Single cells that were transferred from permissive conditions to solid pads of LB medium with glucose first continued to divide regularly, forming microcolonies in which the number

of cells initially increased exponentially. Then, after about four divisions, cell division slowed down and stopped (Figure 1b and Additional file 4 – movie 3). Analysis of the time-lapse images (Additional file 4 – movie 3) showed that, during this transition, cells size decreased (Figure 2a). This indicates a disturbance in of cell size homeostasis [19] – that cells divide before their cell size doubled. Figure 2 Depletion of YgjD lead to a ON-01910 mw change in cell size homeostasis. The figure is based on data from one microcolony of TB80 (Para-ygjD) depleted for YgjD (A; also Selleckchem Mocetinostat see Additional File 4 – movie 3) and E. coli wildtype MG1655 (B; also see Additional File 2 – movie 2). Each point represents information about one cell, and the color of the point indicates which generation this cell belongs to (for a definition of ‘generation’ see main text). A) Changes in cell size during YgjD depletion. Cell size at division PD-1/PD-L1 inhibitor decreases continuously during the depletion experiment; B) Growth characteristics of MG1655 on single cell level. MG1655 exhibits a nearly constant cell size at division, and a slight increase of growth rate over consecutive divisions.

We used elongation rates of single cells and the time interval between two divisions to analyze the change in cell size homeostasis during YgjD depletion. Since we were interested in how these parameters changed during depletion, we separated data from different cell generations of the depletion process. The first cell that is founding a microcolony is generation 0; this cell divides into two cells of generation 1, which divide into four cells of generation 2, and so on (also see Additional File 5 – Figure S2). To avoid comparisons between cells that are in different phases of their cell cycle, we only used cell size measurements (and later

fluorescence intensities) of cells immediately before division. Also, to avoid incomplete and biased sampling, we removed data from above generation 6. This analysis revealed that the small size (-)-p-Bromotetramisole Oxalate of cells depleted for YgjD was a consequence of two effects: first, the rate of elongation (cell length increase over time) decreased (Figure 3a). Second, cells did not respond to the decrease in elongation rate by adjusting the frequency at which they divided; the interval between two cell divisions remained initially constant. As a direct consequence, cell length at division decreased continuously (Figure 2a). Figure 3 Cell elongation rate and the interval between two divisions are coupled during YgjD depletion. The contour line depicts all combinations of cell elongation rate and interval between divisions that correspond to a cell size doubling before division.

salinarum was performed essentially as described by [117]. Transformed cells were grown with 0.15 μgm l −1 novobiocin (Sigma). E.coli strains DH5α, ccdB survival™2 T1 R , Mach1™-T1 R

and transformants were grown in LB medium (1% tryptone, 0.5% yeast extract, and 1% NaCl) at 37°C and supplemented with ampicillin (100 μgm l −1), kanamycin (25 μgm l −1), or chloramphenicol (50 μgm l −1), if necessary. Construction of vectors The plasmid pMS4 was obtained by cloning the promoter PrR16 [118, 119] and the CBD (both amplified from the plasmid pWL-CBD [55] by PCR), the Gateway vector conversion cassette (Invitrogen), again the CBD, a His tag and transcriptional terminator from the Hbt.salinarum bop gene into the plasmid pVT [120] which provides a novobiocin resistance gene [121] and the bgaH marker selleckchem gene [122] as well as an E.coli origin of GSK872 molecular weight replication and an ampicillin resistance cassette. pMS6 was derived from pMS4 by removing both CBDs by restriction digest with NcoI and XbaI and subsequent reconstitution of the Gateway cassette. Gateway destination vectors were propagated in ccdB survival cells grown in LB medium containing chloramphenicol and ampicillin. For generation of expression plasmids, bait protein

coding sequences were amplified by PCR using the primers listed in Additional file 10 with Phusion polymerase (Finnzymes) according to supplier’s recommendations. The purified PCR products were cloned into the pENTR/D-TOPO vector (Invitrogen) according to manufacturer’s instructions, and transformed into E.coli One Shot®;Mach1™-T1 R competent cells. Kanamycin-resistant (kanR) colonies were screened by colony PCR using the primers M13F (-20) and M13R (-26) to verify insert size, and positive clones sequence-verified Thymidylate synthase using the same primers. Inserts were shuttled

