avium has a fifth paralog that is similar to cysQ). While levels of homology between the different M. tuberculosis IMPase paralogs are moderate (22-30% amino acid identity), similarities

between orthologs are much higher (for example, 75-79% identity between M. tuberculosis and M. leprae, and 51-67% identity between M. tuberculosis and M. smegmatis). The genomic contexts of these genes are shown in Figure 2. As with M. smegmatis [24], the impA gene (Rv1604) lies in the middle of the main his operon between hisA and hisF. The stop codon of hisA overlaps with the putative start codon of impA, and the stop codon of impA overlaps with the putative start codon of hisF. These impA genes are 70% identical. Figure 2 Genomic context of M. tuberculosis IMPase genes. White arrows: imp genes; black arrows: other genes; open rectangles deleted regions in knock out Selleckchem MEK inhibitor plasmids. The suhB gene (Rv2701c) was named in the original genome annotation [35], because it is the gene most similar to the Escherichia coli suhB gene. The E. coli suhB gene

was so-named because deletion of the gene resulted in a cold-sensitive phenotype, and suppression of a thermosensitive rpoH mutation [36]. It has also been shown to suppress secY [37], MAPK inhibitor dnaB [38], and era [39] mutations. However, these phenotypes are not related to the enzymatic properties of the protein, as they are unaffected by a null point mutation in the active site [40] (Figure 1B). Furthermore, inositol production is not believed to occur in E. coli, so the biological context is very different from that in mycobacteria. Recombinant SuhB from M. tuberculosis has been confirmed to have IMPase

activity [41]. SuhB is monocistronic in M. tuberculosis (Figure 2). The third homologous gene is Rv3137, which we have called impC. It appears to be the first gene in a two-gene operon; a 457 bp intergenic gap upstream of impC suggests it has its own promoter., and a second gene, pflA, is predicted to start only 14 bp downstream, so is probably co-transcribed. PflA shows homology to pyruvate formate lyase-activating proteins. Beyond this is a cluster of fad genes (fadE24-fadE23-fadB4), but the gap beyond pflA and fadE24 is 79 bp, so is less likely to be part of the same operon. The fourth homologous gene is cysQ (Rv2131c), so-named because it is most similar to the E. ZD1839 molecular weight coli cysQ gene. E. coli cysQ mutants are cysteine auxotrophs during aerobic growth [42]. Interestingly M. smegmatis contains two paralogs of this gene. Two sequence motifs have been described for IMPases in the Prosite database [43] (see legend to Figure 1B). One motif, near the N-terminus contains the metal-binding aspartate residues of the active site, and the other lies near the C-terminus. All of the gene products except SuhB had small Brigatinib cell line differences from at least one of the two IMPase motifs (Figure 1B). However, they all contain the important metal-binding residues in both motifs. The M.

AEM 2007, 73:5320–5330. 25. Martin KJ, Rygiewicz RT: Fungal-specific PCR primers developed for analysis

of the ITS region of environmental DNA extracts. BMC Microbiol 2005, 5:28.CrossRefPubMed 26. Dickie IA, Xu B, Koide T: Vertical niche differentiation of ectomycorrhizal hyphae in soil as shown by T-RFLP analysis. New selleck chemicals Phytol 2002, 156:527–535.CrossRef 27. Genney DR, Anderson IC, Alexander IJ: Fine-scale distribution BIRB 796 mw of pine extomycorrhizas and their extrametrical mycelium. New Phytol 2005, 170:381–390.CrossRef 28. Rothberg JM, Leamon JH: The development and impact of 454 sequencing. Nature Biotechnol 2008, 26:1117–1124.CrossRef 29. Volokhov DA, Rasooly K, Chumakov K, Rasooly A: Identification of Listeria species by microarray

