Kim KM, Kawada T, LGX818 mouse Ishihara

K, Inoue K, Fushiki T: Increase in swimming endurance capacity of mice by capsaicin-induced adrenal catecholamine secretion. Biosci Biotechnol Biochem 1997,61(10):1718–1723.CrossRefPubMed 51. Ohnuki K, Haramizu S, Oki K, Watanabe T, Yazawa S, Fushiki T: Administration of capsiate, a non-pungent capsaicin analog, promotes energy metabolism and suppresses body fat accumulation in mice. Biosci Biotechnol Biochem 2001,65(12):2735–2740.CrossRefPubMed 52. Oh TW, Oh TW, Ohta F: Dose-dependent effect of capsaicin on endurance capacity in rats. Br J Nutr 2003,90(3):515–520.CrossRefPubMed 53. Oh TW, Ohta F: Capsaicin increases endurance capacity and spares tissue glycogen through lipolytic function see more in swimming rats. J Nutr Sci Vitaminol (Tokyo) 2003,49(2):107–111. 54. Lim Selonsertib in vivo K, Yoshioka M, Kikuzato S, Kiyonaga A, Tanaka H, Shindo M, Suzuki M: Dietary red pepper ingestion increases carbohydrate

oxidation at rest and during exercise in runners. Med Sci Sports Exerc 1997,29(3):355–361.PubMed 55. Kawada T, Sakabe S, Watanabe T, Yamamoto M, Iwai K: Some pungent principles of spices cause the adrenal medulla to secrete catecholamine in anesthetized rats. Proc Soc Exp Biol Med 1988,188(2):229–233.PubMed 56. Reanmongkol W, Janthasoot W, Wattanatorn W, Dhumma-Upakorn P, Chudapongse P: Effects of piperine on bioenergetic functions of isolated rat liver mitochondria. Biochem Pharmacol 1988,37(4):753–757.CrossRefPubMed 57. Capuzzi DM, Morgan JM, Brusco OA Jr, Intenzo CM: Niacin dosing: relationship to benefits and adverse effects. Curr Atheroscler Rep 2000,2(1):64–71.CrossRefPubMed 58. Borg G: Borg’s Rating of Percieved Exertion and Pain Scale. Champaign, IL: Human Kinetics 1998. 59. Whaley M: ACSM’s Guidelines for Exercise Testing and Prescription. 7 Edition Lippincott, Williams, & Wilkins 2005. 60.

Cramer JT, Coburn JW: Fitness Testing Protocols and Norms, in NSCA’s Essentials of Personal Training. Champaign, Flavopiridol (Alvocidib) IL: Human Kinetics 2004. 61. Graham TE, Helge JW, MacLean DA, Kiens B, Richter EA: Caffeine ingestion does not alter carbohydrate or fat metabolism in human skeletal muscle during exercise. J Physiol 2000,529(Pt 3):837–847.CrossRefPubMed 62. Graham TE: Caffeine and exercise: metabolism, endurance and performance. Sports Med 2001,31(11):785–807.CrossRefPubMed 63. Doherty M, Smith PM: Effects of caffeine ingestion on rating of perceived exertion during and after exercise: a meta-analysis. Scand J Med Sci Sports 2005,15(2):69–78.CrossRefPubMed 64. Magkos F, Kavouras SA: Caffeine use in sports, pharmacokinetics in man, and cellular mechanisms of action. Crit Rev Food Sci Nutr 2005,45(7–8):535–562.CrossRefPubMed 65. Bell DG, Jacobs I, Zamecnik J: Effects of caffeine, ephedrine and their combination on time to exhaustion during high-intensity exercise. Eur J Appl Physiol Occup Physiol 1998,77(5):427–433.CrossRefPubMed 66.

As a result, it is desirable to investigate the pumping effect of the Thiazovivin solution with different concentrations. As reported by Tavares and McGuffin [23], the zeta potential varied linearly with the

logarithm of the ion concentration, meaning that the zeta potential decayed exponentially with respect to the ion concentration. Thus, the relation between the EO flow rate and the ion concentration is an exponentially decay function under the influence of the electric field strength according to Equation 1. To examine the effect of the concentration dependency with respect to our device, the EO flow rates were measured at different ion concentrations when a ARRY-438162 supplier constant voltage of 3 V was applied, where the ion concentration refers

to the concentration of analytes in PBS 4EGI-1 mouse in this case. The ion concentrations were normalized by the standard PBS with a K2HPO4 concentration of 27.5 mM and a KH2PO4 concentration of 20.0 mM. After analyzing the fluorescent intensity of the acquired images using imaging software, the relation of EO flow rates versus different analyte concentrations was determined and is shown in Figure  6. The analytical relation between the EO flow rate and the ion concentration was determined and exhibited exponential decay characteristics. The resulting relation is v = 1.10583 + 15.7236 × e - 18.0505 ⋅ c , where v is the flow rate in the unit of picoliter per second and c represents the analyte concentration after normalization by standard

