Mei Li and Wen-rui Chang, as well as James P Allen, Chenda Seng,

Mei Li and Wen-rui Chang, as well as James P. Allen, Chenda Seng, and Chadwick Larson describe, in two separate contributions, the basics of Protein Crystallography and X-ray Diffraction. Depending on the resolution, this approach can give very detailed buy ICG-001 information on the geometric structure of the proteins, their cofactors, and sometimes of bound substrates or products; “snapshots” are taken on deep frozen crystalline samples and provide the structural basis for understanding how proteins function. Junko Yano and Vittal Yachandra describe how X-ray Spectroscopy

can be employed to obtain high-resolution data of metal–metal and metal–ligand distances in active sites of proteins without the need for crystallization of the protein. This technique and the related X-ray Fluorescence method described by Uwe Bergmann and Pieter Glatzel provide important information on the electronic structures of (metal) cofactors. While these X-ray spectroscopy experiments are currently mostly performed with samples frozen in different intermediate states of the catalytic cycle, kinetic X-ray spectroscopy experiments at room temperature can also

selleckchem be performed and these experiments have started to give important information on dynamic changes at (metal) cofactors sites. Solution structures and protein dynamics can be studied by X-ray Scattering (reviewed by David M. Tiede, Kristy L. Mardis and Xiaobing Zuo) and Neutron Scattering (reviewed by Jörg

Pieper, and Gernot Renger). These techniques promise to give us important insights into how motions help to tune the energetics of biological reactions. Carsten Krebs and J. Martin Bollinger explain in their review how the combination of Rapid Freeze-Quenching and Mössbauer Spectroscopy is able to reveal structural and electronic changes occurring at iron sites during biochemical reactions. Magnetic Resonance methods are the driving force to access photosynthesis at the molecular level. Martina Huber starts with an Introduction to Magnetic Resonance Methods in Photosynthesis. Anton Savitsky and Klaus Möbius discuss how High field EPR and its offshoots Electron Spin Echo (ESE), Electron-Nuclear Double Resonance (ENDOR), Electron Spin Echo Envelope Modulation (ESEEM), and Pulsed Electron Double Resonance www.selleck.co.jp/products/pci-32765.html (PELDOR), in conjunction with site-specific isotope or spin labeling and with the support of modern quantum-chemical computation methods, is capable of providing new insights into the photosynthetic transfer processes. Art Van der Est describes the application of Transient EPR to probe the geometry, electronic structure, and kinetics of electron transfer in reaction centers (RCs). Gerd Kothe and Marion C. Thurnauer demonstrate What you get out of High-time Resolution EPR. They describe the quantum oscillation phenomenon observed at short delay times, after optical excitation, from the spin-correlated radical pair in photosynthetic RCs.

Finally, two strains from women with mastitis (CJ11 and DG2S) wer

Finally, two strains from women with mastitis (CJ11 and DG2S) were resistant to streptomycin (> 1000 μg mL-1) and one strain (AQLI2) from the same group was resistant to vancomycin (16 μg mL-1). No strains resistant to these two antibiotics were found among the strains from healthy women. Table 2 Distribution of MIC’s to several antibiotics amongS. epidermidisisolated from mastitis and healthy women       Percentage of strains for which the MIC (μg mL-1) was as follows: Antibiotics Breast milk N° of strains ≤ 0.03 0.12 0.25 0.5 1 2 4

8 > 8   PEN H 36 17 8   8 14 14 8 11 19     M 40 10 5 5 8 10 33 8 8 18   AMP       ≤ 0.12 0.25 0.5 1 2 4 8 100 > 100   H 36   19 6 17 22 8 8 6 14     M 40 Doxorubicin research buy   15 8 5 23 20 10 5 13 3 OXA         ≤ 0.25 0.5 1 2 > 2         H 36     11 31 11 8 39         M 40     5 8 13 8 68       CIP         ≤ 0.25 0.5 1 2 > 2         H 36     47 39 8   6         M 40     30 38 18 3 13       CHL                   ≤ 8 16 > 16   H 36               75 17 8   M 40               78 10 13 ERY         ≤ 0.25 0.5 1 2 4 > 4       H 36     39 14 6 8   33       M

