The nuclear protein was incubated for 1 hour at 25°C with biotinylated PCR product bound to streptavidin agarose beads in protein binding buffer (12% (v/v) glycerol, KU55933 order 24 mM HEPEs PH 7.9,

8 mM Tris PH 7.9, 300 mM KCl, 2 mM EDTANa2 0.25 mg/ml poly(dI-dC)). The magnetic beads were washed three times with protein binding buffer and the fractions were eluted with elution buffer (2.0 M NaCl, 20 mM Tris-HCL, pH 8.0, 10%(v/v) glycerol, 0.01%(v/v)Triton X-100, 1.0 mM EDTA, 1 mM dithiothreitol) and were stored at -80°C. 2.5 Transcription factor profiling TranSignal Protein/DNA Microarray I (SuperArray, Bethesda, MD) was used to characterize the transcription factor profiles of SMMC-7721 and HCCLM6 cells. The chip included 254 transcription factors. The nuclear protein from DNA pull-down assay was incubated for 30 minute at 15°C with the TranSignal probes, and then the compounds was washed three times with wash buffer and eluted with elution buffer to get the probes. When used, probes from three independent expreriments were taken and mixed by equal volume. Then, probes were hybridized with microarrays performed according

to the manufacturer’s instructions as described previously [15]. 2.6 Electrophoretic Mobility Shift Verubecestat Assays (EMSA) Nuclear extract preparation and electrophoretic mobility shift assays were conducted as described previously [12]. The oligonucleotides containing c-Myb-binding site were used in EMSA according to the manufacturer’s instructions (Chemiluminescent nucleic acid detection module, Pierce). Bcl-w The oligonucleotides were Ferroptosis mutation labeled with biotin according to standard protocols. The sequences of the oligonucleotides

were as follows: 5′Biotin-TAC AGGCATAACGGTTCCGTAGTGA-3′. The point mutant (underlined) of oligonucleotides was constructed: 5′Biotin-TACAGGCATA T CGGTTCCGTAGTGA-3′. The oligonucleotides was annealed to its complementary oligonucleotides and incubated with nuclear proteins for 30 minute at 25°C. Samples were run on a 6% polyacrylamide gel, which was transfered into Nylon member and then blocked and washed. Bands were detected by chemiluminescent method. 2.7 Luciferase Assay The OPN promoter was amplified by from HCCLM6 cells as described above [12]. The amplified OPN promoter encompassed all c-Myb binding sites to test transcriptional activity [16]. The resulting 1673-bp fragment (-1488 to +185) was ligated into the Kpn I and Xhol I sites of the pGL3-Basic luciferase reporter vector (Promega, Madison, WI). In brief, 4 x105 cells were seeded the day before transfection. Then, 2 ug of plasmid DNA and 4 ul of LipofectAMINE 2000 (Invitrogen, Carlsbad, CA), diluted with Opti-MEM, were mixed gently and incubated with cells. Together, the small RNA interference (siRNA) targeting c-Myb was chemically synthesized and tranfected into cells using LipofectAMINE 2000. Culture medium was changed after 6 hours of transfection.

Of these, ALS3 and HWP1 appear to play the most prominent role in biofilm development [11, 19, 35],

and evidence PCI-32765 nmr suggests that their differential expression could play a role in mediating detachment events [19]. We found that BCR1 was necessary for establishment of adhesion of the C. albicans biofilm to the silicone elastomer surface and that ALS3 was necessary for establishment of firm adhesion, while HWP1 was not required. Although there was a slight trend of decreased expression of TEC1 in the time course analysis, there was no indication that BCR1 was differentially regulated during detachment and overexpression of ALS3 had only a modest effect on the detachment phenotype. The time course analysis indicated that the detachment process coincided with differential regulation of a relative abundance of genes coding for plasma membrane proteins, cell surface proteins and cell wall proteins, with a modest enrichment in these categories (data not shown). These genes were scrutinized more closely for clues that would indicate

