Analysis of chaperone function in vitro Effects of PpiD proteins on the thermal aggregation of citrate Selleckchem Capmatinib synthase were determined GDC-0941 nmr according to [34]. Aggregation was monitored on a Hitachi F-4500 spectrofluorometer with both excitation and emission

wavelengths set to 500 nm at a spectral bandwidth of 2.5 nm. Data points were recorded every 0.5 s. Acknowledgements We thank C.A. Gross for providing strains and plasmids, D. Kahne and T. Silhavy for sharing strains, M. Ehrmann for the gift of plasmids and antibodies, and A. Charbit, E. Deuerling, B. Bukau, and K. Williams for providing antibodies. We also thank W. Kramer for helpful discussions. The work was supported by grants of the DFG to S.B. Electronic supplementary material Additional file 1: Similarity between the N-terminal region of PpiD and the chaperone modules of SurA and Trigger factor (TF). (A and B) The N-terminal region of PpiD shows sequence similarity with the N- and C-terminal regions of SurA (A, 25.2% identity) and TF (B, 19.9% identity), respectively. The sequence alignments were generated with CLUSTALW2 [63]. Gray shaded regions indicate the regions of high similarity that were initially identified with LALIGN [64] (31.1% (A) and 24.1% (B) identity, respectively). Identical amino acid residues are indicated by asterisks; conserved and semi-conserved

residues are marked with colons and dots, respectively. (C-E) I-BET-762 Three-dimensional homology modeling suggests structural similarity of the N-terminal region of PpiD with the chaperone modules of SurA and TF. All structures were visualized in PyMol and are depicted in ribbon representation. (C) Comparative model structure of the N-terminal region of

PpiD (red colored) and the N-Ct chaperone module of SurA (blue colored) based on the sequence alignment shown in (A). The model was generated in the Swiss-Model workspace [65] using the structure coordinates of SurA (PDB 1m5y; [42]) as a template. Helices of the N-terminal region of SurA are numbered. A region of PpiD that corresponds to the C-terminal Glutamate dehydrogenase helix (“”C helix”") of SurA has not yet been identified. (D) Model structure of the N-terminal region of PpiD generated by the automatic program 3D-JIGSAW [66]. (E) Fold of the C-terminal chaperone domain of TF (PDB code 1w26; [41]). The region that shares similarity with PpiD is highlighted in red (corresponding to the gray shaded sequence in (B)). (PDF 257 KB) Additional file 2: Complementation of the growth defect of ppiD skp surA cells by wild-type PpiD and its PPIase domain mutants. Growth of the SurA-depletion strain P Llac-O1 -surA Δskp ppiD::kan (SB44961) carrying the empty vector pASK75 or plasmids encoding wild-type proteins and variants of SurA, Skp, and PpiD, respectively.

Molecular techniques and sequencing Plasmids pILL788, pILL791, pILL792, pILL793, pILL794, pILL795, pILL2328 correspond to H. pylori ssrA WT , ssrA DD , ssrA resume , ssrA wobble , ssrA smpB , ssrA STOP genes cloned into the E. coli/H. pylori shuttle vector pILL2150 [24], respectively. SsrA mutagenesis has been described in [10]. The H. pylori ssrA gene see more amplified by PCR with primers H367 (5′-CGGGATCCCTCACCTGTTCTTTCTGA-3′) and H368 (5′-GGGGTACCCGGATCCTT AATCGAATAAAAATCAGG-3′) was cloned into the pEXT21 low copy number vector (1-3 copies per cell) [25] using BamHI/KpnI

restriction sites (Table 1). The resulting plasmid was designated pILL2318. The E. coli ssrA gene amplified by PCR with primers H365 5′-CTATCCCGGCGC TGGGTAACATCGGG-3, and H366 5′-GCTTTTCGTTGGGCCTATCAATGGGCC-3′ was cloned into pILL2150, to generate pILL2334. The H. pylori smpB