40     23 15     3 60     CLI           ≤ 0.5 1 2 > 2         H 36       81 8 3 8         M 40       70 3   28       TET                 ≤ 4 8 > 8     H 36             56 19 25     M 40             68 8 25   VAN           ≤ 0.5 1 2 4 8 16 ≥ 16   H 36         44 50 6         M 40         43 48 5 3 3   MUP                 ≤ 4 256 > 256     H 36             78 11 11     M 40             58 13 30   H: strains

isolated from healthy women; M: strains isolated from mastitis-suffering women; PEN: penicillin; AMP: ampicillin; OXA: oxacillin; CIP: Pirfenidone ic50 ciprofloxacin; new CHL: chloramphenicol; ERY: erythromycin; CLI: clindamycin; TET: tetracycline; VAN: vancomycin; MUP: mupirocin. Statistically-significant differences between isolates from mastitis and healthy women are in bold. Presence ofmecAand SCCmectyping Among the 41 strains showing oxacillin resistance, themecA gene could be detected by PCR in 37 (25 from mastitic milk and 12 from milk of healthy women). No amplification was observed in two strains of each group (F12 and CJ9; LI5081 and LC047, respectively), which had shown an oxacillin MIC value of > 2 μg mL-1. In contrast, themecA gene was detected in five oxacillin susceptible strains, one from a mastitis case (YLIC13) and four from healthy women (LO5RB1, LX5RB3, LV221 and LCC5082). The type of SCCmecwas determined in all themecA+strains. TheccrB gene could be amplified from 22 of the 26mecA+strains from the mastitis group and, on the basis of theccrB restriction pattern withHinfI (type IV: 264, 227 and 154 bp; type III: 537 and 106 bp) or withHinfI/BsmI (type IV: 227, 171, 153 and 93 bp; type III: 320, 174, 106 and 44 bp), 19 strains were assigned to type IV and the remaining three (S1LDC12, Z2LDC17 and DF2LAB) to type III (see additional file 1).

Chitosan is water soluble in acidic conditions

due to pro

Chitosan is water soluble in acidic conditions

due to protonation of primary amines in the chitosan chains. The Ag NP suspension was also acidic (pH 5.23 to 6.25) [25]. Although the acidity of these two solutions was maintained during mixing, partial precipitation of the Ag NP/Ch composites was observed at all conditions tested, suggesting that decreased solubility of the chitosan chains was induced by the binding of Ag NPs to selleck chemicals the chitosan amino and hydroxyl groups [28]. Addition of excess NaOH completely precipitated the composite. Figure 1 shows a typical SEM micrograph of the composite. Ag NP/Ch composites were obtained as flocculated, aggregated, spherical sub-micrometer particles. The composites were yellow or brown; darker composites were obtained when larger amounts of Ag NPs were reacted with the chitosan. Figure 2 shows UV-visible spectra of the original Ag NP suspension and of the reaction mixes containing high amounts of Ag NP. Since spherical Ag NPs provide a peak near 400 nm [25, 29], the absence of this peak shows that

Ag NPs are not present in the supernatant of the post-reaction mixture and that the Ag NPs were completely bound to the chitosan. Figure 1 A SEM micrograph of chitosan/SN129. Weight ratio of Ag NPs in the composite is 23.5 wt%. Figure 2 UV-visible spectra of the original Ag NP suspension and of the post-reaction mixture supernatant. Procaspase activation Solid line and dashed line correspond to the original Ag NP suspension and the post-reaction mixture supernatant, respectively. (a) SN35 and the supernatants obtained from 1 mg of chitosan and 328.5 μg of SN35, (b) SN65 and the supernatants obtained from 1 mg of chitosan and 279 g μof SN65, (c) SN129 and the supernatants obtained from 1 mg of chitosan and 308 μg of SN129. The peak due to Ag NPs is marked with a vertical line. The supernatants were obtained from