changes in cell surface properties related to detachment. Genes involved in transport (ALP1, TNA1, CTR1, GNP1, HGT1, HGT15, and DUR7) were highly represented indicating a shift in metabolism. selleck chemical There was no clear trend indicating that these transcripts were generally either increased or decreased during the time course. There was a general decrease in transcripts for genes involved in hyphal penetration (RAC1, PLB1) which is suggestive of a response to reject surface association. It would be reasonable to expect that induction of release from the surface would involve cell wall restructuring and two genes (SCW11, XYL2) are related to this function. Patterns of gene expression uncovered by K means analysis indicated that genes involved in similar biological processes were regulated together which provides some support for the hypothesis that the detachment process was associated with some form of coordinated transcriptional regulation. Genes involved in DNA

packaging (HTB1, HTA1, HHF22, HHT2, and NHP6a) and host interaction (RAS1, SAP5, ALS1, and TEC1) were generally down regulated (groups 1 and 7, respectively), while genes involved in carbohydrate/glycoprotein 5-Fluoracil research buy (CWH8, PSA2, and TPS3) biosynthetic processes and energy derivation/generation of precursor metabolites (TPS2, MRF1, and ADH5) were generally up regulated (groups 3 and 5, respectively). Among group 1 there were a number of genes coding for Selleckchem GF120918 histones that were found to be differentially regulated by the quorum sensing agents farnesol or tyrosol (HTA1, HHT2, and NHP6a), both of which have been shown to influence biofilm development [43, 44]. There are a substantial number of genes whose expression levels have been shown previously to influence C. albicans biofilm formation.

Res Microbiol 1996,147(6–7):541–551.PubMedCrossRef 16. Redfield RJ, Cameron AD, Qian Q, Hinds J, Ali TR, Kroll JS, Langford PR: A novel CRP-dependent regulon controls expression of competence genes in Haemophilus influenzae . J Mol Biol 2005,347(4):735–747.PubMedCrossRef 17. Busby S, Ebright RH: Transcription activation by catabolite activator protein (CAP). J Mol Biol 1999,293(2):199–213.PubMedCrossRef 18. MacFadyen LP, Dorocicz IR, Reizer J, Saier MH Jr, Redfield RJ: Regulation of competence

development and sugar utilization in Haemophilus PFT�� mw influenzae Rd by a phosphoenolpyruvate:fructose phosphotransferase system. Mol Microbiol 1996,21(5):941–952.PubMedCrossRef 19. Larson TJ, Cantwell JS, van Loo-Bhattacharya AT: Interaction at a distance between multiple operators controls the adjacent, divergently transcribed glpTQ-glpACB operons of Escherichia coli K-12. J Biol Chem 1992,267(9):6114–6121.PubMed 20. Wickstrum JR, Santangelo TJ, Egan SM: Cyclic Savolitinib datasheet AMP receptor protein and RhaR synergistically activate transcription from the L-rhamnose-responsive rhaSR promoter in Escherichia coli . J Bacteriol 2005,187(19):6708–6718.PubMedCrossRef 21. Egan SM, Schleif RF: A regulatory Cell Cycle inhibitor cascade in the induction of rhaBAD . J Mol Biol 1993,234(1):87–98.PubMedCrossRef 22. Plumbridge

JA: Repression and induction of the nag regulon of Escherichia coli K-12: the roles of nagC and nagA in maintenance of the uninduced state. Mol Microbiol 1991,5(8):2053–2062.PubMedCrossRef 23. Plumbridge JA: Induction of the nag regulon of Escherichia coli by N -acetylglucosamine and glucosamine: role of the cyclic AMP-catabolite activator protein complex in expression of the regulon. J Bacteriol 1990,172(5):2728–2735.PubMed 24. Plumbridge J, Kolb A: DNA loop formation between Nag repressor molecules bound Niclosamide to its two operator sites is necessary for repression of the nag regulon of Escherichia