gene amplified by PCR with primers H225 (5′-GGACTAGTAGGAAGAGAATAATGAAACTCATTGCCAG CAAC-3′) and H236 (5′-CGGGGTACCTTATCCTTTAAAGTGGTGTTTTAAATCAGC-3′), was cloned into pILL2150 [24] using SpeI/KpnI restriction sites to generate pILL786. Test of λimmP22 propagation in E. coli The efficiency of plating (EOP) strains was determined by plating tenfold serial dilution of phage λimm P22 on top agar mixed with 100 μl E. coli overnight liquid culture in LB with 0.4% maltose and 10 mM MgSO4. The number of CFU·ml-1 was calculated for each E. coli strain. The EOP is the ratio between the titer of phage on a bacterial lawn of the indicated strain (Table YAP-TEAD Inhibitor 1 supplier 3) and that of the wild type strain. Western blot Western blot to detect SmpB proteins was performed with E. coli whole cell sonicates prepared as in [26]. Protein Immune system concentrations were measured with Bradford assay (Bio-Rad). Twenty μg of crude extracts were separated by 15% SDS-PAGE and blotted on a polyvinylidene difluororide membrane (PVDF, Millipore). Hp-SmpB and Ec-SpmB were detected

with rabbit polyclonal antibody raised against Ec-SmpB (a generous gift of B. Felden). Binding of the IgG anti-rabbit coupled peroxydase antibody (Amersham) was revealed with the ECL Plus reagent (Pierce). RNA extraction, riboprobe synthesis and AZD0530 northern blot RNAs were extracted using the phenol-chloroform method as described in [27]. An E. coli 5S rRNA riboprobe was synthesized using both primers H357 (5-GCCTGGCGGCAGTAGCG CG GTGG-3′) and H358 (5′-CTAATACGACTCACTATAGGGAGAGCCTGGCAGTTCCC TACTCTCGC-3′). Riboprobes synthesis for H. pylori SsrA was as in [10]. The ladder used corresponds to pBR322 vector digested by MspI and labeled at the 5′end with γ 32P ATP. Intensities of the bands were determined with Quantity One Software (Bio-Rad). The northern blot procedure was as described in [10]. Acknowledgements The authors thank A. Labigne for her support. We also want to thank B. Felden for the gift of anti-EcSmpB antibodies and for constructive comments. We are grateful to J. Collier and P. Bouloc for the gift of E. coli strains MG1655ΔssrA and ΔsmpB and to H. Neil, K. Zemam and C.

Still, S63845 supplier establishing bowel continuity may need to be delayed in patients who are unable to tolerate a lengthy procedure or have inadequate capacity for tissue healing[38]. Specific Surgical Pathologies Appendicitis Acute appendicitis is the most common intra-abdominal surgical emergency[19]. Lifetime risk is approximately 7-9%[39]. Currently, imaging is recommended for all patients suspected of having appendicitis except men under

40 years of age[40]. Generally, CT scan is the accepted imaging modality, however, ultrasound may have a role in women at risk for other pelvic pathologies, in pregnancy and in children[41]. The sensitivity and specificity of CT scan in the diagnosis of acute appendicitis are 87-100% and 91-98%, respectively[42, 43]. Ultrasound is very user PCI-34051 dependent, and results can be affected by patient selleck compound body habitus, however overall sensitivity is 76-96% and specificity is 91-100%[44]. Ultrasound, with its decreased cost, lack of ionizing radiation and ability to assess ovarian pathology, has been the preferred

initial imaging modality in children[45–47]. However, CT should be used in children when the initial ultrasound is negative or non-diagnostic and there is a high clinical suspicion for appendicitis[45, 48]. Ultrasound is also the initial imaging procedure of choice in pregnant women, however, the appendix is visualized only 13-50% of the time. Magnetic resonance imaging (MRI) is an emerging imaging modality for cases of appendicitis in pregnancy with non-visualization of the appendix on ultrasound. Its sensitivity and specificity are 100% and 93.6%, respectively[49]. Though acute appendicitis is a very common entity, its management PRKD3 still contains areas of controversy including the role of laparoscopy, and the emerging role of medical management. These decisions can be complicated by the presence of an abscess or phlegmon. Surgical management of acute appendicitis has been the gold standard of treatment for decades. However, many groups have proposed that in select

patients, acute uncomplicated appendicitis can be treated with antibiotics alone. Initial success rates for conservative management of acute appendicitis range from 88-95%; however, recurrence is common, occurring in up to 35% of cases[50]. Both laparoscopic and open appendectomy are safe and effective. In large reviews, laparoscopic appendectomy has been associated with fewer surgical site infections, less pain, shorter hospital stays, and more rapid return to normal activity[51]. Common disadvantages found include increased cost and longer operative times[52, 53]. Additionally, laparoscopy has been associated with increased risk of intra-abdominal abscess formation, especially in the presence of perforation or gangrene. In these cases, open surgery may be preferred[54].