into pMS4 and pMS6 using Gateway®;LR Clonase™II Enzyme mix (Invitrogen) and the resulting expression plasmids verified by restriction digest. Generation of Hbt.salinarum bait expression strains Expression plasmids were transformed into Hbt. salinarum R1. Transformants were identified by their novobiocin resistance and their blue color on X-gal containing plates. Expression of the tagged bait protein in pMS4 transformants was verified by affinity purification on cellulose and subsequent PAGE. Bait-control strains transformed with pMS6 were checked by western blot with an anti-penta-his HRP conjugate (QIAGEN). Affinity purification of CBD-tagged proteins The bait expression strain was precultured in 35 ml complex medium containing 0.15 μgm l −1 novobiocin at 37°C on a shaker (150 rpm) until an O D 600of 0.6 was reached. This preculture was used to GDC-0941 cell line inoculate 100 ml complex medium at an O D 600 of 0.01. When the main culture had reached an O D 600of 0.6 to 1.0, cells were harvested by centrifugation (8000 rpm, 15 min, 15°C) and resuspended in 1-2 ml CFE buffer (3 M KCl, 1 M NaCl, 400 mM N H 4 Cl, 40 mM MgC l 2, 10 mM Tris/HCl, pH 7.

CCL2 has been demonstrated to have an important role in defence against L. monocytogenes infection. It is highly upregulated during the early phase of L. monocytogenes ARN-509 datasheet infection and attracts inflammatory monocytes, T lymphocytes, and natural killer cells to the site of microbial infection [49–51]. In the spleen, CCL2 is produced by ERTR-9+ marginal zone macrophages which are early targets of L. monocytogenes infection and

are crucial for innate immune defence [52]. High levels of CCL2, as for example induced by over expression in transgenic mice, have been demonstrated to be associated with increased sensitivity to L. monocytogenes infection [53]. Thus, elevated CCL2 levels in C3HeB/FeJ mice are likely to contribute to the overall increased detrimental inflammatory response that we have find more observed in these mice. However, this cannot explain the general host susceptibility of this mouse strain. Importantly, C3HeB/FeJ mice are susceptible to selleck chemicals llc many pathogens including Mycobacterium tuberculosis[54], Salmonella Typhimurium [55, 56], Plasmodium chabaudi[57], Trypanosoma rhodesiense[58], Listeria monocytogenes[59], and Streptococcus pyogenes[60, 61]. Susceptibility to M. tuberculosis and L. monocytogenes infection

in C3HeB/FeJ mice correlates with induction of severe necrotic lesions in the lung or liver and spleen, respectively [54, 59]. The multifocal abscess formation in both mouse infection models is controlled by the sst1 (supersusceptibility to tuberculosis) locus on mouse chromosome 1. Sst1 encodes the Sp110/Ipr1 nuclear body protein which belongs to the SP100/SP140 family of nuclear body proteins [54, 62]. The type I and II interferon inducible Sp110/Ipr1 gene is not expressed in C3HeB/FeJ mice due to a complex structural rearrangement at the Sst1 locus which left incomplete

copies of the Sp110/Ipr1 gene in this mouse strain [54, 62]. Consequently, mice which carry the Sst1 susceptibility allele are impaired in their innate immune response against intracellular pathogens such as M. tuberculosis and L. monocytogenes. Another host factor which greatly influences susceptibility to L. monocytogenes infection is Racecadotril the amount of interferon-β produced in response to infection [20, 21, 23, 28, 31, 32]. Production of interferon-β induces further release of type I interferons via autocrine and paracrine loops which can be detrimental due to induction of apoptosis in T cells and macrophages [63]. In addition, interferon-β is a major driver of TNF-α induced lethal shock by enhancing apoptosis of enterocytes and hepatocytes which results in bowel and liver damage [31]. We have compared induction of interferon-β responses in Lmo-InlA-mur-lux and Lmo-EGD-lux infected mice by using a luciferase reporter system and BLI in vivo imaging. Although we used Infb1-reporter mice on the L.

