Despite the higher probability of errors in gene assignments char

Despite the higher probability of errors in gene assignments characterizing draft genomes, we decided to include them to expand the scope of our genomic comparison. A whole genome scanning was performed using a PWM derived from the region comprising several experimentally validated VirR binding sites [7, 8]. A new PWM was generated from the targets identified in the first scanning by using 30 motifs found in the promoters of genes that are orthologous to known targets and then used for a second genome scanning. In this way we avoid the biases that affect the first

matrix, obtained from only a few sequences mainly coming from one check details strain. After our two-step strategy, we collected all genes with a motif scoring more than 0.88, which is the lowest value observed for an experimentally

tested VirR target gene (corresponding to gene CPF_1074, [8]). At this threshold we retained at end 53 occurrences of the VirR motif. Analysis of their location with respect to the start codon of the downstream coding sequence revealed thet most of them are at around 100 bp from the beginning of the gene (figure 2). The larger distance observed for some of the motifs may be due to longer 5′ untranslated regions or may account for some different level of regulation for those genes. Cell Cycle inhibitor The list of genes putatively regulated by VirR was splitted in three different groups after clustering similar sequences (see Methods), by defining the: i) conserved VirR regulon as formed by chromosomal genes retrieved in at least two different genomes; ii) the accessory regulon with chromosomal genes present in a single strain; iii) the mobile regulon, including Ceramide glucosyltransferase genes found on plasmids. Figure 2 Distribution of distances from gene. The distance of the motifs with respect to the translation start site (selleck screening library x-axis) is shown. Motifs are grouped by homology of the downstream gene (cluster identifier is on the y-axis). Most of the targets are located in the first 200 nt from the start of the gene, but some of them (and notably several corresponding to characterized ones) are

located at larger distances. Red circles correspond to orthologous groups from Table 2. The conserved VirR regulon The conserved regulon (Table 2), appeared to contain all known target genes [7, 8] with the exception of CPR 0761 and virT. The former can be identified in the genome of strain SM101 only, while the latter has been found in strain 13 and ATCC3626; in both cases we were able to identify a VirR binding motif in their promoter (Table 3). Table 2 Conserved VirR regulon Product Genomes REF   ATCC13124 Str.13 SM101 F4969† JGS1721† JGS1495† JGS1987† ATCC3626†   α -clostripain CPF_0840 CPE0846 CPR_0833 AC5_0918 CJD_0991 CPC_0878 AC3_1028 AC1_0991 [7] ccp 1.52 1.52 1.52 1.52 1.52 1.52 1.52 1.52   Reg.

As all CEACAM-binding bacteria greatly differ in their pathogenic

As all CEACAM-binding bacteria greatly differ in their pathogenic potential, but share the same ecological niche, it is highly likely that CEACAM-binding promotes colonization of the mucosa. Indeed, in vitro experiments have suggested that CEACAM-binding is not only a means to firmly attach to the host cell surface, but also suppresses the detachment of infected epithelial cells [16]. CEACAM-targeting bacterial adhesins might Selleckchem ��-Nicotinamide therefore represent colonization factors that promote the ability of bacteria to establish a firm foothold in their ecological niche. Whether this specialization is also a determinant of the host range of these bacterial pathogens is not known. Though bacterial species

expressing CEACAM-binding adhesive proteins S3I-201 clinical trial are in most cases human-specific, and have no other

natural host organism, it has not been experimentally tested whether their adhesins selectively recognize human CEACAMs or can Selleck JQ1 also bind to orthologues from other mammalian species. In the present study, we analysed the binding of CEACAM1 orthologues from several mammals to bacterial pathogens with distinct adhesive proteins. In particular, we tested Opa protein-expressing N. gonorrhoeae and N. meningitidis as well as UspA1-expressing M. catarrhalis for their ability to recognize CEACAM1 homologues of human, murine, canine or bovine origin. Biochemical binding studies clearly demonstrate that these bacteria selectively interact with human CEACAM1. Furthermore, analyses of bacterial internalization show that the observed amino acid changes in the amino-terminal domain of mammalian CEACAM1 ROS1 orthologues have clear-cut functional consequences. Accordingly, our data not only demonstrate that bacterial adhesins have co-evolved with the receptor molecules of their mammalian host, but also support the view that the diversification of CEACAMs in mammalian lineages is a pathogen-driven process. Methods Amino acid sequence alignment For the amino acid sequence alignment of the N-terminal domains of CEACAM1 following sequences were used: human CEACAM1 (hCEA1,

