coli core enzyme saturated with E chaffeensis recombinant σ70 su

coli core enzyme saturated with E. chaffeensis Selleckchem GF120918 recombinant σ70 subunit (Figure 7). Figure 6 Transcriptional analysis of recombinant E. chaffeensis -σ 70 using pRG198 transcriptional template. C, transcription products by E. coli core enzyme alone; σ70, transcription products by the recombinant E. chaffeensis σ70 protein; N, transcription products by purified E. chaffeensis RNAP; C + σ70, transcription products by by E. coli core enzyme saturated with recombinant

E. chaffeensis σ70; N + σ70, transcription products by native purified enzyme saturated with recombinant E. chaffeensis-σ70. Figure 7 Transcription of pRG198 with varying potassium acetate concentrations showing transcription by E. chaffeensis RNAP GSK2118436 datasheet saturated with the recombinant σ 70 and Selleckchem ACP-196 by E. coli core RNAP reconstituted with recombinant σ 70 . Modulation of E. chaffeensis RNAP activity by whole-cell protein We evaluated the effect of E. chaffeensis whole-cell protein lysate, prepared from the bacteria grown in macrophage cell line, on transcription of p28-Omp14 and p28-Omp19 constructs using the native purified enzyme. The resulting

transcripts were analyzed by two independent methods; densitometry of radiolabeled transcripts and the Taq-Man probe-based, real-time RT-PCR. These analyses showed enhanced transcriptional activity in the presence of 4 μg of E. chaffeensis whole-cell lysate. Densitometric analysis revealed a 1.8-fold increase in transcriptional signal for the p28-Omp14 promoter construct and a 2.1-fold increase for p28-Omp19 construct

(Table 2). Addition of the same amount of protein yielded a Decitabine mouse similar fold increases when transcription was assessed with E. coli core enzyme saturated with E. chaffeensis recombinant σ70. No transcription occurred with the addition of whole-cell lysate alone in the absence of an enzyme, a potential source of E. chaffeensis RNAP. Similarly, the addition of boiled lysate did not cause any change in transcriptional signals. Quantitation by real-time RT-PCR for the calculation of fold increase in transcription in the presence of E. chaffeensis whole-cell protein lysate was carried out as described previously [30, 31]. Transcription of p28-Omp19 construct with purified E. chaffeensis RNAP, as quantified by real-time RT-PCR, showed a 2.24 fold enhancement in the presence of 4 μg of the protein lysate, whereas transcription of p28-Omp14 promoter construct resulted in a 1.81 fold-enhancement (Table 2), indicating a higher degree of agreement between the data generated by densitometric and real-time RT-PCR methods of quantitation (Table 2). Table 2 Effect of macrophage-culture grown E.

Next, the nanobelts were transformed on another silicon chip, and

Next, the nanobelts were transformed on another silicon chip, and Au markers BX-795 research buy had been produced on the silicon chip in advance through photolithography. The prepared samples were mounted into the vacuum chamber of the ion implanter and implanted by N+ ions with

30 keV. The choice implantation fluences include 5 × 1015, 1 × 1016, and 5 × 1016 ions/cm2. The photoluminescence spectra of every marked CdS nanobelts were detected by the micro-Raman system (LabRAM HR800, HORIBA Ltd., Minami-Ku, Kyoto, Japan) both before and after ion implantation. Surface morphology images of CdS nanobelts were acquired through SEM (FEI Sirion FEG, FEI Company, Hillsboro, OR, USA). Figure 13a,b shows schematic diagrams of the transfer process and implantation process, respectively. Figure 13c,d,e displays the SEM and optical image of the CdS nanobelts. Figure 13 Schematic diagram and optical and SEM images of processes. The schematic diagram of (a) the transform process and (b) implantation process. (c, d) The optical and (e)

SEM image of the nanobelts grown by thermal evaporation process. Figure 14 shows the PL emission spectrum of single CdS nanobelts at room temperature. All the curves in Figure 14a signify the PL emission spectrum of the same nanobelt; Figure 14b,c represents two other nanobelts. In the case of the dose of 5 × 1015 ions/cm2, the PL emission spectrum of the unimplanted nanobelt has three emission peaks at about 505, 617, and 770 nm. The peak at