0. Hydrogenase activity-staining was done as described in [18] with 0.5 mM benzyl viologen (BV) and 1 mM 2,3,5,-triphenyltetrazolium

chloride (TTC) and continuous flushing with highly pure hydrogen gas until the activity bands appeared except that the buffer used was 50 mM MOPS pH 7.0. Alternatively, staining was done in hydrogen-flushed buffer using 0.3 mM phenazine methosulfate (PMS) as mediator and 0.2 mM nitroblue tetrazolium (NBT) as electron acceptor [52]. When formate was added as substrate to the buffer, a final concentration of 50 mM was used. When used in native-PAGE molecular mass standard proteins from a gel filtration markers kit 29-700 kDa (Sigma) were mixed in equal amounts and 6 μg of each were loaded on the gel. Immunological and enzymic methods Western blotting was performed as described in [53] by transferring proteins to nitrocellulose membranes and challenging them with monoclonal penta-His antibody from mouse (Qiagen) or AMN-107 chemical structure polyclonal anti-Hyd-1 antibody (1:20000). Secondary goat-anti-mouse or anti-rabbit antibody, respectively conjugated with HRP enzyme (Bio-Rad, USA) was used for visualisation with the Immobilon Western chemiluminescent HRP substrate (Millipore, USA). Purification

of active Hyd-1 from a 5 L culture of strain FTH004 (His-HyaA) grown in TGYEP, C646 chemical structure pH 6.5 supplemented with 5 μM Ni2+ was carried out as described [34]. Determination of protein concentration was done by the method of Bradford (Bio-Rad, USA) [54]. Measurement of redox potential Aliquots of 50 mM MOPS buffer pH 7.0 containing the concentrations of the respective oxyclozanide redox dyes indicated above were either incubated overnight in an anaerobic chamber with

an atmosphere containing 5% hydrogen for 6 h or was bubbled with hydrogen gas (100% atmosphere) for 30 min and the redox potential determined using a EMC 30-K010-D redox micro-electrode (Sensortechnik Meinsburg GmbH, Germany) attached to a Lab850 pH/redox meter (Schott Instruments, Germany). The electrode was standardized using a redox buffer provided by the company. Measurements were performed two times. Acknowledgements We are grateful to Alison Parkin for providing the oxygen-sensitive hydrogenase 1 strains and to Stefanie Hartwig for help with the redox potential measurements. Martin Sauter is thanked for providing strain HDK101. This work was supported by the BBSRC grant BB/I02008X/1 to FS and DFG grant SA 494/3-1 to RGS. References 1. Forzi L, Sawers RG: Maturation of [NiFe]-hydrogenases in Escherichia coli. Biometals 2007, 20:565–578.PubMedCrossRef 2. Böck A, King P, Blokesch M, Posewitz M: Maturation of hydrogenases. Adv Microb Physiol 2006, 51:1–71.PubMedCrossRef 3. Menon NK, Robbins J, Wendt J, Shanmugam K, Przybyla A: Mutational analysis and characterization of the Escherichia coli hya operon, which encodes [NiFe] hydrogenase 1. J NVP-BSK805 clinical trial Bacteriol 1991, 173:4851–4861.PubMed 4.

Interestingly, reads assigned to Gardnerella were only identified in 3/8 urine samples, even though this genus was the 3rd most abundant group in the pooled sequence

check details dataset for both the V1V2 and V6 regions (Figure 2A). Three other genera and a group of 5 genera were identified by reads belonging to 3 or 2 urine samples, respectively. 24 genera were only detected in 1 out of the 8 samples. Species richness and diversity estimates of the female urine microbiota Bacterial taxonomic richness and diversity varied greatly among urine eFT508 nmr samples investigated in this study. Community richness and diversity were determined using rarefaction plots, Chao1 and Shannon index estimations (Figure 3 and Table 2). Figure 3 Number of OTUs as function of the total number of sequences. A and B: Rarefaction curves of individual samples for the V1V2 (A) and the V6 datasets (B). Curves were generated at 3% genetic difference using MOTHUR v1.17.0 [39]. C and D: Rarefaction curves of the pooled dataset for both V1V2 reads (C) and V6 reads (D). OTUs with ≤3%, ≤6% and ≤10% pairwise sequence click here difference generated using MOTHUR v1.17.0 [39] are assumed to belong to the same species, genus and family, respectively. Rarefaction curves were generated for 3% genetic difference level (e.g., at the species level).