PBS. For a constant applied voltage, the higher the Celecoxib concentration, the lower the EO flow rate due to the decrease in zeta potential. After obtaining this relation, it is possible to estimate the flow rate of any diluted PBS driven by an applied voltage of 3 V. This method of investigating the effect of ion concentration on the EO flow rate is also applicable to other types of solution containing different analytes. Figure 6 The influence of ion concentration on the electroosmotic flow rate that exhibited an exponential function. The ion concentration was normalized by standard PBS with a K2HPO4 concentration of 27.5 mM and a KH2PO4 concentration of 20.0 mM. Program-controlled reaction in continuous flow Controlled chemical reaction is one of the potential applications of our nanofluidic device, and we employed the binding reaction between Fluo-4 and calcium chloride to demonstrate the feasibility of such application. Fluo-4 is a kind of chemical widely used in living cells as a calcium indicator. Its emitted fluorescent intensity was found to be linearly proportional to the calcium concentration for a particular range [24]. Here, pumping of calcium ions was controlled by LabVIEW which generates square waves with a fixed applied voltage of 3 V and different duty cycles. The EO flow rate of the calcium chloride from channel A to channel B was measured to be 1.

Cophenetic correlations are shown next to the branches. Bacterial growth and biochemical identification All strains were stored at −70°C, plated on sheep blood agar (Columbia blood agar, Oxoid, UK) and grown at 30°C overnight. Biochemical characterization was performed on pure cultures by using API 50 CH cassettes (bioMérieux, Marcy l’Etoile, France) according to the instructions given

by the manufacturer [41]. Color changes were examined after 24 and 48 h at 30°C and compared to the Bacillus identification profile database, API Lab1 XAV 939 (version 4.0). The reaction profiles of these tests were compared with the ApiwebTM database provided by the manufacturer. DNA extraction Bacteria were grown on sheep blood agar at 30°C overnight. Single colony material was inoculated in 20 ml Luria broth (LB). The bacterial culture

was grown overnight at 30°C and centrifuged at 3000 × g for 10 min. The supernatant Sepantronium was discarded and the pellet resuspended in 1 ml enzymatic lysis buffer (20 mM Tris·Cl, pH 8.0, 20 mM Tris·Cl, pH 8.0, 1.2% Triton® X-100, 20 mg/ml lysozyme). Further DNA extraction was performed according to the protocol provided by DNeasy Blood and Tissue Kit (Qiagen, USA). The final DNA concentration ranged from 8–72 ng/ul with a mean 260/280

absorbance ratio of 1, 89 (Nanodrop ND-1000 Spectrophotometer, Thermo Fisher Scientific, USA). MLST scheme Primer design The MLST scheme was created according to general guidelines described in [42]. Primers were designed to amplify internal fragments of candidate-genes of the publicly available B. licheniformis ATCC14580 genome (GenBank: NC_00627) using the Primer3 software [43]. The choice of candidate-genes was based previously published genotyping schemes for members of the Bacillus genus [28, 32, 36]. The primers targeted much 400-718 bp fragments of the nine house-keeping genes adk, ccpA, glpT, gyrB, pyrE, recF, rpoB, sucC and spo0A which were dispersed over the entire genome. The primers targeting rpoB have been described in a previous publication and was included for comparison [28]. All primers were synthesized by see more Invitrogen Life Sciences, Norway. Primers and their targets are listed in Table  1 Primers that were used in the final MLST scheme are typed in bold.