based assay. J Clin Microbiol 2002, 40:4720–4728.CrossRefPubMed 30. Townsend MB, Dawson ED, Mehlmann M, Smagala JA, Dankbar DM, Moore CL, Smith CB, Cox CUDC-907 concentration NJ, Kuchta RD, Rowlen KL: Experimental Evaluation of the FluChip Diagnostic Microarray for Influenza Virus Surveillance. J Clin Microbiol 2006, 44:2863–2871.CrossRefPubMed 31. Vialle A, Feau N, Allaire M, Didukh M, Martin F, Moncalvos JM, Hamelin RC: Evaluation of mitochondrial genes as DNA barcode for basidiomycota. Mol Ecol Resources 2009, 9:99–113.CrossRef 32. Buée M, Courty PE, Le Tacon F, Garbaye J: Écosystèmes forestiers: Diversité et fonction des champignons. Biofutur 2006, 268:42–45. 33. Frøslev TG, Jeppesen T, Læssøe T, Kjøller R: Nitroxoline Molecular phylogenetics and delimitation of

species in Cortinarius section Calochroi (Basidiomycota, Agaricales) in Europe. Mol Phylogenetics Evol 2007, 44:217–227.CrossRef 34. Smith ME, Douhan GW, Rizzo DM: Ectomycorrhizal community structure in a xeric Quercus woodland based on rDNA sequence analysis of sporocarps and pooled roots. New Phytol 2007, 174:847–863.CrossRefPubMed 35. Tedersoo L, Kõljalg U, Hallenberg N, Larsson KH: Fine scale distribution of ectomycorrhizal fungi and roots across substrate layers including coarse woody debris in a mixed forest. New Phytol 2003, 159:153–165.CrossRef 36. Prévost A, Pargney JC: Comparaison des ectomycorhizes naturelles entre le hêtre (Fagus sylvatica) et 2 lactaires (Lactarius blennius var viridis et Lactarius subdulcis). I. Caractéristiques morphologiques et cytologiques. Ann Sci For 1995, 52:131–146.CrossRef 37.

Although many reports have been reported on the rGO sensing devices, it is still a great challenge to develop chemiresistive sensors based on rGO with miniature, low-cost, and portable characteristics. In order to fabricate

chemiresistive sensors based on nanomaterial, there are generally two main methods. One is to deposit nanomaterial on substrates followed by patterning electrodes on top of sensing materials [34]. However, the XAV-939 solubility dmso process is complicated and requires exquisite skills. The other fascinating method is to drop-cast nanomaterial solution onto the pre-patterned electrode surfaces [29, 35]. This technique is facile, less expensive with higher yields, since it can be operated in solution, which benefits for the large-scale fabrication of the sensing devices. However, drop-casting method is very hard to ensure the reproducibility of the fabricated devices, which needs to be improved and applied in the realistic detection fields. Herein, we report PD-1/PD-L1 inhibitor drugs a facile and controllable self-assembly technique to fabricate rGO sensors, which could be

used as an excellent NH3 gas sensing device. Negative GO sheets with large sizes (>10 μm) can be easily electrostatically attracted onto positive Au electrodes modified LY2835219 mouse with cysteamine hydrochloride in aqueous solution. The assembled GO sheets on Au electrodes can be directly reduced into rGO sheets by hadrazine or pyrrole vapor and consequently provide the sensing devices based on self-assembled rGO sheets. In addition, pyrrole-vapor-reduced rGO-based sensor exhibits excellent response to NH3. We expect the easy, reproducible, green, and scalable fabrication of the sensors based on rGO reduced by pyrrole, with excellent performance, miniature,

low-cost, and portable characteristics, can pave a new avenue for the application of assembled rGO devices in gas sensing field. Methods Materials The natural graphite (32 meshes) used in this study was obtained from Qingdao Jinrilai Co. Ltd, Qingdao, China. Pyrrole was obtained from Shanghai Chemical Reagents Co. Ltd. (Shanghai, China) and purified by distillation. Pre-determined NH3 gas (1 ppm) mixed with air was purchased from Beijing Beiyang Special Gases Institute Co. Ltd. (Beijing, China). Concentrated ammonia solution (25 wt.%) and all of other chemicals (analytical reagent grade) C-X-C chemokine receptor type 7 (CXCR-7) were purchased from Shanghai Chemical Reagents Co. Ltd. (Shanghai, China) and were used without further purification. All of organic solvents were purified by distillation. Self-assembly of GO sheets on Au electrodes GO sheets with large sizes were prepared similar to the method reported by Zhao et al. [36]. Large-size GO aqueous solution with the concentration at 2.5 mg/mL was prepared by mild sonication (80 W for 5 min) and stored for the further self-assembly process. The standard microfabrication procedures were exploited to obtain the Au electrodes according to the method illustrated by us before [37].

