Int J Eat Disord 1995, 18:49–57.PubMed 208. Balon TW, Horowitz JF, Fitzsimmons KM: Effects of carbohydrate loading and weight-lifting on muscle girth. Int J Sport Nutr 1992, 2:328–334.PubMed 209. Costill DL, Cote R, Fink W: Muscle water and electrolytes following varied levels of dehydration in man. J Appl Physiol 1976, 40:6–11.PubMed 210. Goldfield GS, Blouin AG, Woodside DB: Body image, binge eating, and bulimia nervosa in male bodybuilders. Can J Psychiatry 2006, 51:160–168.PubMed 211. Mangweth B, Pope HG Jr, Kemmler G, Ebenbichler C, Hausmann A, De Col C, Kreutner B, Kinzl J, Biebl W: Body image and psychopathology

in male bodybuilders. Psychother Psychosom 2001, 70:38–43.PubMed 212. Baghurst T, Lirgg C: Characteristics of muscle dysmorphia in male football, weight training, and competitive natural

and non-natural Selleckchem GSK126 bodybuilding samples. Body Image 2009, 6:221–227.PubMed 213. Pickett TC, Lewis RJ, Cash TF: Men, muscles, and body image: comparisons of competitive bodybuilders, weight trainers, and athletically active controls. Br J Sports Med 2005, 39:217–222. discussion 217–222PubMedCentralPubMed 214. Jankauskiene R, Kardelis K, Pajaujiene S: Muscle size CH5424802 price satisfaction and predisposition for a health harmful practice in bodybuilders and recreational Selleck Ispinesib gymnasium users. Medicina (Kaunas) 2007, 43:338–346. 215. Walberg Niclosamide JL, Johnston CS: Menstrual function and eating behavior in female recreational weight lifters and competitive body builders. Med Sci Sports Exerc 1991, 23:30–36.PubMed 216. Sundgot-Borgen J, Garthe I: Elite athletes in aesthetic and Olympic weight-class sports and the challenge of body weight and body compositions. J Sports Sci 2011,29(Suppl 1):S101-S114.PubMed Competing interests The authors declare that they have no competing interests. Authors’ contributions

ERH developed the concept for this manuscript and wrote the sections on caloric intake, macronutrients, psychosocial issues and “peak week”. AAA wrote the sections on nutrient timing and meal frequency. PJF wrote the abstract, methods, limitations, and the section on dietary supplementation. All authors read and approved the final manuscript.”
“Background Colon cancer is a result of an evolving process characterized by alterations of multiple genes and dysregulated cell signal transduction pathways. It has been well known that mutations of key genes in the Wnt/β-catenin signaling pathway play an important role in the occurrence and development of colon cancer [1, 2]. Under physiological conditions, Wnt contributes to the stabilization of β-catenin. Once stabilized, β-catenin accumulates and migrates to the nucleus.

Biofilm formation is a trait commonly found among CAUTI isolates and results in the

growth of bacteria on the inner surface of the PLX4032 mouse urinary catheter. Biofilm formation promotes encrustation and protects the bacteria from the hydrodynamic forces of urine flow, host defenses and antibiotics [4]. A perquisite to biofilm growth is adherence to the catheter surface. A number of mechanisms by which Gram-negative pathogens mediate adherence to biotic and abiotic surfaces have been described and include fimbriae (e.g. type 1, type 3, type IV, curli and conjugative pili), cell surface adhesins (e.g. autotransporter proteins such as antigen 43, UpaH and UpaG) and flagella [5–16]. The expression of type 3 fimbriae has been described from many Gram-negative pathogens [17–28]. Type 3 fimbriae are 2-4 nm wide and 0.5-2 μm long surface organelles that are characterised by their ability to mediate agglutination of tannic acid-treated human RBC (MR/K selleck chemicals llc agglutination) [29]. Several studies have clearly demonstrated a role for type 3 fimbriae in biofilm formation [17, 28, 30–33]. Type 3 fimbriae also mediate various