The isogenicity of the variants was previously OSI-906 ic50 confirmed by amplified fragment length polymorphism [13]. The variants

had the s1a/m2 vacA genotype and were cagA positive displaying an ABC EPIYA genotype [16, 80]. The presense of the cagα, cagβ, cagE, cagL, cagM, cagX and cagY genes indicated that the variants harboured an intact cag pathogenicity island (cagPAI) and were capable of CagA translocation (unpublished data). Both variants displayed a truncated LPS. The bacteria were cultured on blood agar plates under microaerobic conditions at 37°C for 48 h. After cultivation, the bacteria were harvested and suspended in phosphate buffered saline (PBS). Bacterial concentrations were estimated by measuring OD600. Aliquots of the OMPLA+ and OMPLA- bacterial suspensions were transferred to separate cell culture flasks at appropriate concentrations. Dilutions of the suspensions were also plated Pexidartinib manufacturer onto blood agar plates. After 5 days of microaerobic incubation, the colonies were counted and inspected for any OMPLA phase shifts. AGS cell line and inoculation of cell cultures The gastric epithelial

cell line AGS (American Type Culture Collection no: CRL 1739) was grown on RPMI supplemented with 2 mM L-glutamine and 10% foetal calf serum at 37°C in a CO2 incubator at a gas composition of 5% CO2 and 20% O2. When cells grew to a confluent monolayer of approximately 5,1 × 106 cells/flask (60%) the medium was changed to RPMI supplemented with 2 mM L-glutamine only. After an equilibration period of about 30 min, bacteria in PBS were added. To study AGS cell gene expression during the first 24 h, the cells were co-cultured with the H. pylori at a multiplicity of infection (MOI) of 300:1. The two phase variants (OMPLA+ and OMPLA-) were assigned to separate co-cultures, to allow the investigation of the whole genome response to H. pylori

infection per se, and also to study possible differences in the response to the OMPLA+ and OMPLA- variants. Co-cultured cells were incubated for 30 min, 1, 3, 6, 12 and 24 h, before RNA was stabilized by RNAlater (Applied Biosystems, United States), and the cells were harvested. GNE-0877 To ensure that the obtained gene response was adequate, a dose-response experiment was performed, adding bacteria to AGS cells at a MOI of 15:1, 150:1, 300:1, 600:1, 900:1 and 1200:1. Cells were co-incubated for 3 h, before being immersed in RNAlater LY2835219 order followed by harvesting of the cells. Non-infected AGS cells served as a negative control. Both the time-course and the dose-response experiments were carried out in three cell culture replicates and independently performed twice on separate days. Microscopy and immunofluorescent staining Briefly, the bacteria were added to AGS cells grown on glass coverslips at a MOI of 300:1. The cells were co-incubated for 3 and 6 h and then fixed by 4% formalin.

Details of each region are shown. Note that regions 1 and 4 are Xcc exclusive regions. Being exclusive to Xcc, regions 1 and 4 deserve special attention (Fig. 5). The XAC3263, XAC3285 and XAC3294 ORFs, which encode hypothetical proteins of unknown roles and that showed different expression patterns under the conditions mentioned above, are in region 4. This region is found

in the ORF XAC3260 (plasmid mobilization protein) and extends until XAC3298 (one integrase downstream of a tRNA Gly ), totaling 37.546 kb. In terms of composition, this region has mainly hypothetical ORFs. The encoded product of one of these ORFs (XAC3266) interacts with the protein VirD4, a gene classically correlated Mdivi1 datasheet with the type IV secretion system [51]. It is important to emphasize that upstream of this region there are ORFs that encode a virulence regulator (xrvA) (XAC3256), transposases (XAC3247) and regulated www.selleckchem.com/products/s63845.html component colSR (XAC3249/50). Most curious is the ORF XAC3245, which PCI-34051 in vitro encodes an rhsD protein, and the respective mutants also show massive reduction of the necrosis phenotype (mutants 14G01 and 14G12), which also was

