ReRAM is highly expected to replace conventional flash memory due

ReRAM is highly expected to replace conventional flash memory due to its low power consumption, small bit cell size, and fast switching speed. The underlying mechanism of the resistance switching behavior is still poorly

understood, although there have been various proposed models of the resistance BAY 11-7082 in vivo switching mechanism such as formation and rupture of conductive filament paths [3, 4], field-induced electrochemical migration such as oxygen vacancy creation/diffusion [5, 6], alteration of the width and/or height of a Schottky-like barrier by trapped charge carriers in the interface states [7], trap-controlled space-charge-limited current [8–12], injecting electrons into and extracting electrons from the interface [13], and oxidation/reduction reaction at the interface [14–20]. It was also reported that the resistance switching is significantly dependent on electrode materials in the ReRAM devices [14, 18, 21–26]. The precise identity of the switching location where resistance change mainly occurs has not been revealed. The comprehensive understanding for the origin of the resistance switching is required to meet the requirement for the next-generation nonvolatile memory application. Impedance spectroscopy

is a useful technique for characterizing the resistance switching in metal oxide films, which indicates whether the overall resistance of the device is dominated MI-503 by a bulk, grain CAL-101 nmr boundary, or interface component [30–39]. In this work, the resistance switching mechanism in PCMO-based Cediranib (AZD2171) devices was investigated by impedance spectroscopy. In order to study the resistance switching mechanism in the PCMO-based

devices, the frequency response of complex impedance was measured in the PCMO-based devices with various metal electrodes. Based on impedance spectral data, the electrode material dependence of the resistance switching in the PCMO-based devices was discussed by correlating with the standard Gibbs free energy of the formation of metal oxides and the work function of each electrode metal. Methods Polycrystalline PCMO films were deposited on prefabricated Pt/SiO2/Si substrates by radio-frequency (rf) magnetron sputtering with a Pr0.7Ca0.3MnO3−δ target. The base pressure was 1 × 10−6 Torr. Before the deposition, the target was presputtered for 30 min to obtain a clean target surface. A mixture of Ar and O2 gases with 25% oxygen content was used for the sputter deposition. The process pressure was controlled at 20 mTorr. The rf power was 80 W. The substrate temperature was 450°C. The film thickness was obtained by cross-sectional scanning electron microscopy. All films were about 100 nm thick. In order to measure the electrical properties of the deposited films, we prepared layered structures composed of PCMO sandwiched between a Pt bottom electrode and top electrodes.

metallidurans     CH34 Zn, Cd, Co, Pb, Cu, Hg, Ni and Cr resistan

metallidurans     CH34 Zn, Cd, Co, Pb, Cu, Hg, Ni and Cr resistance [6] AE104 Plasmid-cured C. metallidurans strain- sensitive to toxic Small molecule library metals [6] Plasmid Description Reference or source pET32LIC Apr Overexpression plasmid for ligation-independent cloning Novagen pET32LIC pbrR Apr pbrR cloned into pET32LIC This study pMa5/8 Apr Cms Mutagenesis vector [32] pMc5/8 Aps Cmr Mutagenesis vector [32] pMaPbrR/PpbrA Apr Cms

Mutagenesis vector with pbrR/PpbrA cloned in to it This study pMOL1139 Kmr, The pbr operon cloned into plasmid pRK415 B. Borremans pMU2385 Tpr 13.3 kb low copy selleckchem number lacZ reporter plasmid [33] pMUPpbrA Tpr pMU2385 containing the PpbrA promoter directing lacZ transcription This study pMUPpbrA-1 Tpr pMU2385 containing the PpbrA promoter with a 1 bp deletion This study pMUPpbrAcon Tpr As pMUPpbrA, but −10 sequence changed to E. coli consensus This study pMUPpbrAmer Tpr As pMUPpbrA, but −10 sequence changed to mer promoter This study pMUPbrR/PpbrA Tpr, pMU2385 containing pbrR, PpbrA ΔpbrA directing