The kinetic properties of the Rv1096 protein toward M. smegmatis PG were determined as described previously [19]. The molarity of M. smegmatis PG was calculated based the assumption that M. smegmatis PG is primarily composed of repeat units of GlcNAc-MurNAc (MurNGlyc)-L-Ala-D-Glu-A2pm, MW 868.8 [20–22]. First, the initial velocity was evaluated according to the duration of each reaction (5, 10, selleck 15, 30 or 45 min) and the Rv1096 concentration (1.22, 2.88 or 3.65 μg/ml) curves. Then, the optimal

conditions for the enzymatic reactions were determined. Based on the initial velocity and the optimal conditions that we identified, the steady-state kinetic parameters were determined by a Lineweaver-Burke plot. Lysozyme susceptibility assays To investigate whether the Rv10196 protein contributed to lysozyme resistance in M. smegmatis, wild-type M. smegmatis or M. smegmatis/Rv1096 with over-expressed Rv1096 protein were treated with lysozyme. Both bacterial strains were incubated in LBT medium at 37°C. When the OD600 reached ~0.2, the cultures were divided into two equal volumes parts. One part was treated with lysozyme (Sigma-Aldrich) at a final concentration of 200 μg/ml; the other was not given this treatment. Bacterial growth was monitored by measuring eFT508 concentration the optical density at 600 nm. Bacterial viability was evaluated by counting

the number of colony forming units (CFU) per milliliter on LB agar [23]. Morphology of the M. smegmatisstrains after lysozyme treatment Light microscopy and electron microscopy were used to investigate whether the Rv1096 protein affected the morphology of M. smegmatis in the presence of lysozyme. Bacteria that were treated with lysozyme for 9 h were harvested by centrifugation at 4,500 × g at 4°C for 10 min, after which the pellets were washed with sterilized 1 M PBS (pH 7.0), three times. Samples were prepared for Ziehl-Neelsen acid-fast staining as described previously [24], and observed under a light microscope (Olympus CHB, Japan). The cells for electron microscopic analysis

were fixed with 2.5% glutaraldehyde, followed by post-fixation at room temperature for 2 h with 1% osmium tetroxide. The samples were dehydrated with ethanol, which was replaced with liquid carbon dioxide by critical point drying. The dried samples check details were applied to a silicon wafer slide and sputter-coated with gold before Selleck LY333531 examination by an electronic microscope (JSM-6360 scanning electron, JEOL, Japan). Statistical analysis Data are summarized as mean value ± standard deviation (SD). Data were assessed by two-tailed unpaired t tests. A p value of <0.05 was considered statistically significant. Results Rv1096 shares homology with other deacetylases The amino acid sequences of the Rv1096 protein and other known polysaccharide deacetylases [5, 8–12] were compared by Multalin analysis. The S. pneumoniae PgdA protein (spPdgA), L. monocytogenes PgdA (lmo0415) and L.

Conclusions The effects of the aluminum nanofeatures (nanopores and nanofibers) for enhanced light absorption

were studied in this article. The nanofeatures, which are generated inside and around the periodic microholes, were synthesized Inhibitor Library concentration by femtosecond laser irradiation. The generation of the nanostructures was explained by nucleation and condensation of plasma plume grown during the irradiation process. Significant reduction in light reflection with acceptable improvement of the absorption intensity has been observed with long irradiation time (dwell time) and high repetition rate. The interaction between the small size of nanopores and the bulk quantity of nanoparticles could restore the resonance of the surface plasmons. Acknowledgements This research

