8 to induce SPI2 expression as well as protein secretion by the SPI2-T3SS. For analyses of protein synthesis, equal amounts of bacterial cells as adjusted by OD600 were harvested and resuspended in SDS-PAGE sample buffer (T, total cell fraction). Secreted protein bound to the bacterial surface was released by mechanical shearing and precipitated from bacteria-free supernatant (D, detached fraction) and secreted proteins in the supernatant were precipitated by addition of LOXO-101 nmr 10% TCA (final concentration).

For Western blot analysis, samples corresponding to equal amount of bacteria or supernatant were separated by SDS-PAGE and transferred to nitrocellulose membranes and protein was detected with antiserum raised against SseB. As loading control and control for cell lysis, the bacterial heat shock protein DnaK was detected. The position of SseB and various mutant forms of SseB was indicated by asterisks. The quantification of the signal intensities is shown in Additional Combretastatin A4 research buy file 1. We then investigated the effect of the various deletions in SseB on the secretion of SseC and SseD and the partitioning of secreted

SseC and SseD between the soluble and cell-bound fractions. For unknown reasons, larger amounts of DnaK were observed in the detached fraction of the sseB strain, but the mutation per se did not affect cell integrity since the complemented strains did not show increased release of cytosolic protein. In accordance with our previous report [7] we observed that the majority of SseD secreted by WT Salmonella is present in the detached fraction (Fig. 3). Strains Torin 1 supplier expressing sseBΔ5, sseBΔ6 and, to a certain extend sseBΔ3 resulted in reduced amounts of

the secreted SseD in the supernatant fraction. The expression of the other deletion alleles of sseB resulted in the presence of secreted SseD in the culture supernatant as well as in the detached fraction (Fig. 3). Deletions in sseBΔ5, sseBΔ6 affect the binding site for SseA that acts as chaperone for SseB and SseD [9]. The altered partitioning observed for strains expressing these alleles may be due to the altered binding of chaperone SseA to its targets and altered Ergoloid stability of these proteins. The partitioning of SseD in the complemented sseB strain was different from that observed for the WT strain and most of SseD was present in the total cell fraction rather than in the detached fraction. This may be due to the over expression of sseB in the sseB [psseB] strain leading to more secretion of SseB in the supernatant and reduces the binding of SseB to the surface (compare Fig. 2). Therefore, the binding of SseD to the surface would be reduced and the release of SseD in the supernatant is increased. Most of the mutant alleles of sseB also resulted in higher amounts secreted SseD in the supernatant. Figure 3 Effect of various deletions in sseB on secretion and partitioning of SseD in vitro. S.

4 kDa). The ferric aerobactin transport system is a well-known virulence factor in E. coli strains causing extraintestinal infections (reviewed in [22]), such as urinary tract infections [23]. Although its role as a virulence determinant in

intestinal E. coli is not well understood, it has been proposed that it contributes to the strong colonizing capacity of those strains carrying the aerobactin genes [24]. For this reason, we evaluated the contribution of this iron transport system in the colonization capabilities of E. coli O104:H4. Figure 2 Detection of differentially BMS202 clinical trial expressed surface proteins in E. coli O104:H4 strains 15% SDS-PAGE of heat-extracted proteins from E. coli O104:H4 strain 2050 (lanes 1), 2071 (lanes 2), and C3493 (lanes 3) grown on LB or MacConkey agar. The arrows indicate the location of the aerobactin ASP2215 manufacturer transport receptor (Arrow A) and the chain A, dipeptide-binding protein (Arrow B). Low iron concentration

in MacConkey induces aerobactin receptor expression MacConkey agar is considered a low iron-containing medium which has been used to identify high-affinity iron and zinc uptake systems [25]. Therefore, expression of the aerobactin receptor in the E. coli O104:H4 wild type and the iutA mutant was investigated by using heat-extracted preparations of bacteria grown on agar plates with and without the addition of the iron chelator 2,2’-dipyridyl (DP). Expression was monitored on MacConkey as well as LB agar supplemented with DP, because the addition of Lck the iron chelator is known to induce expression of iron transport systems in E. coli[17]. No production of IutA (the 80.9 kDa aerobactin receptor) was observed on Coomassie-stained 12.5% SDS-PAGE gels containing LB agar-recovered bacterial extracts, while abundant IutA was evident in samples from MacConkey plates (Figure 3, panel