CYT387 manufacturer lacZ transcription This study pMUPbrRC14S/PpbrA As pMUPbrRPpbrA, but PbrR C14S This study pMUPbrRC55S/PpbrA As pMUPbrRPpbrA, but PbrR C55S This study pMUPbrRC79S/PpbrA As pMUPbrRPpbrA, Branched chain aminotransferase but PbrR C79S This study pMUPbrRC114S/PpbrA As pMUPbrRPpbrA, but PbrR C114S This study pMUPbrRC132S/PpbrA As pMUPbrRPpbrA, but PbrR C132S This study pMUPbrRC134S/PpbrA

As pMUPbrRPpbrA, but PbrR C134S This study pMUPbrRC132,134 S/PpbrA As pMUPbrRPpbrA, but PbrR C132S/C134S This study pUC21 Apr, high copy number cloning vector; ColE1 replicon [34] pUK21 Kmr, intermediate copy number cloning vector; p15A replicon [34] pUK21pbr1 Kmr, HindIII/SalI pbrR/PpbrA/ΔpbrA from pMOL1139 cloned into pUK21 This study DNA manipulations DNA manipulations were as described by [30]. Oligonucleotides were synthesized by Alta Bioscience, the University of Birmingham; or MWG Biotech, Germany. The DNA sequence of all mutants and cloned PCR products were confirmed by sequencing using a PE Applied Biosystems Big Dye version 2.0 sequencing kit according to the manufacturer’s protocol, followed by analysis on an ABI 3700 sequencer in the Functional Genomics Laboratory, School of Biosciences, the University of Birmingham. The primers used for sequencing were: pMUforward and pMUreverse, complementary to the sequences flanking the multiple cloning site of pMU2385, and PbrApe for pMapbrR/PpbrA clones (Table 2).

J Biomed Mater Res A 2008, 85A(2):498–505 CrossRef 45 Alexander

J Biomed Mater Res A 2008, 85A(2):498–505.CrossRef 45. Alexander EH, Rivera FA IM, Anguita J, Bost KL, Hudson MC: Staphylococcus aureus-induced tumor necrosis factor-related apoptosis-inducing ligand expression mediates apoptosis and caspase-8 activation in infected osteoblasts. BMC Microbiol 2003, 3:5.PubMedCrossRefPubMedCentral 46. Marriott I, Gray DL, Rati DM, Fowler VG, Stryjewski ME, Levin LS, Hudson MC, Bost KL: Osteoblasts produce monocyte chemoattractant protein-1 in a murine CP673451 model of Staphylococcus aureus osteomyelitis and infected human bone tissue. Bone 2005,

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Jiang B, Boyce BM, Lindsey BA: Multilayer polypeptide nanoscale coatings incorporating IL-12 for the prevention of biomedical LY411575 in vivo device-associated infections. Biomaterials 2009, 30(13):2552–2558.PubMedCrossRefPubMedCentral 52. Jiang BB, Li BY: Polypeptide nanocoatings for preventing dental and orthopaedic device-associated Oxalosuccinic acid infection: pH-induced antibiotic capture, release, and antibiotic efficacy. J Biomed Mater Res B 2009, 88B(2):332–338.CrossRef 53. Noore J, Noore A, Li BY: Cationic Antimicrobial Peptide LL-37 Is Effective against both Extra- and Intracellular Staphylococcus aureus. Antimicrob Agents Chemother 2013, 57(3):1283–1290.PubMedCrossRefPubMedCentral 54. Hamza T, Dietz M, Pham D, Clovis N, Danley S, Li B: Intra-cellular Staphylococcus aureus alone causes infection in vivo. Eur Cell Mater 2013, 25:341–350. discussion 350.PubMedPubMedCentral 55. Eze MO, Yuan L, Crawford RM, Paranavitana CM, Hadfield TL, Bhattacharjee AK, Warren RL, Hoover DL: Effects of opsonization and gamma interferon on growth of Brucella melitensis 16 M in mouse peritoneal macrophages in vitro. Infect Immun 2000, 68(1):257–263.PubMedCrossRefPubMedCentral 56.

