Triplicate experiments were performed independently. Western blottings Western blottings using rabbit anti-human Bcl-2 antibody (#2876, Cell Signalling Technology)

and rabbit anti-human Bcl-xL antibody (556361, BD Biosciences) were performed according to standard protocols. Chemiluminescent detection was performed and images were captured by the FUJIFILM LAS-3000 system (Fujifilm, Tokyo, Japan). Extraction of RNA and RT –PCR Total RNA was extracted using TRIzol reagent (Invitrogen) according to the manufacturers’ this website recommendations. RT-PCR(Reverse-Transcription PCR) was used to compare the relative mRNA expression of Bcl-2 and Bcl-xL in breast cancer cell lines. The primer sequences used were: Bcl-2, sense, 5′- GTGAACTGGGGGAGGATTGT-3′ and antisense, 5′- GGAGAAATCAAACAGAGGCC-3′ and Bcl-xL, sense, 5′-CCCAGAAAGGATACAGCTGG-3′ and antisense, 5′- GCGATCCGACTCACCAATAC-3′. Thirty-two cycles of PCR were performed using the program of 30 s at 94°C, 30 s at 56°C and 1min at 72°C. The PCR products were electrophoresed on 2% agarose gel and imaged using a ChemiImag 5500 Imaging System (Alpha Innotech, San Leandro, CA, USA). Apoptosis assay MDA-MB-231 and MDA-MB-231R cells (1 × 106) were plated in 10 mm dishes for each data point. Following incubation overnight

at 37°C, the cells were treated with ABT-737 (1 μM, 24 hours) and irradiated with 4 or 12 Gy. After 24 h, apoptotic analyses were performed by flow cytometry, as described previously [18], using a FACS Calibur system (Becton Dickinson Biosciences, San Diego, CA) with ModFit GSK872 supplier LT™ software (Verity Software House, Inc.,

Topsham, ME). The apoptotic cells were analyzed by using quadrant statistics on the propidium iodide-negative and Annexin V-positive cells. Caspase-3 colorimetric assay The cells were collected and washed with phosphate-buffer saline (PBS, pH 7.2). After Epigenetics inhibitor centrifugation, the caspase 3 colorimetric assays were performed according to the manufacturer’s specifications (ab39401, Abcam) using a Sunrise Microplate Reader(Tecan US, Inc.,Charlotte, NC). Cell viability Cell viability was evaluated using Cell Counting Kit-8 (CCK-8; Selleckchem Cobimetinib Dojindo Molecular Technologies Inc., Gaithersburg, MD) assay. The cells were plated in 96-well plates at 1 × 104 cells/well with media only, media with ABT-737 (1 μM) or DMSO, which were changed with media 24 hours later. To evaluate cell viability, 10 μl of CCK-8 was added per well, and the cells were incubated for an additional 4 hours, Following the incubation, the absorbance at 450 nm was recorded using a 96-well plate reader (Sunrise Microplate Reader, Tecan US, Inc.,Charlotte, NC). Animal experiments The animals used in this study were 4 to 6-week-old athymic female BALB/c nu/nu mice which were provided by the Shanghai Institute of Materia Medica, Chinese Academy of Science. MDA-MB-231R cells (106) were implanted into the mammary fat pad.

VX-689 clinical trial Corrected visual acuity [16], contrast sensitivity [17], and depth perception [18] were measured. Orthostatic hypotension was defined

as a drop in systolic blood pressure of 20 mm Hg or more upon standing from a supine position after 1 min or if the standing systolic blood pressure is 90 or less. Cognitive function was assessed using the short Mini Mental State Examination [19] and impairment scored as <23 of 26 possible. Medications Participants were also asked to bring all of their prescription and nonprescription medications and supplement pills to the clinic. Use of central nervous system (CNS)-active medications at baseline (1986–1988) was obtained by self-report by asking questions focused on indication selleck compound for use; verification of use was accomplished by inspection of medication containers. Current use of antidepressants, antihistamines, barbiturates, benzodiazepines, muscle relaxants, and nonbenzodiazepine sedative hypnotics were assessed using two questions

“taken any medications in the past 12 months for anxiety or nerves or to relax muscles” and “taken any medications in the past 12 months to help you sleep.” Any use of antiepileptics was assessed using two questions “ever taken medications for seizures” and “what is the name of the drug you used the longest.” All medications taken for seizures (if current use), anxiety or nerves find more or to relax and help with sleep were reviewed and categorized by medication class. Physical function Self-reported difficulty (yes/no) on five Instrumental

