(32 KB, PDF) (PDF 32 kb) (PDF 33 KB) References 1. Hobson P, Wheatley A: Anaerobic digestion: Modern Theory and Practice. Elsevier, London; 1993. 2. Zehnder AJB: Ecology of methane formation. Edited by: Mitchell R. John Wiley & Sons, London; 1978:349–376. 3. Okabe S, Kamagata Y: Wastewater treatment. In Environmental Molecular Microbiology. Edited by: Liu W. Caister Academic Selleck LY411575 Press, Norfolk, UK; 2010:191. 4. McHugh S, Carton M, Mahony T, O’Flaherty V: Methanogenic population structure in

a variety of anaerobic bioreactors. FEMS Microbiol Lett 2003,219(2):297–304.PubMedCrossRef 5. Bagge E, Sahlström L, Albihn A: The effect of hygienic treatment on the microbial flora of biowaste at biogas plants. Water Res 2005,39(20):4879–4886.PubMedCrossRef

6. Leven L, Eriksson AR, Schnürer A: Effect of process temperature on bacterial and archaeal Epacadostat in vitro communities in two methanogenic bioreactors treating organic household waste. FEMS Microbiol Ecol 2007,59(3):683–693.PubMedCrossRef 7. Zinder SH, Anguish T, Cardwell SC: Effects of Temperature on Methanogenesis in a Thermophilic (58 degrees C) Anaerobic Digestor. Appl Environ Microbiol 1984,47(4):808–813.PubMed 8. Fernandez A, Huang S, Seston S, Xing J, Hickey R, Criddle C, Tiedje J: How stable is stable? Function versus community composition. Appl Environ Microbiol 1999,65(8):3697–3704.PubMed 9. Jetten MSM, Stams AJM, Zehnder AJB: Acetate treshold values and acetate activating enzymes in methanogenic bacteria. FEMS Microbiol Lett 1990,73(4):339–344.CrossRef Dipeptidyl peptidase 10. McMahon KD, Stroot selleck products PG, Mackie RI, Raskin L: Anaerobic codigestion of municipal solid waste and biosolids under various mixing conditions–II: Microbial population dynamics. Water Res 2001,35(7):1817–1827.PubMedCrossRef 11. Goberna M, Insam H, Franke-Whittle IH: Effect of biowaste sludge maturation on the diversity of thermophilic bacteria and archaea in an anaerobic reactor. Appl

Environ Microbiol 2009,75(8):2566–2572.PubMedCrossRef 12. Schnürer A, Schnürer J: Fungal survival during anaerobic digestion of organic household waste. Waste Manag 2006,26(11):1205–1211.PubMedCrossRef 13. Kymäläinen M, Lähde K, Arnold M, Kurola JM, Romantschuk M, Kautola H: Biogasification of biowaste and sewage sludge – Measurement of biogas quality. J Environ Manage 2012, 95:S122-S127. SupplementPubMedCrossRef 14. Münch E, Greenfield PF: Estimating VFA concentrations in prefermenters by measuring pH. Water Res 1998,32(8):2431–2441.CrossRef 15. Koskinen K, Hultman J, Paulin L, Auvinen P, Kankaanpää H: Spatially differing bacterial communities in water columns of the northern Baltic Sea. FEMS Microbiol Ecol 2011,75(1):99–110.PubMedCrossRef 16. Rincon B, Raposo F, Borja R, Gonzalez JM, Portillo MC, Saiz-Jimenez C: Performance and microbial communities of a continuous stirred tank anaerobic reactor treating two-phases olive mill solid wastes at low organic loading rates. J Biotechnol 2006,121(4):534–543.PubMedCrossRef 17.

In an alternative approach, current density of a potentiostatic electrochemical method using poly(vinyl pyrrolidone) was kinetically controlled to synthesize vertically cross-linking Ag nanosheets of several micrometers in width [8, 18]. However, there are very limited studies on the facile and large-scale synthesis of Ag nanosheets by an electrochemical deposition without any templates and surfactants. In this study, we report a facile, large-scale, one-step process of synthesizing Ag nanosheets (tens of micrometers in size and several tens of nanometers in thickness).