coli in vivo . Mol Microbiol 1993,10(5):973–981.PubMedCrossRef 25. Campagnari AA, Gupta MR, Dudas KC, Murphy TF, Apicella MA: Antigenic diversity of lipooligosaccharides of nontypable Haemophilus influenzae . Infect Immun 1987,55(4):882–887.PubMed 26. Herriott RM, Meyer EM, Vogt M: Defined nongrowth media for stage II development of competence in Haemophilus influenzae . J Bacteriol 1970,101(2):517–524.PubMed 27. Fan X, Pericone CD, Lysenko E, Goldfine H, Weiser JN: Multiple mechanisms for choline transport and utilization in Haemophilus influenzae . Mol Microbiol 2003,50(2):537–548.PubMedCrossRef 28. Copass M, Grandi G, Rappuoli R: Introduction of unmarked mutations in the Helicobacter pylori vacA gene with a sucrose sensitivity marker. Infect Immun 1997,65(5):1949–1952.PubMed 29. Peterson S, Cline RT, Tettelin H, Sharov V, Morrison DA: Gene expression analysis of the Streptococcus pneumoniae competence regulons by use of DNA microarrays. J Bacteriol 2000,182(21):6192–6202.

pylori pathogenesis but have not been able to reproduce completely clinical outcomes associated with H. pylori infection [6,13–15]. Moreover, rodent models of wild-type mice, knock-out or transgenic mice and mongolian gerbils have been used to reproduce H. pylori persistent infection and disease [16–18]. However, these mammalian models are very expensive and time-consuming because they require specific animal facilities not widely accessible to all research groups, a large number of animals in order to obtain statistically

significant results, and a formal approval by the local Ethics Committee. Invertebrate hosts, such as nematodes or insects, can selleck chemicals be used as alternative models of infection. Caenorhabditis elegans has been used as an infection model for a diverse range of bacterial and fungal

pathogens [19,20]. However, C. elegans cannot survive at 37°C and lacks functional homologues of cellular components of the mammalian immune system, such as specialized phagocytic cells [21]. Models of infection based on insects, such as Drosophila melanogaster and LY2603618 Galleria mellonella (wax moth) larvae offer the advantage that they can survive at 37°C. For example, a transgenic Drosophila AZD0156 manufacturer model with Leukotriene-A4 hydrolase inducible CagA expression has been used to study the signal transduction pathways activated by CagA [22,23]. In addition, insects possess specialized phagocytic cells, also known as hemocytes [21], which resemble mammalian phagocytes because they are able to engulf pathogens and kill them by using antimicrobial peptides and reactive oxygen species through proteins homologous to the NADPH oxidase complex of human neutrophils

[24]. Moreover, genes that are known to mediate recognition of pathogen-associated molecular patterns, such as at least three different toll-like receptors and the transcription factor nuclear factor-κB (NFkB), and apoptosis-related signaling, such as caspases-1, −3,-4, and −6, are expressed in G. mellonella larvae [25,26]. Although G. mellonella does not reproduce all aspects of mammalian infection, their larvae are increasingly used as mini-hosts to study pathogenesis and virulence factors of several bacterial and fungal human pathogen for the following advantages: i) low overall costs of breeding large numbers of larvae and worldwide commercial availability; ii) adaptation to human physiological temperature (37°C); iii) presence of a well-characterized phagocytic system; iv) availability of a comprehensive transcriptome and immune gene repertoire [21,24–26]. G.

Photosynth Res 48(1–2):1–319 1995 Cogdell R, Nechusthtai R, Malkin R (eds) (1995) Structure, function and biogenesis of chlorophyll–protein complexes. Photosynth Res 44(1–2):1–219 Melis A, Buchanan BB (eds) (1995) A tribute to Daniel I Arnon. Photosynth Res 46(1–2):1–377 1994 Falkowski PG, Long SP, Edwards GE (eds) (1994) Photosynthesis and global BIX 1294 changes in the environment. Photosynth Res 39(3):207–495 Olson JM, Amesz J, Ormerod JG, Blankenship RE (eds) (1994) Green and heliobacteria. Photosynth Res 41(1):1–294 1993 Govindjee, Renger G (eds) (1993) How plants and Cyanobacteria make oxygen: 25 years of period four oscillations. Photosynth Res 38(3):211–482 1992 Hartman