Activities of Daily Living (IADLs) were recorded: walking two to three blocks, climbing up ten steps, preparing meals, doing heavy household chores, Farnesyltransferase and shopping [20]. Isometric hand-grip strength at 90° (Preston Grip Dynamometer; Takei Kiki Kogyo, Tokyo, Japan) was measured using the average of the right and left hands. Standing balance was assessed using a series of three tandem stands (side by side and semi- and full tandem). Each stance was held up to 10 s with eyes open and closed. Women were scored as poor if unable to hold the side by side or semi-tandem, fair if unable to hold the full tandem, and good if able to hold the full tandem. Time to perform five chair stands without using arms was recorded. Walking speed was measured over 6 m at a usual pace. Timed toe-tapping involved ten repetitions between alternating 7.5-cm-diameter circles on the floor spaced 30 cm apart. The number of step-ups completed while grasping a handrail in 10 s was obtained on a 23-cm-high step. Lifestyle Women were queried about smoking and alcohol. Smoking status (e.g.

Adv Mater 2011, 23:4918–4922.CrossRef 5. Balci S, Bittner AM, Hahn K, Scheu C, Knez click here M, Kadri A, Wege C, Jeske H, Kern K: Copper nanowires within the central channel of tobacco mosaic virus particles. Electrochim Acta 2006, 51:6251–6257.CrossRef 6. Klug A: The tobacco mosaic virus particle: structure and assembly. Philos Trans Biol Sci 1999, 354:531–535.CrossRef 7. Wang XN, Niu ZW, Li SQ, Wang Q, Li XD: Nanomechanical characterization of polyaniline coated tobacco mosaic virus

nanotubes. J Biomed Mater Res A 2008, 87A:8–14.CrossRef 8. Lee LA, Nguyen QL, Wu LY, Horyath G, Nelson RS, Wang Q: Mutant plant viruses with cell binding motifs provide differential adhesion strengths and morphologies. Biomacromolecules 2012, 13:422–431.CrossRef 9. Petrie TA, Raynor JE, Dumbauld DW, Lee TT, Jagtap S, Templeman KL, Collard DM, Garcia AJ: www.selleckchem.com/products/VX-680(MK-0457).html Multivalent integrin-specific ligands enhance tissue healing and biomaterial integration. Sci Transl Med 2010, 2:1–6.CrossRef 10. Kaur G, Wang C, Sun J, Wang Q: The synergistic

effects of multivalent ligand display and nanotopography on osteogenic differentiation of rat bone marrow stem cells. Biomaterials 2010, 31:5813–5824.CrossRef 11. Kaur G, Valarmathi MT, Potts JD, Jabbari E, Sabo-Attwood T, Wang Q: Regulation of osteogenic differentiation of rat bone marrow stromal cells on 2D nanorod substrates. Biomaterials 2010, 31:1732–1741.CrossRef 12. Wu LY, Zang JF, Lee LA, Niu ZW, Horvatha GC, Braxtona V, Wibowo AC, Bruckman MA, Ghoshroy S, zur Loye HC, Li XD, Wang Q: Electrospinning fabrication, structural and mechanical characterization check details of rod-like virus-based composite nanofibers. J Mater Chem 2011, 21:8550–8557.CrossRef 13. Li T, Winans RE, Lee B: Superlattice of rodlike virus particles formed in aqueous solution through like-charge attraction. Langmuir 2011, 27:10929–10937.CrossRef

14. Li T, Zan X, Winans RE, Wang Q, Lee B: Biomolecular assembly of thermoresponsive Quisqualic acid superlattices of the tobacco mosaic virus with large tunable interparticle distances. Angew Chem Int Ed 2013, 52:6638–6642.CrossRef 15. Agrawal BK, Pathak A: Oscillatory metallic behaviour of carbon nanotube superlattices – an ab initio study. Nanotechnology 2008, 19:135706–135706.CrossRef 16. Hultman L, Engstrom C, Oden M: Mechanical and thermal stability of TiN/NbN superlattice thin films. Surface Coatings Technol 2000, 133:227–233.CrossRef 17. Jaskolski W, Pelc M: Carbon nanotube superlattices in a magnetic field. Int J Quantum Chem 2008, 108:2261–2266.CrossRef 18. Wu MJ, Wen HC, Wu SC, Yang PF, Lai YS, Hsu WK, Wu WF, Chou CP: Nanomechanical characteristics of annealed Si/SiGe superlattices. Appl Surf Sci 2011, 257:8887–8893.CrossRef 19. Xu JH, Li GY, Gu MY: The microstructure and mechanical properties of TaN/TiN and TaWN/TiN superlattice films. Thin Solid Films 2000, 370:45–49.CrossRef 20.