505 nm originates from the near-band-edge emission of CdS, and the broad emission band at 617 nm is associated with the low density of sulfur vacancies in the CdS nanobelt [65]. The peak at buy Dinaciclib 770 nm is related to the transitions between the surface states and the valence band of CdS [66, 67]. After ion implantation, the near-band-edge emission peak was red-shifted, and the defect emission Metalloexopeptidase peak was quenched. Later, all the samples were annealed in an argon atmosphere at 350°C for 40 min. The crystalline quality of the CdS nanobelts recovered obviously after annealing in argon atmosphere. In the red emission region, the annealed nanobelts have an emission peak at 750 nm. This may be attributed to the surface defect similar to that of unimplanted nanobelts and/or the high density of sulfur vacancies caused by ion implantation [65, 68]. Unimplanted nanobelts have a defect emission peak at 617 nm caused by a small number of sulfur vacancies generated during growth process. After ion implantation and the annealing process, the concentration of sulfur vacancies increased observably; although the annealing process could recover the crystal lattice and reduce sulfur vacancies, a mass of sulfur vacancies still remained in the lattice after annealing. The emission peak at 526 nm may be attribute to the N+ ions implanted into the crystal lattice and selleck products substituted S as a shallow acceptor; this process resulted in the red shift of the band-edge emission peak.

1% (95% CI 79 6, 92 1; p < 0 0001) during the first follow-up per

1% (95% CI 79.6, 92.1; p < 0.0001) during the first follow-up period.[24] Similar results were also demonstrated in the second follow-up period (2005–6) and when both follow-up periods were combined. For all follow-up periods, vaccine efficacy was also significant (p < 0.0001) against severe

RVGE (defined as a score of ≥11 on the 20-point Vesikari scale), RVGE requiring hospitalization, and RVGE requiring medical attention. In addition, vaccine efficacy against any and severe RVGE caused by each of the rotavirus G types identified (G1, G2, G3, G4, and G9) was significant (p ≤ 0.02) in the combined efficacy follow-up period.[24] Various naturalistic studies conducted selleckchem in developed countries have demonstrated the ‘real-world’ effectiveness of rotavirus vaccination after introduction of the vaccine for routine use in the community setting. Typically, these studies compared various outcomes, such as the numbers of RVGE cases, RVGE-related hospitalizations, and/or emergency department visits, that occurred during the

pre-vaccination period with those that occurred during a specific Emricasan period after widespread or universal introduction of a rotavirus vaccination program. Studies conducted in the Australian state of Queensland[27] and in European countries[28–30] involved rotavirus vaccination programs with either the monovalent or pentavalent rotavirus vaccine, whereas studies conducted in the US generally focused only on the pentavalent vaccine (reviewed elsewhere[31,32]). Rotavirus vaccine RIX4414 was generally well tolerated in clinical trials,

with an overall tolerability profile similar to that of placebo.[21,23] heptaminol There was no increased risk of MAPK inhibitor intussusception with rotavirus vaccine RIX4414 in a large (n = 63 225), placebo-controlled, pre-licensure safety study conducted in Latin America and Finland.[21,25] However, interim results from a postmarketing active surveillance study conducted in Mexico, along with worldwide passive surveillance data, suggest that there may be an increased risk of intussusception during the first 7 days after administration.[21] Both the US prescribing information[21] and the EU summary of product characteristics[23] state that rotavirus vaccine RIX4414 should not be administered to infants with a previous history of intussusception or to those with uncorrected congenital malformation of the gastrointestinal tract (e.g. Meckel’s diverticulum) that would predispose them to intussusception. 3.

The activity of each promoter was measured

using a β-gala

The GDC-0994 clinical trial activity of each promoter was measured

using a β-galactosidase assay during exponential growth. Although ΔrpoE was observed to have a slightly prolonged lag phase relative to wild type cells under these experimental conditions, at later time points the mutant grew similarly to wild type. To account for any differences in growth kinetics of the cultures, all data was normalized to the optical density at 600 nm of the culture, which permitted direct comparisons. In wild type cells, promoter activity from all the transcriptional fusions was high, as expected, because LPM medium is highly inducing for SsrB activity [21]. In contrast, promoter activity for sseA, ssaB, and sifA decreased in the rpoE mutant compared to wild type cells (Figure 2A, B and 2D), whereas promoter activity from the ssaG and srfN reporters was upregulated in the rpoE mutant (Figure 2C and 2F). β-galactosidase activity observed from the Adriamycin sseL reporter was unaltered in the rpoE deletion compared