adherence functions such as binding to epithelial cells (from the respiratory and urinary tracts) and extracellular matrix proteins (e.g. collagen V) [31, 34–36]. Type 3 fimbriae belong to the chaperone-usher class of fimbriae and are encoded by LXH254 datasheet five genes (mrkABCDF) arranged in the same transcriptional orientation [29, 37]. The mrk gene cluster is similar to other fimbrial operons of the chaperone-usher class in that it contains genes encoding major (mrkA) and minor (mrkF)

subunit proteins as well as chaperone- (mrkB), usher- (mrkC) and adhesin- (mrkD) encoding genes [37, 38]. A putative regulatory gene (mrkE) located upstream Carbohydrate of mrkA has been described previously in Klebsiella pneumoniae [37]. The mrk genes have been shown to reside at multiple genomic locations, including the chromosome [39], on conjugative plasmids [17, 30] and within a composite transposon [40]. Transfer of an mrk-containing conjugative plasmid to strains of Salmonella enterica serovar Typhimurium, Klebsiella pneumoniae, Enterobacter aerogenes and Kluyvera species has also been demonstrated [17]. Taken together, these data strongly support spread of the mrk genes between Gram-negative pathogens by lateral gene transfer. Recently, we identified and characterised the role of type 3 fimbriae in biofilm formation from an Escherichia coli strain isolated from a patient with CAUTI [28]. We also demonstrated that the mrkB chaperone-encoding gene and the ability to mediate MR/K agglutination was common in uropathogenic Klebsiella pneumoniae, Klebsiella oxytoca and Citrobacter koseri strains (86.7%, 100% and 100% of strains, respectively) but rare in uropathogenic E. coli and Citrobacter freundii strains (3.2% and 14.3% of strains, respectively) [28].

Up to now, most of the research on superhydrophobic surface focused on Ralimetinib in vitro measuring the CAs and sliding angles (SAs) of water droplets with a volume not smaller than 2 μL (approximately 1.6 mm in diameter). However, we often observe water droplets with a volume lower than 2 μL, such as fog droplets, existing or

sliding on a solid surface in nature. There is a need to reveal the interfacial interaction between superhydrophobic surface and tiny water droplets. Generally, pristine carbon nanotubes (CNTs) are hydrophobic materials, which have also been used to H 89 cell line construct a superhydrophobic surface [15, 16]. By making micropatterns, the hydrophobicity of a CNT surface is further enhanced. The CA between water and CNT pattern is usually larger than 150°, but the SA is

also large (usually larger than 30°) [17, 18]. However, the superhydrophobic CNT forest might also selleck absorb water, resulting in collapsing into cellular foams when water evaporates from interstices of nanotubes [19]. After wetting, the CNT forest might lose its superhydrophobic properties. It needs to construct a stable and durable superhydrophobic surface even wetted by vapor or tiny water droplets. Here, we fabricate the superhydrophobic hierarchical architecture of CNTs on Si micropillar array (CNTs/Si-μp) with large CA and ultralow SA. The CNTs/Si-μp show a durable superhydrophobic surface even after wetting using tiny water droplets. Methods Si micropillar (Si-μp) arrays with defined squares (see Figure  1a, inset) were etched