826 nm), a big compressive phosphatase inhibitor stress may appear at the interface of the substrate and as-grown top film on it, and it will gradually release with the increase of the thickness of the film in order to reduce the compression. In our case, with enhancing film thicknesses from 200 to 1,030 nm, the residual stresses decrease

from 0.101 to 0.076. It is indicated that the compressive Ro-3306 stress caused by the lattice mismatch of the CeO2 cap layer and the above GdBCO film can be released when the film thickness comes up to a certain value such as 1,030 nm. It should be noted that a stress conversion appears at the thickness of 1,030 nm. Tensile stresses occur at one location far away from the CeO2 cap layer. Xiong et al. [10] found that the tensile stress appeared when the film thickness reached 1,000 nm.

Zeng et al. [11] have reported similar results. Xiong et al. believed that oxygen vacancies were the reason of the tensile stress [10], while Zeng et al. attributed Epigenetics inhibitor the tensile stress to the more a-axis grains and the bigger surface roughness value with increasing thickness of the film [11]. In our case, we believe that the increase of residual stress for thicker films, such as F1450 and F2100, may be due to the increase of a-axis grains in the GdBCO film, which will cause the tensile stresses in GBCO film’s (a, b) plane. A possible and simple growth model (shown in Figure 6) considering the lattice change is used to explain the variation of the stress with increasing thickness of the film. Figure 6 Schematic diagram of possible growth model for thick GdBCO films on CeO 2 /YSZ/CeO Tangeritin 2 -buffered Ni-W substrates. For the thinner GdBCO film, the film grows with lattice distortion, which results in compressive stresses. As the film thickness increases to a critical thickness, such as 1,030 nm, the GdBCO film grows with a standard lattice. Therefore, the compressive stresses are released. With the further increase of the thickness of GdBCO films, a-axis grains appear. At the same time, the bigger roughness value for thicker films will lead to tilted GdBCO

grains. The two factors result in tensile stress emergence. Oxygen content analysis by XPS XPS is performed to determine the oxygen content of the studied GdBCO films. The XPS measurement is under slot mode, and the analysis area is 700 × 300 μm2. The analysis chamber pressure is less than 5 × 10−9 Torr. Generally, only information from the surface of the film (5 to 10 nm) can be examined by XPS measurement. However, all the films are fabricated under the same conditions except for fabrication time. Hence, the XPS measurement of GdBCO films with different thicknesses is equivalent to the XPS depth profiling measurement of one thicker film. The spectra obtained for O 1s is shown in Figure 7. The O 1 s spectra consist of two peaks. The main peak at E B = 528 to 528.

Transport Cilengitide in vitro of 6-LP VLPs depends on E protein It is known that E protein interacts with viral receptors on the host cells [22–28] resulting in the induction of receptor mediated endocytosis [25, 29, 30]. To examine whether E protein is involved in the transport of VLPs, we generated chimeric VLPs using 6-LP and Eg VLPs. 6-LP

CM Eg E VLPs have C and M/prM proteins derived from 6-LP strain and E protein from Eg strain. Eg CM 6-LP E VLPs have C and M/prM protein from Eg strain and E protein from 6-LP strain. HUVEC were exposed to wild type or chimeric VLPs and transported VLPs were detected by IFU assay at 24 h p.i (Fig. 3). The transport of Eg CM 6-LP E VLPs was similar to that of wild type 6-LP VLPs and was MDV3100 cost significantly higher than those of 6-LP CM Eg E VLPs and wild type Eg VLPs (p < 0.01). 6-LP CM Eg E VLPs www.selleckchem.com/products/gsk1120212-jtp-74057.html were rarely transported across HUVEC as well as wild type Eg VLPs. These results suggest that the transport of VLPs across HUVEC is strongly affected by E protein. Figure 3 Role of WNV E protein in the transport of VLPs. HUVEC were exposed to 6-LP, Eg, 6-LP CM Eg E or Eg CM 6-LP E VLPs. After 24 h, media at the lower chamber were collected and subjected to IFU assay. The graphs show