NM_001712), murine CEACAM1a (mCEA1, BC016891), canine CEACAM1 (cCEA1, NM_001097557.1), bovine CEACAM1 (bCEA1, AY345129), bovine CEACAM1 isoform b (bCEA1b, AY487418). The alignment was performed using CLUSTALW. Cell culture and transfection The human embryonic kidney cell line 293T (293 cells) was cultured in Dulbecco’s modified Eagle’s medium (DMEM) containing 10% calf serum at 37°C in 5% CO2 and subcultured every second to third day. 293T cells were transfected by calcium-phosphate coprecipitation using 5 – 8 μg of plasmid DNA for each 10 cm culture dish. Bacteria and infection Opa52-expressing (OpaCEA), non-piliated N. gonorrhoeae MS11-B2.1 (strain N309), and non-piliated, non-opaque gonococci MS11-B2.1 (strain N302) were kindly provided by T.F. Meyer (Max-Planck Institut für Infektionsbiologie, Berlin, Germany) and were cultured as described previously [17].

The antibiotics tested were amikacin, aztreonam, cefepime, ceftaz

The antibiotics tested were amikacin, aztreonam, cefepime, ceftazidime, ciprofloxacin, colistin, gentamicin, fosfomycin, imipenem, levofloxacin, meropenem, piperacillin-tazobactam and tobramycin. For the isolates resistant to imipenem and/or meropenem, the determination of metallo-β-lactamases (MBLs) using E-test strips with Imipenem-EDTA was RG7112 performed (bioMérieux, Marcy d’Etoile, France). The classification of multiresistance was performed according to Magiorakos et al. [11].

The isolates were classified according to the resistance pattern as multidrug resistant (MDR, non-susceptible to at least one agent in three or more antimicrobial categories), extensively drug resistant (XDR, non-susceptible to at least one agent in all but two or fewer antimicrobial categories; i.e. bacterial isolates remain susceptible to only one or two categories), pandrug-resistant (PDR, non-susceptible Vistusertib purchase to all agents in all antimicrobial

categories), and non-multidrug resistant (non-MDR). DNA extraction: PCR amplification and DNA sequencing Bacterial genomic DNA for PCR amplification was obtained as previously described [12]. The housekeeping genes acsA, aroE, guaA, mutL, nuoD, ppsA and trpE were amplified and sequenced for the 56 isolates using the primers described previously [8]. The PCR conditions have been slightly modified. The reactions were performed using an Eppendorf thermocycler, with an initial denaturation step at 96°C 2 min, followed by 35 cycles of denaturation at 96°C for 1 min for all of Selleckchem NVP-BSK805 the genes, a primer annealing temperature, depending on the gene (55–58°C for aroE and nuoD; 58°C for acsA and guaA; and 58–60°C for mutL, ppsA and trpE), for 1 min and a primer extension at 72°C for 1 min for all of the genes, with

the exception of aroE (1.5 min). A final elongation step was performed Isoconazole at 72°C for 10 min. The PCR amplification reactions were performed as previously described [12]. The amplified products were purified with Multiscreen HTS PCR 96-well filter plates (Millipore). Sequence reactions were carried out using the ABI Prism BigDye Terminator version 3.1 and the sequences were read with an automatic sequence analyser (3130 genetic analyzer; Applied Biosystems). Sequence analysis and allele and nucleotide diversity Sequence analysis was performed as described previously [12]. Individual phylogenetic trees and concatenated analyses of the sequenced gene fragments were constructed [12]. The allelic and nucleotide diversities were calculated from the gene sequences using the DnaSP package, version 3.51 [13]. For each isolate, the combination of alleles obtained at each locus defined its allelic profile or sequence type (ST). The ST and allele assignment were performed at the P. aeruginosa MLST website (http://​pubmlst.​org/​paeruginosa/​). If a sequence did not match with an existing locus in the database, it was designated as a “new” allele.