A). In contrast, the iutA mutant lacked detectable expression of IutA on either media find more tested. To confirm that aerobactin receptor expression responded to iron depletion, the media was supplemented with 200 μM of DP. As shown in Figure 3, panel A, iron chelation resulted in the expression of IutA in bacteria grown on LB + DP as well as MacConkey + DP. As expected, the aerobactin receptor was absent in heat extracts obtained from the CSS001 strain (iutA::cat) grown on either of the iron-depleted media. However, for reasons that remain unclear, the expression of the IutA receptor does not appear to be further induced on MacConkey agar supplemented with DP. Figure 3 IutA protein induction and qRT-PCR analysis of iutA expression. A. Heat-extracted proteins of E. coli O104:H4 strains C3493 (German isolate) and CCSS001 (iutA::cat) grown on MacConkey (MC) or LB agar in the absence (MC or LB) or presence (MC + DP or LB + BS) of 2,2’-dipyridil (DP) were separated in 12.5% SDS-PAGE gels and stained with Coomassie brilliant blue. Molecular mass markers are indicated on the left and the heat-extracted IutA protein is depicted by an arrow on the right. B. E.

The cultures have been transformed with a self replicative vector, pSUN202, where truncated versions of the hupSL promoter have been fused to gfp (constructs A to E).

Dilutions of the cultures, ranging from 3–30 μg Chl a/ml, have been plotted against the Vistusertib solubility dmso intensity (%). All dilutions have been measured in triplicates and the total fluorescence in the sample is 100%. Generation of hupSL reporter gene constructs To define and identify Ricolinostat concentration regulatory regions in the promoter controlling hupSL transcription a deletion analysis of the promoter was carried out. Five hupSL promoter sequences of various lengths (A-E; Fig. 1) were cloned by PCR and coupled to gfp, encoding the reporter protein GFP, or to luxAB encoding the reporter enzyme Luciferase (Fig. 1). The lengths of the truncated promoter fragments were designed according to the positions of the putative binding sites for Integration Host Factor (IHF) and NtcA, identified in the hupSL

promoter using bioinformatics (Fig. 1) [14]. Confirmation of the insertion of correct promoter deletions constructs Cells from N. punctiforme were transformed by electroporation with vector constructs containing various lengths of the hupSL promoter coupled to gfp (A-E) or luxAB (1–5) (Fig. 1). Positive clones were confirmed by colony PCR. The primers used for the colony PCR anneal to the vector sequences flanking the inserted promoter region and hence the product spans the full length of the insert (Table 1). Analysis of the obtained results indicates that all the cloned fragments were of LB-100 cell line a length expected for the correct construct (data not shown). Optimization of GFP fluorescence measurements To be able to compare the GFP

expression from the different promoter deletions, dilution series were made to confirm that measurements were done in a range where the GFP signal are linear for all the constructs. The curves show high R2 values, ranging between 0.96 to 1.0, confirming that there is only very little or no saturation of the signal using the cell density chosen for the measurements (assessed by Chlorophyll a concentration) (Fig. 3). Experiments with dilution series Tau-protein kinase of the bioluminescence measurements showed high R2 values ranging from 0.79 – 0.99 Expression from the hupSL promoter deletions The measurements of GFP intensity and hence promoter activity were performed on living cells grown under nitrogen fixing conditions. The shortest promoter fragment, E, (stretching from -57 to tsp), showed the highest expression level (Fig. 4) in all experiments. This was also confirmed in the measurements of bioluminescence, where construct E showed the highest expression levels (data not shown). This part of the hupSL promoter lacks the putative IHF and NtcA binding sites (Fig. 1). There were minor variations between the promoter activities of the four longer promoter fragments (construct A-D).