was funded by the Natural Sciences and Engineering Research Council of Canada and the Ministry of Research and Innovation, Ontario, Canada. References 1. Sámson ZL, MacDonald KF, Zheludev NI: Femtosecond active plasmonics: https://www.selleckchem.com/products/VX-765.html ultrafast control of surface plasmon propagation. J Optic Pure Appl Optic 2009, 11:114031.CrossRef 2. Yu ET, Derkacs D, Lim SH, Matheu P, Schaad DM: Plasmonic nanoparticle scattering for enhanced performance of photovoltaic and photodetector devices. Proc SPIE 2008, 7033:70331V.CrossRef 3. Liz-Marzán LM: Nanometals: formation and color. Metals Today 2004,7(2):26–31.CrossRef 4. Bohren CF, Huffman DR: Absorption and Scattering of Light by Small Particles. New York: Wiley; 1998.CrossRef 5. Maier SA: Plasmonics: Fundamentals and Applications. New York: Springer; 2007. 6. Bethe H: Theory of diffraction by small holes. Phys Rev 1944,66(7,8):163.CrossRef 7. Najiminaini M, Vasefi F, Kaminska B, Carson JJL: Optical resonance transmission properties of nano-hole arrays in a gold film: effect of adhesion layer. Optics

Express 2011, 19:27.CrossRef 8. Csáki A, Steinbrück A, Schröter S, Fritzsche W: Combination of nanoholes with metal nanoparticles–fabrication and characterization of novel plasmonic nanostructures. Plasmonics 2006, 1:147–155.CrossRef 9. Chang S-H, Gray SK, Schatz GC: Surface plasmon generation and light transmission by isolated nanoholes and arrays of nanoholes in thin metal films. MAPK inhibitor Optics Express 2005,13(8):3150–3165.CrossRef 10. Genet C, Ebbesen TW: Light in tiny holes. Nature 2007, Rucaparib datasheet 445:39–46.CrossRef 11. Degiron A, Ebbesen TW: Analysis of the transmission process through single apertures surrounded by periodic corrugations. Optics Express 2004,12(16):3694–3700.CrossRef 12. Kelly KL, Coronado E, Zhao LL, Schatz GC: The optical properties of metal nanoparticles: the influence of size, shape, and dielectric environment. J Physic Chem 2003, 107:668–677.CrossRef 13. Luk’yanchuk BS, Marine W, Anisimov SI, Simakina GA: Condensation of vapor and nanoclusters formation within the vapor plume produced by nanosecond laser ablation of Si, Ge and C.

haemolyticus and methicillin-resistant S. aureus (MRSA) [13] and appears to play a vital role in generating mosaicism in the genetic contexts of mecA. The insertion of IS431 and homologous recombination between different copies of IS431 can result in acquisition, loss and re-arrangements of genetic components [14, 15]. Therefore, IS431 apparently serves as the “adapters” allowing genetic components to be linked and clustered together to form complicated genetic contexts of mecA. In GenBank and literature, e.g. [3], there are many cases in which

mecA is bracketed by two copies of IS431, either at the same or opposite orientations, i.e. the class C1 or C2 mec complex. In these cases, two copies of IS431 have the potential to form a composite transposon mediating the mobilization of mecA but no 8-bp DR could be identified flanking the class C1 or C2 mec complexes. This suggests that the two copies #Buparlisib randurls[1|1|,|CHEM1|]# of IS431 might have inserted in tandem rather than mobilize together as a unit. Alternatively, IS431 might behave likes IS26[16], an insertion sequence also of the IS6 family, that could lead to adjacent deletions, leaving no DR. No ccr

genes could be identified in this large region containing mecA. In the 1970s and 1980s, it was found that methicillin resistance could be transferred by phages [17–21] in experimental conditions and could be also carried by a transposon, Tn4291, located on a naturally occurring plasmid, CB-5083 purchase pI524 [21]. However, these studies were carried out before the identification of mecA and no sequence information was available for the phages carrying methicillin resistance, Tn4291 and pI524. It remains unclear whether methicillin resistance in these experiments was due to the expression of mecA. In particular, Tn4291 mediated resistance