to that in wild type cells (Figure 2E). These data are consistent with the protein levels detected for these gene products. Together, these data indicate that σE can have a variable and bidirectional effect on SsrB-regulated virulence genes. Figure 2 The transcriptional activity of SsrB-regulated virulence genes is affected by an rpoE deletion. Wild type and ΔrpoE cells carrying single-copy PU-H71 cost chromosomal transcriptional reporters of (A) PsseA::pPsseA-lacZ, (B) PssaB::pPssaB-lacZ, (C) PssaG::pPssaG-lacZ, (D) PsifA::pPsifA-lacZ, (E) acetylcholine PsseL::pPsseL-lacZ and (F) PsrfN::pPsrfN-lacZ were grown in LPM (pH 5.8). At the indicated time β-galactosidase activity was measured

and expressed as relative light units (RLU) normalized to optical density of the culture. Wild type and ΔrpoE cells lacking the transcriptional reporters were used as controls in each experiment. Data are the means with standard error from triplicate determinations from three independent experiments. The effect of RpoE on virulence genes is downstream of ssrB expression The variable effects of rpoE deletion on SsrB-regulated effectors suggested that RpoE might direct transcription downstream of ssrB expression. To test this, we replaced the ssrB gene in ΔrpoE and wild type cells with an ssrB::FLAG allele [19] and examined the levels of SsrB protein in the strains by western blot. There was no change in the levels of SsrB-FLAG between wild type and ΔrpoE cells (Figure 3), indicating that the effects of RpoE on the four classes of virulence gene promoters examined here was not mediated through changes to SsrB protein levels. Together these data establish a role for RpoE in the fine-tuning of virulence gene expression in S. Typhimurium. Figure 3 The effect of RpoE on SsrB-regulated genes is downstream of ssrAB expression. The ssrB gene in wild type and ΔrpoE cells was replaced with an ssrB-FLAG allele in its native location on the chromosome.

(A) DNA: effect of NaCl (0 to 500 mM), Imu3 concentrations 0 3, 0

(A) DNA: effect of NaCl (0 to 500 mM), Imu3 concentrations 0.3, 0.6 and 1.2 μg. (B) DNA: effect of temperature (10-min incubation), Imu3 additions 0.0625 to 1.0 μg (two fold increase/step). (C) DNA: effect of Mg2+ ions, Imu3 concentrations 0.3, 0.6 and 1.2 μg. (D) RNA: Imu3 additions 0.312 to 10 μg (two fold concentration increase/step). (A, B, C, D) M: λ/PstI DNA marker; C: control (pUC19/EcoRI alone). Furthermore, thermal denaturation JNK-IN-8 curves (A260) showed a stabilising

effect of Imu3 on the linear double-stranded DNA molecule. The melting temperature (determined graphically) of DNA alone was 73°C, which increased by 3°C (Tm = 76°C) when an aliquot eFT508 purchase of 0.3 μg Imu3 was added in the EMSA studies. The DNA melting temperature was further raised by an additional 13°C

(Tm = 89°C) when a 1 μg aliquot of Imu3 was added. This concentration of Imu3 saturated the DNA, and the melting curve revealed a two-phase thermal transition. One transition showed a stabilisation effect (89°C), whereas the other transition (at 63°C) was shown to be destabilising (in terms of thermal stability), most probably due to partial DNA precipitation (Figure  5). Figure 5 Thermal denaturation curves of 100 ng pUC19/ Eco RI DNA. DNA alone (solid CH5424802 datasheet line); DNA with Imu3 at 0.3 μg (dashed line) and 1.0 μg (dotted line). Signal of Imu3 alone was subtracted where necessary, and all curves were normalised. The arrows indicate the Tm values. Minimal DNA length for Imu3 binding Binding of short DNA fragments to Imu3 occupied all