H (Ed) (1992) Photosynthesis and the origin of life. Photosynth Res 33(2):73–176 Rich PR (ed) (1992) Robin Hill. Photosynth Res 34(3):319–488 1989 Blankenship RE, Amesz J, Holten D, Jortner J (eds) (1989) Tunneling FHPI concentration processes in photosynthesis. Part 1. Photosynth Res 22(1):1–122 1988 Govindjee, Bohnert HJ, Bottomley W, Bryant DA, Mullet JE, Ogren WL, Pakrasi H, Somerville CR (eds) (1988) Molecular biology of photosynthesis 1. Photosynth Res 16(1–2):5–186 Govindjee, Bohnert HJ, Bottomley W, Bryant DA, Mullet JE, Ogren WL, Pakrasi H, Somerville CR (eds) (1988) Molecular biology of photosynthesis 2. Photosynth Res 17(1–2):5–194

Govindjee, Bohnert HJ, Bottomley W, Bryant DA, Mullet JE, Ogren WL, Pakrasi H, Somerville CR (eds) (1988) Molecular biology of photosynthesis 3. Photosynth Res 18(1–2):5–262 Govindjee, Bohnert HJ, Bottomley W, Bryant DA, Mullet JE, Ogren WL, Pakrasi H, Somerville CR (eds) (1988) Molecular biology of photosynthesis 4. Photosynth Res 19(1–2):5–204 1986 Amesz J, Hoff AJ, van Gorkom HJ (eds) (1986) Double special issue dedicated to Professor Louis NM Duysens

on the occasion of his retirement. Photosynth Res 9(1–2):vii+ 1–283 6 VI Conferences 2008 learn more Prasil O, Farnesyltransferase Suggett DJ, Cullen JJ, Babin M, Govindjee (2008) Aquafluo 2007: chlorophyll fluorescence in aquatic sciences, an international conference held in Nové Hrady. Photosynth Res 95(1):111–115 2007 Blankenship RE (2007) 2007 Awards of the International Society of Photosynthesis Research (ISPR). Photosynth Res 94(2–3):179–181 Govindjee, Telfer A (2007) Six young research investigators were honored at an international conference in Russia. Photosynth Res 92(1):139–141 Govindjee, Yoo H (2007) The International Society of Photosynthesis Research (ISPR) and its associated international congress on photosynthesis (ICP): a pictorial report. Photosynth Res 91(2–3):95–106 Govindjee, Rutherford AW, Britt RD (2007) Four young research investigators were honored at the 2006 Gordon research conference on photosynthesis. Photosynth Res 92(1):137–138 2006 Aro EM, Golbeck JH, Osmond B (2006) Message from the International Society of Photosynthesis Research (ISPR).

Another research focus will be whether the lichens have photobiont populations that are different within the same lichen species and also geographically. An increasing number of scientific publications show, that chlorolichens use local populations of green algae as photobionts, while cyanobacterial lichens seem to preferably select highly efficient cyanobiont strains, which are shared by ecologically similar lichenized fungi (Printzen et al. 2010; Fernández-Mendoza et al. 2011). Finally WP 6 ensures the coordination and successful delivery

of material with end-users. This WP performs the important functions of overseeing NVP-BSK805 both the science part of the project and providing the link with the stakeholders. For this reason the WP team is composed of the leaders of the other packages, although others will naturally be involved, and a science education specialist. The scientific outputs shall be changed into a form that is more easily understood by stakeholders and end-users, and most importantly, assure the awareness and appreciation of BSCs as an important component of the landscape (see also homepage of the project at http://​www.​soil-crust-international.​org/​). Materials and methods Investigation sites 1. Nature Reserve Gynge Alvar, Öland, Sweden (Fig. 2a). The site (56°32′′N, 16°28′E) is situated in Mörbylånga comunity, Resmo parish, about

20 m above sea level (a.s.l.), on Erismodegib nmr the island of Öland, during Sweden. Öland has a maritime RG7112 molecular weight climate, but is situated in a rain shadow and, with 500 mm/year, has the lowest mean precipitation of any Swedish provinces. The mean temperature is about −2 °C in February and 17 °C in July (annual mean 1961–1990). Gynge Alvar Nature Reserve is part of the ca. 26,000 ha large Stora Alvaret (the Great Alvar) which together with other agricultural areas on southern