the post-reaction mixture of 1 mg of chitosan Phospholipase D1 and 328.5 μg of SN35 (dotted line), 279 μg of SN65 (short dashed line), and 308 μg of SN129 (long dashed line). The solid line corresponds to the original suspension of SN129. TEM micrographs of the Ag NPs and Ag NP/Ch composites are shown in Figure 3. Compared to Ag NPs before reaction, Ag NPs in the composites are dispersed in the chitosan matrix and appear as uneven gray domains. The thickness of the TEM specimen of the composites is uneven due to the direct casting of the composite floc. Uneven contrast of the chitosan domains is due to the uneven thickness of the specimen. Ag NPs in thick areas of the chitosan matrix are overlapped. Meanwhile, Ag NPs in thin areas appeared non-overlapped. The particle sizes of Ag NPs in the composites are similar to that of the original Ag NPs. Although some minor aggregation of Ag NPs was observed, there was no macroscopic aggregation, showing that the particle size of the Ag NPs in the Ag NP/Ch composites was controlled. Figure 3 TEM micrographs of Ag NPs. (a) SN35, (b) SN65, (c) SN129; Ag NP/Ch composites (d) 24.7 wt% of SN35, (e) 21.

A Germination rate were tested after wet-heat exposure to temper

A. Germination rate were tested after wet-heat exposure to temperature of 45°C for 0, 1.0, 1.5 2.0, 2.5 and 3.0 h. B. Germination rate after UV-radiation exposure for

0, 1, 2, 3 and 4 h. Standard deviation bars denote standard deviations for three independent experiments. *: significant difference, p <0.05; **: significant difference, p <0.01. Discussion Adenylate cyclase regulates LBH589 mw a variety of physiological processes in phytopathogenic fungi, including conidiation, conidial germination, vegetative growth, appressoria formation and virulence. In this study, an adenylate cyclase gene, MaAC, was identified in a locust-specific entomopathogenic fungus, M. acridum. Bioinformatic analysis showed that the cloned MaAC had significant similarity to its homolog from M. oryzae and to many other fungal adenylate cyclase genes; the highest degree of similarity Seliciclib mouse was found with the adenylate cyclase of M. anisopliae (98% identity). The cAMP level of the MaAC RNAi mutant was significantly reduced, and the exogenous addition of cAMP could restore the growth of the RNAi mutant, thus confirming that the MaAC gene encodes adenylate cyclase in M. acridum. These results were similar to previous studies on other fungi [10, 12,

14]. Following the deletion of the entire SAC1 coding sequence of S. sclerotiorum[10], cAMP underwent a four-fold reduction in the SAC1 deletion strain compared to the wild type. In BAC1- and UAC1-defective

mutants, intracellular cAMP was detected, which contrasted with the wild type [13, 15]. In this report, the downregulation of MaAC led to inhibited growth on in vitro media, including PDA and Czapek-dox medium. In PD liquid culture, it caused similar effects to previously described adenylate cyclase mutants, such as the SAC1 mutant in S. sclerotiorum[10] and the BAC1 mutant in B. cinerea[12]. Furthermore, MaAC is also involved in the growth of M. acridum inside locusts. The virulence of the MaAC mutant was also significantly reduced, thus indicating that MaAC is required for M. acridum virulence. This finding is consistent with the role of adenylate cyclase in the virulence of Cyclin-dependent kinase 3 other fungi, including M. oryzae[11], B. cinerea[12] and U. maydis[15]. Previous research has demonstrated that the tolerance of fungi to stresses such as high temperature [13], UV-B radiation [8, 16], oxidative [13] and osmotic stress [4, 5, 17] is a factor that limits their widespread use. The elevated thermo- and H2O2-tolerance of the ΔFpacy1 mutants indicated that the adenylate cyclase may have negative regulatory roles on the stress response mechanisms of fungal cells [13]. However, the tolerance of the RNAi mutant to the osmotic-, H2O2-, UV-B and thermal stress was reduced in this study, thus indicating that MaAC may affect the tolerance to multiple stresses through similar regulatory mechanisms in fungal cells.