TssM is expressed and secreted inside cells following infection w

TssM is expressed and secreted inside cells following infection with B. mallei [29], however, secretion occurs independently SYN-117 in vitro of T3SS3 and T6SS1 [31]. BsaN was also found to activate expression of a mTOR inhibitor review putative non-ribosomal peptide synthase (NRPS)/polyketide synthase (PKS) biosynthesis locus. The diversity of polyketides, PKSs and NRPS/PKS hybrid systems was recently reviewed by Hertweck [37]. The B. pseudomallei locus is

similar in gene content to that of a recently described plasmid encoded NRPS/PKS system in the marine bacterium Alteromonas macleodii, which was suggested to produce a bleomycin-related antibiotic Unlike A. macleodii, the gene encoding the putative bleomycin-family resistance protein (BPSL2883) is not co-localized with the NRPS/PKS gene cluster, although they are similarly regulated by BsaN (Table 1). BsaN is homologous to the Salmonella typhimurium InvF, Shigella flexneri MxiE and Tanespimycin mw the Yersinia enterocholitica YsaB transcriptional regulators [38–40]. All belong to the AraC/XylS family of transcriptional

regulators, which act in complex with a chaperone to activate their respective T3SS genes. The chaperones not only serve as cognate partners to the transcriptional activators but also pair with T3SS translocase proteins, which are secreted into the host membrane to facilitate the injection of effector proteins [41]. We currently, have no understanding of the timed mechanism that frees BicA and allows it to partner with BsaN. The

S. typhimurium chaperone SicA was shown to partition the translocase SipB and SipC, and it is sequestered by SipB [42]. Once apparatus assembly is complete, translocases are secreted and SicA is free to complex and thus activate InvF. The InvF-SicA split feedback regulatory loop, which includes positive autoregulation of invF, is conserved in Y. enterocholitica [40]. 3-mercaptopyruvate sulfurtransferase However, in S. flexneri MxiE-dependent activity is inhibited via sequestration by the T3SS substrate OspD1 when the apparatus is inactive [43]. Only when OspD1 is secreted, can MxiE partner with its chaperone IpgC to activated transcription of effector genes. Regulation by BsaN-BicA is distinct from the previously described systems. The designation of BsaN-BicA as a dual-function regulatory protein complex is illustrated by its role in activating T3SS effector and accessory genes while repressing the system’s structural and secretion components as summarized in Figure 7. BsaN was also found to suppress the transcription of 51 additional genes in the B. pseudomallei genome including those belonging to the fla1 flagellar and chemotaxis locus on chromosome 1 (Figure 1E). Fla1 is the sole flagellar system in Southeast Asian B. pseudomallei strains such as KHW, in contrast to Australian B. pseudomallei isolates which possess a complete second system encoded on chromosome 2 (Fla2) [9,44].

Biochim Biophys Acta 1987, 901:138–146 CrossRef 25 Hirano K: Cha

Biochim Biophys Acta 1987, 901:138–146.CrossRef 25. Hirano K: Change in membrane fluidity of sand dollar egg cortices caused by Ca2+-induced exocytosis: microscopic analysis with fluorescence anisotropy. Dev Growth Differ 1991,33(5):451–458.CrossRef 26. Olofsson CS, Håkansson J, Salehi A, Bengtsson M, Galvanovskis J, www.selleckchem.com/products/qnz-evp4593.html Partridge C, SörhedeWinzell M, Xian X, Eliasson L, Lundquist I, Semb H, Rorsman selleck inhibitor P: Impaired insulin exocytosis in neural cell adhesion molecule−/− mice due to defective reorganization of the submembrane F-actin network. Endocrinology 2009,150(7):3067–3075.CrossRef Competing interests The authors declare that they have no competing interests.

Authors’ contributions QPS and SML carried out the fabrication of samples and the AFM and LSCM measurements and drafted the manuscript. XHL carried out the immunoassays. HYJ performed the molecular genetic studies and participated in the sequence alignment. Selleck HDAC inhibitor JYC, LXZ, and LF initiated, planned, and controlled the research process. All authors read and approved the final manuscript.”
“Background Since flexible electronic system (FES) appeals to be light, convenient, has conformal contingence