upstream of region 4 (Fig. 5). In addition, for ORFs XAC3263, XAC3285 and XAC3294, no classically described domain was found in the probable proteins encoded by these hypothetical ORFs and an analysis by Psort [39] revealed that they are cytoplasmic proteins

and, in a similar the manner, no clusters of orthologous groups (COGs) of proteins [52] were found, demonstrating that there is no similarity with any other sequences. In a different way, region 1 also calls attention by containing 5 transposases, alternating with hypothetical ORFs (Fig. 5). Among ORFs with functions previously predicted by genome annotations, there is ORF XAC1927, which encodes an Fe-S oxidoreductase that has been knocked out, and another that encodes a hemolysin related protein (XAC1918). For this ORF, XAC1918, it has also been proven experimentally that its product is connected to the virD4 product [51]. Related to the structural aspect, this region, besides having abnormal variations in the constitution of its nucleotides, is located between two major conserved gene clusters related to flagellum biosynthesis and regulation. In other organisms, including some Xanthomonas, these genes are concatenated, evidence that reinforces the hypothesis that this region was acquired by a lateral transfer process. Because of all of these peculiarities, these five regions qualify as strong candidates for classification as probable lateral transfer islands and, in this particular case, as probable pathogeniCity islands, as they present many of the typical characteristics found in these regions [6].

Only one subject dropped out after the initial baseline. At the completion of the experimental trial, six subjects correctly identified the order of ED vs. placebo, four did not, and five were not sure. Figure 1 Respiratory exchange ratio vs. exercise intensity as a percentage of ventilatory threshold (% of VT) for GSK872 cell line energy drink and placebo conditions. Values are mean ± standard deviation. Only 30% of VT intensity was different from experimental vs. placebo (*p < 0.046). Discussion This was

the first study to investigate preexercise ingestion of the ED Monster in relation to ride TTE and cardiovascular parameters. Cardiovascular parameters at rest did show an increase in HR after consuming the ED, but there were no changes in any HRV parameters. Ride TTE during cycle

ergometery testing, peak RPE, and peak HR during exercise were not different between the two conditions. The RER measurements during each intensity were not different between the two conditions, Torin 1 research buy except for the RER at 30% of VT where the placebo condition was lower. Exercise effects The main finding in this study is consistent with data by Candow et al. [14] who conducted a high-intensity run TTE study in young adults (VO2max of 45.5 ± 6.3 ml • kg–1 • min–1) using a double-blind, crossover, repeated-measures method. They showed no increase in run time or change in RPE with the energy drink Red Bull given preexercise. However, CYC202 concentration Ivy et al. [10] did see an improvement with preexercise Red Bull. Their study also used

a double-blind, randomized, crossover design, but was conducted in athletes with a higher VO2max (54.9 ± 2.3 ml • kg–1 • min–1) and employed a time trial format. Kazemi et al. [32] demonstrated that Phantom and Dragon energy drinks also significantly increased Paclitaxel clinical trial TTE vs. placebo by 9.3% and 6.5% respectively during a Bruce treadmill test. Caffeine One reason for the lack of increased ride time was possibly the lower dose of caffeine standardized at 2 mg · kgBM-1. The recent International Society of Sports Nutrition (ISSN) position stand on energy drinks [33] concluded that although they contain a number of nutrients, the primary ergogenic nutrients appear to be carbohydrate and/or caffeine. The exact mechanism of how caffeine works is still debated, but it is believed to primarily function by acting as an adenosine receptor antagonist, increasing release of free fatty acids, and increasing calcium release and uptake [34]. The track record of positive effects of caffeine is quite good and most studies showed an improvement in exercise capacity in the range of 3–13 mg · kgBM-1[9, 33, 35–40], although Cox et al. [41] did show a decreased time during a time trial performance undertaken at the end of a prolonged cycling bout with a low dose at approximately 1.5 mg · kgBM-1. Denadai, et al. [39] used a dose of around 3 mg · kgBM-1 and showed that in untrained subjects who exercised below their anaerobic threshold, caffeine increased ride TTE and reduced perceived exertion.