Öland is designated as a World Heritage Site by UNESCO. The site at Gynge Alvar is a typical open limestone pavement alvar area, with Ordovician sedimentary limestone as bedrock and a very thin layer of gravel and scattered siliceous moraine rocks. It is currently grazed by cattle. On the open soil-crust dominated areas higher plants are scarce and the cryptogam vegetation is dominated by lichens such as Cladonia symphycarpia, C. rangiformis, C. foliacea, Thamnolia vermicularis, Squamarina cartilaginea, Fulgensia bracteata, Fulgensia fulgens, Psora decipiens, and cyanobacteria (Albertson 1950; Fröberg 1999). The alvar regions are usually seen as semi-natural open areas on limestone pavement which have existed since the last glaciation (ca 11,000 years before present), containing both relicts from postglacial arctic conditions and from later steppe-like conditions in warm periods. These areas were thus originally open and dependent on grazing from larger herbivores to remain so. Later human settlers have continued the grazing activities with cattle, horses and sheep.

This growth factor interferes with the essential intercellular SB431542 epithelial junctional complexes of epithelial (E)-cadherin and β-catenin, whereby E-cadherin-mediated sequestration of β-catenin at the cell membrane is abolished. As a result, β-catenin localizes to the nucleus and subsequently activates transcriptional factors, such as Snail, which will ultimately down-regulate E-cadherin expression and lead to loss of intercellular cohesion [32, 33]. On clinical grounds,

reduced expression of E-cadherin in oral carcinomas has been consistently found to be associated with an invasive growth pattern and a shortened 5-year survival [19, 34]. In tongue carcinoma, in particular, low expression of E-cadherin was found to be predictive for cervical lymph node metastases [35]. Our positive double immunostaining results revealed a continuum of cells with undistinguishable intercellular borders, ranging from unmistakably epithelial membrane antigen-positive carcinoma cells to weakly-to-no epithelial membrane antigen staining,

further to both epithelial membrane antigen—and α-smooth muscle actin—stained carcinoma cells, and finally, to strongly α-smooth SB202190 order muscle actin-stained SMF. This is the first study on human oral carcinoma that used a double immunostaining method to show progressive reduction in the expression of epithelial membrane antigen with concomitant gain of α-smooth muscle actin. These changes reflect one aspect of the plasticity in the phenotype of the malignant epithelial cells, as long as it serves the aim of facilitating local invasion and metastatic dissemination [11, 16]. In a previous study in an animal model of tongue dipyridamole carcinoma, we showed at an ultrastructural

level that neoplastic cells at the tumor-connective tissue interface acquired morphologic modifications approaching smooth muscle differentiation by developing a cytoplasmic system of contractile microfilaments, probably as part of the epithelial-mesenchymal transition process [21]. Epithelial membrane antigen was used in this study as a structural marker for epithelial differentiation [23]. Other studies on epithelial-mesenchymal transition used E-cadherin as a functional marker for epithelial intercellular junctional complexes and showed its ABT-737 cost down-regulation as a reflection of underlying epithelial-mesenchymal transition, principally mediated by transforming growth factor-β [12, 32]. Although epithelial membrane antigen and E-cadherin belong to different classes of molecules with various functions, a recent study on breast cancer showed restricted expression of both molecules during the epithelial-mesenchymal transition process [36]. In summary, the present study was the first to use a double immunohistochemical technique in human tongue carcinoma in order to investigate the possibility of an epithelial-mesenchymal transition process.