These genes come from different families, with different functions, so this shRNA knockdown method appears robust and not specific to only one gene or gene family. Methods Culture of trophozoites E. histolytica strain HM1:IMSS trophozoites were grown C59 axenically in TYI-S-33 (Trypticase-yeast extract-iron-serum)

(TYI) medium supplemented with 1× Diamond’s vitamins (SAFC Biosciences, Lenexa, KS, USA), 15% heat-inactivated adult bovine PD173074 manufacturer serum (Gemini Bio-Products, West Sacramento, CA), 100 U of penicillin/ml and 100 μg streptomycin sulfate/ml (Gibco/Invitrogen, Carlsbad, CA, USA), at 37°C in 25 cm2 tissue culture flasks [47] in a volume of 50 ml, and then transfected as described below. Transfection of amebae Plasmid DNA was prepared selleck inhibitor using the HiSpeed Qiagen Maxi Kit (Qiagen, Valencia, CA, USA). Medium 199 (M199) (Gibco BRL/Invitrogen, Carlsbad, CA, USA) was supplemented with 5.7 mM cysteine, 25 mM HEPES, and 0.6 mM ascorbic acid [48], adjusted to pH

7.0 and filter-sterilized. Twenty μg plasmid DNA diluted in 100 μl supplemented M199s medium (M199S) in 2-ml microcentrifuge tubes was mixed with 15 μl of SuperFect or Attractene transfection reagent (Qiagen, Valencia, CA, USA), and incubated at room temperature to allow transfection-complex formation as per the manufacturer’s instructions. Heat-inactivated bovine serum was added to the remaining M199S to a 15% concentration. Amebae were harvested by tapping the tissue culture flasks on a benchtop, were centrifuged at 200 × g for 5 min at 4°C, and suspended in M199S with serum to 2.5 × 105 amebae/ml. Tubes containing transfection complexes were filled with the suspended trophozoites, the contents mixed by inversion, and the tubes were incubated horizontally for 3 hours at 37°C. Tube contents were added to warm TYI in 25 cm2 tissue culture flasks, and incubated overnight at 37°C. 15 μg/ml hygromycin (Invitrogen, Carlsbad, CA, USA) was added for selection after the overnight incubation [49]. After 4–5 days, 25 ml of the TYI was removed to

a new 25 cm2 tissue culture flask, and 25 ml fresh TYI with hygromycin Thymidylate synthase was added to each of the flasks. Transfectants were usually apparent 1–2 weeks after transfection. E. histolytica shRNA constructs All short hairpin RNAs used in this study were expressed by the U6 promoter [GenBank:U43841] [41] (Figure 1A) and cloned into the amebic expression vector pGIR310, a modification of pGIR308 [49, 50] by the addition of a short polylinker containing HindIII, SalI, and NotI restriction sites (Figure 1B). Modified pGIR310 conferred resistance to hygromycin in E. histolytica and to ampicillin in Escherichia coli (E. coli). All shRNA constructs used in these studies had the same structure: a short hairpin consisting of a 29-nucleotide sense strand, followed by the 9-nucleotide loop and the 29-nucleotide complementary antisense strand (Figure 1).

It is produced by the thick ascending limb of the loop of Henle in mammalian kidneys. While the monomeric molecule has a molecular weight

of approximately 68 kDa, it is physiologically present in urine in large aggregates of up to several million daltons [20]. Uromodulin may act as a constitutive inhibitor of calcium crystallization in renal fluids [20]. Excretion of uromodulin in urine may provide defense against urinary tract infections caused by uropathogenic bacteria [21]. The amounts of uromodulin in the urine of the clinical specimens used in this examination were measured. The healthy controls and the kidney disease this website patients had similar concentrations of uromodulin in urine (data not shown). Although the possibility remains, urinary uromodulin may

undergo minor constructional changes in IgAN as reported by Wu et al. [16]. Antibodies to Tamm–Horsfall protein have been seen in Vactosertib various forms of nephritis (e.g., Balkan nephropathy); however, it remains unclear whether there is any (patho-) physiological relevance to these findings [22]. The level of urinary IgA and its complexes were reported to be higher in IgAN [17]. We have confirmed the level of urinary IgA is higher in kidney disease than in healthy volunteers, but the value of IgA divided by urinary protein concentration is not much higher in IgAN than in other kidney diseases (data not shown). We made new monoclonal antibodies which specifically recognize mesangial cells. The ICs of IgA and the unknown antigens www.selleckchem.com/products/PF-2341066.html recognized by these antibodies were also found in the urine of IgAN patients; however, these were not superior to the IgA–uromodulin complex in sensitivity (data not shown). The urine of IgAN is known to have a rather Metalloexopeptidase high concentration of the albumin–uromodulin complex [23]. The IgA–uromodulin complex might include IgA–uromodulin–albumin complex, but this three-component complex is considered to be a minor component,