the mean of three determinations. The error bars show SD. The results are representative of 2 independent experiments. * represents p < 0.01 (versus 6-LP). Multiple amino acid residues of E protein influence the transport of 6-LP VLPs The E proteins of the 6-LP and Eg strain differ at 4 amino acid residues. To determine

the residues that enhance the transport of 6-LP VLPs, we produced mutant VLPs (Table 1). 6-LP S156P VLPs and 6-LP V159I VLPs had significantly reduced transport compared to wild type 6-LP VLPs (p < 0.01) although the amount of transported VLPs was much higher than that of Eg VLPs (p < 0.01; Fig. 4A). As shown in Fig. 4B, Eg K93R VLPs and Eg T126I VLPs showed increased transport compared to wild type Eg VLPs (p < 0.05). The FER transport of Eg I159V was significantly increased (p < 0.01), although it was much lower than 6-LP VLPs. Previous studies reported that Ser 156 is involved in the N-linked glycosylation at 154, which is important for virulence and neuroinvasion [31–34]. Therefore, we expected that the transport of Eg P156 S would be increased. However, the transport of Eg P156 S VLPs was significantly lower than that of WT Eg VLPs (p < 0.01). These results suggest that multiple residues of E protein can influence the transport of VLPs. Table 1 Single and double mutant VLPs Name Wild type Position1 Substitution2 6-LP R93K 6-LP 93 R→K 6-LP I126T 6-LP 126 I→T 6-LP S156P 6-LP 156 S→P 6-LP V159I 6-LP 159 V→I Eg K93R Eg 93 K→R Eg T126I Eg 126 T→I Eg P156S Eg 156 P→S Eg I159V Eg 159 I→V 6-LP S156P V159I 6-LP 156, 159 S→P, V→I Eg P156 S I159V Eg 156, 159 P→S, I→V 1 Amino acid position of E protein.

PubMedCrossRef 43. Larkin MA, Blackshields G, Brown NP, Chenna R, McGettigan PA, McWilliam H, Valentin F, Wallace IM, Wilm A, Lopez R, Thompson JD, Gibson TJ, Higgins DG: Clustal W and Clustal X version 2.0. Bioinformatics 2007, 23:2947–2948.PubMedCrossRef 44. Drummond

AJ, Ashton B, Cheung M, Heled J, Kearse M, Moir R, Stones-Havas S, Thierer T, Wilson A: Geneious v4.0. 2008. 45. Swofford D: PAUP*. Phylogenetic analysis using parsimony (*and other methods). 4th edition. Sunderland, MA: Sinauer Associates; 2003. 46. Ronquist F, Huelsenbeck J: MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 2003, 19:1572–1574.PubMedCrossRef 47. Posada D, Crandall K: MODELTEST: testing the model of DNA substitution. Bioinformatics 1998, 14:817–818.PubMedCrossRef Authors’ contributions HL discovered the first asymmetric divider. RAZ and HL designed the study. HL collected the data. RAZ CDK activation provided reagents and equipment. RAZ Entospletinib clinical trial R406 clinical trial and HL analyzed and

interpreted the data and wrote the manuscript. Both authors read and approved the final manuscript.”
“Background Urease catalyzes the chemical hydrolysis of the urea molecule into CO2 and ammonia. These equilibrate in water causing a rise of the pH of the medium. Accordingly, bacterial ureases serve two main purposes: to neutralize acidic conditions, and to provide a source of assimilable nitrogen. Pathogenic bacteria exploit urease activity in different ways along the infectious Cyclooxygenase (COX) process. In Brucella spp, as well as in Helicobacter pylori, Klebsiella and Yersinia, urease allows bacteria to survive the acidic conditions encountered in the stomach during the gastrointestinal infection [1–5]. The role of bacterial ureases in infectious disease has been recently reviewed [6]. Ureases are complex enzymes generally composed of three structural subunits (UreABC). To assemble a functional urease, the cooperation of several accessory proteins is required