Nat Rev Microbiol 2007,5(11):883–891 PubMedCrossRef

18 B

Nat Rev Microbiol 2007,5(11):883–891.PubMedCrossRef

18. Bitter W, Houben EN, Bottai D, Brodin P, Brown EJ, Cox JS, Derbyshire B-Raf cancer K, Fortune SM, Gao LY, Liu J, et al.: Systematic genetic nomenclature for type VII secretion systems. PLoS Pathog 2009,5(10):e1000507.PubMedCrossRef 19. Burts ML, DeDent AC, Missiakas DM: EsaC substrate for the ESAT-6 secretion pathway and its role in persistent infections of Staphylococcus aureus. Mol Microbiol 2008,69(3):736–746.PubMedCrossRef 20. Anderson M, Chen YH, Butler EK, Missiakas DM: EsaD, a secretion factor for the Ess pathway in Staphylococcus aureus. J Bacteriol 2011,193(7):1583–1589.PubMedCrossRef 21. Garufi G, Butler E, Missiakas D: ESAT-6-like protein secretion in Bacillus anthracis. J Bacteriol 2008,190(21):7004–7011.PubMedCrossRef 22. Desvaux M, Hebraud M, Talon R, Henderson IR: Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue. Trends Microbiol 2009,17(4):139–145.PubMedCrossRef 23. Dreisbach A, Otto A, Becher D, Hammer E, Teumer A, Gouw JW, Hecker M, Volker U: Monitoring of changes in the membrane proteome during stationary phase adaptation of Bacillus subtilis

using in vivo labeling techniques. Proteomics 2008,8(10):2062–2076.PubMedCrossRef 24. Driessen AJ, Nouwen N: Protein translocation across the bacterial cytoplasmic membrane. Annu Rev Biochem 2008, 77:643–667.PubMedCrossRef 25. Lee VT, Opaganib Schneewind O: Protein secretion and the pathogenesis of bacterial infections. Genes Dev 2001,15(14):1725–1752.PubMedCrossRef Florfenicol 26. Waksman G: Bacterial secretion comes of age. Philos Trans R Soc Lond B Biol Sci 2012,367(1592):1014–1015.PubMedCrossRef 27. van Kranenburg R, Golic N, Bongers R, Leer RJ, de Vos WM, Siezen RJ, Kleerebezem M: Functional analysis of three plasmids from Lactobacillus plantarum. Appl Environ Microbiol 2005,71(3):1223–1230.PubMedCrossRef 28. Coros A, Callahan B, Battaglioli E, Derbyshire KM: The specialized secretory apparatus ESX-1 is essential for DNA transfer in Mycobacterium smegmatis. Mol Microbiol 2008,69(4):794–808.PubMed 29. Mazmanian SK, Liu G, Jensen

ER, Lenoy E, Schneewind O: Staphylococcus aureus sortase mutants defective in the display of surface proteins and in the pathogenesis of animal infections. Proc Natl Acad Sci U S A 2000,97(10):5510–5515.PubMedCrossRef 30. Leake MC, Greene NP, Godun RM, Granjon T, Buchanan G, Chen S, Berry RM, Palmer T, Berks BC: Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging. Proc Natl Acad Sci U S A 2008,105(40):15376–15381.PubMedCrossRef 31. Wang IN, Smith DL, Young R: Holins: the protein clocks of bacteriophage infections. Annu Rev Microbiol 2000, 54:799–825.PubMedCrossRef 32. Bae T, Schneewind O: Allelic replacement in Staphylococcus aureus with inducible counter-selection.

2 Vokes EE, Weichselbaum RR, Lippman SM, Hong WK: Head and neck

2. Vokes EE, Weichselbaum RR, Lippman SM, Hong WK: Head and neck cancer. N Engl J Med 1993, 3: 184–94.CrossRef 3. Pignon JP, Bourhis J, Domenge C, Designe L: Chemotherapy added to locoregional treatment for head and neck squamous-cell carcinoma: three meta-analyses of updated individual data. MACH-NC Collaborative Group. Meta-Analysis of Chemotherapy on Head and Neck Cancer. Lancet 2000, 355 (9208) : 949–55.PubMed 4. Baldetorp B, Dalberg M, Holst Barasertib nmr U, Lindgren G: Statistical evaluation of cell kinetic data from DNA flow cytometry (FCM) by the EM algorithm. Cytometry 1989, 6: 695–705.CrossRef

