% atom economy, exhibits good functional group tolerance, and can be conducted in gram scale

    Mn(II) and Fe(II) modulate the binding activity of DR2539 <i>in vivo</i>.

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    <p>(A) Effects of divalent metals (50 µM) on expression of pRAZH in <i>D. radiodurans</i>. Data shown are the means ± standard deviations of three independent experiments. (B) Effects of Mn(II) (squares) and Fe(II) (circles) on the expression of pRAZH in wild-type samples expressing DR2539. (C) Effects of Mn(II) (squares) and Fe(II) (circles) on the expression of pRAZH in the <i>dr2539</i> null mutant. (D) Rea-time PCR analysis of the <i>dr1709</i> gene expression using <i>dr0089</i> as internal control gene. Longitudinal axes indicate the change fold of <i>dr1709</i> mRNA relative to controls. Control cells were cultured in medium without Mn(II). *, <i>P</i><0.05 relative to control. The data are the means ± standard deviations of three independent experiments.</p

    Sequence alignment of the metal binding sites of DR2539 with other DxtR/MntR family members.

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    <p>ScaR (<i>Streptococcus gordonii</i>), SloR (<i>Streptococcus suis</i>), LCAS (<i>Lactobacillus casei</i>), SirR (<i>Corynebacterium glutamicum</i>), TroR (<i>Treponema pallidum</i>), TroR (<i>Treponema denticola</i>), IdeR (<i>Mycobacterium tuberculosis</i>), DtxR (<i>Corynebacterium diptheriae</i>), DR2539 (<i>Deinococcus radiodurans</i>), MntR (<i>Staphylococcus aureus</i>), MntR (<i>Escherichia coli</i>), and MntR (<i>Bacillus subtilis</i>). The sequences were aligned using the CLUSTAL W software. Residues shaded with black represent metal-binding sites that have been studied while residues shaded with grey represent predicted metal binding sites.</p

    His98 plays an important role in DNA binding activity of DR2539.

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    <p>(A) 10 µl cell dilution was dripped on the TGY plate to which 6 mM of Mn(II) had been added. The cells were cultured for 3 days. (B) H98Y mutant and wild-type DR2539 proteins were incubated with p1709b at different concentrations of Mn(II). (C) Quantification of the fluorescence intensity of binding bands was performed using ImageJ. *, <i>P</i><0.05.</p

    DR2539 binds to the MntH promoter DNA fragment in a Mn(II)- and Fe(II)-dependent manner.

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    <p>(A) Schematic of <i>dr1709</i> promoter (p1709a and p1709b) DNA sequence region. The inverted repeat region is shown by the inverted arrows. (B) DR2539 binding to p1709b with increasing quantities of DR2539 and 25 µM Mn(II). (C) and (D) EMSA analysis was performed using DR2539 and p1709b with increasing concentration of Mn(II) or Fe(II). RBS, ribosome binding site; Start, transcription start codon. p1709a and p1709b sequence regions are underlined by straight lines and dashed lines, respectively.</p

    DR0865 binds to the promoter of MntABC in an ion-dependent manner.

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    <p>(A) and (B) DR0865 binding to p2523 and p2284 as the concentration of DR0865 increased. (C) Wild-type R1, <i>dr2539</i> null mutant (<b>Δ</b><i>dr2539</i>), and <i>dr0865</i> null mutant (<b>Δ</b><i>dr0865</i>) were cultured on TGY plates overlaid with filter discs saturated with 1 M solution MnCl<sub>2</sub>. (D) The zone of inhibition was measured from edge of disc after three days. *, <i>P</i><0.05. Data represent the means±deviations of three independent experiments.</p

    Single cell nucleus/cytoplasm ratios under 5 µg of dsRNA stimulation (IRF3, red channel fluorescence).

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    <p>Strawberry -IRF3 hAECs were electroporated with different dosages of synthetic dsRNA analog Poly IC and dynamic live cell imaging was performed. Time presented in hr. Green trend lines are third-order polynomials, fitted using least-squares minimization. Upper row: Raw time series. Middle row: Detrended time series. Bottom row: Fourier periodograms. Columns 1–4: Observed single cells. Column 5: Two simulated cells.</p
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