because the concentration of the IgA−albumin complex was even lower than that of the IgA–uromodulin complex (data not shown). Because the IgA–uromodulin complex is found in the urine of almost all kidney diseases by ELISA, it does not seem to be specific to IgAN. Many kinds of proteins are found from IgA complexes that exist in the urine of patients with IgAN (Fig. 1a); IgA itself might tend to bind to some kind of proteins. Underglycosylated IgA which is found in IgA of IgAN patients seems to be adherent to some proteins, such as IgA, fibronectin, etc. [14]. Uromodulin seems to be a protein of this kind. The IgA–uromodulin complex might be a marker of IgAN in a similar way as HbA1c in diabetes; however, the mechanism and the meaning where such a complex is formed are problems that are still uncertain, and needs to be clarified in the future. Our results indicated that IgAN can be discriminated from other proteinuric kidney diseases such as DMN, MN, FGS and MCNS by the value of the urinary IgA–uromodulin complex.

of India. We would like to thank Mr. Ashok for his valuable laboratory assistance. Electronic supplementary material Additional file 1: Figure S1. FISH staining of LY2835219 Portiera and Cilengitide price Arsenophonus in whole mount of whitefly B. tabaci in RNase digested insect sample. No signal is detected for either Portiera (A.b) or Arsenophonus (A.c) when using LNA probes at similar conditions as in Figures 1 and 4. a and d panels show

the merged and DIC images. (TIFF 5425 kb) (TIFF 296 KB) Additional file 2: Figure S2. Negative control without any probe. No signal was detected in the negative control. a and d panels show the merged and DIC images. (TIFF 4571 kb) (TIFF 9 MB) Additional file 3: Figure S3. FISH staining of Arsenophonus in whole mount of whitefly B. tabaci at different laser settings. At low laser settings, the signal produced by DNA probe for Arsenophonus was not detectable (A.b). While LNA probe at the same settings could easily detect bacteria, giving EX 527 ic50 good signal and minimum or no background (B.b). But when laser power was increased such that DNA

probe signal could be detected, the LNA probe showed very high signal sensitivity and background (C.b). a and c panels show the merged and DIC images. (TIFF 295 kb) (TIFF 5 MB) Additional file 4: Figure S4. FISH staining of Arsenophonus in whole mount of whitefly B. tabaci at low probe concentration. Following the protocol as described, at lower probe concentration (0.6 pmoles) we could not detect Arsenophonus using DNA probe (A.b). LNA probe detects Arsenophonus at the same probe concentration (B.b). a and c panels show the merged and DIC images of the respective probes. (TIFF 4 MB) References 1. McFadden GI: Methods Cell Biol. 1995, 49:165–183.PubMedCrossRef 2. Matsuyama H, Pan Y, Skoog L, Tribukait B, Naito K, Ekman P, Lichter P, Bergerheim US: Deletion mapping of chromosome 8p in prostate cancer by fluorescence in situ hybridization. Oncogene 1994, 9:3071–3076.PubMed 3. Huang SF, Xiao S, Renshaw A, Loughlin KR, Hudson TJ, Fletcher J: Fluorescence

in situ hybridization evaluation of chromosome deletion patterns in prostate cancer. Am J Pathol 1996,149(5):1565–1573.PubMed 4. Koga R, Tsuchida T, Fukatsu T: Quenching autofluorescence Janus kinase (JAK) of insect tissues for in situ detection of endosymbionts. Appl Entomol Zool 2009,44(2):281–291.CrossRef 5. Olsen KN, Henriksen M, Bisgaard M, Nielsen OL, Christensen H: Investigation of chicken intestinal bacterial communities by 16 S rRNA targeted fluorescence in situ hybridization. A Van Leeuw J Microb 2008,94(3):423–437.CrossRef 6. West NJ, Schönhuber WA, Fuller NJ, Amann RI, Rippka R, Post AF, Scanlan DJ: Closely related Prochlorococcus genotypes show remarkably different depth distributions in two oceanic regions as revealed by in situ hybridization using 16 S rRNA-targeted oligonucleotides. Microbiology 2001,47(Pt 7):1731–1744. Reading, England 7.