Two hundred μl of the supernatant was transferred to a 96-well plate and the A562 determined in a microplate reader (Paradigm, Beckman Coulter, Bromma, Sweden). The iron content of the sample was calculated by comparing its absorbance to that of samples with FeCl3 concentrations in the range of 0-5,000 ng/ml that had been prepared identically to the test samples. The correlation coefficients

of the standard curves varied between 0.998 and 0.999. The detection limit of the assay was 50 ng/ml Fe. The intra-sample variations (i.e., samples from the same culture) were less than 17 ng/OD600. H2O2 susceptibility test Bacteria were cultivated overnight in CDM and thereafter cultured in fresh CDM for 2 h at PI3K Inhibitor Library cell assay 37°C and 200 rpm. The density of the cultures was measured and Mocetinostat purchase cultures were serially diluted in PBS to approximately 106 bacteria per ml. The exact number of bacteria at the start of the experiment was determined by viable count. The bacterial suspension was divided in 2 ml aliquots in 10 ml screw cap tubes. To some tubes H2O2 (Sigma) was supplied to reach a final concentration of 0.1 mM and other tubes were left untreated as controls. The tubes were incubated at 37°C 200 rpm. After 0 and 2 h of incubation, bacterial samples

were collected and viable bacteria determined by plating click here 10-fold serial dilutions. The plates were incubated for 3 days at 37°C 5% CO2 before enumeration of the colony forming units (CFU). Statistical analysis For statistical evaluation, two-tailed Student’s Vildagliptin t-test and two-tailed Pearson’s correlation test in the statistical software program SPSS, version 16 were used. Results Growth of LVS and ΔmglA under aerobic or microaerobic conditions CDM is a liquid medium that effectively supports growth of F. tularensis. Accordingly, LVS grew to an OD600 of approximately 3.0 within 24 h under aerobic conditions, however, ΔmglA reached an OD600 of only slightly above 1.0 (Figure 1). In some experiments, LVS grew as well under microaerobic and aerobic conditions, but in other experiments, the growth was slightly reduced under the former condition (Figure 1).

ΔmglA grew as well in the microaerobic as in the aerobic milieu during the first hours, but after approximately 24 h, its growth rate was reduced in the aerobic milieu, whereas it reached the same density as LVS in the microaerobic milieu after 48 h (Figure 1). FUU301 (ΔmglA expressing mglA in trans) exhibited an intermediary growth in the aerobic milieu and its density was 2.09 ± 0.05 vs. 2.59 ± 0.05 for LVS, whereas growth of the two strains was similar in the microaerobic milieu. Figure 1 Growth of LVS (squares) and Δ mglA (triangles) in CDM in an aerobic (closed symbols) or microaerobic (open symbols) milieu. The diagram shows one representative experiment and similar results were seen in three additional experiments.

The room-temperature PL spectrum of the as-grown ZnO nanoflowers and the samples coated by the ZnO

thin films with varied thicknesses. The inset shows the PL spectra of the ZnO thin film by ALD on silicon substrate. To improve the optical properties, the as-grown sample was coated by a ZnO thin film by ALD. It was shown that ZnO films grown by ALD would have few zinc interstitials Selleck Adriamycin and oxygen vacancies [17]; hence, it is a good way to improve the optical properties of the nanostructures. After a ZnO film was coated, with thickness about 15 nm (the blue squares), the deep-level emission decreased dramatically about 80%; moreover, the intensity of band-edge transition increased about 30%. The ratio α is about 1.65. This result reveals that the AZD3965 concentration very thin film on the surface of the nanoflowers can effectively enhance their optical properties without altering the morphologies. With the increasing thickness in the coating of ZnO films, the deep-level emission decreases and the band-edge transition increases, as shown in Figure 6. The deep-level emission of the sample coated with 45 nm ZnO is only 4% of that from the as-grown sample. In addition, the intensity of the band-edge transition from the sample coated with 45-nm

ZnO is 300% more than that from the as-grown sample. The ratios of the intensity of the band-edge transition to the deep-level emissions are 5.91 and 16.5 for the samples with 30-nm and 45-nm ZnO, respectively. These results show