Persoonia 14:233–235 Bataille F (1910) Flore monographique des Hygrophores. Mém Soc ému Doubs, sér 8(4):132–189 Beisenherz (2002) Zur ökologie und taxonomie der saftlinge und ellerlinge (Hygrocybe, Agaricales). Regensburger Mykologische Schriften 10:3–65 Benton MJ (2010) New take on the Red queen. Nature 463:306–307PubMed Bergelin K (2012) Kromvaxskivling (Hygrocybe

vitellina) funnen i Sverige. Svensk Myko Tidisdrift 33:2–8 Bigelow HE (1970) Omphalina in North America. Mycologia 62:1–32 Bigelow HE (1982) Species described in Clitocybe by H. selleckchem Peck and W.A. Murrill. Sydowia 35:37–74 Bigelow HE, Smith AH (1973) Cantharocybe, a new genus of Agaricales. Mycologia 65:485–488 Binder M, Larsson K-H, Matheny PB, Hibbett DS (2010) Amylocorticiales ord. nov. And jaapiales ord. nov.: early diverging clades of agaricomycetidae were dominated by corticioid forms. Mycologia 102:865–880PubMed Boertmann D (1990) The identity of Hygrocybe vitellina and related species. Nord J Bot 10:311–317 Boertmann D (1995) The genus Hygrocybe. Fungi of Northern Europe v I, 1st edn. Danish Mycological Society, Greve Boertmann D (2010) The genus Hygrocybe. Fungi of Northern Europe v I,

2nd edn. Danish Mycological Society, learn more Denmark Boertmann D (2012) MM-102 Update on Hygrocybe nitida. Omphalina 3(1):12–13 Bon M (1976) Novetates. Docums Mycol 24(6):41–46 Bon M (1985) [1984] Le genre Cuphophyllus (Donk) st. nov. Docums Mycol 14:9–12

Bon M (1989) Nouveaux taxons (Hygrophoraceae). Docums Mycol 75:55–56 Bon M (1990) Flore mycologique d’Europe 1. Les Hygrophores. Docums Mycol Memoire hors série 1 Bon M (1991) Novitates. Docums Mycol 81:55–56 Bory de St. Vincent JBGM (1797) Mèmoires sur les genres conferva et byssus, du Chevaller C. Linnè. 1–58 Brébisson (1839) Botrydina Bréb. Mém Soc Acad Agric Industr Instruct Arrond Falaise :36 Bresinsky A (2008) Belträge zu einer Mykoflora Deutschlands (2): Die Gattungen Hydropus bis Hypsizygus mit Angaben zur Ökologie und Verbreitung der Arten. Regensburger Mykol Schriften 15:1–304 Bresinsky A, Kronawitter I (1986) Zur Kenntis der Hygrocybenpigmente (A contribution to the knowledge of the pigments of Hygrocybe). Dichloromethane dehalogenase Zeit Mykol 52:321–334 Brock PM, Döring H, Bidartondo MI (2009) New Phytol 181:719–724PubMed Brummitt RK (1996a) In defense of paraphyletic taxa. In: van der Maeson LJG, van der Burgt XM, Van Medebach De Rooy JM (eds) The biodiversity of African plants. Klewar Academic Publishers, Dordrecht, pp 371–384 Brummitt RK (1996b) Quite happy with the present code, thank you. In: Reveal JL (ed) Biological nomenclature in the 21st century, proceedings of a mini-symposium at the Univ. Maryland 4 Nov 1996. http://​www.​plantsystematics​.​org/​reveal/​pbio/​nomcl/​brum.​html. Accessed 12 Nov 2010 Bruns T, Shefferson RP (2004) Evolutionary studies of mycorrhizal fungi: milestones and future directions.

Tissue between perithecia hyphal. Stroma interior below perithecia formed of RO4929097 nmr degenerating, large-celled hyphae. Part-ascospores monomorphic, subglobose, distal part (2.7–)3.0–3.5(−3.7) × (2.2–)2.7–3.5 μm, proximal part (2.2–)2.7–3.5(−2.2) × (2.5–)3.0–3.2(−3.5) μm, finely spinulose, hyaline. Asci