with the crooked surface, and excellent interfaces with humans, it ought to be a prospective existing form of electronic product to substitute its clumsy predecessors manufactured and packaged by traditional bulk silicon technology [1, 2]. Up to now, multifarious electronic components, such as integrated circuits (ICs) [3, 4], active matrix organic light-emitting diodes [5], sensors [6], radiofrequency identification antennas [7], and solar cells [8, 9], have been fabricated on flexible Ribonuclease T1 substrates and are delved by many researchers. As we know, among all the components used in ICs, good and reliable memories [10, 11] will maximize the functionality of ICs, and it is also important for the FES. Among all the memories, nonvolatile resistive random access memory (RRAM) is the most promising candidate because of its low power consumption,

high speed, simple structure, and high packaging density, compared with its counterparts such as flash memory and DRAM [12–14]. Currently, oxides, such as STO [15], HfO2[16], NiO [17], Al2O3[18], ZnO [19], and GO [20], have received much interest in resistive switching research. Among the oxides mentioned, HfO2 has been profoundly studied and contains great potentiality to be put into applications. However, the application of HfO2-based RRAM on flexible substrate is still rare. In recent years, atomic layer deposition (ALD) has emerged as a new technique for depositing films, particularly for fabricating oxide films. Owing to its self-limiting mechanism during the process, excellent step coverage and conformal thickness of the film can be achieved [21].

05% Congo Red (w/v) SD1 in vitro samples were prepared by inocul

05% Congo Red (w/v). SD1 in vitro samples were prepared by inoculating a single colony into Luria-Bertani (LB) medium grown to stationary phase at 37°C with agitation. The bacteria were harvested by centrifugation and washed twice with ice-cold PBS (6,000 × g, 15 min) at 4°C. The inoculum for in vivo experiments

was prepared by growing a typical SD1 colony selected from a TSA plate in LB medium overnight. Gnotobiotic piglets used for the animal experiments were delivered by Caesarian section at Tufts University Cummings School of Veterinary Medicine. Of several animals inoculated with SD1, three piglets were chosen for isolation of SD1 bacterial AZD8931 cells from the intestine in this comparative study. One of the piglets inoculated with 1 × 108 SD1 cells developed diarrhea 24 h later and was euthanized 4 d later when the gut contents GW3965 order were collected for bacterial purification. Another piglet inoculated with 5 × 108 SD1 cells developed diarrhea within 18 h and was euthanized 3 d post-inoculation. A third piglet inoculated with 5 × 109 SD1 cells developed diarrhea within 20 h and the

gut contents collected 2 d post-inoculation. SD1 bacterial cells were isolated from the gut contents as described previously [15]. Briefly, the gut contents from cecum and colon were pooled and transferred to sterile histological cups placed on ice, suspended in ice-cold PBS at 4°C and pelleted at 5,000 × g. After resuspension of the pellet in 65% isotonic Barasertib mouse Percoll solution and centrifugation at 14,500 × g, the bacterial layer near the bottom was collected using a 3-5 ml syringe with needle. The bacteria were washed twice with ice-cold PBS at 4°C and processed for proteomic analysis. Lysis of S. dysenteriae cells and trypsin digestion of extracted proteins After the PBS wash steps, bacterial cell pellets from in vitro or in vivo culture conditions were re-suspended in a hypotonic lysis buffer composed of 25 mM Tris-HCl (pH 7.8) with 150 μg/mL lysozyme, 0.05% Triton X-100, 5 mM EDTA, protease inhibitors (1 mM benzamidine and AEBSF) for 30 Morin Hydrate min at

room temperature (RT) with gentle agitation. The samples were then placed at -80°C until further processing. For nucleic acid digestion, bacterial samples suspended in the lysis buffer were thawed and gently agitated for 1 h at RT after the addition of DNase I, RNase and leupeptin (10 μg/mL each) and 20 mM MgCl2. Cell lysates were centrifuged at 16,000 × g for 30 min at 4°C, and the supernatants containing bacterial cell lysate proteins were recovered. Following cell lysis, the extracted bacterial proteins were precipitated in six volumes of ice-cold acetone at -20°C for at least 1 h. Acetone-precipitated proteins were recovered as a pellet after centrifugation at 5,000 × g for 10 min. The protein pellet was resuspended in 0.1 M TAB buffer, pH 8.5, and the total protein concentration measured using the BCA assay. Proteins were denatured in 0.