its free DNA binding sites, and therefore prevented subsequent binding of Imu3 to indicator DNA (EcoRI linearised pUC19). Cytidine deaminase These EMSA tests showed that free Imu3 starts to bind to oligonucleotides longer than 11 base pairs, observed as the reappearance of unbound indicator DNA (absence of precipitation). These results indicate that 11 base pairs is the minimal DNA length required for Imu3 binding (Figure  6). Figure 6 Electromobility shift assay with short DNA fragments on 0.8% agarose gel. pUC19, plasmid alone; pUC19 + I, plasmid with Imu3 protein. Lane numbers correspond to number of bases in single-stranded DNA oligonucleotides used (i.e. 6, 7, 8, 9, 10, 11, 12, 13, 14 and 15 bases long). Lanes 6-15, after incubation of Imu3 and corresponding oligonucleotide, 100 ng linear pUC19/EcoRI DNA (target) was added. M: λ/PstI marker. EMSA tests with short double stranded DNA fragments (re-annealed oligonucleotides) were also performed however, the results were inconclusive since we repeatedly observed the recurring effect of unbound Imu3 that re-/dis-appeared every 3-5 nucleotides of the oligonucleotide length; however, the underlying basis of this phenomena is unclear. Separation of Imu3 from DNA and subsequent DNA integrity analysis Separation of the DNA-Imu3 complex, was examined under different conditions.

Nat New Biol 1971,233(35):12–14 PubMed 11 Lafontaine D, Vandenha

Nat New Biol 1971,233(35):12–14.PubMed 11. Lafontaine D, Vandenhaute J, Tollervey D: The 18S rRNA dimethylase Dim1p

is required Selleck Natural Product Library for pre-ribosomal RNA processing in yeast. Genes Dev 1995,9(20):2470–2481.PubMedCrossRef 12. Condon C: RNA processing and degradation in Bacillus subtilis. Microbiol Mol Biol Rev 2003,67(2):157–174.PubMedCrossRef 13. Bergman MA, Loomis WP, Mecsas J, Starnbach MN, Isberg RR: CD8(+) T cells restrict Yersinia pseudotuberculosis infection: bypass of anti-phagocytosis by targeting antigen-presenting cells. PLoS Pathog 2009,5(9):e1000573.PubMedCrossRef 14. Shah DH, Zhou X, Kim HY, Call DR, Guard J: Transposon mutagenesis of Salmonella Enteritidis identifies genes that contribute to invasiveness in human and chicken cells and survival in egg albumen. Infect Immun in press 15. McCoy LS, Xie Y, Tor Y: Antibiotics that target protein synthesis. Wiley Interdiscip Rev RNA 2011,2(2):209–232.PubMedCrossRef 16. Comartin DJ, Brown ED: Non-ribosomal factors in ribosome subunit assembly are emerging targets for new antibacterial drugs. Curr Opin Pharmacol 2006,6(5):453–458.PubMedCrossRef 17. Campbell TL,

Henderson J, Heinrichs DE, Brown ED: The yjeQ gene is required for virulence of Staphylococcus aureus. Infect Immun 2006,74(8):4918–4921.PubMedCrossRef 18. Clatworthy AE, Pierson E, Hung DT: Targeting virulence: a new paradigm for antimicrobial therapy. Nat Chem Biol 2007,3(9):541–548.PubMedCrossRef Veliparib chemical structure 19. Barczak AK, Hung DT: Productive steps toward an antimicrobial targeting virulence. Curr Opin Microbiol 2009,12(5):490–496.PubMedCrossRef 20. Arnaud M, Chastanet A, Debarbouille M: New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, gram-positive bacteria. Appl Environ Microbiol 2004,70(11):6887–6891.PubMedCrossRef

21. O’Farrell HC, Pulicherla N, Desai PM, Rife JP: Recognition Clomifene of a complex substrate by the KsgA/Dim1 family of enzymes has been conserved throughout evolution. RNA 2006,12(5):725–733.PubMedCrossRef Competing interests The authors declare that they have no competing interests. Authors’ contributions HCO carried out all experiments and drafted the manuscript. JPR conceived of the study, participated in its design and coordination, participated in construction of the knockout strain, and helped to draft the manuscript. All authors read and approved the final manuscript.”
“Background Streptococcus pneumoniae infections remain a major cause of morbidity and mortality worldwide, causing diseases which range in severity from otitis media and sinusitis, to pneumonia, septicaemia and meningitis [1]. S. pneumoniae is a commensal of the human nasopharynx [2]. The diversity of pneumococci was first evidenced by serotyping of their capsular polysaccharides resolving into more than 93 serotypes [3, 4]. However, only 16 serotypes cause approximately 90% of invasive disease worldwide [1, 5].