FEMS Microbiol Rev 2002, 26:141–148.PubMedCrossRef 13. Kagambèga A, Haukka K, Siitonen A, Traoré AS, Barro N: Prevalence of Salmonella enterica and the hygienic indicator

Escherichia coli in raw meat at markets in Ouagadougou, Burkina Faso. J Food Prot 2011, 74:1547–1551.PubMedCrossRef 14. Kagambega A, Barro N, Traoré AS, Siitonen A, Haukka K: Characterization of Salmonella enterica and detection of the virulence genes specific to diarrheagenic Escherichia coli from poultry carcasses in Ouagadougou, Burkina Faso. Foodborne Pathog Dis 2012, 9:589–593.PubMedCrossRef 15. CDC: African pygmy hedgehog-associated salmonellosis. MMWR Morb Mortal Wkly Rep 1995, 44:462–463. 16. Craig C, Styliadis S, Woodward D,

Werker D: African pygmy hedgehog-associated Salmonella tilene in Canada. Can Commun selleck chemical Dis Rep 1997, 23:129–131.selleck chemicals PubMed 17. Bonkoungou IJO, Haukka K, Österblad M, Hakanen AJ, Traoré AS, Barro N, Siitonen A: Bacterial and viral etiology of childhood diarrhea in Ouagadougou. IWR-1 research buy Burkina Faso. BMC Pediatr 2013, 13:36.CrossRef 18. Mølbak K, Olsen JE, Wegener HC: Salmonella infections. In Foodborne Infections and Intoxications. 3rd edition. Edited by: Riemann HP, Cliver DO. The Netherlands: Elsevier; 2006:57–136. 19. Ishihara K, Takahashi T, Morioka A, Kojima A, Kijima , Asai T, Tamura Y: National surveillance of Salmonella enterica in food-producing animals in Japan. Acta Vet Demeclocycline Scand 2009, 51:35.PubMedCrossRef 20. Dione MM, Ikumapayi UN, Saha D, Mohammed NI, Geerts S, Ieven M, Adegbola RA, Antonio M: Clonal differences between non-typhoidal salmonella (NTS) recovered from children and animals living in close contact in the Gambia. PLoS Negl Trop Dis 2011, 5:1148.CrossRef 21. Fashae

K, Ogunsola F, Aarestrup FM, Hendriksen RS: Antimicrobial susceptibility and serovars of Salmonella from chickens and humans in Ibadan, Nigeria. J Infect Dev Ctries 2010, 4:484–494.PubMed 22. Milnes AS, Sayers AR, Stewart I, Clifton-Hadley FA, Davies RH, Newell DG, Cook AJ, Evans SJ, Smith RP, Paiba GA: Factors related to the carriage of Verocytotoxigenic E. coli , Salmonella , thermophilic Campylobacter and Yersinia enterocolitica in cattle, sheep and pigs at slaughter. Epidemiol Infect 2009, 137:1135–1148.PubMedCrossRef 23. Molla B, Alemayehu D, Salah W: Sources and distribution of Salmonella serotypes isolated from food animals, slaughterhouse personnel and retail meat products in Ethiopia: 1997–2002. Ethip J Health Dev 2003, 17:63–70. 24. Lomonaco S, Decastelli L, Bianchi DM, Nucera D, Grassi MA, Sperone V, Civera T: Detection of Salmonella in finishing pigs on farm and at slaughter in Piedmont, Italy. Zoonoses Public Health 2009, 56:137–144.PubMedCrossRef 25. Kikuvi GM, Ombui JN, Mitema ES: Serotypes and antimicrobial resistance profiles of Salmonella isolates from pigs at slaughter in Kenya. J Infect Dev Ctries 2010, 4:243–248.PubMedCrossRef 26.

