24 research outputs found
MOESM5 of H3K27me1 is essential for MMP-9-dependent H3N-terminal tail proteolysis during osteoclastogenesis
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
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
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
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
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
MOESM6 of H3K27me1 is essential for MMP-9-dependent H3N-terminal tail proteolysis during osteoclastogenesis
Additional file 6: Fig. S6. Schematic representation of ChIPac-qPCR assay
Evaluation of Electroless Pt Deposition and Electron Beam Pt Evaporation on p‑GaAs as a Photocathode for Hydrogen Evolution
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
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
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