to methicillin eltoprazine but not to penicillin, raising the possibility that the methicillin resistance determinant carried by Tn4291 was actually not mecA. mecA is usually transferred by SCCmec, but mecA existed in the absence of any known types of ccr genes have been found in both MRSA and CoNS previously. In particular, no known ccr genes were detected for an half of methicillin-resistant S. haemolyticus isolates from a hospital in Tunisia [22], suggesting that elements carrying mecA but lacking ccr genes might be common in S. haemolyticus. However, the detailed genetic context of mecA were not characterized in these cases and therefore the exact reasons for the absence of ccr genes remain unclear [2]. The present study provides a detailed example that mecA was in a context without ccr genes and might be able to be transferred by a MGE other than SCCmec. A complex SCC-like remnant containing components with various origins This 40-kb region between orfX and orf39 contained five copies of IS431 (designated IS431-1 to −5 from upstream of to downstream of mecA, respectively) and three terminal inverted repeats (IR) of SCC elements (Figure 1).

Also initial ΔQ/Δt values (Fig. 1B) declined with increasing antibiotic concentration, but Q max Raf inhibitor tended to a maximum value (~9 J) independent of antibiotic concentration. The calorimetric method thus highlighted differences in action of the two cephalosporines.

E. coli and penicillins. (Fig. 2). Ampicillin and piperacillin were tested as members of the penicillin family. Additionally, the monobactam aztreonam was included in this group, because it is another antibiotic interacting with cell wall this website synthesis but with a different mode of action. The grouping with ampicillin and piperacillin also facilitated a comparison of the curve profile differences. For ampicillin, the MIC could not be determined by either method with the range of concentrations used, although a decrease in heatflow could be detected for 8 mg l-1. For piperacillin, the MIC for E. coli was determined as 4 mg l-1 which corresponds to the value for quality control in the CLSI manual [15]. At the beginning of the experiment, a slight transient increase of the heatflow curve was detected at the MIC as well as on the delayed heatflow curve for a concentration of 2 mg l-1 piperacillin (Fig. 2). The MIC for aztreonam was “”on ASK inhibitor the edge”" of determination as 0.25 mg l-1 using standard methods (OD600 0.06). However, the results of IMC show that the

MIC was higher, and the tested concentrations were too low (Fig. 2). As discussed above, the concentrations of ampicillin were too low to provide much information. However, at 8 mg l-1 P max

decreased. The profiles of the heatflow curves were similar for piperacillin and aztreonam and (Fig. 2A). The heatflow curve at the highest subinhibitory concentration of aztreonam (0.25 mg l-1) had a higher t delay than the one for piperacillin (2 mg l-1) – roughly 950 min vs. 445 min. As is generally the case, antibiotics tended to lower P max . For the heat curves (Fig. 2B) the initial ΔQ/Δt values declined with increasing antibiotic concentration, but the effect was stronger for Flavopiridol (Alvocidib) aztreonam. As before, Q max values tended toward a maximum of 9–10 J not related to antibiotic concentration. E. coli and bacterial protein synthesis inhibitors. (Fig 3.) Two antibiotics inhibiting bacterial protein synthesis were evaluated, amikacin and gentamycin. For gentamycin, the MIC was determined as 1 mg l-1 which is in concordance with the reference MIC as proposed by the CLSI manual [15]. For amikacin, the MIC could not be determined with the tested concentration range by either method. For IMC, after approx. 1100 min (~18 hours) the heatflow curve of the highest concentration of 4 mg l-1 started to increase. The growth of E. coli at this concentration was also confirmed using the standard method, resulting in an OD600 of 0.2 for the samples in the calorimeter and 0.7 for the samples in the water bath.

Only one subject dropped out after the initial baseline. At the completion of the experimental trial, six subjects correctly identified the order of ED vs. placebo, four did not, and five were not sure. Figure 1 Respiratory exchange ratio vs. exercise intensity as a percentage of ventilatory threshold (% of VT) for energy drink and placebo conditions. Values are mean ± standard deviation. Only 30% of VT intensity was different from experimental vs. placebo (*p < 0.046). Discussion This was

the first study to investigate preexercise ingestion of the ED Monster in relation to ride TTE and cardiovascular parameters. Cardiovascular parameters at rest did show an increase in HR after consuming the ED, but there were no changes in any HRV parameters. Ride TTE during cycle