from a Si (100) wafer by ultraviolet lithography (UVL) and deep reactive-ion etching (DRIE) in sulfur hexafluoride (SF6) and perfluoro-2-butene (C4F8). The height of the Si-μp was controlled by etching time. A standard cleaning process developed by the company Radio Corporation of America (RCA) was carried out to eliminate residual metal and organic species followed by removing Si oxide in a buffered HF solution. The Si micropillar arrays and planar Si wafer were coated with a thin layer of aluminum (10 nm) using an e-beam evaporator for CNT growth. CNTs were grown by floating chemical vapor deposition method, using xylene as carbon source, Oxymatrine ferrocene as catalyst precursor, and a mixture of Ar and H2 as carrier gas, according to our previous report [20]. During the growth of CNTs, the ferrocene/xylene solution (20 mg/mL) was fed into the reactor at a rate of 0.2 mL/min, and Ar and H2 were fed at 400 and 50 sccm, respectively. Figure 1 SEM characterization of various samples. (a) Si micropillar array. (b) Hierarchical architecture of CNTs/Si-μp. (c) Connection between a Si micropillar and CNT forests. (d) CNT forest growing on a planar Si wafer. The samples were characterized using a scanning electron microscope (SEM). The CA and SA were measured using a contact angle goniometer (Rame-hart 300, Rame-hart Instrument Co., Succasunna, NJ, USA).

Immuno17DMAG order Staining of p-MEK and p-ERK and RKIP Immunohistochemical staining was carried out by the streptavitin-biotin method using a Histofine SAB-PO kit (Nichirei Co., Tokyo, Japan). Polyclonal rabbit antibody against p-ERK was purchased from Abcam® (Cambridge, UK), monoclonal Rabbit antibody against p-MEK 1/2 (Ser221)

was purchased from Cell Signaling ACY-241 datasheet Technology, Inc. (Beverly, MA, USA), and RKIP antibody was purchased from Santa Cruz Biotechnology, Inc. (Santa Cruz, CA, USA). All available haematoxylin-and-eosin-stained slides of the surgical specimens were reviewed. For each case, representative paraffin blocks were selected for immunohistochemical studies. Three-micrometer-thick sections were cut from each formalin-fixed, paraffin-embedded tissue block. After deparaffinisation and rehydration, antigen retrieval treatment was carried out at 98°C (microwave) for 15 min in 10 mmolL sodium citrate buffer (pH 6.0), followed by treatment with 3% hydrogen peroxide for 15 min to quench endogenous peroxidase activity. Nonspecific binding was blocked by treating the slides with 5% EzBlock (including 10% normal goat serum) for 10 min at room temperature. The slides were incubated

with primary antibodies including p-ERK (dilution 1:50), p-MEK (1:50), and RKIP (1:100) overnight at 4°C. Immunodetection was performed by the conventional streptavidin-biotin method with peroxidase-labeled Nichirei SAB-PO kits. Diaminobenzidine CB-5083 mouse substrate was used for colour development. Farnesyltransferase The slides were counterstained with 1% Mayer’s haematoxylin. Expression levels of p-ERK, p-MEK, and RKIP were classified into groups based on staining intensity and positive frequency. We counted stained cells under a microscope to derive the scores. The cytoplasmic and nuclear staining patterns were separately quantified, using a semiquantitative system to evaluate and grade the immunostaining pattern, as successfully applied by others [16]. Staining intensity was scored into four grades:

0 (none), 1 (weak positive), 2 (moderate positive), and 3 (strong positive). Staining extent (positive frequency) was also scored into four grades: 0 for complete absence of staining, 1 for < 10%, 2 for 10% to 50%, and 3 for tumours with staining of 50% or more cells. Composite scores were derived by multiplying the intensity score by the staining extent score. For statistical analysis, composite scores of ≥4 were defined as cytoplasmic expression positive, and scores of < 4 were considered negative. We assessed the cytoplasmic expressions of RKIP and MEK and the nuclear expression of ERK as described previously [16, 17]. Statistical analysis The χ2 test was used to test possible associations between the expression of p-ERK, p-MEK, or RKIP and clinicopathological factors. It was also used to assess correlations between p-ERK, p-MEK, and RKIP expressions.