N Engl J Med 2007, 356:1670–4 PubMedCrossRef 43 Fischer OM, Stre

N Engl J Med 2007, 356:1670–4.PubMedCrossRef 43. Fischer OM, Streit S, Hart S, Ullrich A: Beyond Herceptin and Gleevec. Curr Opin Chem Biol 2003, 7:490–5.PubMedCrossRef 44. Garrett TP, McKern NM, Lou M, Elleman TC, Adams TE, Lovrecz GO, Kofler M, Jorissen RN, Nice EC, Burgess AW, Ward CW: The crystal structure of a truncated ErbB2 ectodomain reveals an active conformation, poised to interact with other ErbB receptors. Mol Cell 2003, 11:495–505.PubMedCrossRef 45. Haffty BG, Yang Q, Reiss M, Kearney T, Higgins SA, Weidhaas J, Harris L, Hait W, Toppmeyer D: Locoregional relapse and distant metastasis in conservatively managed triple negative early-stage breast cancer.

J Clin Oncol 2006, 24:5652–7.PubMedCrossRef 46. Leong CO, Vidnovic N, DeYoung MP, Sgroi DNA Damage inhibitor D, Ellisen LW: The p63/p73 network mediates chemosensitivity to cisplatin in a biologically defined subset of primary breast cancers. J Linsitinib in vivo Clin Invest 2007, 117:1370–80.PubMedCrossRef 47. Rakha EA, El-Sayed ME, Menon S, Green AR, Lee AH, Ellis IO: Histologic grading is an independent prognostic factor in invasive lobular carcinoma of the breast. Breast Cancer Res Treat 2008, 111:121–7.PubMedCrossRef 48. Kriege M, Seynaeve C, Meijers-Heijboer H, Collee JM, Menke-Pluymers MB, Bartels CC, Tilanus-Linthorst

MM, Blom J, Huijskens E, Jager A, van den OA, van GB, Hooning MJ, Brekelmans CT, Klijn JG: Sensitivity to First-Line Chemotherapy for Metastatic Breast Cancer in BRCA1 and BRCA2 Mutation Carriers. J Clin Oncol 2009. 49. Imyanitov EN: Breast cancer therapy for BRCA1 carriers: moving towards platinum standard? Hered Cancer Clin Pract 2009, 7:8.PubMedCrossRef 50. Farmer H, McCabe N, Lord CJ, Tutt AN, Johnson DA, Richardson TB, Santarosa M, Dillon KJ, Hickson I, Knights C, Martin NM, Dichloromethane dehalogenase Jackson SP, Smith GC, Ashworth A: Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy. Nature 2005, 434:917–21.PubMedCrossRef

51. Lord CJ, Garrett MD, Ashworth A: Targeting the double-strand DNA break repair pathway as a therapeutic strategy. Clin Cancer Res 2006, 12:4463–8.PubMedCrossRef 52. Fong PC, Boss DS, Yap TA, Tutt A, Wu P, Mergui-Roelvink M, Mortimer P, Swaisland H, Lau A, O’Connor MJ, Ashworth A, Carmichael J, Kaye SB, Schellens JH, de Bono JS: Inhibition of Poly(ADP-Ribose) buy PD0332991 Polymerase in Tumors from BRCA Mutation Carriers. N Engl J Med 2009. 53. Calabrese CR, Almassy R, Barton S, Batey MA, Calvert AH, Canan-Koch S, Durkacz BW, Hostomsky Z, Kumpf RA, Kyle S, Li J, Maegley K, Newell DR, Notarianni E, Stratford IJ, Skalitzky D, Thomas HD, Wang LZ, Webber SE, Williams KJ, Curtin NJ: Anticancer chemosensitization and radiosensitization by the novel poly(ADP-ribose) polymerase-1 inhibitor AG14361. J Natl Cancer Inst 2004, 96:56–67.PubMedCrossRef 54.