To our knowledge, this is the first description of mef(A/E) in the genera Pediococcus and Weissella, and lnu(A) in the genus Pediococcus. The detection of resistance genes for macrolide and lincosamide in non-enterococcal strains suggests a wider distribution of this group of genes than previously anticipated. The in vitro subtractive screening proposed in this work also include

the assessment of bile salts deconjugation, mucin degradation, biogenic amine production and other potentially detrimental enzymatic activities such as the β-glucuronidase activity, which should be absent in probiotic candidates [54–56]. Excessive deconjugation of bile salts may be unfavourable in animal production since unconjugated bile acids are less efficient than their

conjugated counterparts in the emulsification of dietary lipids. In addition, the formation of micelles, lipid digestion and absorption of fatty acids and Selleckchem Small molecule library monoglycerides could be Sapanisertib mw impaired by deconjugated bile salts [57]. Similarly, excessive degradation of mucin may be harmful as it may facilitate the translocation of bacteria to extraintestinal tissues [55]. In this respect, it is worthy to note that none of the 49 tested LAB deconjugated bile salts nor exhibited mucinolytic activity, the latter indicating their low invasive and toxigenic potential at the mucosal barrier. These results are in accordance with previous findings showing that LAB do not degrade mucin in vitro[58, 59]. Moreover, β-glucuronidase ��-Nicotinamide nmr activity has been associated with the generation of potential carcinogenic metabolites [56]; however, none of the LAB tested in our study displayed this harmful enzymatic activity. In a previous work [60], we demonstrated that none of the 40 non-enterococcal strains evaluated herein produced histamine, tyramine or putrescine. With regard to enterococci, the nine Avelestat (AZD9668) E. faecium strains only produced tyramine, being E. faecium CV1 a low producer of this biogenic amine. Although the lack of biogenic amine production by

probiotic strains is a desirable trait, it should be borne in mind that tyramine production by enterococci is a very frequent trait [60, 61]. Finally, several studies have suggested that probiotic microorganisms might exert a beneficial effect in the digestion process of fish due to the production of extracellular enzymes [62–65]. In our work, the LAB strains of aquatic origin within the genera Pediococcus, Enterococcus and Lactobacillus showed a higher number of enzymatic activities than Lactococcus, Leuconostoc and Weissella, being the enzymatic profiles similar amongst strains within the same genus. In this respect, nearly all the strains produced phosphatases, which might be involved in nutrient absorption [64], and peptidases and glucosidases that breakdown peptides and carbohydrates, respectively. However, the tested LAB showed weak lipolytic activity and no proteolytic activity.

Proc Natl Acad Sci USA 2012, 109:7439–7444.PubMedCrossRef 37. Lin HE, Tsai WY, Liu IJ, Li PC, Liao MY, Tsai JJ, Wu YC, Lai CY, Lu CH, Huang JH, Chang GJ, Wu HC, Wang WK: Analysis of Epitopes on Dengue Virus Envelope Protein Recognized by Monoclonal Antibodies and Polyclonal Human Sera by a High Throughput Assay. PLoS Negl Trop Dis 2012, 6:e1447.PubMedCrossRef 38. Hughes HR, Crill WD, Chang GJ: Manipulation of immunodominant dengue GANT61 cell line virus

E protein epitopes reduces potential antibody-dependent enhancement. Virol J 2012, 9:115.PubMedCrossRef 39. Wahala WM, Huang C, Butrapet S, White LJ, de Silva AM: Recombinant dengue type 2 viruses with altered E protein domain III epitopes are efficiently neutralized by human immune sera. J Virol 2012, 86:4019–4023.PubMedCrossRef 40. Falconar AK: Identification of an epitope on the dengue virus membrane (M) protein defined by cross-protective monoclonal

antibodies: design of an improved epitope sequence based on common determinants present in both envelope (E and M) proteins. Arch Virol 1999, 144:2313–2330.PubMedCrossRef 41. Huang KJ, Lin YS, Cheng YT, Huang JH, Liu HS, Yeh TM, Liu CC, Lei HY: Anti-prM Antibody as an Autoantibody in Dengue Virus Infection. Am J Infect Dis 2008, 4:59–67. 42. Rodenhuis-Zybert IA, van der Ende-Metselaar H, Wilschut J, Smit JM: Functional importance of dengue virus maturation: infectious properties of immature virions. J Gen Virol 2008, 89:3047–3051.CrossRef 43. Kohler G, Milstein selleck C: Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 1975, 256:495–497.PubMedCrossRef 44. Yenchitsomanus PT, Sricharoen