The number of OTUs calculated for the eight individual samples ranged from 20-504 and 63-499 OTUs for the V1V2 and V6 regions, respectively PAK5 (Figure 3A, B and Table 2). OTU numbers of the total bacterial

community in the female urine at 3% difference for the V1V2 sequence pool was calculated to 1209 OTUs and to 1435 OTUs for the V6 sequence pool (Figure 3C, D and Table 2). Furthermore, total unique OTUs for the V1V2 pooled reads were 1354 and for the V6 pooled reads 2069 (Table 2). To compare the diversity between the eight different urine samples, the Shannon diversity index was determined both with the original, and with normalized numbers of sequences (Table 2). There was no substantial difference between the two Shannon indices calculated for the same sample. Discussion In this work we sequenced two different variable regions of 16S rDNA isolated from eight culture-negative urine samples. Urine samples are at risk of contamination by the bacterial flora of the female urogenital system [82, 83], therefore sampling of mid-stream urine was performed by the clean catch method, under guidance of an experienced urotherapy nurse. To avoid further bacterial growth, which could skew the results, the samples were kept on ice and analyzed within an hour. Amplicon lengths used here exceed the typical fragment size (150-200 bp) of circulating cell-free DNA in urine [84], thus reducing the frequency of such DNA in our analyses.

Clustering analysis was performed using UPGMA (unweighted pair group method using arithmetic averages) with the categorical similarity coefficient, and the maximum parsimony was analyzed. Stability of 17 loci via in-vitro and in-vivo passage To determine the stability of each locus via in-vitro passage, B. abortus 544, B. abortus 2308, and two B. abortus isolates were inoculated on a 20-ml tryptic soy broth supplemented with 5% bovine

serum at 37°C, under 5% CO2, and were sub-cultured to fresh media 30 times, by serial passages, at two- to three-day intervals. The DNA of the strains cultivated FG-4592 purchase in each passage was extracted and was subjected to MLVA analysis. For the in-vivo experiments, six approximately eight-month-old Vorinostat in vitro Korean native cattle (Hanwoo) were vaccinated with one dose of the B. abortus RB51 vaccine (Colorado Serum Company, USA). Four weeks after the inoculation, two cows were slaughtered at two-week intervals, and vaccine strains were re-isolated from their lymph nodes.

The isolated strains were confirmed using AMOS PCR and the classical biotyping scheme. The eight re-isolated strains were compared with the original Small molecule library supplier strain to assess the stability of 17 loci. Moreover, the B. abortus 2308 strains were inoculated in six mice via the intraperitoneal route. They were re-isolated from each spleen of dead mouse after two to three days. Two strains from each mouse were randomly selected onto 5% sheep blood plate. The 12 recovered strains were tested to assess the stability of 17 loci based on the changes in the host. (This experiment has been approved to animal experiment ethical committee of NVRQS. Approval number is NVRQS-AEC-2008-12) Janus kinase (JAK) Acknowledgements This work was supported by a fund of the Veterinary Science Technical Development Research Project from the National Veterinary Research & Quarantine

Service, Republic of Korea (Project No: C-AD13-2006-09-03 and P-AD13-2006-09-01). Electronic supplementary material Additional file 1: Dataset of B. abortus strains used in this study. The data provided the strains information, their genotypes and MLVA data of 17 loci. (XLS 82 KB) References 1. KVMA, ed: The history of Korean veterinary medicine during 60 years. Seongnam: KVMA 1998. 2. Wee SH, Nam HM, Kim CH: Emergence of brucellosis in cattle in the Republic of Korea. Vet Rec 2008, 162:556–557.CrossRefPubMed 3. KCDC, ed: 2007 Communicable diseases surveillance yearbook. Seoul: KCDC 2008. 4. Moore CG, Schnurrenberger PR: A review of naturally occurring Brucella abortus infections in wild mammals. J Am Vet Med Assoc 1981, 179:1105–1112.PubMed 5. Thorne ET, Morton JK: Brucellosis in elk. II. Clinical effects and means of transmission as determined through artificial infections. J Wildl Dis 1978, 14:280–291.PubMed 6. Corner LA, Alton GG, Iyer H: Distribution of Brucella abortus in infected cattle. Aust Vet J 1987, 64:241–244.CrossRefPubMed 7.