02; df = 1; p < 0 001 Bryophytes 24 1 (406) 34 4 (323) 5 6 (5)c χ

02; df = 1; p < 0.001 Bryophytes 24.1 (406) 34.4 (323) 5.6 (5)c χ2 = 141.60; df = 2; p < 0.001 Birds (red listed) 12.8 (67) 11.1 (44) 2.0 (1)d χ2 = 5.31; df = 2; p = 0.070 Birds (SPECs)e 43.1 (226) 38.0 (89) 22.0 (11) χ2 = 9.20; df = 2; p = 0.010 aThe functional groups of plants: PI plants listed in policy instruments, CWR crop wild relatives, AP aquatic plants bBased on local red list of vascular plants cBased on national red list of bryophytes dBased on list of birds threatened in Europe e SPEC species of European conservation concern Species of lower extinction risk The group of species placed into lower threat

categories contained ten bird species assessed as declining or depleted (equivalent of near threatened category) at the European

level, and 86 vascular plants. The plant species were HDAC inhibitor classified as being of least concern or near threatened in the local red list (10), and of least concern in the European red list, including 40 CWR, 38 aquatic species, and 2 species listed in PI (with Akt inhibitor several joint species, Online Resource 1). We did not record any bryophytes assigned to the lower threat categories. One bird species (the turtle dove Streptopelia turtur) was assessed as being of data deficient at the national level. Birds of conservation concern Eight of the eleven bird species of unfavorable conservation status were classed as SPEC 3 (9.7 % of breeding pairs) LY3039478 purchase and three as SPEC 2 (3.2 % of breeding pairs). Birds of conservation concern were noted in 95.7 % of study plots. The most numerous species was the Red-backed shrike

(Lanius collurio), which Amobarbital bred in 80 % of field margins, and was one of six dominants (>5 % pairs) in the bird community (Online Resource 1). Significance of vegetation structure The volume of trees and shrubs was positively correlated with species richness in each of the three taxonomic groups and the number of breeding pairs in birds (p < 0.001 in each of the Kendall’s tau correlations, Fig. 2A). The relationship between the volume of trees and shrubs and the number of TCCS was significant only with respect to the number of SPEC birds (Kendall’s tau = 0.246, p = 0.003, N = 70) and marginally significant with respect to the number of pairs of SPECs (Kendall’s tau = 0.154, p = 0.059, N = 70) and number of threatened bryophytes (Kendall’s tau = 0.146, p = 0.073, N = 70). These relationships imply that the increasing complexity of the vegetation structure led to an increase in total species richness, abundance of birds, and richness of SPECs. However, in percentage terms the occurrence of TCCS was nonlinearly related to the volume of trees and shrubs, with highest values recorded in the intermediate volume (Fig. 2B). Calculated separately in the three field margin types, the percentages of threatened vascular plants, bryophytes and birds of conservation concern tended to be higher in the shrubby margins (Table 4), but only the number of breeding pairs was significantly related.

We use flow cytometry to carefully monitor the inflammatory respo

We use flow cytometry to carefully monitor the inflammatory response during the initiation of PanIN formation. Additionally, we show that components of the immune system VRT752271 are significantly involved in acinar cell damage that occurs during a mouse model of pancreatitis. This damage, along with a genetic activation of Kras, leads to the development of preneoplastic lesions and promotes tumor development (Carriere

et al 2009, Morris et al, in revision). Our study also indicates an important role for the inflammatory response in promoting progression of neoplastic lesions to invasive disease. Clark, CE, Hingorani, SR, Mick, R, Combs, C, Tuveson, DA and Vonderheide, RH. Dynamics of the immune reaction to pancreatic cancer from inception to invasion. Cancer Res. 2007 Oct 1;67(19):9518–27. Morris, JM, Cano, DA, Sekine, S, Wang, SC and Hebrok, M. Beta-catenin serves as a molecular switch between acinar regeneration and Kras induced acinar to ductal metaplasia. In revision. Carriere, C, Young, AL, Gunn,