880, 0.863, 0.729, 0.699, and 0.799 respectively, and all these comparisons were statistically

significant at p ≤ 0.0001 (Figure 4A–E). Figure 3 Representative example of human breast cancer specimens from TMA3 that expressed either low (left panel) or high (right panel) eIF4E. Matching specimens from the same patient are shown for c-Myc, cyclin D1, ODC, TLK1B, and VEGF (200 × magnification). Figure 4 CP673451 Correlation of immunohistochemical expression of eIF4E vs c-Myc [A], cyclin D1 [B], ODC [C], TLK1B [D], VEGF [E] from TMA3. Figures represent the integrated optical density (IOD) of immunohistochemical staining intensity normalized to cytokeratin. Protein expression of eIF4E and TLK1B were also find more compared by western blot analysis [F], in which values represent expression of eIF4E and TLK1B as fold- over benign. All comparisons were done using Spearman’s rank correlation. Rho- and p- values for each comparison are displayed in each panel. Western blot analysis: Correlation of eIF4E with TLK1B We have previously shown by western blot analysis that the expression of eIF4E correlated with that of TLK1B [23]. As further validation of our TMA results, we also compared eIF4E with TLK1B using the corresponding fresh-frozen specimens from the same tumors as those used for TMA3 (Figure 4F). Due to limited

amounts of fresh-frozen specimens, the other proteins were not analyzed. Protein expressions of eIF4E to TLK1B were positively correlated (rho value 0.485, p

value 0.0054). Non-correlation to independent markers We have previously demonstrated that western blot analysis MGCD0103 mw of eIF4E did not correlate with node status, ER, PR, or HER-2/neu [18, 19]. In the current study, expression of eIF4E (by both TMA-IHC and western blot) was also compared to ER, PR, and HER-2/neu expression. There was no correlation of eIF4E on TMA3 with any of these independent markers by either TMA-IHC or western blot analysis of eIF4E (Table 2). Table 2 Lack of correlation of ER, PR, or HER-2/neu with eIF4E     95% Confidence Interval       Rho Value Lower Upper n P TMA expression of eIF4E a eIF4E and ER -0.137 -0.469 0.228 31 0.452 eIF4E and PR -0.069 -0.413 0.293 31 0.707 eIF4E and HER-2/neu -0.013 -0.406 0.384 25 0.949 Western blot expression of eIF4E b eIF4E and ER -0.192 -0.479 0.132 39 0.237 eIF4E and PR -0.295 -0.558 0.023 39 0.069 eIF4E and Dimethyl sulfoxide HER-2/neu -0.143 -0.469 0.216 32 0.425 a For the first three rows, comparisons were made of immunohistochemical staining of each protein normalized to cytokeratin to ER, PR, and HER-2/neu.bLast three rows, comparison of protein expression of eIF4E assayed by western blot (fold- over benign) to ER, PR, and HER-2/neu. All comparisons were done using Spearman’s Rank Correlation. Discussion In the current study, we have analyzed the expression of eIF4E along with 5 of its downstream effector proteins in human breast carcinoma specimens using immunohistochemical analysis of TMAs.

The first stage consisted of an attenuated exponential phase of 20 h (if compared with that of the wild type) followed by 30 h of arrested growth with OD600 values of around 0.5 units. In the second one, growth was restarted, showing a second exponential phase during 40 h, followed by a second stationary phase with absorbance values comparable to those of the wild type strain (Figure

5A). As Berzosertib clinical trial in otsAch cells collected at the beginning of the first stationary phase (see Figure 4B), trehalose was absent from extracts prepared from samples harvested at the entrance of this second stationary phase. Instead, they contained large amounts of glutamate (Figure 4C). However, when glucose and trehalose were used as the sole carbon source, this biphasic 10058-F4 pattern of growth was