P, Jaruthasana I, Pattanakitsakul SN, Nitayaphan S, Mongkolsapaya J, Malasit P: Rapid detection and identification Casein kinase 1 of dengue viruses by polymerase chain reaction (PCR). Southeast Asian J Trop Med Public Health 1996, 27:228–236.PubMed 45. Innis BL, Nisalak A, Nimmannitya S, Kusalerdchariya S, Chongswasdi V, Suntayakorn S, Puttisri P, Hoke CH: An enzyme-linked immunosorbent assay to characterize dengue infections where dengue and Japanese encephalitis co-circulate. Am J Trop Med Hyg 1989, 40:418–427.PubMed 46. Hoop TP, Woods KR: Prediction of protein antigenic determinants from amino acid sequences. Proc Natl Acad Sci USA 1981, 78:3824–3828.CrossRef 47. Grantham R: Amino acid difference formula to help explain protein evolution. Science 1974, 185:862–864.PubMedCrossRef 48. Jameson BA, Wolf H: The anigenic index: a novel EPZ015938 in vitro algorithm for predicting antigenic determinants. Comput Appl Biosci 1988, 4:181–186.PubMed 49. Bhaskaran R, Ponnuswamy PK: Positional flexibilities of amino acid residues in globular proteins. Int J Peptide Protein Res 1988, 32:241–255.CrossRef 50.

Though mutating srtB has no effect on establishing infection, SaSrtB is required for persistence of the bacterium in mice [17]. Clostridium difficile, an anaerobic Gram-positive, spore-forming bacillus, is the leading cause of hospital-acquired infectious diarrhea in North America and Europe. Infection with C. difficile can result in a range of

clinical presentations, from mild self-limiting diarrhea to the life-threatening LY2874455 datasheet pseudomembranous colitis (PMC), known collectively as C. difficile infection (CDI) [19]. MLST studies have identified that the C. difficile population structure forms at least five distinct lineages that are all associated with CDI [20–22]. Complications of severe CDI can lead to toxic megacolon, YH25448 molecular weight bowel perforation, sepsis and death in up to 25% of cases [23]. Broad-spectrum antibiotic usage is the greatest risk factor for development of CDI due to the consequent disruption of the intestinal microflora. Treatment of CDI with https://www.selleckchem.com/products/kpt-8602.html metronidazole and vancomycin

can exacerbate the problem by continuing to disrupt the intestinal microflora. This leaves the patient susceptible to relapse or re-infection. Approximately one third of patients experience CDI relapse following treatment, and those who relapse have a greater risk of succumbing to the infection [23]. A current imperative is the development of therapies that selectively target C. difficile, whilst leaving the intestinal microflora intact. The C. difficile reference CHIR-99021 molecular weight strain 630 encodes a single predicted sortase, CD630_27180, which has high amino-acid similarity with SrtB of S. aureus and B. anthracis [24]. A second sortase encoded within the genome is interrupted by a stop codon prior to the catalytic cysteine and is considered a pseudogene.

Thus, in contrast to other Gram-positive bacteria, C. difficile appears to have only a single functional sortase. As such, a compound that inhibits the activity of C. difficile sortase could target the pathogen without disrupting the numerous Gram-negative bacteria that make up the intestinal flora. In this study, we demonstrate that the predicted sortase encoded by CD630_27180 recognizes and cleaves an (S/P)PXTG motif between the threonine and glycine residues. The cleavage of this motif is dependent on the conserved cysteine residue at position 209 in the predicted active site of the sortase. We have also identified seven putative sortase substrates, all of which contain the (S/P)PXTG motif. These substrates are conserved among the five C. difficile lineages and include potential adhesins, a 5’ nucleotidase, and cell wall hydrolases. Furthermore, we identified a number of small-molecule inhibitors by means of an in silico screen that inhibit the activity of the C. difficile SrtB. Results Conservation of the catalytically active residues of sortase The genome sequence of C.

Three additional libraries that were used are unique at the HZI: iv) the NCH collection consisting

of 154 secondary metabolites from myxobacteria [33]; v) the library Various Sources (VAR) contained at the time of this study 1,936 synthetic organic molecules that were provided by various collaborators; and vi) the Peptide library contained 1,045 short linear or cyclic peptide sequences synthesized at the HZI [6]. All test compounds were utilized CH5183284 as stock solutions in DMSO. Growth assay 50 μl or 25 μl of LB-Km medium were inoculated in clear flat-bottom 96-well or 384-well MTP, respectively. Test compounds were added from DMSO stocks in amounts that resulted in assay concentrations between 20 and 50 μM. 50 μl or 25 μl of bacterial culture in LB-Km medium with an absorbance of 0.2 at 600 nm (OD600) (Ultraspec 2100 selleck chemicals llc Pro photometer, Pharmacia, GE Healthcare, Chalfont St Giles, UK) were added to the 96-well or 384-well MTP, respectively. The seeding of bacteria and addition of the compounds was carried