5. Schutte B, Reynders MM, Bosman FT, Blijham GH: Flow cytometric determination of DNA ploidy level in nuclei isolated from paraffin-embedded tissue. Cytometry 1985, 6 (1) : 26–30.CrossRefPubMed 6. Jin C, Mertens F, Jin Y, Wennerberg TSA HDAC nmr J, Heim S, Mitelman F: Complex karyotype with an 11q13 homogeneously staining region in esophageal squamous cell carcinoma. Cancer Genet Cytogenet 1995, 82 (2) : 175–6.CrossRefPubMed 7. Tanner MM, Tirkkonen M, Kallioniemi A, Collins C, Stokke T, Karhu R, Kowbel D, Shadravan F, Hintz M, Kuo W, Waldman FM, Isola JJ: Increased copy number at 20q13 in breast cancer: defining the critical region and exclusion of candidate genes. Cancer Res 1994, 54 (16) : 4257–60.PubMed 8. Fioretos T, Strombeck B, Sandberg T, Johansson B, Billstrom R, Borg A, Nilsson PG, Berghe

HVD, Hagemeijer A, Mitelman F, Höglund M: Isochromosome 17q in blast crisis of chronic myeloid leukemia and in other hematologic malignancies is the result of clustered breakpoints in 17p11 and is not associated with coding TP53 mutations. Blood 1999, 94 (1) : 225–32.PubMed 9. Henriksson E, Kjellen E, Wahlberg P, Wennerberg J, Kjellstrom JH: Differences in estimates of cisplatin-induced cell kill in vitro between colorimetric and cell count/colony assays. In Vitro Cell Dev Biol Anim 2006, 42 (10) : 320–3.PubMed 10. Pekkola K, Raikka A, Joensuu H, Minn H, Aitasalo K, Grenman R: Permanent in vitro growth is associated with poor prognosis in head and neck cancer. Acta Otolaryngol

2004, 124 (2) : 192–6.CrossRefPubMed 11. Johns ME, Mills MS: Cloning efficiency. A possible prognostic indicator in squamous cell carcinoma of head and neck. Cancer 1983, 52 either (8) : 1401–4.CrossRefPubMed 12. Johns M: The clonal assay of head and neck tumor cells: results and clinical correlations. Laryngoscope 1982, 92 (7 Pt 2 Suppl 28) : 1–26.CrossRefPubMed 13. Kim SYCK, Lee HR, Lee KS, Carey TE: Establishment and characterization of nine new head and neck cancer cell lines. Acta Otolaryngol 1997, 117 (5) : 775–84.CrossRefPubMed 14. Mattox DE, Von Hoff DD, Clark GM, Aufdemorte TB: Factors that influence growth of head and neck squamous carcinoma in the soft agar cloning assay. Cancer 1984, 53 (8) : 1736–40.CrossRefPubMed 15.

*** p ≤ 0 001, ** p ≤ 0 01, * p ≤ 0 05 (one-way ANOVA) (JPEG 126

*** p ≤ 0.001, ** p ≤ 0.01, * p ≤ 0.05 (one-way ANOVA). (JPEG 126 KB) References 1. Baker DM, Jones JA, Nguyen-Van-Tam JS, Lloyd JH, Morris DL, Bourke JB, Steele RJ, Hardcastle JD: Taurolidine peritoneal lavage as prophylaxis against infection after elective colorectal surgery. Br J Surg 1994, 81:1054–1056.PubMedCrossRef 2. Simon A, Ammann RA, Wiszniewsky G, Bode U, Fleischhack G, Besuden MM: Taurolidine-citrate

lock solution (TauroLock) significantly reduces CVAD-associated grampositive infections in pediatric cancer patients. BMC Infect Dis 2008, 8:102.PubMedCrossRef 3. Koldehoff M, Zakrzewski JL: Taurolidine is effective in the treatment of central venous catheter-related bloodstream infections in cancer patients. Int J Antimicrob Agents 2004, 24:491–495.PubMedCrossRef 4. Jacobi CA, Menenakos C, Braumann C: Taurolidine–a new drug with anti-tumor GDC-0449 manufacturer and anti-angiogenic