cylindrical, (43–)51–63– (67) × (3.0–)3.5–4.5(−4.7) μm, apex Selleck SGC-CBP30 thickened and with a ring. Etymology: named in honor of G. Gilles, French entrepreneur and collector of tropical Hypocreales. Habitat: bark. Known distribution: known only from the type locality. Holotype: France, Isle de la Réunion, Salazie, on dead wood, 11 March 2000, G. Gilles comm F. Candoussau 690 (BPI 882294, and a dried culture ex ascospores of Hypocrea sp. BPI 842330; ex-type culture CBS 130435 = G.J.S. 00–72). Sequences: tef1 = JN175583, cal1 GSK2126458 = JN175409, chi18-5 = JN175468, rpb2 = JN175527. Comments: In this species there is a tendency for phialides to be held in divergent whorls. The dark brown, somewhat peltate stromata with an ostiolar area that is green in lactic acid and the subglobose Part-ascospores strongly suggest H. jecorina, the teleomorph of the pantropical species T. reesei. Trichoderma gillesii

belongs in a clade with T. aethiopicum, T. konilangbra, and T. sinense. The closest relative (Druzhinina et al. 2012) of T. gillesii is T. sinense, which is known only from Taiwan and which has subglobose conidia. Trichoderma gillesii has the most narrow conidia in the clade. For a further discussion of members of this clade see T. flagellatum. 9. Trichoderma gracile Samuels et Szakacs, sp. nov. Figs. 2g, h and 11. Fig. 11 Trichoderma gracile. a, b. Pustules. c–j. Conidiophores (Arrows in e, j show intercalary phialides). k Conidia. l Chlamydospores. All from SNA. All from G.J.S. 10–263. Scale bars: a = 1 mm, b = 0.5 mm; c–h, l = 20 μm; i–k = 10 μm MycoBank MB 563906 Trichodermati longibrachiato Rifai simile sed ob incrementum tardius, radium coloniae < 60 mm in agaro dicto PDA

post 72 h ad temperaturam 35°C distinguendum. Holotypus: BPI 882295 Teleomorph: none known Optimum temperature for growth on PDA and SNA 25–30°C; after 96 h in darkness with intermittent light colony on PDA completely or nearly completely filling a 9-cm-diam mafosfamide Petri plate, somewhat slower at 25°C; within 96 h in darkness with intermittent light completely filling a 9-cm-diam Petri plate, somewhat slower at 30°C. A yellow diffusing pigment forming on PDA within 48 h at 25–35°C; conidia only appearing in colonies incubated at 35°C, on PDA after 96 h in colonies incubated in darkness (not under fluorescent light), on SNA in colonies incubated in darkness or under light. Conidial production sparse. Pustules formed on SNA gray green, 0.5–1 mm diam, hemispherical or pulvinate, with stiff, erect, terminally fertile projecting conidiophores. Individual conidiophores not visible within pustules.

15% higher than that of flat surfaces (92.74%). In Veliparib supplier particular, this high transmittance is sustained over the UV-vis-NIR ranges (i.e., T ave@300–1,800 nm = 96.64%). These broadband AR characteristics afford a possibility this website of the use of this AR glass as a substrate or a cover glass for photovoltaic applications. In case of glass with a 10-min etching, the antireflective property seems to increase from 600 to 900 nm while the broadband AR property is degraded. One of the possible causes on this detrimental change is the reduced density of grassy nanostructures compared to

that of glass with a 7-min etching. It is needed to conduct more systematic characterization/analysis to figure out the effect of size, density, and shape of randomly distributed nanostructures on optical properties. Figure 4 SEM morphologies of the grassy surfaces fabricated by self-masked etch. SEM morphologies of the grassy surfaces fabricated by the self-masked etch process of glass substrates with etch times of (A) 1, (B) 4, (C) 7, and (D) 10 min, respectively. Scale bar, 1 μm. Figure 5 Transmittance of UV to NIR light and pictures of flat glass and AR glass. (A) Transmittance of UV to NIR light through a flat reference glass (black solid line) and AR glasses with four different grassy surfaces on both sides. Inset: cross-section SEM image of grassy nanostructures selleck chemical with 7 min etch time. (B) Picture of a flat glass (left) and an AR glass (right) with bright illumination

light. (C) Wetting behavior of the corresponding samples of (B). Inset: contact angle measurement results. The reflectance difference between the glasses with flat and grassy surface is revealed visually in Figure  5B. An intense light reflection from the flat glass is observed and as a result, reflections occurring at both sides of the glass make the words