AZD8931 Our process uses a template- and surfactant-free electrochemical deposition in an ultra-dilute electrolyte of low electrical conductivity (less than 50 μS∙cm−1). https://www.selleckchem.com/products/gw3965.html The growth mechanism was revealed by time-dependent growth analyses. The present method is environment friendly and low cost because the precursor concentration of Ag ions is very low (several tens of μM) compared with that (above several mM) used in conventional electrochemical methods. Methods Preparation of Ag nanosheets Ag nanosheets were deposited on a substrate by a reverse-pulse potentiodynamic electrochemical

deposition. The aqueous electrolyte was composed of 0.02 mM AgNO3 (#209139, reagent A.C.S., Sigma-Aldrich, St. Louis, MO, USA) and 1.32 mM NH4OH (#13370-0380, Guaranteed Reagent, Junsei Chemical Co., Ltd., Chuo-ku, Tokyo, Japan). The AgNO3 concentration was varied as 0.2 and 2 mM, mafosfamide respectively, to observe

the effects of concentration on the morphologies of Ag deposits. A two-electrode system that comprised a Ag plate (1 mm in thickness and 5 cm in length, 99.9%, Alfa Aesar, Wardhill, MA, USA) as a counter electrode and a Au film-coated Si substrate as a working electrode was used. The exposed area of Au film (90-nm thick) was 0.5 cm × 0.5 cm. The electrolyte was supplied into the rectangular Teflon bath at the constant flow rate of 200 ml/min using a peristaltic pump (# S 600, dslab 24, Gyeonggi-do, Korea). The interdistance between the working and counter electrodes was set at 1 cm. For the reverse-pulse potentiodynamic mode, the reduction potentials (V R) were set to be 10, 15, and 20 V, and oxidation potentials (V O) were set to be 0.05, 0.2, and 0.4 V. The deposition time was varied as 20, 40, 70, and 120 min, respectively. The frequency was controlled as 1, 10, 100, and 1,000 Hz, respectively. The reduction period of the reverse-pulse was set at 3%. Instruments and characterization The homemade two-electrode system was composed of a dual DC power supply (Agilent E3620A, Agilent Technologies, Santa Clara, CA, USA) and a selleckchem function generator (Agilent 33220A). The detailed description can be found in previous work [19]. The microstructures of Ag nanosheets were observed using a field-emission scanning electron microscope (SEM; Hitachi S-4800, Hitachi Ltd., Chiyoda-ku, Japan).

of patients, %)

EGFR mutation     Positive this website Negative pTyr1068 + – p + – p Total 84 8 – 80 33 – TKI therapy 78 8 – 69 31 – ORR(CR + PR) 53.8(42/78) 12.5(1/8) 0.029 23.2(16/69) 3.2(1/31) 0.01 DCR CR + PR + SD 85.9(67/78) 62.5(5/8) 0.118 69.6(48/69) 35.5(11/31) 0.001   PD 14.1(11/78) 37.5(3/8) 30.4(21/69) 64.5(20/31) PFS(months) Median 9.1 4.6 0.224 3.6 1.2 <0.001   95% CI 6.25-11.94 0.00-11.53   1.03-6.30 1.00-1.46   Abbreviations: EGFR, epidermal growth factor receptor; pTyr, phophorylated tyrosine; CR, complete remission; PR, partial response; SD, stable disease; PD, progressive disease; ORR, objective response rate; DCR, disease click here control rate; PFS, progression-free survival. Of 194 patients who received EGFR-TKIs therapy, 54 (27%) patients received EGFR-TKIs as first-line therapy and 140 (73%) patients as second- or more-line. 60 patients (31%) experienced PR, 71(37%) patients

got SD and 63(32%) had PD. No CR was observed. The ORR and DCR of EGFR-TKIs treatment were both higher in patients with EGFR mutations than those without EGFR mutation; ORR was 50.0% (43/89) vs. 17.0% (17/105) P < 0.001, DCR was 83.7% (72/89) vs. 59.0% (59/105) P < 0.001. In a multivariate analysis involving tumor histology, smoking status, sex, and tumor stage, EGFR mutation was an independent factor for tumor response (OR 0.18, 95% CI 0.09 to 0.38, P < 0.001) (Table 1). PFS was significantly different between patients with EGFR mutation and check details those without EGFR mutation (Figure 3). Patients with mutation had a median PFS of 8.8 months v 2.1 months for patients without EGFR mutation (P = 0.024). Evaluation of OS was available for no more than 50% deaths (85/194) at the last follow-up. Figure 3 Progression-free survival curves according to epidermal growth factor receptor mutational