The PCR amplifications were performed in a 25 μl volume containin

The PCR amplifications were performed in a 25 μl volume containing 0.4 μM of each universal primer, 1.5 mM MgCl2, 0.2 mM of each dNTP, 0.5 U Taq polymerase and 1 × reaction buffer (Bioline) and 8 ng template DNA. The PCR amplification consisted of 35 cycles of denaturation at 94°C

for 30 sec, primer annealing at 50°C for 45 sec, and primer extension at 72°C for 1 min; an initial denaturation step of 94°C for 5 min, and a final extension at 72°C for 5 min. Amplicons were then sent for sequencing to Inqaba Biotec (Pretoria, South Africa). Sequenced fragments were aligned using ClustalX [30] in order to identify polymorphisms. For species that showed no significant polymorphisms of the internal transcribed spacer (ITS) regions of the rRNA complex, a different conserved region, namely the elongation factor selleck compound 1- alpha (EF-1 α) gene, was amplified using primers EF1 and EF2 [31]. The monoplex PCR amplifications were performed in a 20 μl volume containing 0.4 mM of each forward and reverse primer, 0.25 mM of each dNTP, 1× reaction buffer (Bioline), 0.5 U Taq polymerase (Bioline) and 6 ng template DNA. The PCR amplification consisted of 30 cycles of denaturation at

94°C for 30 sec, primer annealing at 57°C for 45 sec, and primer extension this website at 72°C for 1 min; an initial denaturation of 94°C for 5 min, and a final extension of 72°C for 7 min. The amplified fragments were then column-purified (QIAquick PCR purification Kit, QIAGEN GmbH) and sent for sequencing to Inqaba Biotec (Pretoria, South Africa). The ITS and EF-1 α sequences were then submitted to selleck chemicals llc GenBank [GenBank:FJ864706, GenBank:FJ864709, GenBank:FJ864710, GenBank:FJ864708, GenBank:FJ864711, GenBank:FJ864703, GenBank:FJ864704, GenBank:FJ864705,

GenBankFJ864707, and GenBank:FJ864712] and served as targets for the design of multiple probes for each species which are able to discriminate between the forty Levetiracetam fungal isolates. The sequences of the conserved regions were aligned using the ClustlX software [30], manual adjustments were made and areas of interspecies variation were identified. These regions were used for the design of genus- and species-specific probes of various lengths (14-25 bases) and within a narrow range of the melting temperature of 56°C (± 5°C). All oligonucleotide probes were designed using the Primer Designer 4 package (Version 4.2, Scientific and Educational Software, Cary, NC). The probe set was then extended by searching public databases (NCBI and EMBL) for genus-or species-specific oligonucleotide probes. The specificity of each oligonucleotide was assessed by conducting BLAST searches and only unique oligonucleotide probes were chosen to be printed onto the array.

2 (a) For each of 12 activities selected on the basis of a previ

2. (a) For each of 12 activities selected on the basis of a previous study (Wind et al. 2005) as representative of the physical work ability of claimants with MSD (walking, sitting, standing, lifting/carrying, dynamic movement of the trunk, static bending of the trunk, reaching, movement above shoulder height, kneeling/crouching and three activities related RAD001 cost to hand and finger movements), the IP was asked whether the FCE information caused him to revise his initial assessment of the claimant’s ability upwards or downwards, or if it did not change the original assessment. (b) The IP was asked whether the FCE information had reinforced his initial assessment of the claimant’s physical work ability. The response categories were,

again, dichotomous: yes or no.   3. Finally, the IP was asked whether he would consider using FCE in the future to support assessment of the physical work ability of disability benefit claimants; and if so, why, and for what groups of claimants in particular. If

he did not favor the use of the FCE, the IP could also state their reasons for this view.   Data analysis Descriptions of IPs and claimants were calculated. Age and years of experience of IPs were expressed as mean and standard deviation (SD). The other characteristics of STA-9090 datasheet IPs, such as gender and familiarity with FCE, were noted in numbers and percentages. The age of the claimants was expressed as mean and SD. The distribution of the location of the MSD (upper extremity, lower extremity, back and neck, or more than one location) was noted using numbers and percentages. The answer to the first question in the IP questionnaire (whether FCE information was regarded as having complementary value for the assessment of physical work ability) was scored as affirmative when at least 66% of the IPs answered yes to this question. Farnesyltransferase Differences between the groups of IPs that did and did not consider FCE information to be of complementary value, were studied using independent t tests for the relationship between work experience of IP and the outcome on the question about the complementary value of FCE information. Chi square tests

were used to assess differences between the two groups—IPs who do and do not consider the FCE information to be of complementary value—on familiarity with FCE (IPs), location of disorder of the S63845 cell line claimant, and claimant’s work status. Kendall’s tau-c was used to test the association between the two groups of IPs regarding the scores of the revised Oswestry outcome of the claimants. For the answers to the question about the change in IP judgment based on FCE information, the numbers and percentages of IPs in the three categories (IP’s assessment remained unchanged, increased, or decreased with respect to the claimant’s abilities) were noted for each of the 12 activities. In addition, these data and their relation to whether the IPs did or did not consider the FCE information to be of complementary value were tested using Chi square tests.