(UreEFGD) and, as a consequence, large gene clusters are needed to encode for functional ureases. Brucella contains two urease operons, both located in chromosome I. The Brucella ure1 operon contains the genes ureDABCEFG, and the Brucella ure2 locus shows the structure ureABCEFGDT [1]. The last gene of ure2, ureT, encodes a putative urea transporter homologous to Yut from Yersinia pseudotuberculosis [7]. Most Brucella species show a strong urease activity, derived from ure1 but not from ure2, and this activity is responsible for the ability of Brucella to survive stomachal transit and to establish a systemic infection [1, 2]. B. ovis is not able to infect the host by the gastrointestinal route, a fact that has been linked to its lack of urease activity [8]. Furthermore, purification and characterization of urease from B. suis showed the presence of urease subunits from ure1 but not from ure2 [9]. Strikingly, ure2 genes are transcribed in vivo [1, 2], suggesting that they play a role in Brucella.

To further investigate if the capsular polysaccharide accumulated in the cell, as would be anticipated if the exportation of capsule were interrupted, immunoblots and stains-all/silver stain with different cell fractions were performed (Figure 6). There was no TSA HDAC in vitro difference in K-antigen present outside or inside the cells between the Δwzabc mutant and the wild type. Therefore, our results suggested that the wza, wzb and wzc exportation system was not required by either K6-antigen or O3-antigen production in V. parahaemolyticus O3:K6. Figure

6 Immuno blot and stains-all/silver-stain of cell fractions. Outer membrane (OM) and cytoplasmic (CP) fractions were separated on polyacrylamide gel, then were either transferred to PVDF membrane and probed with K6 specific antiserum (A), or stained with stains-all/silver PXD101 datasheet stain (B). Lane1, wild type CP; lane 2, ∆wzabc CP; lane 3, ∆EPS CP; lane 4, wild type OM; lane 5, ∆wzabc OM; lane 6, ∆EPS OM. However, a K-antigen processing system similar to the O-antigen/capsule

polysaccharide genes in V. cholerae O139 [13, 20, 21] is present in V. parahaemolyticus. VP0219-0221 are homologous to wbfE, wbfF and wzz genes in V. cholerae O139, sharing 49%, 69% and 54% amino acid identities. Therefore a similar capsule processing mechanism may exist for both taxa. We generated an in frame deletion of VP0220, the wbfF homolog. Mutant ∆0220 displayed an intermediate level of translucence. Immunoblots indicated that deletion of VP0220 did not affect O3 antigen synthesis (Figure 4). However, the midpoint of the K-antigen band shifted https://www.selleckchem.com/products/shp099-dihydrochloride.html in this mutant, suggesting a role of VP0220 in the later Histamine H2 receptor stage of the K-antigen processing. Complementation of ∆0220 with over expressed wild type VP0220 gene restored mostly the pattern of the wild type K antigen (Figure 4). However, there was more reactive material away from the midpoint of the K-antigen band in the complemented mutant than the wild type (Figure 4), possibly due to the over expression of VP0220 or other reasons that remain unclear. Other K-antigen region features

A complete set of genes of the rhamnose pathway rmlBADC are present in the K-antigen genes of V. parahaemolyticus. However, four open reading frames, VP0225-0228, are inserted between the rmlD and rmlC genes. Analysis of the GC percentage revealed that the average GC percentage in VP0225-0228 is lower than the rest of the genes in this operon (Figure 2). The unusual arrangement of the rhamnose gene order and the mosaic GC percentage pattern indicated that there was a recent recombination event in the K antigen genes. Between gmhD and the K-antigen operon like genes, there are four genes (VP0215-0218) transcribed to the opposite direction (Figure 2). In frame deletion of these four genes led to the over expression of K-antigen polysaccharides (Figure 4), suggesting these genes may have a regulatory role in capsule expression.