not observed. Growth of the otsAch strain with both carbon sources was delayed with respect to the wild-type strain, even in the absence of osmotic stress (see Additional file 3: Figure S2). At 35°C, R. etli wild-type strain was able to grow well in B- medium with NaCl concentrations ranging from 0 to 0.15 M. As described above (see Figure 1), growth of the wild type was impaired at 35°C with 0.2 M NaCl, showing absorbance values not exceeding 1.0 unit of OD600(Figure 5B). At this temperature, growth of the otsA mutant was severely affected, regardless of the salinity of the culture medium, with cultures showing OD600 around 0.5 OD units. The above data suggest that trehalose is essential for growth of R. etli at high temperature. Osmotically induced trehalose synthesis improves desiccation tolerance in R. etli Involvement

of trehalose in desiccation tolerance in rhizobia has been firmly established in R. leguminosarum bv. trifolii[7]. On the other hand, in S. meliloti[55] or rhizobia nodulating Acacia[56], Urease desiccation tolerance was stimulated by osmotic and/or temperature pre-treatment. To check the influence of trehalose on desiccation tolerance of R. etli, wild type and otsAch PF-6463922 datasheet strains were grown at 28°C in minimal medium B-alone or additioned with 0.2 M NaCl, and harvested at early stationary phase. For cell drying, we used two variants of the protocol described by Manzanera et al. for E. coli[39], a drying process (induced by vacuum at 30°C) or a drying + high temperature process (including a second step with a controlled increase of temperature from 20 to 30°C under vacuum). In the absence of osmotic stress, both wild type and otsAch strains showed survival levels under 0.01%, regardless of the drying protocol (data not shown). In contrast, wild type cells osmotically pre-conditioned by the presence of 0.2 M NaCl showed ca. 35% survival levels after drying, although viability after 4 days storage dropped down to 1.4% (Figure 6). Compared to the drying treatment, the drying + high temperature protocol did not enhance wild type cell survival (Figure 6).

Seo HS, Cartee RT, Pritchard DG, Nahm MH: A new model of pneumococcal lipoteichoic acid structure resolves biochemical, biosynthetic, and RO4929097 cost serologic inconsistencies of the current model. J Bacteriol 2008, 190:2379–2387.PubMedCentralPubMedCrossRef 15. Song JH, Ko KS, Lee JY, Baek JY, Oh WS, Yoon HS, Jeong JY, Chun J: Identification of essential genes in Streptococcus pneumoniae by allelic replacement mutagenesis. Mol Cells 2005, 19:365–374.PubMed 16. Laursen BS, Sørensen HP, Mortensen

KK, Sperling-Petersen HU: Initiation of protein synthesis in bacteria. Microbiol Mol Biol Rev 2005, 69:101–123.PubMedCentralPubMedCrossRef 17. Denapaite D, Brückner R, Nuhn M, Reichmann P, Henrich B, Maurer P, Schähle Y, Selbmann P, Zimmermann W, Wambutt R, et al.: The genome of Streptococcus mitis B6 – what is a commensal? PLoS

ONE 2010, 5:e9426.PubMedCentralPubMedCrossRef 18. Reichmann P, Nuhn M, Denapaite D, Brückner R, Henrich B, Maurer P, Rieger SGC-CBP30 molecular weight M, Klages S, Reinhard R, Hakenbeck R: Genome of Streptococcus oralis strain Uo5. J Bacteriol 2011, 193:2888–2889.PubMedCentralPubMedCrossRef 19. Czyz A, Wegrzyn G: The Obg subfamily of bacterial GTP-binding proteins: essential proteins of largely unknown functions that are evolutionarily conserved from bacteria to humans. Acta Biochim Pol 2005, 52:35–43.PubMed 20. Hoskins J, Alborn WEJ, Arnold J, Blaszczak LC, Burgett S, DeHoff GSK2126458 order BS, Estrem ST, Fritz L, Fu D-J, Fuller W, et al.: Genome of the bacterium Streptococcus pneumoniae strain R6. J Bacteriol 2001, 183:5709–5717.PubMedCentralPubMedCrossRef 21. Sauerbier J, Maurer P, Rieger M, Hakenbeck R: Streptococcus