difficult to read. The grassy surface showed improved readability due to the reduced reflection. In addition to the AR property, the wetting property is also affected by both the structured surface [18] and the oxygen plasma treatment. To confirm the antifogging performance, the SWS-integrated glass and the bare glass were exposed to steam at the same time. Figure  5C shows the Rho antifogging behavior of the glasses with flat and grassy surface. The water droplets beaded up on the flat surface of the bare glass substrate and the bead-like water droplets caused light scattering, which degrades the readability of the words. However, the water droplets on the roughened surface of the SWS-integrated glass evenly spread over the whole surface, and the hydrophilic glass still remained transparent, and the words below it were clearly readable. Water contact angle measurement results also support this hydrophilic effect. The contact angles of glass with and without grassy surface were 12.5° and 71.5°, respectively. The surface energy of structured glass was 87.8 mN/m, which is a higher value than that of bare glass (39.0 mN/m).

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for high-purity straight and helical carbon nanofibers. ACS Nano 2012, 6:8611–8619.CrossRef 6. Jian X, Jiang M, Zhou Z, Yang M, Lu J, Hu S, Wang Y, Hui D: Preparation of high purity helical carbon nanofibers by the catalytic decomposition of acetylene and their growth mechanism. Carbon 2010, 48:4535–4541.CrossRef 7. Jayatissa A, Guo K: Carbon helixes produced by hot filament assisted chemical vapor deposition. J Mater Sci Mater Electron 2010, 21:509–513.CrossRef 8. Mukhopadhyay K, Porwal D, Ram K, Rao KUB: Synthesis of carbon coiled micro/nano-structures in the

absence of sulphurous promoter. Proteases inhibitor J Mater Sci 2007, 42:379–383.CrossRef 9. Ding Q, Song X, Yao X, Qi X, Au C-T, Zhong W, Du Y: Large-scale and controllable synthesis of metal-free nitrogen-doped carbon nanofibers and nanocoils over water-soluble Na 2 CO 3 . Nanoscale Res Lett 2013, 8:545.CrossRef 10. Yu L, Qin Y, Sui L, Zhang Q, Cui Z: Two opposite growth modes of carbon nanofibers prepared by catalytic decomposition of acetylene at low temperature. J Mater Sci 2008, 43:883–886.CrossRef 11. Dong L, Yu L, Cui Z, Dong H, Ercius P, Song C, Duden T: Direct imaging of copper catalyst migration inside helical carbon nanofibers. Nanotechnology 2012, 23:035702.CrossRef 12. Chen X, Takeuchi K, Yang S, Motojima S: Morphology and growth mechanism of single-helix spring-like carbon nanocoils with laces prepared Silibinin using Ni/molecular sieve (Fe) catalyst. J Mater Sci 2006, 41:2351–2357.CrossRef 13. ARN-509 in vitro In-Hwang W, Kuzuya T, Iwanaga H, Motojima S: Oxidation characteristics of the graphite micro-coils, and growth mechanism of the carbon coils. J Mater Sci 2001, 36:971–978.CrossRef 14. Shang Y, He X, Li Y, Zhang L, Li Z, Ji C, Shi E, Li P, Zhu K, Peng Q, Wang C, Zhang X, Wang R, Wei J, Wang K, Zhu H, Wu D, Cao A: Super-stretchable

spring-like carbon nanotube ropes. Adv Mater 2012, 24:2896–2900.CrossRef 15. Raghubanshi H, Hudson MSL, Srivastava ON: Synthesis of helical carbon nanofibres and its application in hydrogen desorption. Int J Hydrogen Energ 2011, 36:4482–4490.CrossRef 16. Nitze F, Mazurkiewicz M, Malolepszy A, Mikolajczuk A, Kędzierzawski P, Tai C-W, Hu G, Kurzydłowski KJ, Stobinski L, Borodzinski A, Wågberg T: Synthesis of palladium nanoparticles decorated helical carbon nanofiber as highly active anodic catalyst for direct formic acid fuel cells. Electrochim Acta 2012, 63:323–328.CrossRef 17. Lau K, Lu M, Hui D: Coiled carbon nanotubes: synthesis and their potential applications in advanced composite structures. Compos Part B 2006, 37:437–448.CrossRef 18.