that an ALD coating Guanylate cyclase 2C of ZnO thin films can effectively enhance the optical properties of the ZnO nanostructures. However, we should know whether the PL result is due to the original ZnO nanoflower or from the ALD ZnO. Hence, we fabricated the ZnO thin film on silicon substrate by ALD using the same parameters. The thickness of this ZnO film is 45 nm, and the PL spectrum of this sample is shown as the inset of Figure 6. A strong peak around 382 nm can be observed, which is attributed to the band-edge transition. Moreover, there is nearly no deep-level emission in the sample. Hence, we can make a conclusion that the stronger peak of the band-edge transition is mostly from the ZnO thin films by ALD, while the weaker peak of the deep-level emission is from the original ZnO nanoflowers. Usually, in the ZnO nanostructures, there are many oxygen vacancies and zinc interstitials, so their optical properties are very poor. Our result reveals that we could coat an epitaxial ZnO thin film by ALD on these nanostructures. This method can effectively enhance the optical properties without changing the morphologies. Another point should be noted that there is a blue shift in the band-edge transitions and a red shift in the deep-level emissions with increasing the thickness of the coating ZnO films. This reason needs Emricasan order further investigation. Conclusions In conclusion, we have synthesized ZnO nanoflowers by reactive vapor deposition.

34 EU673338 EU673203 EU673259 EU673307 EU673138 Neodeightonia phoenicum CBS 122528 EU673340 EU673205 EU673261 EU673309 EU673116 Neodeightonia phoenicum CBS 123168 EU673339 EU673204 EU673260 EU673308 EU673115 Neodeightonia sp MFLUCC 11-0026 JX646804 JX646837 JX646821 JX646869 JX646852 Neodeightonia subglobosa MFLUCC 11-0163 JX646794 – JX646811 JX646859 JX646842 Neodeightonia subglobosa CBS 448.91 EU673337 EU673202 DQ377866 EU673306 EU673137 Neofusicoccum luteum CBS 110299 AY259091 EU673148 AY928043 AY573217 DQ458848 Neofusicoccum

luteum CBS 110497 EU673311 EU673149 EU673229 EU673277 EU673092 Entinostat Neofusicoccum mangiferum CBS 118531 AY615185 EU673153 DQ377920 – AY615172 Neofusicoccum mangiferum

CBS 118532 AY615186 EU673154 DQ377921 DQ093220 AY615173 Neofusicoccum parvum MFLUCC 11-0184 JX646795 JX646828 JX646812 JX646860 JX646843 Neofusicoccum parvum CMW 9081 AY236943 EU673151 AY928045 AY236888 AY236917 Neofusicoccum parvum CBS 110301 AY259098 EU673150 AY928046 AY573221 EU673095 PFT�� nmr Neoscytalidium dimidiatum CBS 251.49 FM211430 – DQ377923 – FM211166 Neoscytalidium dimidiatum CBS 499.66 FM211432 – DQ377925 EU144063 FM211167 Neoscytalidium novaehollandiae WAC 12691 EF585543 – EF585548 EF585574 – Neoscytalidium novaehollandiae WAC 12688 EF585542 – EF585549 EF585575 – Otthia spiraeae 1 CBS 114124 – EF204515 EF204498 – – Otthia spiraeae 2 CBS 113091 – EF204516 EF204499 – – Phaeobotryon mamane CPC 12440 EU673332 EU673184 EU673248 EU673298 EU673121 Phaeobotryon mamane CPC 12442 EU673333 EU673185 DQ377899 EU673299 EU673124 Phaeobotryon mamane CPC 12443 EU673334 EU673186 EU673249 EU673300 EU673120

Carbohydrate Phaeobotryon mamane CPC 12444 EU673335 EU673187 DQ377900 EU673301 EU673123 Phaeobotryon mamane CPC 12445 EU673336 EU673188 EU673250 EU673302 EU673122 Phaeobotryosphaeria citrigena ICMP 16812 EU673328 EU673180 EU673246 EU673294 EU673140 Phaeobotryosphaeria citrigena ICMP 16818 EU673329 EU673181 EU673247 EU673295 EU673141 Phaeobotryosphaeria eucalyptus MFLUCC 11-0579 JX646802 JX646835 JX646819 JX646867 JX646850 Phaeobotryosphaeria eucalyptus MFLUCC 11-0654 JX646803 JX646836 JX646820 JX646868 JX646851 Phaeobotryosphaeria porosa CBS 110496 AY343379 EU673179 this website DQ377894 AY343340 EU673130 Phaeobotryosphaeria porosa CBS 110574 AY343378 – DQ377895 AY343339 – Phaeobotryosphaeria visci CBS 186.