The concentration of butyrate we used is well within the concentrations known to occur in the lumen of the lower gastrointestinal tract [37]. Figure  2C shows that zinc at 0.1 to 0.5 mM significantly protected cells from the drop in TER inflicted by XO + 400 μM hypoxanthine. Likewise, Figure  2D shows that 0.1 to 0.3 mM zinc, but not 0.4 mM zinc,

reduced Stx2 translocation triggered by XO + 400 µM hypoxanthine. Thus, while Figure  2C did not show the arch shape seen in Figure  1C, Figure  2D does have the “U” shape similar to that seen in Figure  1D with hydrogen peroxide as the injuring oxidant. In monolayers treated with hypoxanthine + XO, the amount of Stx2 that translocated across the monolayer in 24 h was 8.5 ± 3.0% (mean ± SD

of 5 experiments) of the total amount added to the upper chamber. find protocol Figures  1 and 2 showed that zinc acetate could protect against oxidant-induced drop in TER, a measure of intestinal barrier function, and inhibit the translocation of Stx2 Captisol concentration across T84 cell monolayers as well. Figure 2 Effect of selleckchem hypoxanthine plus xanthine oxidase on barrier function and Stx2 translocation in T84 cells. Panels A-C show effects on TER, while Panel D shows effect on Stx2 translocation. The “standard” concentration of hypoxanthine was 400 μM if not otherwise stated, and the standard concentration of XO was 1 U/mL. Panel A, effect of DNA ligase various concentrations of hypoxanthine on TER. The “zero” hypoxanthine condition received 1% DMSO vehicle alone. Panel B, additive effect of zinc with butyrate on TER. Panel C, protection by zinc against the drop in TER induced by hypoxanthine plus XO. Panel D, protection by zinc against Stx2 translocation triggered by hypoxanthine plus xanthine oxidase. In Figure  3 we examined the effects of other metals on TER and Stx2 translocation. We focused on the transition metals nearest to zinc in atomic number, including manganese, iron, nickel, and copper. Figure  3A shows the effects of two of these metals on TER, while Panels B-D show

the effects on Stx2 translocation. Figure  3A shows that in contrast to zinc (top curve), FeSO4 and MnCl2 had no protective effect against the drop in TER triggered by XO + hypoxanthine. Copper (as CuSO4) also failed to protect against the drop in TER (data not shown). When Stx2 translocation was measured, FeSO4 seemed to slightly enhance Stx2 translocation triggered by H2O2 (Figure  3B), but this did not reach statistical significance. Nevertheless, iron has been shown to be able to potentiate oxidant-induced damage, and this has often been attributed to iron’s ability to catalyze the Fenton reaction, in which H2O2 is split into 2 molecules of hydroxyl radical (HO•). Figure  3C shows that manganese (as MnCl2) failed to protect against Stx22 translocation, and at 0.

For example, we observed increased levels of certain glycolytic enzymes such as fructose-bisphosphate aldolase (gbs0125), glyceraldehyde 3P-dehydrogenase (gbs1811),

phosphoglycerate kinase (gbs1809), enolase (gbs0608), pyruvate dehydrogenase (acoAB), and L-lactate dehydrogenase (gbs0947) (Table 1). This finding is similar to the results reported recently by Chaussee et al [19] Idasanutlin showing that transcripts encoding proteins involved in carbohydrate utilization and transport were more abundant in S phase, presumably to maximize carbohydrate utilization. The authors suggested that increased transcription of genes involved in central metabolism and sequential utilization of more complex carbohydrates might be a particularly useful selleckchem adaptation during infection of tissues where the concentration of carbohydrates is low [19]. In GAS, transcripts of genes involved in transport and metabolism of lactose, sucrose, mannose, and amylase were also more abundant during the stationary phase of growth [19], similar to our findings in GBS (Additional file 2). Similar to links between carbohydrate metabolism and virulence in GAS [21], also carbohydrate metabolism in GBS might be connected to strain invasiveness and strain tissue-disease specifiCity [24]. Figure 3 Trends in transcript levels of genes involved in metabolism and cellular