mafosfamide pneumonia e R6 interspecies transformation: genetic analysis of penicillin resistance determinants and genome-wide recombination events. Mol Microbiol 2012, 86:692–706.PubMedCrossRef 22. Fani F, Brotherton MC, Leprohon P, Ouellette M: Genomic analysis and reconstruction of cefotaxime resistance in Streptococcus pneumoniae . J Antimicrob Chemother 2013, 68:1718–1727.PubMedCrossRef 23. Shaw N: Bacterial glycolipids. Bacteriol Rev 1970, 34:365–377.PubMedCentralPubMed 24. Rottem S: Transbilayer distribution of lipids in microbial membranes. Curr Top Membr Trans 1982, 17:235–261.CrossRef 25. Weik M, Patzelt H, Zaccai G, Oesterhelt D: Localization of glycolipids in membranes by in vivo labeling and neutron diffraction. Mol Cell 1998, 1:411–419.PubMedCrossRef 26. Henderson R, Jubb JS, Whytock S: Specific labelling of the protein and lipid on the extracellular surface of purple membrane. J Mol Biol 1978, 123:259–274.PubMedCrossRef 27. Kamio Y, Nikaido H: Outer membrane of Salmonella typhimurium : accessibility of phospholipid head groups to phospholipase c and cyanogen bromide activated dextran in the external medium. Biochemistry 1976, 15:2561–2570.PubMedCrossRef 28. Campelo F, McMahon HT, Kozlov MM: The hydrophobic insertion mechanism of membrane curvature generation by proteins. Biophys J 2008, 95:2325–2339.PubMedCentralPubMedCrossRef 29.

30 (1.13–1.49)  4, low 1,401 16.2% 46.9% 1.44 (1.25–1.66)  5, very low (sparsely) 476 5.5% 45.5% 1.37 (1.11–1.70) GP or specialist of start Rx  GP 5,426 62.9% 45.0% –  Specialist 3,200 37.1% 39.8% – Start product  Risedronic ac. weekly and daily Ca 747 8.7% 42.4% –  Risedronic ac. 35 mg weekly 1,818 21.1% 45.4% –  Risedronic ac. 5 mg daily 82 1.0% 40.2% –  Alendronic ac. 10 mg daily 241 2.8% 23.2% 0.31 (0.23–0.43)  Alendronic ac. 70 mg weekly 3,698 42.9% 43.4% –  Ibandronic ac. 150 mg monthly 443 5.1% 46.3% –  Etidronate cyclic and daily Ca 281 3.3% 28.5% 0.42 (0.32–0.56)  Raloxifene 60 mg daily 63 0.7% 33.3% 0.53

(0.31–0.92)  Alendronic Selleckchem Pexidartinib ac. 70 mg and vitD weekly 965 11.2% 52.7% 1.41 (1.21–1.63)  Strontium ranelate 288 3.3% 21.9% 0.27 (0.20–0.36) Drug burden in lookback selleck inhibitor period  0 509 5.9% 43.4% excl.  1, 2 2,584 30.0% 43.1% excl.  3, 4 3,228 37.5%

42.3% excl.  5+ 2,305 37.4% 44.0% excl. Medication lookback period  With_any_medication 8,153 94.5% 43.1% excl.  Without_any_medication 473 5.5% 42.7% excl.  Osteoporosis 1,221 14.2% 43.3% –  Calcium and/or vit. D 2,408 27.9% 47.4% 1.26 (1.13–1.39)  Statins 1,689 19.6% 45.8% –  Cardiovascular medication 4,551 52.8% 44.0% 0.88 (0.79–0.97)  Anti-inflammatory 2,537 29.4% 46.1% –  Gastric protectors 3,597 41.7% 42.5% –  Asthma/COPD 1,684 19.5% 40.2% –  Diabetic medication Tozasertib price 793 9.2% 45.1% –  Antidepressants 961 11.1% 42.2% –  Thyroid hormone 570 6.6% 41.4% –  Glucocorticoids 2,685 31.1% 37.6% 0.65 (0.59–0.72) Medication trailing period