status (A), phosphorylated tyrosine (pTyr) 1068 expression (B), pTyr1173 expression (C). pTyr1068 expression Of 205 assessable patients, 164 (80.0%) had EGFR phosphorylated at Tyr1068. The proportion of patients with pTyr1068 expression was similar across different demographic characteristics (Table 1). Among 194 patients receiving EGFR TKIs, there was a significant difference in ORR or DCR between pTyr1068 expression positive and negative Rho patients; ORR 39.5% (58/154) vs. 5.1% (2/40) P < 0.001, DCR 78.2% (115/154) vs. 41.0% (16/40) P < 0.001(Table 1). Patients with pTyr1068 expression had a prolonged PFS of TKIs treatment compared with those with unphosphorylated Tyr1068 (7.0 months vs. 1.2 months, P < 0.001, Figure 3). A logistic model further confirmed the significant correlation between pTyr1068 and response (OR 0.24, 95% CI 0.16 to 0.37, P < 0.001). The potential role of pTyr1068 expression in predicting clinical outcomes of EGFR-TKIs therapy in patients without EGFR mutation was investigated. The results were encouraging because of the conspicuous positive correlation with a better outcome from EGFR-TKIs therapy among patients with wild-type EGFR.

In contrast to the magnon band structures of arrays of Py stripes separated by air gaps studied earlier [12], near-dispersionless modes exist below the fundamental mode branch (M1) of our Py/BARC sample. One reason is that the Py stripes in our sample

are thicker. In comparison to the Py/Fe(Ni) structures [7], Py/BARC has a generally less-dispersive magnon band structure; however, its measured 1.8 GHz first and 0.7 GHz second bandgaps are of the same order of magnitude as those of the former. It is to be noted that the magnon branches can be classified into two groups. One group comprises branches (labeled M1 to M3 in Figure  3a) whose modes have profiles that are similar, i.e., near-uniform across the Py stripe thickness (z direction), to those observed in Py/air stripe arrays [12, www.selleckchem.com/products/ulixertinib-bvd-523-vrt752271.html 29]. The other dispersionless group (labeled N1 to N5) comprises the selleck products perpendicular GSK2879552 mouse standing spin waves (PSSW). The frequencies of these PSSW modes, with quantization numbers n = 1 and m = 0 to 4 across the thickness and width, respectively, were also analytically calculated [11] and found to be 8.64, 8.94, 9.78, 11.1, and 12.8 GHz, in good agreement with experiment. It is noteworthy that the dynamic magnetizations (represented by arrows in Figure  3b) of the PSSW modes form one or more closed loops, each

resembling the vortex configuration of a ferromagnetic ring [30]. As the dipolar field outside a magnetic vortex vanishes, the dipole-dipole coupling between the PSSW modes is expected to be very weak. This is evidenced by their nearly flat dispersion curves. Interestingly, mode hybridizations exist between the fundamental mode M1 and the respective PSSW modes N2 and N4, as borne out by the simulated hybridized

mode profiles. Hybridization of the fundamental mode M1 with the N3 mode is however precluded due to their different symmetries. The M1 mode possesses odd symmetry, as under a π-rotation about the symmetry axis (y direction) of a Py stripe, its dynamic magnetizations are reversed. The N2 and N4 modes have odd symmetry, while the N3 mode has even symmetry. Beta adrenergic receptor kinase Conclusions In summary, we have measured the simultaneous magnonic and phononic bandgaps of the Py/BARC magphonic crystal by Brillouin light scattering. The measured phononic Bragg gap opening and hybridization bandgap are much wider than those previously observed in laterally patterned multi-component phononic crystals. This is mainly ascribed to the high elastic and density contrasts between the stripe materials, Py and BARC. The hybridization bandgap is found to have an unusual origin in the hybridization and avoided crossing of the zone-folded Rayleigh and pseudo-Sezawa waves. The magnonic dispersion relation comprises near-dispersionless PSSW branches, with some of them lying below the highly dispersive fundamental mode branch.