An estimate of relative abundance of specific bacterial groups in samples was calculated by dividing their count on specific medium by that of total viable count selleck chemicals (LH) of each respective sample. This was done to compare the relative abundance of cultivated bacteria to those obtained via 16S rRNA analysis. DNA extraction During the shelf life

trials, fractions of tenfold diluted fish samples were collected and kept at -80°C until DNA extraction. Raw material and 20 storage trial samples were selected for 16S rRNA analysis. Template genomic DNA was isolated from one ml of these diluted samples as described before [44]. The sample was centrifuged at 11000 × g for 7 min to form a pellet. The supernatant was discarded and DNA was recovered from the pellet using Promega Magnesil KF, Genomic system (MD1460) DNA isolation kit (Promega Corporation, Madison, USA) in combination with KingFisher magnetic beads automatic DNA isolation instrument (Thermo Labsystems, Waltham, USA). 16S rRNA analysis The raw material and two samples from each treatment were selected for DNA analysis, from early storage (days 6-7) and late storage (13-15 in air samples and 21-28 in MA samples) resulting in a total of 21 samples. The PCR reaction was done by

amplifying the 16S rRNA gene with universal primers, 9F and click here 1544R (5′-GAGTTTGATCCTGGCTCAG-3 and ’5-CCCGGGATCCAAGCTTAGAAAGGA-3′ respectively). PCR reaction conditions, cloning and sequencing of the PCR products obtained from the cod samples was performed essentially as described before [45]. Sequencing was performed directly after the PCR reaction. Partial sequencing was performed with R805 primer; ’5-GACTACCCGGGTATCTAATCC-3′ resulting in 500-600 bp read length. The species coverage by the 16S analysis was estimated using the equation where C is coverage, n1 is the number of unpaired sequences (number of sequences that did not group with any other in the annealing) and Nt is the number of total clones analyzed. Multiple alignments were carried out using ClustalW

(v.1.83) and subsequent phylogenetic dendrogram of the 16S rRNA was plotted with the neighbour-joining software using NjPlot. Protirelin Terminal restriction fragment length polymorphism (t-RFLP) Extracted DNA from duplicate samples was pooled prior to PCR for the t-RFLP analysis. The PCR was performed with 9F forward primer (sequence above) with a 5′ FAM terminal label and HEX labelled reverse primer 805R. The labelled PCR products were digested with HaeIII and AluI (Fermentas, Hanover, MD, USA) in a 10 μL reaction volume for 2 h. The digested PCR product was diluted 1:20 and 2 μL added to 8 μL of GeneScan 500 LIZ internal size standard (Applied Biosystems, Warrington, UK) in formamide. The fragment analysis was carried out in ABI3730 DNA analyzer. A peak in the chromatogram, here after called terminal restriction fragment (t-RF), is regarded as one taxonomic unit. Data analysis was carried out on the GeneMapper software (v.4.

J Coastal Res 19:287–295 Yamano H, Kayanne H, Chikamori M (2005) An overview of the nature and dynamics of reef islands. Glob Environ Res 9:9–20 Yamano H, Kayanne H, Yamaguchi T, Kuwahara Y, Yokoki H, Shimazaki H, Chikamori M (2007) Atoll island vulnerability to flooding and inundation revealed by historical reconstruction: Fongafale Islet, Funafuti Atoll, Tuvalu. Glob Planet Change 57:407–416CrossRef Zachariasen J, Sieh K, Taylor FW, Edwards RL, Hantoro WS (1999) Submergence and uplift associated with the giant 1833 Sumatran subduction earthquake: evidence from coral microatolls. J Geophys Res 104:895–919CrossRef”
“Babel Fish: “Arthur Dent commented only ‘Eurgh!’ when first inserting

the fish into his ear. It enabled him to understand Vogon Poetry—not necessarily a good thing”. The Hitchhiker’s Guide to the Galaxy, Douglas Selleckchem P505-15 Adams. Introduction

We rely on common systems and quantitative signals (e.g., price, temperature, food calories) to support everyday decisions. Timely decisions are made, not with precise measures, but with familiarity and suitable approximations. Such quantitative intuition about sustainability is, for the most part, absent. There is a glaring void in our ability to quantify and capture the impact of our actions on sustainability. Although separate data streams are measured with increasing granularity, we do not have a way to grasp quantitatively the impact across different domains—e.g., Nintedanib (BIBF 1120) driving a car, heating a house, running an air conditioner or watering a lawn. Whether it is in formulating national policy, corporate GDC-0449 price strategy, or individual actions, we are muddling through a fog. This gap is not adequately filled with CO2 accounting. While CO2 addresses climate change, it is difficult to measure, does not provide quantitative intuition, and has also become a divisive issue that hinders the coalescence of political support. These concerns have