ergometery testing, peak RPE, and peak HR during exercise were not different between the two conditions. The RER measurements during each intensity were not different between the two conditions, find more except for the RER at 30% of VT where the placebo condition was lower. Exercise effects The main finding in this study is consistent with data by Candow et al. [14] who conducted a high-intensity run TTE study in young adults (VO2max of 45.5 ± 6.3 ml • kg–1 • min–1) using a double-blind, crossover, repeated-measures method. They showed no increase in run time or change in RPE with the energy drink Red Bull given preexercise. However, VX-680 supplier Ivy et al. [10] did see an improvement with preexercise Red Bull. Their study also used

a double-blind, randomized, crossover design, but was conducted in athletes with a higher VO2max (54.9 ± 2.3 ml • kg–1 • min–1) and employed a time trial format. Kazemi et al. [32] demonstrated that Phantom and Dragon energy drinks also significantly increased check TTE vs. placebo by 9.3% and 6.5% respectively during a Bruce treadmill test. Caffeine One reason for the lack of increased ride time was possibly the lower dose of caffeine standardized at 2 mg · kgBM-1. The recent International Society of Sports Nutrition (ISSN) NSC23766 molecular weight position stand on energy drinks [33] concluded that although they contain a number of nutrients, the primary ergogenic nutrients appear to be carbohydrate and/or caffeine. The exact mechanism of how caffeine works is still debated, but it is believed to primarily function by acting as an adenosine receptor antagonist, increasing release of free fatty acids, and increasing calcium release and uptake [34]. The track record of positive effects of caffeine is quite good and most studies showed an improvement in exercise capacity in the range of 3–13 mg · kgBM-1[9, 33, 35–40], although Cox et al. [41] did show a decreased time during a time trial performance undertaken at the end of a prolonged cycling bout with a low dose at approximately 1.5 mg · kgBM-1. Denadai, et al. [39] used a dose of around 3 mg · kgBM-1 and showed that in untrained subjects who exercised below their anaerobic threshold, caffeine increased ride TTE and reduced perceived exertion.

Hoff et al. (2008) suggested in their study of P. chrysogenum that closely related species could be mating types of the same biological species. However, no Cilengitide cell line differences in extrolite patterns and phenotype could be observed in isolates CH5424802 of different mating types of Paecilomyces variotii (Houbraken et al. 2008, Samson et al. 2009). Furthermore, our studies showed that

the two mating types discovered in Aspergillus fumigatus (O’Gorman et al. 2009) and Penicillium chrysogenum (Hoff et al. 2008) produced the same pattern of extrolites and are identical in their phenotype (Houbraken, Samson and Frisvad, unpublished data). In case of P. subericola we have observed differences in both growth patterns and extrolite production and hence the description of a new species is warranted. The cork isolates now classified as P. glabrum species showed a high intraspecific variability. The macro- and micromorphologies, extrolites profiles and results of the sequencing of partial regions of the β-tubulin and calmodulin genes supported that variability. If the results were analyzed separately (e.g. the extrolite profile and β-tubulin sequencing) KU55933 chemical structure probably some of them could indicate the existence of at least two different species. The analysis of more isolates of this species isolated from different sources and from different geographic locations is needed to determine species boundaries in P. glabrum and related species. Penicillium subericola

Baretto, Frisvad & Samson, sp. nov.—Mycobank MB 517383 – Fig. 4. Penicillio glabro simile, sed bene crescenti in agaro creatino et formatione mixtionis chemicae obscurae (sed in P. glabro non producenti) distinguitur. Culture ex type: CBS 125096, ex raw cork, Portugal Colony diameters at 7 days in mm: CYA at 25 º C: 37–44; CYA at 30°C: 16–34; CYA at 37°C: no growth; MEA 35–42; YES 39–46; CREA