processes. 1,994 of GBS transcripts represented on the chip were grouped into functional categories (see Table 1 and Additional file 2). The Dichloromethane dehalogenase total PX-478 purchase number of genes in each category is shown as 100% and the number of transcripts more highly expressed

in ML or S phase and transcripts with unchanged expression are presented as a fraction of the 100%. Changes in expression of regulators and signal transduction systems TCSs are especially important in the control of global gene expression, especially in the absence of alternative sigma factors. Of the multiple TCSs in GBS, only covR/S (gbs 1671/2) has been well characterized. CovR/S in GBS controls expression of multiple virulence factors, such as hemolysin, CAMP factor, and multiple adhesins [25]. The transcript levels of covR/S are down regulated in S phase, which may be responsible for the observed changes in transcription of virulence factors such as cyl genes encoding hemolysin. However, because the putative effect of CovRS on the camp and cyl genes seems to be opposite to those observed in covRS NEM316 mutant [26] it suggests that these genes are under influence of additional regulators. Several other GBS genes encoding putative TCSs and regulators had significant changes in transcript levels during the growth phases studied. For example, transcript levels of gbs1908/9 increased 10/14 times between ML and S phases.

Paraffin tissue sections (4 μm) were deparaffinized in 100% xylene and re-hydrated in descending ethanol series and water according to standard protocols. Heat-induced antigen retrieval was performed in 10 mM citrate buffer for 2 min at 100°C. Endogenous peroxidase activity was blocked by hydrogen peroxidase (3%) in Tris-buffered saline (TBS) for 30 min. Then the sections were

boiled for 10 min in citrate buffer for antigen retrieval. Nonspecific binding was blocked by incubation with 5% goat serum in TBS for 30 min. Tissue sections were incubated with mouse anti-αB-crystallin antibody (Stressgen, Victoria, Canada; GW786034 cell line 1:300) in TBS containing 1% bovine serum albumin for 1 h. After washing, sections were incubated with EnVision goat anti-mouse/horseradish peroxidase antibody (EB-2305, ZhongShan, Godbridge, China; 1:2000) for 1 h. The replacement of the primary antibody with PBS see more served as negative controls. Finally, the sections were developed with 3,3-diaminobenzidine (DAB) chromogen solution and counterstained with hematoxylin. Four fields in each slide were randomly selected and counted, and the percentage of positive staining was determined by two clinical pathologists independently using immunohistochemistry score (IHS) [16]. When a conclusion differed, the final decision was made by consensus. The results were analyzed according to the method described previously [17]. Briefly, IHS was determined by the evaluation of both staining density and intensity.

The percentage of positive tumor cells was scored as follows: 1 (0-10% positive cells),

Arachidonate 15-lipoxygenase 2 (11-50% positive cells), 3 (51-80% positive cells), selleck chemical 4 (81-100% positive cells); and the intensity of staining was scored as follows: 0 (negative), 1 (weakly positive), 2 (moderately positive), and 3 (strongly positive). Multiplication of the intensity and the percentage scores gave rise to the ultimate IHS: a sum score below 3 indicated low expression of αB-crystallin, and a sum score above 4 indicated high expression of αB-crystallin. Statistical analysis The relationship between αB-crystallin expression and clinicopathological factors was analyzed by chi-square test. Survival rate was estimated by Kaplan-Meier method. Univariate and multivariate analysis was carried out using Cox’s proportional hazards regression models. For all tests, the significance level for statistical analysis was set at P < 0.05. Statistical analyses were performed using STATA Version 12.0 (Stata Corporation, College Station, TX). Result High expression of αB-crystallin mRNA in LSCC RT-PCR amplicons were detected by 1.5% agarose gel electrophoresis, confirming that αB-crystallin was expressed in LSCC tissues (Figure  1). Moreover, mRNA levels of αB-crystallin in LSCC tissues and tumor-adjacent tissues were determined by qPCR. Normalized to β-actin, αB-crystallin mRNA level in LSCC tissues (n = 6) and tumor-adjacent normal tissues (n = 6) was 6.808 ± 1.781 and 2.475 ± 0.757, respectively (t = 5.484, P = 0.001).