JR, Longnecker, YH25448 supplier DS and Korc M. Acute pancreatitis markedly accelerates pancreatic cancer progression in mice expressing oncogenic Kras. Biochem. Biophys. Res. Commun, 2009 May 8;382(3):561–5. Poster No. 37 Modulation of Telomerase by Scutellaria barbata at Transcriptional Level: An in vitro and in vivo Study Christine MN Yow 1 , Ellie SM Chu1, Stephen CW Sze2 1 Department of selleck inhibitor Health Technoloy & Informatics, The Hong Kong Polytechnic University, Hong Kong, Hong Kong, 2 School of Chinese Medicine, LKS Faculty of Medicine, University of Hong Kong, Hong Kong, Hong Kong Traditional Chinese Medicine (TCM) has long been practiced in China over thousands of years. Currently, TCM medications are gaining much attention from modern pharmaceutical institutes and have been studied systematically. Recent studies illustrated that Scutellaria barbata (SB) is one of the potential herbs exhibiting anti-tumor efficacy on several tumors, such as head and neck carcinoma, lung cancer

and ovarian cancer. Human telomerase reverse transcriptase (hTERT), a human catalytic subunit of telomerase, which highly expressed in over 80% human until cancers, is an indicative marker for treatment efficacy and therapeutic monitoring. In Hong Kong, colorectal cancer ranks the second of the leading cause of cancer death. This study aimed to comparatively study the modulation of hTERT mRNA expression by Scutellaria barbata (SB) at transcriptional level in colorectal cancer cell (HT-29) and the HT-29 immunized BALB/c nude mice models. The efficacy of SB on HT-29 cancer cells was determined by MTT assay; whereas the size of the colon cancer in xenografts was monitored by magnetic resonance interference (MRI) at pre- and post-SB treatment.

Fresh stromata (a

Fresh stromata (a. immature; f, g. eaten by insect larvae). h–k, m–o. Dry stromata (h–k. immature; i. stroma initial with anamorph). l. Hairs on stroma surface. p. Perithecium in section. q. Stroma surface in face view. r. Cortical and subcortical tissue in section. s. Subperithecial tissue in section. t, u. selleck screening library Asci with ascospores. v, w. Ascospores in cotton blue/lactic acid. a, g. WU 29451. b, e, h. WU 29450. c, f, k, l, p–t, v, w. WU 29448. d. WU 29447. i, j. WU 29449. m, o. WU 29446. n. WU 29453. u. WU 29456. Scale bars: a = 0.2 mm. b, e = 2 mm. c, d, f, i, m, o = 0.8 mm. g, j, k,

n = 0.4 mm. h = 1.5 mm. l, r, s = 15 μm. p = 30 μm. q, u = 10 μm. t, v, w = 5 μm Anamorph: Trichoderma rogersonii Samuels, Stud. Mycol. 56: 125 (2006a). Fig. 17 Fig. 17 Cultures and anamorph of Hypocrea rogersonii. a–d. Cultures after 14 days (a. on CMD; b. on PDA; c. on PDA, 30°C; d. on SNA). e. Conidiation shrub (CMD, 7 days). f–h. Conidiophores on growth plates (f, h. CMD, 5 days; g. conidial heads, SNA, 7 days). i–m. Conidiophores (CMD, 5 days). n, o. Phialides (CMD, 5 days). p, q. Chlamydospores (SNA, 30°C, 21 days). r, s. Conidia (CMD, 7 days). a–s. All at 25°C except c, p, q. a–e, g, i–s. CBS 119503. f, h. C.P.K. 2422. Scale bars: a–d = 15 mm. e, f = 50 μm.

g, i = 30 μm. h, k, l = 20 μm. j, m = 15 μm. n, o, q–s = 5 μm. p = 10 μm Stromata SB525334 nmr when fresh 1–8(–20) mm long, to ca 1 mm thick, solitary, gregarious or aggregated, generally in small numbers, thinly effuse, discoid or pulvinate; outline variable. Margin often white when young, first attached, cottony, later concolorous, free, sometimes irregularly crenate. Stroma surface velutinous, smooth or tubercular, typically without ostiolar dots; ostioles invisible or find more appearing as minute, inconspicuous light dots under high magnification. Perithecia entirely immersed, sometimes translucent as dark, indistinct, diffuse Rolziracetam dots. Stromata first white, then yellow, ochre, orange to orange-brown with brown or rust hairs, 6B6–7, 6C7–8, 7CD6–8, 8CD5–6; white, sometimes yellowish inside. Spore deposits white. Stromata when dry 0.5–4(–20) × 0.4–2(–4) mm, 0.15–0.3(–0.4) mm (n = 30) thick,