effects. Anticancer Drugs 2005, 16:917–921.PubMedCrossRef 5. Braumann C, Schoenbeck M, Menenakos C, Kilian M, Jacobi CA: Effects of increasing doses of a bolus injection and an intravenous long-term therapy of taurolidine on subcutaneous (metastatic) tumor growth in rats. Clin Exp Metastasis 2005, 22:77–83.PubMedCrossRef 6. Chromik AM, Daigeler A, Hilgert C, Bulut D, Geisler A, Liu V, Otte JM, Uhl W, Mittelkotter U: Synergistic effects in apoptosis induction by taurolidine and TRAIL in HCT-15 colon carcinoma cells. J Invest Surg 2007, 20:339–348.PubMedCrossRef 7. Daigeler A, Chromik AM, Geisler A, Bulut D, Hilgert C, Krieg A, Klein-Hitpass L, Lehnhardt M, Uhl W, Mittelkötter U: Synergistic apoptotic effects of taurolidine and TRAIL on squamous carcinoma Rebamipide cells of the esophagus. Int J Oncol 2008, 32:1205–1220.PubMedCrossRef Fulvestrant clinical trial 8. Stendel R, Stoltenburg-Didinger G, Al Keikh CL, Wattrodt M, Brock M: The effect of taurolidine on brain tumor cells. Anticancer Res

2002, 22:809–814.PubMed 9. Stendel R, Biefer HR, Dekany GM, Kubota H, Munz C, Wang S, Mohler H, Yonekawa Y, Frei K: The antibacterial substance taurolidine exhibits anti-neoplastic action based on a mixed type of programmed cell death. Autophagy 2009, 5:194–210.PubMedCrossRef 10. Braumann C, Jacobi CA, Rogalla S, Menenakos C, Fuehrer K, Trefzer U, Hofmann M: The tumor suppressive reagent taurolidine inhibits growth of malignant melanoma–a mouse model. J Surg Res 2007, 143:372–378.PubMedCrossRef 11. Sun BS, Wang JH, Liu LL, Gong SL, Redmond HP: Taurolidine induces apoptosis of murine melanoma cells in vitro and in vivo by modulation of the Bcl-2 family proteins. J Surg Oncol 2007, 96:241–248.PubMedCrossRef 12. Opitz I, Sigrist B, Hillinger S, Lardinois D, Stahel R, Weder W, Hopkins-Donaldson S: Taurolidine and povidone-iodine induce different types of cell death in malignant pleural mesothelioma. Lung Cancer 2007, 56:327–336.PubMedCrossRef 13. Aceto N, Bertino P, Barbone D, Tassi G, Manzo L, Porta C, Mutti L, Gaudino G: Taurolidine and oxidative stress: a rationale for local treatment of mesothelioma.

Hence, in their study, unlike in this present work, Dunens et al

Hence, in their study, unlike in this present work, Dunens et al. were required to further impregnate their ash with iron in order for CNT/CNF growth to occur. In a similar manner,

Diamond [49], using acid etching techniques, demonstrated that the location of the iron and its morphology greatly differed for every fly ash particle within the sample. This, he suggested, was caused by the inhomogeneous nature of coal. The magnetic feature for the as-received sample was fitted with three sextets (SX1_U, SX2_U and SX3_U) and the spectrum for the acetylene-treated sample was analysed with one buy Idasanutlin sextet (SX1_T), while the non-magnetic spectral components for both samples were fitted with two quadrupole split doublets. Conclusions CNFs (and a small amount of CNTs) were successfully produced by directly using an as-received South African coal fly ash. The smooth, glassy and inert surfaces of the South African coal fly ash were covered with irregularly shaped CNFs in the presence of acetylene and hydrogen at temperatures as low as 400°C. Laser Raman spectroscopy confirmed the formation of CNFs. TGA showed that there

were different forms of carbon present, i.e. graphitic and amorphous. On the other hand EDS, XRD and Mössbauer spectroscopy selleck kinase inhibitor confirmed that iron, most likely in the form of iron carbide, was directly associated with the formation of CNFs. Therefore, this study has demonstrated the successful synthesis of carbon nanostructured materials from waste South African coal fly ash without chemical selleck pre-treatments (such as the impregnation of other metals) or thermal modifications. Since CNFs may in the future be beneficial for applications such as particulate nanofillers in polymer matrices, this intervention could result in the reduction of environmental pollutants.