47), angiotensin I (m/z 1, 296.69), Glu1-fibrinopeptide B (m/z 1, 570.68), ACTH (1-17)(m/z 2093.08), ACTH (18-39)(m/z 2, 465.20). nLC-MS/MS and Endopep-MS data processing nLC-MS/MS data Data obtained from the QTof-Premier were processed by use of Waters’ ProteinLynx Global Server (PLGS v2.3; Milford, MA) and searched against a curated C. botulinum database consisting of 22, 000 NCBI entries, including the protein standard Alcohol dehydrogenase (ADH, Waters Corp; Milford, MA) and contaminants such as trypsin. Tandem Olaparib in vitro mass spectra were analyzed by use of the following parameters: variable modification of oxidized M, 1% false positive rate,

a minimum of three fragment ions per peptide and seven fragment ions per protein, a minimum

of 1 peptide match per protein, and with up to two missed cleavages per peptide allowed. Root mean square mass accuracies were typically within 8 ppm for the MS data and within 15 ppm for MS/MS data. Tandem mass spectra, obtained from the LTQ-Orbitrap, were extracted by Mascot Distiller (Matrix Science; London, UK; v2.2.1.0) and subsequently searched by use of Mascot (Matrix Science; v2.2.0) against a NCBI database consisting of seven million entries. All files generated by Mascot Distiller were searched with the following parameters: 200 ppm parent MS ion window, INCB018424 purchase 0.8 Da MSMS ion window, and up to 2 missed cleavages allowed. Variable modifications for the Mascot searches were deamidation and oxidation. PD 332991 Scaffold (Proteome Software Inc.; Portland, OR; v2.1.03) was used to validate all MS/MS-based peptide and protein identifications. Peptide identifications were accepted if they could be established at greater than 95.0% probability, as

specified by the Peptide Prophet algorithm [29]. Protein identifications were accepted if they could be selleck screening library established at greater than 99.0% probability and if they contained at least two identified peptides. Protein probabilities were assigned by the Protein Prophet algorithm [30]. Proteins that contained similar peptides and that could not be differentiated on the basis of MS/MS analysis alone were grouped to satisfy the principles of parsimony. With the stringent parameters of Peptide Prophet and Protein Prophet, the false discovery rate was zero. Endopep-MS data The MS Reflector data, obtained from the Endopep-MS reactions, were analyzed by hand. A visual comparison (by an expert researcher) of the intact substrate and its cleavage products was enough to confirm a positive or negative reaction. Relative quantification of type G NAPs The six in solution digestions, three per lot of toxin, of BoNT/G complex were spiked with a known amount of standard yeast ADH digest (100 fMol on column) and analyzed as four technical replicates by use of the QTof-Premier operated in data independent acquisition mode [31, 32].

6°

and 8.45°, indicating d spacings of 1.01 nm and 1.04 nm, respectively (based on Bragg’s equation). The slightly increased d spacing of DGO-Br over DGO-OH can be also attributed to the esterification of DGO-OH with α-bromoisobutyryl bromide. Thermal properties of the Elafibranor research buy graphene-PMMA nanocomposites learn more were compared with pristine PMMA by differential scanning calorimetry (DSC) and TGA. Figure 3 shows the DSC and TGA results for pristine PMMA and graphene-PMMA nanocomposite (GP-5) samples. For DSC (Figure 3a), the midpoints between the onset and offset points of the transition temperature were chosen as the T g values. The graphene-PMMA nanocomposite showed a higher T g than that of the pristine PMMA, which can be attributed to the interactions between GO and PMMA. The decomposition patterns for PMMA and GP-5 are shown in Figure 3b. About 15% of GP-5 nanocomposites decomposed between 130°C and 340°C, whereas pure PMMA decomposition started at 250°C. The initial decomposition of GP-5 may be due to the presence of additional labile functional groups after surface modification using quaternization followed by esterification onto the surface of GO [23]. On the other hand, the main decomposition of PMMA ends at 400°C, whereas that of the graphene-PMMA nanocomposite ends at 430°C. The difference in the thermal stability between pristine PMMA and GP-5 indicates

that the presence of graphene layers improves the thermal properties selleck of graphene-PMMA nanocomposites after in situ polymerization on the functionalized GO surface. The increased thermal stability of graphene-PMMA nanocomposites can be attributed to the attractive nature of graphene toward free radicals generated during decomposition as well as the tortuous path formation during the decomposition process