References 1 Bouxsein ML, Karasik D (2006) Bone geometry and ske

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The impact of temperature nutrients and UVBR explained 18 8%, 11

The impact of temperature nutrients and UVBR explained 18.8%, 11.0% and 8.4% of the variance of the small eukaryotes structure respectively. While Bouvy et al. (2011) could not detect any significant responses of pico- or nano-eukaryotic plankton in the same experimental conditions, we demonstrated here, at a different taxonomic resolution, that small eukaryotes community structure

was actually affected by this multi-factorial pressure. The simultaneous use of molecular and morphological methods was therefore essential to provide evidence of rapid shifts that occur at various taxonomic levels (abundance of large groups or community composition at OTU level) under the influence of temperature, UVBR and nutrient treatments. Among the 3 regulatory factors tested, both sequencing and CE-SSCP demonstrated 4-Hydroxytamoxifen ic50 that increased temperature had the greatest influence on the small eukaryote community structure and composition. The single effect of temperature (without any significant interaction with UVBR and nutrients) on total pigmented

eukaryote abundance was observed by microscopy. Considering the different phylogenetic groups within pigmented eukaryotes, complex interaction effects were also suggested. For instance, our results showed that under multi-factorial environmental changes, the general impact on the molecular diversity and abundance of pigmented Dinophyceae resulted Thiamine-diphosphate kinase from complex interactive (non-additive) effects. Alpelisib price Multi-factorial interactions were also apparent for Cryptophyceae which experienced antagonistic effects of nutrient

addition (significantly negative impact) and temperature (positive impact on relative abundance). In addition to the manipulated factors (temperature, UVBR and nutrients), some biotic interactions such as predation, viral lysis and competition, are involved in the responses observed in this experiment. For example, the general reduction of Mamiellophyceae (Micromonas and Ostreococcus) in all treatments might be linked to (i) manipulation effects since these fragile cells might have been affected by filtration steps, (ii) limitation by inorganic nutrients under the rather low orthophosphate concentrations at T96h (from 0.05 to 0.08 μM of PO4), (iii) the grazing impact of heterotrophic flagellates: these YM155 purchase microorganisms are known to play a significant role in the regulation of Ostreococcus populations in the Thau lagoon [56] and were shown to exert a strong control of bacterioplankton during the study period [24]. We could not detect a link between the dynamics of Micromonas/Ostreococcus and viruses.

XRD, TEM, Raman, and optical transmission techniques have been ut

XRD, TEM, Raman, and optical transmission techniques have been utilized to understand the microstructure characterization of nc-Si:H thin films. XPS results have confirmed that oxygen impurities on the surface of the nc-Si:H films have the dominant formation state of SiO2. The good agreement between the bonded hydrogen content and the volume fraction of grain boundary illustrates that as an important defect structure, the volume fraction of grain boundary in nc-Si:H films can be effectively regulated through hydrogen dilution. The inverse relationship between the integrated intensity of MSM and the oxygen content presents that the oxygen incursions due to

post-oxidation originate from the location of grain boundaries inside nc-Si:H films. The tuning mechanism of hydrogen on oxygen impurities https://www.selleckchem.com/products/EX-527.html is that the hydrides corresponding learn more to the MSM with a certain kind of bonding configuration are formed by the incorporation of H atoms and ions with the silicon dangling bonds located at grain boundaries, which can effectively prevent the oxygen incursions from residing along grain boundaries and further forming the Si-O/Si defects. Therefore, applying an extra negative bias on the substrate during the growth process is proposed

to reduce the probability of oxygen contamination, which can ACY-1215 produce films with better light absorption properties in the solar cell application. Acknowledgements This work was supported by the National Major Basic Research Projects (2012CB934302) and Natural Science Foundation of China (11174202 and 61234005). References 1. Kitao J, Harada H, Yoshida NJ, Kitao H, Yoshidaa HN, Kasuya Y, Nishio M, Sakamoto T, Itoh T, Nonomura S, Nitta S: Absorption coefficient spectra of μc-Si in the low-energy region