 With_any_med 7,083 82.1% 51.9% 9.31 (7.93–40.92)  Without_any_med 1,543 17.9% 2.3% Reference V% volume percentage, excl. variables that were excluded from the logistic regression model due to multicollinearity, – non-significant variables aOdds ratios based on the logistic regression model adjusted for the variables with 95% confidence interval The three most frequently prescribed oral drugs Dichloromethane dehalogenase for starters on osteoporosis were alendronic acid 70 mg weekly (42.9%), risedronic acid 35 mg weekly (21.1%), and the weekly combination of 70 mg alendronic acid together with vitamin D3 (11.2%). The three least frequently prescribed medications were raloxifene (0.7%), risedronic acid 5 mg (1.0%), and alendronic acid 10 mg (2.8%). After 3 months, 70% of patients were persistent and 43%, after 12 months (Fig. 3). Fig. 3 12 months’ persistence (%) of oral osteoporosis medication Compared to the mean persistence of all medications, patients using weekly one-tablet alendronic acid 70 mg combined with 2,800 IU vitamin D3 had the highest persistence after 12 months (52.7%; OR, 1.41; CI, 1.21, 1.63).

In the supplementary materials, Table S5 highlights examples of lion populations showing differences between the major population assessments and compares them to the most recent data used for this analysis. These estimates all used different methodologies. This precludes direct comparison and conclusions on temporal

trends. While the estimates are broadly similar, there is much evidence of population decline and little to support any population increases. We do not discuss trends in lion numbers, densities, demographic indicators such as altered sex-ratios and ranging behaviour, or the impacts of trophy hunting on these factors (Yamazaki 1996; Loveridge et al. 2007; Packer et al. 2009; Davidson et al. 2011). We should consider, however, the spatial distribution of lions and how this has changed. Figure 5 shows the lion areas across the selleck products African continent by their respective size class. Currently 27 countries across Africa contain resident populations of free-ranging lions (Fig. 4; Table S1). Five countries have lost their lions since Chardonnet’s study in 2002 or did not have them. Only nine countries contain at least 1,000 lions; selleck compound Central African Republic, Kenya, Tanzania, Mozambique, Zambia, Zimbabwe, South Africa, Botswana, and possibly Angola. Tanzania alone contains over 40 % of Africa’s lions. Fig. 5 Population

size classes of all lion areas When the IUCN (2006b) assessed lion range in West and Central Africa, they noted 20 LCUs in the region. Henschel et al. VS-4718 mw (2010) found that more than half (11) of these LCUs most likely no longer contain lions. Bauer (2006) noted lion population declines in several national parks in West and Central Africa. We find that 18 LCUs have lost their lions since 2006, with the greatest losses occurring in West and Central Africa (Supplemental materials, Table S3). All of these extirpations came from populations of fewer than 50 Liothyronine Sodium lions, and all but one (Nazinga-Sissili) were classified by the IUCN as having declining populations (IUCN 2006a, b). Strongholds Finally, we asked how many of these lions are in “strongholds?”

We will elaborate on the definition in the “Discussion” section. Given our simple criteria, 10 lion areas qualify. Four of these are in East Africa and six in Southern Africa (Table S1). These strongholds span eight countries, contain roughly 19,000 lions in protected areas alone (more than 50 % of the remaining lions in Africa), and over 24,000 lions in the entire lion areas as delineated. No areas in West or Central Africa qualify. Seven additional lion areas are potential lion strongholds, which contain nearly 4,400 lions (Table S1). These include two populations in West and Central Africa. The only remaining regions with potentially large numbers of lions that could act as future lion strongholds are Angola, Somalia, and the western half of South Sudan.