Phys Stat Sol 2005, 2:1119.CrossRef 14. Gao J, Zhang X, Sun Y, Zhao Q, Yu D: Compensation mechanism in N-doped ZnO nanowires. Nanotechnology 2010, 21:245703.CrossRef 15. Yang X, Wolcott A, Wang G, Sobo A, Fitzmorris RC, Qian F, Zhang JZ, Li Y: Nitrogen-doped ZnO nanowire arrays for photoelectrochemical

water splitting. Nano Lett 2009, 9:2331.CrossRef selleckchem 16. Zervos M, Karipi C, Othonos A: The nitridation of ZnO nanowires. Nanoscale Res Lett 2012, 7:175.CrossRef 17. Li Z, Wang P, Chen H, Cheng X: Structural, electronic and thermodynamic properties of cubic Zn 3 N 2 under high pressure from first-principles calculations. Physica B 2011, 406:1182.CrossRef 18. Partin DE, Williams DJ, O’Keeffe M: Synthesis, stoichiometry and thermal stability of Zn 3 N 2 powders prepared by ammonolysis reactions. J Solid State Chem 1997, 132:56.CrossRef 19. Othonos A, Lioudakis E, Tsokkou D, Philipose U, Ruda HE: Ultrafast time-resolved spectroscopy of ZnSe nanowires: carrier dynamics of defect-related states. J Alloys Comp 2009, 483:600.CrossRef 20. Kuriyama K, Takahashi Y, Sunohara F: Optical band-gap of Zn 3 N 2 films. Phys Rev B 1993, 48:2781.CrossRef 21. Ebru ST, Hamide K, Ramazan E: Structural and optical properties of zinc nitride films prepared by pulsed filtered cathodic vacuum arc deposition.

Chin Phys Lett 2007, 24:3477.CrossRef 22. Othonos A, Zervos M, Christofides C: Carrier dynamics in β-Ga 2

O 3 nanowires. J Appl Phys 2010, 108:124302.CrossRef 23. Long R, Dai Y, Yu L, Guo M, Huang B: Structural, electronic, and optical properties of oxygen defects click here Isoconazole in Zn 3 N 2 . J Phys Chem B 2007, 111:3379.CrossRef 24. Suda T, Kakishita K: Band-gap energy and electron effective mass of polycrystalline Zn 3 N 2 . J Appl Phys 2006, 99:076101.CrossRef 25. Bär M, Ahn KS, Shet S, Yan Y, Weinhardt L, Fuchs O, Blum M, Pookpanratana S, George K, Yang W, Denlinger JD, Al-Jassim M, Heske C: Impact of air exposure on the chemical and electronic structure of ZnO:Zn 3 N 2 thin films. Appl Phys Lett 2009, 94:012110.CrossRef 26. Janoti A, Van de Walle CG: Fundamentals of zinc oxide as a semiconductor. Rep Prog Phys 2009, 72:126501.CrossRef 27. Tisdale WA, Muntwiler M, Norris DJ, Aydil ES, Zhu XY: Electron dynamics at the ZnO (10–10) surface. J Phys Chem C 2008, 112:14682.CrossRef 28. Janotti A, Van de Walle CG: Fundamentals of zinc oxide as a semiconductor. Rep Prog Phys 2009, 72:126501.CrossRef 29. Zervos M, Feiner LF: Properties of the ubiquitous p-n junction in CP-690550 cost semiconductor nanowires. J Appl Phys 2004, 95:1.CrossRef 30. Zervos M: Properties of the ubiquitous p-n junction in semiconductor nanowires. Semiconductor Sci Technol 2008, 23:075016.CrossRef 31. Mohamed HA: Structure and optical constants of electron beam deposited zinc nitride films. Opt Adv Mater Rapid Comm 2009, 3:553. 32.