0.4–1.2 eV. Sol Energy Mater Sol Cells 2001, 66:245–251.CrossRef 2. Zhang R, Chen XY, Zhang K, Shen WZ: Photocurrent response of hydrogenated nanocrystalline silicon thin films. J Appl Phys 2006, 100:104310–104315.CrossRef 3. Chen XY, Shen WZ, He YL: Enhancement of electron mobility in nanocrystalline silicon/crystalline silicon heterostructures. J Appl Phys 2005, 97:024305–5.CrossRef 4. Keppner H, Meier J, Torres P, Fischer D, Shah A: Microcrystalline silicon and micromorph tandem solar cells. Appl Phys A 1999, all 69:169–177.CrossRef 5. Mai Y, Klein S, Geng X, Finger F: Structure adjustment during high-deposition-rate growth of microcrystalline silicon solar cells. Appl Phys Lett 2004, 85:2839–2841.CrossRef 6. Yang J, Yan B, Guha S: Amorphous and nanocrystalline silicon-based multi-junction solar cells. Thin Solid Films 2005, 487:162–169.CrossRef 7. Yamamoto K, Nakajima A, Yoshimi M, Sawada T, Fukuda S, Suezaki T, Ichikawa M, Koi Y, Goto M, Meguro T, Matsuda T, Kondo M, Sasaki T, Tawada Y: A thin-film silicon solar cell and module. Prog Photovolt Res Appl 2005, 13:489–494.

Mock transfection only contained transfection reagents Detection

Mock transfection only contained transfection reagents. Detection of the RNAi efficiency The RNA interference (RNAi) efficiency

was checked by Western-blot. The cells were harvested and lysed with RIPA lysis SB431542 cost SB202190 buffer (Thermo Scientific). One hundred μg of total proteins per well were loaded onto a SDS-PAGE gel and then transferred to a PVDF membrane for western blot detection. GST pull down assay to detect the activation of RhoA and Rac1 16-HBE cells were cultured in six T-75 flasks to reach 100% confluency. Three flasks of cells were infected with T. gondii tachyzoites at a multiplicity of infection (MOI) of 10. The other three flasks of cells were kept as uninfected control (mock). At 3 hr post-infection, the medium from mock and infected flasks was aspirated and cells were trypsinized. Mock and infected cells were lysed in RIPA lysis buffer (Thermo Scientific) with ultrasonication. For negative control, 150 μg (600 μl) of the infected cell extract were aliquoted into two experimental tubes; 60 μl of loading buffer were added to each tube to a final

concentration of 15 mM EDTA; 6 μl of GDP were added to these two tubes to a final concentration of 1.0 mM GDP and the tubes were incubated at room temperature for 15 min; the reaction was stopped by adding 60 μl of stopping buffer to each tube to a Go6983 concentration final concentration of 60 mM MgCl2. The negative control cell lysate incubated with GDP, and 150 μg (600 μl) total protein from the lysate of infected, uninfected cells and T. gondii tachyzoites were added to 30 μg reconstituted GST-tagged Rhotekin-RBD protein on colored agarose beads for RhoA (Cytoskeleton Inc) or GST-tagged PAK-PBD protein bound colored

agarose beads for Rac (Cytoskeleton Inc) respectively, and incubated at 4°C with rotating overnight. The beads were washed with PBS for 3 times. 25 μl protein loading buffer was added to each group of beads and boiled for 5 min then sediment at 12000 rpm for 1 min, the supernatant was used for SDS-PAGE. At the same time, 150 μg of total protein from the lysates of of infected and uninfected cells and the T. gondii tachyzoites were used for SDS –PAGE, and actin in each group was detected via western-blot and used as the equal protein loading control for the GST pull down assay. Western-blot reagents Primary antibodies: monoclonal rabbit anti-human RhoA antibody (Cell Signaling) and polyclonal rabbit anti-human Rac1 antibody (Abcam) were used in 1:1000 dilutions; β-actin was detected for loading control with monoclonal mouse anti-human anti-actin antibody (Cell Signaling) in 1:5000 dilutions. Secondary antibody: polyclonal sheep anti-mouse IgG-HRP antibody (Abcam) and polyclonal goat anti-rabbit IgG-HRP antibody (Abcam) were used in 1:3000 dilutions. ECL Western Blotting detection reagent was purchased from Pierce. Immunofluorescence for endogenous RhoA and Rac1 after T. gondii infection 16-HBE cells were grown on coverslips to 80% confluence.

The authors also acknowledge MSc Ville-Markus Korpijärvi, DSc Juh

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