out with the pipetting system Evolution P3 (PerkinElmer, Waltham, USA). Stationary incubation of the plates for 24 h at 37°C under moist conditions was carried out, followed by determination of absorbance at 600 nm and fluorescence at 485/535 nm (Fusion Universal Microplate Analyzer, PerkinElmer, Waltham, USA). As negative and positive controls DMSO (1%) and Cip (100 μM)

were used, respectively. During the initial screening, approximately 28,300 compounds were investigated with single determinations. Compounds that reduced bacterial growth by at least 50% were retested in a second campaign and the most active substances were reevaluated at different concentrations between 0.1 and 100 μM. MIC and MBC values determination The determination of MIC and MBC values was carried out with V. cholerae wild type strains and several Gram-negative and Gram-positive bacteria (Table  3) following standardized protocol [34] in broth dilution assays. Starting inocula of 2-8×105 colony forming units/ml (CFU/ml) in MH medium at 37°C were used and serial dilutions crotamiton were carried out in 96-well MTP in duplicate. At 2, 6 and 24 h of incubation, 10 μl of the cultures were see more plated on LB agar plates. After an incubation of the plates for 24 h at 37°C, CFU/ml were determined and used for the determination of MBC, which is defined as minimum concentration of the substance required for 99.9% reduction of CFU after an incubation period of 6 h. The 2 h and 24 h measurements were used for additional correlation. MIC values were determined after 24 h of incubation. Cytotoxicity assay The mammalian cell line L929 was utilized to investigate the cytotoxicity of the active compounds in a MTT assay according to a modified protocol of Mosmann [11, 12].

​com/​bio/​dnacopynum.​php” website. All viral RNA stocks (from HAV, SA11 and Wa) containing 109 copies / μL were aliquoted and stored at – 80°C. Propidium monoazide (PMA), ethidium monoazide (EMA) PMA (phenanthridium, 3-amino-8-azido-5-[3-(diethylmethylammonio)propyl]-6-phenyl dichloride) was purchased from VWR (Fontenay sous Bois, France) at 20 mM and diluted in ultra pure RNAse-free water to obtain the solutions used in this study. EMA (phenanthridium, 3-amino-8-azido-5-ethyl-6-phenyl bromide) (Life Technologies) was dissolved EPZ015938 in vitro in absolute

ethanol to create the stock concentration of 5 mg / mL and then dissolved in ultra pure RNAse-free water to obtain the solutions used in this study. The EMA and PMA solutions were stored at −20°C in the dark. All the experiments with dyes were performed in light-transparent 1.5 mL microcentrifuge tubes (VWR). Binding of dyes to purified viral CBL0137 cell line RNA The effect of several EMA and PMA treatment TH-302 in vivo processes on 108 copies genome of viral RNA (RV, HAV) in 100 μL of phosphate-buffered saline (PBS) 1 ×, pH 7.0, were evaluated by testing several final dye concentrations (10, 20, 50, 100, 200 μM), with incubation of 2 h at 4°C in the dark and sample exposure to light for 15 min using the LED-Active® Blue system (IB – Applied Science, Barcelona, Spain). To

determine whether PMA / EMA interfere with the ability only of RT-qPCR to detect viruses, controls consisting of viral RNA that was treated with PMA / EMA without photoactivation were included with each dye concentration used. To attempt to remove the inhibitory effects of residual EMA / PMA on RT-qPCR, viral RNA treated with each dye concentration without photoactivation was purified using the QIAquick PCR purification kit (Qiagen, Courtaboeuf, France) according to the manufacturer’s instructions. Finally, to determine the efficiency of each concentration of PMA / EMA tested, treated viral RNA samples were subjected to photoactivation before the purification step using the QIAquick PCR purification

kit. The negative control was a non-treated 1× PBS sample. The positive control was a non-treated viral RNA sample in 1× PBS. A non-treated viral RNA control sample was subjected to the photoactivation step to check the effect of the lamp. Finally, all these samples were subjected to RNA detection by RT-qPCR assays A. The experiments were performed three times for all viral RNA. Determination of the optimal dye concentration for viruses The best dye (PMA / EMA) and its optimised concentration were determined for each viral target by testing five dye concentrations (5 μM, 20 μM, 50 μM, 75 μM, 100 μM). Briefly, in 100 μL of 1× PBS samples of 105 TCID50 of RV (SA11), 103 TCID50 of RV (Wa) and 6 × 104 PFU of HAV were conserved at 4°C or inactivated at 80°C for 10 minutes.