Cortical and subcortical tissue in section n Subperithecial tis

m. Cortical and subcortical tissue in section. Subperithecial tissue in section. o. Asci with ascospores in cotton blue/lactic acid. Scale bars: a, c, e, g = 0.5 mm. b, d, f = 0.3 mm. h = 0.1

mm. i, m–o = 10 μm. j = 25 μm. k, l = 5 μm Anamorph: Trichoderma koningii Oudem. in Oudemans & Koning, Arch. Néerl. Sci. Exactes Nat., Sér. 2, 7: 291 (1902). Fig. 7 Fig. 7 Cultures and anamorph of Hypocrea koningii (CBS 119500). a–c. Cultures at 25°C (a. on CMD, 14 days; b. on PDA, 13 days; c. on SNA, 14 days). d. Hyphae on agar surface (SNA, 15°C, 3 days). e, f. Chlamydospores (e. intercalary, f. terminal; 11 days). g–j. Conidiation on SNA, observed in the stereo-microscope (g. pustules, 25°C, 7 days; h–j. on aerial hyphae; h, i. 25°C, 3 days, j. 15°C, 8 days). k–n. Conidiophores (k. showing lageniform and ampulliform phialides; Metabolism inhibitor 5–6 days). o, Batimastat in vivo p. Phialides (5 days). q Conidial chains (7 days). r–u Conidia (6 days). e, f, k–u. On CMD, at 25°C. Scale bars: a–c = 15 mm. d = 50 μm. e, k, o, p, r, t = 10 μm. f, s, u = 5 μm. g = 3 mm. h–j, q = 30 μm. l–n = 15 μm Stromata when fresh 0.5–3 mm diam,

0.5 mm thick, solitary or gregarious, pulvinate, smooth, lively orange-brown. Stromata when dry (0.4–)0.8–1.8(–2.4) × (0.3–)0.6–1.3(–1.5) mm (n = 30), 0.15–0.45 mm (n = 20) thick; flat pulvinate, discoid or lenticular; margin free. Outline circular or oblong. Ostiolar dots (17–)22–34(–38) μm (n = 30) diam, typically invisible, only rarely distinct, convex to semiglobose, hyaline, or with a dark ring. Stromata when young white, the centre turning pale yellow or orange, eventually dark orange-brown to reddish brown, 7–8CE7–8, with or without white mycelial margin. Rehydrated stromata light orange-brown; ostiolar openings minute, hyaline; surface smooth, slightly velutinous. No change seen in 3% KOH. Stroma anatomy: Ostioles (42–)49–70(–84) Carnitine palmitoyltransferase II μm long, projecting to 15 μm, (12–)17–37(–50) μm wide at apex (n = 20), conical, without conspicuous apical cells. Perithecia (130–)145–180(–195) × (93–)110–160(–175) μm (n = 20), globose or flask-shaped. Peridium (11–)13–17(–20)

μm (n = 20) thick at the base, (6–)9–14(–16) μm (n = 20) thick at the sides, hyaline. Cortical layer (13–)16–23(–27) (n = 30), an orange-brown t. angularis of minute thin-walled cells (2–)3–6(–7) μm long (n = 60) in face view and in vertical section. Hairs on mature stroma (6–)8–11(–12) × 2–4(–6) μm (n = 20), 1–2 celled, ends rounded, cylindrical or globose, smooth or warty, yellow-orange to pale brown, surface warty by projecting cells. Subcortical tissue a loose t. intricata of hyaline thin-walled hyphae 2.5–4.0(–4.5) μm (n = 10) wide. Subperithecial tissue a dense t. epidermoidea of hyaline thin-walled cells (5–)6–14(–20) × (3–)4–9(–13) μm (n = 30).