14–26, moderate to good growth with moderate to good acid production, base production after prolonged incubation (14 days). Good sporulation on CYA, grey-green, velvety and floccose in centre, non sporulating margins 1–6 mm, few small hyaline exudates droplets present, reverse colour cream to brownish. Colonies on MEA grey-green, good sporulation, floccose some isolates with velvety colonies and/or 4��8C velvety with floccose in the centre, exudate absent, reverse is orange brown. Colonies on YES in various shades of green-grey, none or weak sporulation, mycelium inconspicuous, white margins with 1–2 mm, exudates absent, reverse orange-brown to yellow-brown, strongly sulcated (wrinkled). Conidiophores strictly monoverticillate, stipes vesiculate up to 6 μm, smooth, occasionally short 40 μm, majority longer, width 3.0–4.0, vesicles 4.5–7.0 μm, phialides flask shaped, 10–14 × 2.0–3.0 μm, conidia globose, finely roughened, 3–3.5 μm. Extrolites: asperfuran, deoxybrevianamide E and unidentified compounds which are indols with an extended chromophore similar to penitremone.

Genant—GE/Lunar, Hologic—Consultancies; John A. Shepherd—GE/Lunar, Hologic—Consultancies; Thomas Fuerst as “employee and shareholder in Synarc Inc”. Open Access This article CB-839 order 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. References 1. Genant HK, Grampp S, Gluer CC, Faulkner KG, Jergas M, Engelke K, Hagiwara S, Van Kuijk C (1994) Universal standardization for dual x-ray absorptiometry: patient and phantom cross-calibration results. J Bone Miner Res 9:1503–1514CrossRefPubMed 2. International Committee for

Standards in Bone Measurement (1997) Standardization of proximal femur bone mineral density (BMD) measurements by DXA. Bone 21:369–370CrossRef 3. Hui SL, Gao S, Zhou XH, Johnston CC Jr, Lu Y, Gluer CC, Grampp S, Genant H (1997) Universal standardization of bone density measurements: a method with optimal properties

for calibration among several instruments. J Bone Miner Res 12:1463–1470CrossRefPubMed 4. Lu Y, Fuerst T, Hui S, Genant HK (2001) Standardization of bone mineral density at femoral neck, trochanter and Ward’s triangle. Osteoporos Int 12:438–444CrossRefPubMed 5. Boudousq V, Goulart DM, Dinten JM, de Kerleau CC, Thomas E, Mares O, Kotzki PO (2005) Image resolution and magnification using a cone beam densitometer: optimizing data acquisition for hip morphometric analysis. Osteoporos Int 16:813–822CrossRefPubMed 6. Fan B, Lewiecki EM, Sherman M, Lu Y, Miller PD, Genant HK, Shepherd JA (2008) Improved click here precision with Hologic Apex software. Osteoporos Int 19:1597–1602CrossRefPubMed 7. Bland JM, Altman DG (1999) Measuring agreement in method comparison studies. Stat Methods Med Res 8:135–160CrossRefPubMed 8. Genant HK (1995) Universal standardization for dual X-ray absorptiometry: patient and phantom cross-calibration results. J Bone Miner

Res 10:997–998CrossRefPubMed 9. Shepherd JA, Fan B, Lu Y, Lewiecki EM, Miller P, Genant HK (2006) Comparison of BMD precision for Prodigy and Delphi spine and femur scans. Osteoporos Int 17:1303–1308CrossRefPubMed ifenprodil 10. Pearson D, Horton B, Green DJ (2006) Cross calibration of DXA as part of an equipment replacement program. J Clin Densitom 9:287–BTK inhibitor 294CrossRefPubMed 11. Ozdemir A, Ucar M (2007) Standardization of spine and hip BMD measurements in different DXA devices. Eur J Radiol 62:423–426CrossRefPubMed 12. Henzell S, Dhaliwal SS, Price RI, Gill F, Ventouras C, Green C, Da Fonseca F, Holzherr M, Prince R (2003) Comparison of pencil-beam and fan-beam DXA systems. J Clin Densitom 6:205–210CrossRefPubMed 13. Ellis KJ, Shypailo RJ (1998) Bone mineral and body composition measurements: cross-calibration of pencil-beam and fan-beam dual-energy X-ray absorptiometers. J Bone Miner Res 13:1613–1618CrossRefPubMed 14. Blake GM, Harrison EJ, Adams JE (2004) Dual X-ray absorptiometry: cross-calibration of a new fan-beam system.