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Singh SK, Valence F, Molle D, Lortal S, Altermann E, Klaenhammer TR, van Kooyk Y: S layer protein A of Lactobacillus acidophilus NCFM regulates immature dendritic cell and T cell functions. Proc Natl Defactinib price Acad Sci USA 2008, 105:19474–19479.PubMedCrossRef 53. Martinez MG, Prado Acosta M, Candurra NA, Ruzal SM: buy JQEZ5 S-layer proteins of Lactobacillus acidophilus inhibits JUNV infection. Biochem Biophys Res Commun 2012, 422:590–595.PubMedCrossRef 54. Hallam SJ, Konstantinidis KT, Putnam N, Schleper C, Watanabe Y-i, Sugahara J, Preston C, Torre J, Richardson PM, DeLong EF: Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum. Proc Natl Acad Sci 2006, 103:18296–18301.PubMedCrossRef 55. Lasken RS: Genomic sequencing of uncultured microorganisms

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In our previous and current studies; all patients underwent the active watchful waiting strategy. This excludes that the decision-making process did result strictly from the MCPGS, and was not rather based on the repeated clinical re-evaluation that was adopted also on CPGS. This exactly shows that our proposed score is superior to the real

life common clinical practice. It may be concluded that the use of Veliparib price a modified clinical and THI ultrasonographic grading score (MCPGS) with the rationale of active watchful waiting in suspected appendicitis with at least one time repetition of THI-US was a prudent and safe strategy. It may improve the accuracy of diagnosing acute appendicitis in the pediatric population as it is superior to the real life common FRAX597 chemical structure clinical practice. It leads to fewer negative appendectomies compared with those children

to whom it was not applied or other scoring systems were applied as the CPGS with the same strategy of active watchful waiting and repeated US, without a significant change in the perforation rate. Moreover, inpatient observation for serial examinations was reduced significantly. Our clinical practice grading scores can have considerable impact on the diagnosis of acute appendicitis in children. A larger cohort is necessary to validate our findings. Acknowledgements We would like to acknowledge Dr Essam Abd

El Bari and Dr. M Yasser Ibrahim for their assistance in revising the manuscript. References 1. Zakaria OM, Adly OA, El-Labban GA, Khalil HT: Acute Appendicitis Tyrosine-protein kinase BLK In Children: A Clinical Practice Guideline Scoring System. Suez Canal Univ Med J 2005, 8:20–26. 2. François Y, Bonvoisin S, Descos L, Vignal J: Prospective study of a predictive scoring system for the diagnosis of appendicitis in patients with right lower quadrant pain. Long-term outcome]. Gastroenterol Clin Biol 1991, 15:794–799.PubMed 3. Samuel M: Pediatric appendicitis score. J Pediatr Surg 2002, 37:877–881.PubMedCrossRef 4. Rezak A, Abbas HM, Ajemian MS, Dudrick SJ, Kwasnik EM: Decreased use of computed NCT-501 tomography with a modified clinical scoring system in diagnosis of pediatric acute appendicitis. Arch Surg 2011, 146:64–67.PubMedCrossRef 5. Dado G, Anania G, Baccarani U, Marcotti E, Donini A, Risaliti A, Pasqualucci A, Bresadola F: Application of a clinical score for the diagnosis of acute appendicitis in childhood: A retrospective analysis of 197 patients. J Pediatr Surg 2000, 35:1320–1322.PubMedCrossRef 6. Escribá A, Gamell AM, Fernández Y, Quintillá JM, Cubells CL: Prospective validation of two systems of classification for the diagnosis of acute appendicitis. Pediatr Emerg Care 2011, 27:165–169.PubMedCrossRef 7.

Samples were incubated in the presence (+) or absence (-) of trypsin HDAC inhibitor and analyzed by immunoblot analysis using polyclonal anti-VacA serum #958. To analyze potential differences in folding properties of the VacA mutant proteins compared to wild-type VacA, we analyzed the susceptibility of these proteins to proteolytic cleavage. Lysates of H. pylori strains were generated by sonication, and the solubilized proteins