Conidiation noted after 1–2 days, green after 4–5 days, eventually 26–27F6–8, effuse, verticillium-like, on aerial hyphae in up to 4(–5) indistinctly separated, downy concentric zones, and dry and regularly tree-like in tufts eventually compacted to dense pustules of 0.5–3 mm diam, aggregating to 12 mm length, in Trichostatin A ic50 concentric zones or irregularly distributed on the plate. Conidia formed in numerous wet heads growing to 60(–90) μm diam. At 15°C conidiation in irregular, loose green 26DE4–5 tufts to 6 mm long. At 30°C growth slower than on CMD and PDA; margin with irregular outgrowths; conidiation

effuse, powdery or finely granular. Habitat: on wood and bark of deciduous trees, in Central Europe chiefly on Fagus. Distribution: Central Europe (Austria),

Eastern North America. Holotype: USA, Tennessee, Great Smoky Mts. National Park, vic. Cosby, Albright Trail, on decorticated wood, July 2005, B.E. Overton 04-04 (BPI 870964A; holotype of anamorph BPI CDK inhibitor 870964B; ex-type culture G.J.S. 04-158 = CBS 119233; not examined). Specimens examined: Austria, Kärnten, Klagenfurt Land, Obermieger, Sabuatach, MTB 9452/2, 46°35′22″ N, 14°27′03″ E, elev. 650 m, at forest edge, on twigs of Corylus avellana 2–4 cm thick, on inner bark, soc. Bisporella citrina, 14 Oct. 2006, W. Jaklitsch, W.J. 3020 (WU 29454, culture C.P.K. 2488). St. Margareten im Rosental, Sabosach, MTB 9452/3, 46°32′23″ N, 14°24′40″ E, elev. 550 m, on decorticated branches of Fagus sylvatica 1–2.5 cm thick, on wood, soc. Exidia truncata, old Neodasyscypha cerina; pulvinate, light bluish green anamorph, 25 Oct. 2004, W. Jaklitsch, W.J. 2783 (WU 29448, culture CBS 119503 = C.P.K. 1994). Same locality, on decorticated branch of Fagus sylvatica 5–6 cm thick, on wood, soc. Lophiotrema nucula, Resupinatus applicatus, rhizomorphs, Corticiaceae, a myxomycete; holomorph, 9 Jul. 2007, W. Jaklitsch,

W.J. 3117 (WU 29455). St. Margareten im Rosental, Zabrde, MTB 9452/4, 46°32′59″ N, 14°25′12″ E, elev. 565 m, on learn more partly decorticated branch of Fagus sylvatica Palmatine 1–1.5 cm thick, on wood, 29 Oct. 2005, H. Voglmayr & W. Jaklitsch, W.J. 2869 (WU 29453, culture C.P.K. 2424). Niederösterreich, Hollabrunn, Hardegg, Semmelfeld, between Niederfladnitz and Merkersdorf, MTB 7161/3, 48°48′49″ N, 15°52′43″ E, elev. 450 m, on partly corticated branch of Quercus petraea 4 cm thick, on wood and resupinate polypore, 21 Jul. 2004, H. Voglmayr & W. Jaklitsch, W.J. 2531 (WU 29446, culture CBS 119504 = C.P.K. 1614). Melk, Loosdorf, Dunkelsteiner Wald, 0.7 km south from Umbach, MTB 7758/4, 48°14′04″ N, 15°25′48″ E, elev. 370 m, on branch of Fagus sylvatica on the ground in leaf litter, on wood, 5 Oct. 2004, W. Jaklitsch, W.J. 2768 (WU 29447, culture C.P.K. 1993). Wien-Umgebung, Mauerbach, east from the cemetery, MTB 7763/1, 48°15′11″ N, 16°10′22″ E, elev. 330 m, on partly decorticated branch of Fagus sylvatica 4 cm thick, on wood, soc. young Hypoxylon rubiginosum, holomorph, 24 Sep.