“
“Background The aetiologic agent of Johne’s disease or paratuberculosis, M. avium subsp. paratuberculosis (Map), CP868596 is one of the subspecies included in the Mycobacterium avium Complex (MAC). Based on the comparison of whole-genomes of Map, a biphasic evolution scheme has been proposed distinguishing two major lineages, a sheep lineage and a cattle lineage [1]. In addition to genotypic differences [2, 3], PI3K inhibitor strains belonging to these two lineages exhibit phenotypic differences

including growth rate [2–4], utilization of different iron metabolic pathways [4], profile of cytokine responses induced in bovine macrophages [5] or transcriptional profiles in a human macrophage model [6]. The association of each lineage with either the sheep or cattle host is not exclusive since strains representative of either lineage can cause disease in all types of ruminants. Historically, strains belonging to the sheep lineage have been referred to as ‘Sheep or S-type’ and those of the cattle lineage ‘Cattle or C-type’ according to the species from which they were first isolated. As the technologies for molecular typing advanced and more genotyping studies were undertaken, greater genetic diversity

was detected within both the S- and C-type strains. Pulsed-field gel electrophoresis (PFGE) Fludarabine cost revealed three strain types designated Types I, II and III [7, 8]. Type II is synonymous with C-type and types I and III comprise the S-type. In this paper we will use the term S-type to describe collectively type I and III strains and have designated the types I and III as subtypes. S-type strains have not been characterized to

the same extent as C-type strains due to the difficulty in culturing the strains in vitro resulting in a limited number of strains available for such studies. Here we undertook the first comprehensive genotyping study of a large representative panel of S-type strains using various typing methods that have been applied to Map strains, individually or in combinations, to draw a portrait of S-type strains. We studied both inter and intra-subtype genotypic strain differences using restriction fragment length polymorphism analysis coupled with hybridization to IS900 (IS900 RFLP), PFGE and various PCRs based on variable-number tandem repeat (VNTR) loci and mycobacterial interspersed BCKDHA repetitive units (MIRUs) [9, 10] MIRU-VNTR typing [11], the presence or absence of large sequence polymorphisms (LSPs) [12] and the gyrA and B genes [13]. Our panel of S-type strains comprised strains from different geographic origins with different restriction enzyme profiles and includes pigmented strains. We also incorporated typing data obtained for additional Map C-type isolates to represent the all diversity of the genotypes described and Mycobacterium. avium subsp. avium (Maa) Mycobacterium. avium subsp. silvaticum (Mas) and Mycobacterium avium subsp. hominissuis (Mah) for comparison.

YS was born in 1972 in Shanxi, China. He ACY-738 cost received his M.Sc. MK-8931 price degree in electronic engineering from the North University of China, Shanxi, China in 2003. He has published papers on topics including microinertia device design and MEMS device design. His current research interests include microinertia navigation systems and MEMS sensors. Acknowledgments We acknowledge the support from the National Science Foundation of China (61171056, 51105345) and the China Postdoctoral Science Foundation (2011M500544, 2012T50249). References 1. Wen TD, Xu LP,

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applications. Journal of Crystal Growth 2011, 317:104–109.CrossRef 8. Mohammed AAS, Moussa WA, Edmond L: High sensitivity MEMS strain sensor: design BCKDHA and simulation. Sensors 2008, 8:2642–2661.CrossRef 9. Richter M, Rossel C, Webb DJ, Topuria T, Gerl C, Sousa M, Marchiori C, Caimi D, Siegwart H, Rice PM, Fompeyrine J: GaAs on 200 mm Si wafers via thin temperature graded Ge buffers by molecular beam epitaxy. J Cryst Growth 2011, 323:387–392.CrossRef 10. Vanamu G, Datye AK, Dawson R, Zaidi SH: Growth of high-quality GaAs on Ge/Si 1−x Ge x on nanostructured silicon substrates. Appl Phys Lett 2006,88(251909):1–3. 11. Shi YB, Guo H, Ni HQ, Xue CY, Niu ZC, Tang J, Liu J, Zhang WD, He JF, Li MF, Yu Y: Optimization of the GaAs-on-Si substrate for microelectromechanical systems (MEMS) sensor application. Materials 2012, 5:2917–2926.CrossRef 12. Cho HJ, Oh KW, Ahn CH, Boolchand P: Stress analysis of silicon membranes with electroplated perm alloy films using Raman scattering. IEEE Trans Magn 2001, 37:2749–2751.CrossRef 13. Ferraro JR, Nakamoto K: Introductory Raman Spectroscopy. New York: Academic; 1994. 14.