Concomitantly, this may also bring relief to the financial burden involved in the disposal costs of this and related coal fly ash around the world in the long run. Authors’ information NH holds a master’s degree and is currently a PhD student at the University of the Witwatersrand. AS received his PhD after publishing in high impact factor journals and is now working at the Registrar’s office at the University of the Witwatersrand. PF received his PhD from Cambridge University (UK) and is now working as a lecturer at the University of the Witwatersrand. HM holds a PhD and is a lecturer at the School of Physics. DN holds a PhD and is the head of the Mössbauer facility at the School of Physics. DB holds a PhD, is a professor and is the head of the XRD unit at the Wits School of Chemistry. SD holds a PhD and is currently a senior lecturer and research focus area coordinator for CNTs and strong composites in the DST-NRF Centre of Excellence in Strong Materials at the University of the Witwatersrand. Acknowledgements The authors would like to thank Dr P.

Acknowledgments This study was supported by a grant from the Dutc

Acknowledgments This study was supported by a grant from the Dutch RO4929097 mouse Foundation Institute Gak. Conflict of interest None declared. Open Access This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited. Appendix The Nurses Work Functioning Questionnaire (NWFQ). See Table 5. Table 5

Instructions for sum score calculation Subscales Items Calculation of standardized sum score # of items Total Minimum 1 Cognitive aspects of task execution and general incidents 1, 2, 3, 4, 5, 6, 7, 8, 9, 15, 16 (sum of item scores * 100)/(# of items × 6) 11 9 2 Impaired decision making 48(R), 49(R), 50(R) (sum of item scores × 100)/(# of items × 4) 3 3 3 Causing incidents at work* JQ1 price 14, 26, 27, 28, 29, 30, 31, 32 (sum of item scores × 100)/(# of items × 6) 8 6 4 Avoidance behavior 36, 37, 38, 39, 40, 41, 42, 43 (sum of item scores × 100)/(# of items × 4) 8 6 5 Conflicts and irritations with colleagues 33, 34, 35, 44, 45, 46, 47 (sum of item scores × 100)/(# of items × 4) 7 6 6 Impaired contact with patients and their family 10, 11, 12, 13, 22, 23, 24, 25 (sum of item scores × 100)/(# of items × 6) 8 6 7 Lack of energy and motivation 17, 18, 19, 20, 21 (sum of item scores × 100)/(# of items × 6) 5 4 Technical details – Items followed by (R) need

to be recoded before sum score is calculated

– Item score counting starts with 0 on the outer left category, add 1 point for each category further to the right (e.g., disagree = 0; disagree a little = 1; not agree/not disagree = 2; agree a little = 3; agree = 4) – Calculation of standardized sum scores follows the principle: (sum of item scores × 100)/(# of items × maximum score per item) – For sum scores calculation, subjects need to have filled out at least ¾ of all items of PRKACG a subscale – The range of the standardized sum score is 0–100 for each subscale * The subscale “Causing incidents at work” is not suitable for allied health professionals Electronic supplementary material Below is the link to the electronic supplementary material. Supplementary material 1 (DOC 209 kb) References Aronsson G, Gustafsson K, Dallner M (2000) Sick but yet at work. An empirical study of sickness presenteeism. J Epidemiol Commun Health 54:502–509CrossRef Bartlett MS (1954) A note on the multiplying factors for various chi square approximation. J R Statist Soc B 16((Series B)):296–298 Bultmann U, Kant I, Kasl SV, Beurskens AJ, van den Brandt PA (2002) Fatigue and psychological distress in the working population: psychometrics, prevalence, and correlates. J Psychosom Res 52:445–452CrossRef Catell RB (1966) The scree test for number of factors. Multivar Behav Res 1:245–276CrossRef Dewa CS, Lin E (2000) Chronic physical illness, psychiatric disorder and disability in the workplace.