were treated with trypsin as described in Methods. Trypsin digestion of two of the mutant proteins (Δ511-536 and Δ517-544) yielded proteolytic digest patterns that were identical to each other and similar to that of trypsin-digested wild-type VacA (Fig. 3B). Trypsin digestion of two other mutant proteins (Δ433-461 and Δ484-504) yielded different digest patterns, but these mutant proteins were not completely degraded (Fig. 3B). Four mutant proteins (Δ462-483, Δ559-579, Δ580-607, and Δ608-628) were completely degraded by trypsin (Fig. 3B). In general, the four mutant proteins that exhibited relative resistance to trypsin digestion were secreted at relatively high levels compared to mutant proteins that were completely degraded by trypsin (compare Fig. 2 and Fig. 3B). The observed variation among mutant VacA proteins in susceptibility to trypsin-mediated proteolysis suggested that the individual mutant proteins differed C188-9 in vitro in

folding properties. The proteins that were highly susceptible to trypsin digestion and secreted at very

low levels (Δ462-483, Δ559-579, Δ580-607, and Δ608-628) were probably misfolded. Due to the very low Urocanase concentrations of these four proteins in the broth culture supernatants, these mutant VacA proteins were not studied further. To evaluate whether the four mutant proteins exhibiting relative resistance to trypsin-mediated proteolysis (i.e. VacA Δ433-461, Δ484-504, Δ511-536, and Δ517-544) shared other features with wild-type VacA, we analyzed the reactivity of these proteins with an anti-VacA monoclonal antibody (5E4) that recognizes a conformational epitope [35]. Each of the four mutant VacA proteins was Q-VD-Oph chemical structure recognized by the 5E4 antibody (Fig. 4), which provided additional evidence that these mutant proteins were folded in a manner similar to that of wild-type VacA. Figure 4 Reactivity of VacA mutant proteins with a monoclonal anti-VacA antibody. Wild-type H. pylori strain 60190 and strains expressing mutant VacA proteins were grown in broth culture, and secreted VacA proteins were normalized as described in Methods. Wells of ELISA plates were coated with broth culture supernatants, and reactivity of the proteins with an anti-VacA monoclonal antibody (5E4) that recognizes a conformational epitope was determined by ELISA. Reactivity of a vacA null mutant was subtracted as background. Relative VacA concentrations are indicated. Values represent the mean ± SD from triplicate samples.

Within the

ER, calcium is buffered by calreticulin [2, 3]. Calcium is particularly important for the regulation of proliferation and apoptosis P5091 concentration and the imbalance of cell growth and cell death finally leads to cancer. The aim of this study was therefore to evaluate whether the ER Ca2+-homeostasis is altered in lung cancer cell lines compared to normal bronchial epithelium. Figure 1 Increase in the cytoplasmic Ca 2+ -concentration can be due to Ca 2+ -influx from the extracellular space or due to Ca 2+ -release from the endoplasmic reticulum (ER). The equilibrium of the ER Ca2+-content is maintained by sarcoplasmic/endoplasmic reticulum Ca2+-ATPases (SERCA) pumping calcium into the ER and inositol-1,4,5-phosphate- (IP3R) and ryanodine-receptors (RYR) releasing calcium out of the ER. Within the ER, calcium is mainly buffered by calreticulin. Methods Materials Cell selleck screening library culture reagents were obtained from Life Technologies (Eggenstein, Germany). Other reagents were bought from Sigma-Aldrich (Deisenhofen, Germany) unless stated otherwise. The human lung carcinoma cell lines H1339 (Small Cell Lung Carcinoma), DMI 53 pI (Small Cell Lung Carcinoma), LCLC-103H (Large Cell Lung Carcinoma), EPLC 272 (Squamous Cell Lung

Carcinoma), EPLC M1 (Squamous Cell Lung Carcinoma) and HCC (Adeno-Carcinoma) were purchased from the German Collection of Microorganisms and Cell Cultures (DSMZ, Braunschweig, Germany). Primary normal these human bronchial epithelial cells (NHBE) were purchased from Lonza (Walkersville, MD, USA). Ca2+-imaging For quantification of changes in the [Ca2+]c, cells were loaded MLN8237 cell line for 30 min at 37°C with the calcium indicator dye Fluor-4 AM (10 μM, Molecular Probes, Eugene,