been noted by many, including Mackay (2009), who used basic physics principles to establish a per capita estimate of energy use to quantify sustainability. Having a quantifiable measure is only step one. In order to influence decisions, the measure must be readily observed and interpreted. Van Houwelingen and Van Raaiji 1989) reported that visual monitoring of energy expenses improves energy conservation by more than 12 %, but it persists only as long as the visual reminder is intact. In a recent study, Attari (2010) demonstrated that there is a gap between reality and perception even when limited to decisions involving a single type of energy like electricity used to operate lights and appliances. It adds to a growing literature demonstrating the value of feedback, preferably visual, in a broader decision-making context to motivate behavior leading to energy efficiency (Allcott 2010; Ariely 2008). The unmet need is for a visual, quantitative, and actionable system that can support decisions.

Apical fertile part of dry stromata. h–j. Stroma surface in the stereo-microscope (h. dry, showing inhomogeneous pigment distribution; i. rehydrated; j. in 3% KOH after rehydration). k, l. Stipe surface in the stereo-microscope (l. showing pigment flakes). m. Part of an ostiole in vertical section showing inflated marginal apex cells. n. Surface cells in face view. o. Perithecium in section. p. Cortical and subcortical tissue in section. q. Subperithecial tissue. r–u. Asci with ascospores (u. in cotton blue/lactic acid). a. L. Koukku Aug. 2007 (JOE). b, e, g, s. WU 29308. c, d, f, n, r. S. Huhtinen 07/98 (TUR). eFT-508 manufacturer h–m,

o–q, u. WU 29307. t. WU 29309. Scale bars: a, b, d = 10 mm. c = 5 mm. e–g = 1.5 mm. h = 250 μm. i, l = 0.5 mm. j = 150 μm. k = 2.5 mm. m, n, p–u = 10 μm. o = 30 μm Anamorph: Trichoderma sp. Fig. 33 Fig. 33 Cultures and anamorph of Hypocrea nybergiana. BI 10773 nmr a–c. Cultures after 14

days (a. on PDA. b. on PDA, reverse. c. on SNA). d. Stroma on OA (20°C, 3 weeks; photograph: G. Verkley, CBS). e. Conidiophore on aerial hypha on the growth plate (14 days). f–i. Conidiophores (14 days). j–l. Phialides (j. PDA, 10 days; k, l. 14 days). m. Thickened cell in aerial hypha (14 days). n–p. Conidia (n. PDA, 7 days; o, p. 28 days). a–p. All at 25°C. e–p. All on SNA except j, n. a–c, j, n. CBS 122500. d–i, k–m, o, p. CBS 122496. Scale bars: a–d = 15 mm. e = 30 mm. f, i = 20 μm. g, o = 15 μm. h, j–l, p = 10 μm. m, n = 5 μm Stromata not seen in fresh condition. Buspirone HCl Stromata when dry (37–)46–93(–106) mm (n = 11) long, cylindrical, clavate, sometimes nearly spathulate, straight or curved; sometimes hollow inside. Fertile part (13–)22–60(–76) mm (n = 16) long, comprising 40–60(–80)% of total length; typically gradually merging into the stipe, not sharply delimited, with fertile patches longitudinally decurrent on the stipe; typically laterally compressed and 5–15 × 2–8 mm (n = 12;19) thick. Apex rounded, sometimes strongly laterally compressed, 1–4.5 mm thick. Surface often with coarse, mostly

vertical wrinkles or folds, otherwise smooth to finely tubercular by slightly projecting perithecia. Ostiolar dots (47–)57–148(–236) μm (n = 130) diam, numerous, densely disposed, well-defined, diffuse when young, plane or convex, with roundish or oblong outline, and light centres, bright ochre to brown; large and diffuse close to the stipe. Colour of the fertile part resulting from white to yellow surface and ochre to brown ostiolar dots, always darker at the top, from yellowish, 4A3, close to the stipe, over greyish orange, 5–6B4–5, brown-orange, light brown, 6–7CD4–7(–8) to brown 7E5–8, at the apex. Pigment inhomogeneously distributed, under strong magnification sometimes appearing as minute stripes or appressed scales. Stipe (14–)19–44(–64) mm long, 1–9(–21) × 1–10(–20) mm thick (n = 18); base (2–)3–12(–20) mm (n = 14) thick, sometimes with white to yellowish basal mycelium.