Most typically in mixed coniferous forests Distribution: widespr

Most typically in mixed coniferous forests. Distribution: widespread and locally common. In Europe collected in Austria, Czech Republic, Germany, Netherlands and UK; typically from the end of August to the beginning of October; only rarely found outside this period. Neotype: Belgium, Hestreux near Eupen, on leaf litter including pine needles, Oct. 1985, W. Gams 4031 (CBS 894.85); not examined, but gene sequences verified. Specimens examined: Austria, Burgenland, Mattersburg, Forchtenstein, between Kohlstatt and Weißes Kreuz,

MTB 8263/4, 47°42′26″ N, 16°18′33″ E, elev. 620 m, on soil, leaf litter and bark of Pinus sylvestris, 16 Sep. 2005, H. Voglmayr, W.J. 2856 (WU 29209). Forchtenstein, Wulka-Quellengebiet/Rosalia, MTB 8263/4, 47°42′37″ N, 16°18′09″ E, elev. 600 m, on and around stump of Larix decidua, on wood, bark and debris, 22 Sep. 2007, https://www.selleckchem.com/products/Bortezomib.html W. Jaklitsch & O. Sükösd, W.J. 3170 (WU Crizotinib clinical trial 29213). Kärnten, Klagenfurt Land, St. Margareten im Rosental, MTB 9452/3, 46°32′29″ N, 14°24′31″ E, elev. 500 m, spreading from a stump of Picea abies on leaves, bark and twigs,

24 Sep. 2006, H. Voglmayr & W. Jaklitsch, W.J. 2980 (WU 29210, culture CBS 121271 = C.P.K. 2469). Niederösterreich, Krems, Egelsee, close to Waldhof, MTB 7579/3, 48°25′55″ N, 15°33′25″ E, elev. 420 m, on soil around Fagus and Picea, 28 Aug. 2000, W. Klofac, W.J. 1617 (WU 29535; part BPI 748251). Wien-Umgebung, Gablitz, south of the train station, MTB 7762/4, elev. 300 m, on soil and leaf litter, 30 Sep. 2002, A. Urban, W.J. 1990 (WU 29536). Oberösterreich, Braunau, Wanghausen bei Ach, Oberer Weilhartsforst, forest path from the northern forest margin to Heilbrünnl, MTB 7842/4, elev. 400 m, spreading from a stump onto forest soil, 20 Sep. 2006, I. Krisai-Greilhuber, W.J. 3000 (WU 29211, Adenosine triphosphate culture C.P.K. 3121). Schärding, Raab, Rothmayrberg, mixed forest NE of Rotes Kreuz, MTB 7648/1, elev. 470 m, on the

base of a dead oak tree (Quercus robur), H. Voglmayr, 30 Aug. 2008, W.J. 3214 (WU 29214). Schärding, St. Willibald, Großer Salletwald, MTB 7648/3, 48°20′57″ N, 13°42′22″ E, elev. 660 m, on corticated stump bases of Picea abies, 30 cm thick, spreading on surrounding soil, leaf litter, bark and plants, 8 Sep. 2003, H. Voglmayr, W.J. 2391 (WU 29206, culture CBS 121278 = C.P.K. 956); same place, different stump, 14 Sep. 2003, H. Voglmayr, W.J. 2395 (WU 24803, culture C.P.K. 960). Steiermark, Feldbach, St. Anna bei Aigen, Deutsch Haseldorf, MTB 9261/2, elev. 400 m, on soil and bark of Pinus sylvestris, 11 Sep. 2002, G. Koller, W.J. 1947 (WU 29534). Graz, Gries, Florianigasse, MTB 8958/2, 47°03′30″ N, 15°25′24″ E, elev. 350 m, on soil and plants at the base of a Prunus avium tree in a garden, identified using ITS extracted from stroma, 6 Aug. 2001, H. Teppner, Mycotheca Graecensis 367 (part: WU 29533). Vienna, 23rd district, Maurer Wald, MTB 7863/4, 48°09′00″ N 16°15′11″ E, elev.