24 research outputs found

    MOESM5 of H3K27me1 is essential for MMP-9-dependent H3N-terminal tail proteolysis during osteoclastogenesis

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    Additional file 5: Fig. S5. Determination of the effects of EZH1/EZH2 inhibitors on osteoclastogenic H3NT proteolysis. Chromatin was extracted from OCP-induced cells after treating with an EZH1/EZH2 inhibitor and subject to Western blotting with H3CT antibody

    MOESM4 of H3K27me1 is essential for MMP-9-dependent H3N-terminal tail proteolysis during osteoclastogenesis

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    Additional file 4: Fig. S4. Determination of the effects of EZH1/EZH2 knockdown on osteoclastogenic H3NT proteolysis. a Chromatin was purified from mock-depleted, OCP-induced cells, and Western blot analysis for H3NT proteolysis was performed as described in Fig. 2. b As for (a) but using chromatin from EZH1-depleted, OCP-induced cells. c As for (a) but using chromatin from EZH2-depleted, OCP-induced cells

    MOESM1 of H3K27me1 is essential for MMP-9-dependent H3N-terminal tail proteolysis during osteoclastogenesis

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    Additional file 1: Fig. S1. Workflow of the purification method used for isolation of ectopic H3 nucleosomes

    MOESM2 of H3K27me1 is essential for MMP-9-dependent H3N-terminal tail proteolysis during osteoclastogenesis

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    Additional file 2: Fig. S2. Abolishment of osteoclastogenic H3NT proteolysis by H3K27R mutation. Mononucleosomes containing ectopic H3 were purified from OCP-induced cells expressing H3 wild type or K27R mutant with C-terminal FLAG tag as summarized in Additional file 1: Fig. S1 and analyzed by Western blotting with anti-FLAG antibody

    MOESM3 of H3K27me1 is essential for MMP-9-dependent H3N-terminal tail proteolysis during osteoclastogenesis

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    Additional file 3: Fig. S3. Validation of specific knockdown of EZH1 and EZH2. OCP cells were transduced with lentiviral shRNAs targeting EZH1 (a) and EZH2 (b), and knockdown efficiency and specificity were determined by Western blot

    Evaluation of Electroless Pt Deposition and Electron Beam Pt Evaporation on p‑GaAs as a Photocathode for Hydrogen Evolution

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    This study examines the changes in the photoelectrochemical (PEC) properties with Pt morphology after wet (electroless Pt deposition) and dry (e-beam Pt evaporation) deposition of Pt on p-GaAs. The Pt morphology and composition of the p-GaAs surface differed depending on the Pt deposition method, which in turn affected the optical and PEC properties of Pt on the GaAs electrode. Thus, the findings of this study can help us gain a clearer understanding of the manner in which these changes affect the operation of a GaAs PEC water-splitting electrode

    Resist-Free Direct Stamp Imprinting of GaAs via Metal-Assisted Chemical Etching

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    We introduce a method for the direct imprinting of GaAs substrates using wet-chemical stamping. The predefined patterns on the stamps etch the GaAs substrates via metal-assisted chemical etching. This is a resist-free method in which the stamp and the GaAs substrate are directly pressed together. Imprinting and etching occur concurrently until the stamp is released from the substrate. The stamp imprinting results in a three-dimensional anisotropic etching profile and does not impair the semiconductor crystallinity in the wet-chemical bath. Hole, trench, and complex patterns can be imprinted on the GaAs substrate after stamping with pillar, fin, and letter shapes. In addition, we demonstrate the formation of sub-100 nm trench patterns on GaAs through a single-step stamping process. Consecutive imprinting using a single stamp is possible, demonstrating the recyclability of the stamp, which can be used more than 10 times. The greatest benefit of this technique is the simple method of patterning by integrating the lithographic and etching processes, making this a high-throughput and low-cost technique

    Agmatine-Containing Bioreducible Polymer for Gene Delivery Systems and Its Dual Degradation Behavior

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    Agmatine-containing bioreducible polymer, poly­(cystaminebis­(acrylamide)-agmatine) (poly­(CBA-AG)) was synthesized for gene delivery systems. It could form 200–300 nm sized and positively charged polyplexes with pDNA, which could release pDNA in reducing the environment due to the internal disulfide bonds cleavage. Poly­(CBA-AG) also showed a spontaneous degradation behavior in aqueous condition in contrast to the backbone polymer, poly­(cystaminebis­(acrylamide)-diaminobutane) (poly­(CBA-DAB)) lacking guanidine moieties, probably due to the self-catalyzed hydrolysis of internal amide bonds by guanidine moieties. The cytotoxicity of poly­(CBA-AG) was cell-dependent but minimal. Poly­(CBA-AG) exhibited highly enhanced transfection efficiency in comparison with poly­(CBA-DAB) and even higher transfection efficiency than PEI25k. However, cellular uptake efficiency of the polyplexes did not show positive correlation with the transfection efficiency. Confocal microscopy observation revealed that pDNA delivered by poly­(CBA-AG) was strongly accumulated in cell nuclei. These results suggested that high transfection efficiency of poly­(CBA-AG) may be derived from the efficient pDNA localization in cell nuclei by guanidine moieties and that the polyplexes dissociation via self-catalyzed hydrolysis as well as disulfide bonds cleavage in cytosol also may facilitate the transfection process. Finally, poly­(CBA-AG)/pJDK-apoptin polyplex showed a high anticancer activity induced by apoptosis, demonstrating a potential of poly­(CBA-AG) as a gene carrier for cancer gene therapy
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