OR) in supplemented Hanks Balanced Salt Solution (sHBSS) containing 0.2% Pluronic (Pluronic F-127, Calbiochem, La Jolla, CA). After loading, the cells were incubated for at least 30 min in sHBSS to allow for complete dye deesterification and examined with a fluorescence microscope (Axiovert 200 M, Carl Zeiss, Jena, Germany). Images were recorded in time lapse (1 frame/sec) using a digital CCD camera (AxioCam MRm, Carl Zeiss Vision, Munich, Germany). For each image, regions of interest (ROIs) were defined in single cells, and the average fluorescence intensity of each ROI was measured. Final fluorescence values were expressed as a fluorescence ratio (F/Fo) normalized to the initial fluorescence (Fo). Each analysis was performed using custom written macros in the image analysis software “”Scion”". Western Blot analysis Protein expression was determined by immunoblotting with protein extracts prepared with the Compartmental Protein Extraction Kit according to the manufacturer’s instructions (Chemicon International, Hampshire, United Kingdom). EGFR was used as control for plasma membrane contamination, which was found to be low with no differences between cell types.

The incident power was 0.55 mW, and the accumulation time was 10 s. Results Morphology of fabricated Au nanofilms Figure 1 shows the morphology of fabricated continuous ultrathin gold nanofilms. From Figure 1a,b, the folded nanofilms can be clearly seen as continuous and flexible, and their thickness is about 2 nm. From Figure 1c,d, we know that the nanofilms are composed of gold nanoparticle random arrays with uniform size, steady link, and ultrathin structure. Within the film, the size of the gold nanoparticles is only about 10 nm. The distance between nanoparticles

is in sub-10 nm, filled with even thinner amorphous LGX818 supplier gold, which can be observed from the high-resolution transmission electron microscopy (TEM) images shown in Figure 1b,d. Figure 1 TEM micrographs of the fabricated gold continuous nanofilms. The four panels (a, b, c, d) highlight from different perspectives that the fabricated gold nanofilms are ultrathin continuous films. UV–vis absorption spectrum of the Au nanofilm layer on the ITO glass substrates The localized absorption characteristic of Au films is highly sensitive to the surrounding medium, particle size, surface structure, and shape. The ultrathin Au nanofilm on the ITO glass substrate exhibits an ultraviolet–visible (UV–vis) optical spectrum in Figure 2. The selleckchem continuous and inhomogeneous nanofilm, with a thickness of 2 nm or so and composed of nanometer-sized

metal clusters, exhibits absorption in the UV–vis region attributed to the surface plasmon resonance in the metal islands. It is well known that optical absorption of island films of gold is a function of island density [26]. The absorption band resulting from bounded plasma resonance in the nanoparticles is shifted to longer wavelengths as the nanoisland density increases. The plasmonic absorption band is broadened due to a wider particle size distribution. Figure 2 Visible absorption

spectrum of the continuous Au nanofilm on the ITO glass substrate. The effect of UV–vis absorption spectra of the organic photosensitive layer incorporated in thin Au film Plasmonic enhancement of the P3HT:PCBM bulk heterojunction system is demonstrated in a spin-cast device with an incorporated ultrathin gold nanofilm thickness of Cyclin-dependent kinase 3 2 nm or so. Figure 3 exhibits the absorbance of P3HT:PCBM blend films with and without a layer of nanofilms. An enhanced optical absorption is observed in the spectral range of 350 to 1,000 nm where the P3HT:PCBM blend film is absorbing. The above results indicate that the enhanced absorption is due to the increased Tucidinostat solubility dmso electric field in the plasmon photoactive layer by excited localized surface plasmons around the metallic nanoparticles. This enhancement is attributed to photon scattering and trapping by the surface plasmon generated in the metallic nanoparticles. Figure 3 UV–vis absorption spectra of the blend films of P3HT:PCBM on ITO glass substrates.

PubMedCrossRef 15. Lin YP, Lee DW, McDonough SP, Nicholson LK, Sharma Y, Chang YF: Repeated domains of leptospira immunoglobulin-like proteins interact with elastin and tropoelastin. J Biol Chem 2009, 284:19380–19391.PubMedCrossRef 16. Lin YP, Chang YF: The C-terminal variable domain of LigB from Leptospira mediates binding to fibronectin. J Vet Sci 2008, 9:133–144.PubMedCrossRef 17. Lin YP, Greenwood A, Yan W, Nicholson LK, Sharma Y, McDonough SP, Chang YF: A novel fibronectin type III module binding motif identified on C-terminus selleck screening library of Leptospira immunoglobulin-like protein, LigB. Biochem Biophys Res Commun 2009, 389:57–62.PubMedCrossRef

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