thinly effuse, discoid or flat pulvinate; outline variable, mostly oblong, angular or lobed; broadly attached. Margin first white or yellowish, cottony, attached, becoming free. Surface smooth, tubercular or wrinkled, velvety or hairy. Ostioles typically invisible, under high magnifications appearing as light or concolorous dots, sometimes slightly projecting to semiglobose; sometimes dark dots (23–)30–54(–63) μm (n = 30) diam visible. Colour when young pale orange with white margin, turning yellow-brown, orange-brown to medium brown 5CD6–8, 6CD7–8, 6E6–8, finally dark orange-brown to reddish brown, dark brown 7–8CF6–8. Spore deposits white. Mature stromata slightly thicker upon rehydration; not changing or turning reversibly slightly darker reddish brown in 3% KOH.

These results qualitatively agree with the theoretical analysis a

These results qualitatively agree with the theoretical analysis and the LLG simulation for the Stoner-Wohlfarth grain. Authors’ information TT is an assistant professor in ISEE, Kyushu University. His research interests include micromagnetics, magnetic recording, and high frequency magnetic devices. SK received a B.S. degree in Electrical Engineering from Kyushu University in 2013. YF received an M.S. degree in ISEE from Kyushu University in 2013. YO received a B.S. degree in

Electrical Engineering from Kyushu University in 2012. KM is a professor in ISEE, Kyushu University. His research interests include magnetic devices. Acknowledgements This research was partially supported by the Storage Research Consortium (SRC) and a Grant-in-Aid for Young Scientists (A) (grant no. 25709029) 2013 from the Ministry of Education, Culture, Sports, Science, #A-1155463 mouse randurls[1|1|,|CHEM1|]# and Technology, Japan. References 1. Rottmayer RE, Batra S, Buechel D, Challener WA, Hohlfeld J, Kubota Y, Li L, Lu B, Mihalcea C, Mountfield K, Pelhos K, Peng

C, Rausch T, Seigler MA, Weller D, Yang X: Heat-assisted magnetic recording. IEEE Trans Magn 2006, 42:2417–2421.CrossRef 2. Zhu JG, Zhu X, Tang Y: Microwave assisted magnetic recording. IEEE Trans Magn 2008, 44:125–131.CrossRef 3. Thirion C, Wernsdorfr W, Mailly D: Switching of magnetization by nonlinear resonance studied in single nanoparticles. Nature Mater 2003, 2:524–527.CrossRef 4. Moriyama T, Cao Sepantronium clinical trial R, Xiao JQ, Lu J, Wang XR, Wen Q, Zhang HW: Microwave-assisted magnetization switching of Ni 80 Fe 20 in magnetic tunnel

junctions. Appl Phys Lett 2007, 90:152503.CrossRef 5. Nozaki Y, Ohta M, Taharazako S, Tateishi K, Yoshimura S, Matsuyama K: Magnetic force microscopy study of microwave-assisted magnetization reversal in submicron-scale ferromagnetic particles. Appl Phys Lett 2007, 91:082510.CrossRef 6. Yoshioka T, Nozaki T, Seki T, Shiraishi M, Shinjo T, Suzuki Y, Uehara Y: Microwave-assisted magnetization reversal in a perpendicularly magnetized film. Appl Phys Express 2010, 3:013002.CrossRef 7. Rivkin K, Ketterson JB: Magnetization reversal in the anisotropy-dominated regime using time-dependent magnetic fields. Appl Phys Lett 2006, 89:252507.CrossRef 8. Nozaki Farnesyltransferase Y, Matsuyama K: Numerical study for ballistic switching of magnetization in single domain particle triggered by a ferromagnetic resonance within a relaxation time limit. J Appl Phys 2006, 100:053911.CrossRef 9. Okamoto S, Kikuchi N, Kitakami O: Magnetization switching behavior with microwave assistance. Appl Phys Lett 2008, 93:102506.CrossRef 10. Scholz W, Batra S: Micromagnetic modeling of ferromagnetic resonance assisted switching. J Appl Phys 2008, 103:07F539.CrossRef 11. Gao KZ, Benakli M: Energy surface model and dynamic switching under alternating field at microwave frequency. Appl Phys Lett 2009, 94:102506.CrossRef 12.