[21, 23]. Figure 3 DSC results (a) of (i) PMMA and (ii) DGO-PMMA and TGA curves (b) of (i) PMMA and (ii) DGO-PMMA. Controlled study of radical polymerization Polymerization of MMA was carried out through ATRP using multifunctional DGO-Br, and controlled radical polymerization (CRP) PIK3C2G was studied using GPC. The detailed GPC results ( , , and MWD) are summarized in Table 1. As shown in Figure 4, as time increased, the GPC curves shifted from the lower molecular weight region to the higher molecular weight region due to the CRP mechanism. It is also interesting to note that the PDI values for PMMA become narrower with time, which also supports the CRP mechanism. Figure 5 shows the time vs. conversion and time vs. ln[M]0/[M] plots for MMA polymerization, where [M]0 and [M] represent the initial monomer concentration and the monomer concentration at time t, respectively. The linear relation between time vs. ln([M]0/[M]) shows that the concentration of propagating radicals is almost constant throughout the polymerization process.

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3. Allakhverdiev KR, Yetis MÖ, Özbek S, Baykara TK, Salaev EY: Effective nonlinear GaSe crystal. Optical properties and applications. Laser Phys 2009, 19:1092.CrossRef 4. Mandal KC, Kang SH, Choi M, Chen J, Zhang X-C, Schleicher JM, Schmuttenmaer CA, Fernelius LY2874455 cost NC: III–VI chalcogenide semiconductor crystals for broadband tunable THz sources and sensors. IEEE J Sel Topics Quant Electr 2008, 14:284.CrossRef 5. Rudolph R, Pettenkofer C, Bostwick AA, Adams JA, Ohuchi F, Olmstead MA, Jaeckel B, Klein A, Jaegermann W: GSK461364 purchase Electronic structure of the Si(111): GaSe van der Waals-like surface termination. New J Phys 2005, 7:108.CrossRef 6. Adams JA, Bostwick AA, Ohuchi FS, Olmstead MA: Chemical passivity of III-VI bilayer terminated Si (111). Appl Phys Lett 2005, 87:GSK126 171906.CrossRef 7. Fritsche R, Wisotzki E, Thißen A, Islam ABMO, Klein A, Jaegermann W, Rudolph R, Tonti D, Pettenkofer C:

Preparation of a Si(111): GaSe van der Waals surface termination by selenization of a monolayer Ga on Si(111). Surf Sci 2002, 515:296.CrossRef 8. Late DJ, Liu B, Ramakrishna Matte HSS, Rao CNR, Dravid VP: Rapid characterization of ultrathin layers of chalcogenides on SiO 2 /Si substrates. Adv Funct Mater 1894, 2012:22. 9. Hu PA, Wen Z, Wang L, Tan P, Xiao K: Synthesis of few-layer GaSe nanosheets for high performance photodetectors. ACS Nano 2012, 6:5988.CrossRef 10. Gautam UK, Vivekchand SRC, Govindaraj A, Kulkarni GU, Selvi NR, Rao CNR: Generation of onions and nanotubes of GaS and GaSe through laser and thermally induced exfoliation. J Amer Chem Soc 2005, 127:3659.CrossRef 11. Côté M, Cohen ML, Chadi DJ: Theoretical study of the structural and electronic properties of GaSe nanotubes. Phys Rev B 1998, 58:R4277.CrossRef

12. Chikan V, Kelley DF: Synthesis of highly luminescent GaSe nanoparticles. NanoLett 2002, 2:1015.CrossRef 13. Shao J, Mirafzal H, Petker JR, Cosio JLS, Kelley DF, Ye T: Nanoscale organization of GaSe quantum dots on a gold surface. J Phys Chem C 2009, 113:19102.CrossRef 14. Balitskii OA, Borowiak-Palen E, Konicki W: Synthesis and characterization of MTMR9 colloidal gallium selenide nanowires. Cryst Res Technol 2011, 46:417.CrossRef 15. Allakhverdiev K, Hagen J, Salaeva Z: On a possibility to form small crystallites of layered gallium selenide via ultrasonic treatment. Phys Stat Sol 1997, 163:121.CrossRef 16. Rybkovskiy DV, Arutyunyan NR, Orekhov AS, Gromchenko IA, Vorobiev IV, Osadchy AV, Salaev EY, Baykara TK, Allakhverdiev KR, Obraztsova ED: Size-induced effects in gallium selenide electronic structure: the influence of interlayer interactions. Phys Rev B 2011, 84:085314.CrossRef 17. Scholes GD: Two dimensions are brighter. Nature Mater 2011, 10:906.CrossRef 18.