Antisera for detection of CdtA, CdtB, CdtC, CRP, and HtrA, respectively, were used for the immunoblot analyses and representative results of repeated experiments are shown. Molecular weight markers are shown in the lane (MW) on the left. See materials and methods for details about the relative amount of the extracts used. From this data, we suggest that substantial amounts of the CDT proteins were translocated into the periplasm of the bacterial cells and from there may be included

in the OMVs that are being released from the bacterial cell surface. The CDT proteins might be enclosed in the OMVs In order to further assess the nature of the association between CDT proteins and OMVs, we performed a dissociation Belinostat cell line assay as described in Materials and Methods. As shown in Figure 7A the CDT protein was recovered with OMVs in the

pellet after treatment with NaCl, Na2CO3, Urea, or HEPES buffer pH 7.3. Upon SDS solubilization of the OMVs, however, the CDT proteins could not be detected in the pellet but instead the proteins were released and remained in the supernatant after the subsequent centrifugation (Figure 7A, lanes 4 & 9). These results suggested that CDT was intimately associated with the OMVs. Resistance to high concentration urea (8 M) and liberation after SDS solubilization indicated that the proteins were not merely present as protein aggregates, but were surrounded by a membrane. To verify whether or not the Hsp60 protein was directly associated with OMVs, we monitored its fate in the dissociation assay using small molecule library screening the same procedure as was done for CDT proteins. As shown in Figure 7B, the Hsp60 protein was partially released into the supernatant after treatment with Na2CO3 and SDS but not with Urea. However, most of Hsp60 remained in the pellet

even after SDS treatment (Figure 7B, lane 4). Perhaps the formation of protein aggregates after detergent treatment caused Hsp60 to be retained in the pellet. Nevertheless, our results show that CDT and Hsp60 were not associated with OMVs in a similar manner as judged by these assays and the immunoelectron microscopy analysis. Figure 7 Analyses of CDT dissociation from OMVs. (A) Resminostat Dissociation assays of CDT proteins associated with OMVs from C. jejuni. Samples of vesicles in 50 mM HEPES were treated for 60 min on ice in the presence of: NaCl (1 M), Na2CO3 (0.1 M), urea (8 M) or SDS 1%, respectively. The samples were then centrifuged and the resulting pellets (lanes 1-5) and supernatants (lanes 6-10) were analysed by SDS-PAGE and immunoblot analyses with anti-CdtA, anti-CdtB, and anti-CdtC antisera. (B) Dissociation assays of Hsp60 protein. Samples were treated as in (A), and the immunoblot analysis was done with anti-Hsp60 antiserum. We have also analyzed whether the CDT protein subunits are associated with OMVs in other C. jejuni strains. Tests with OMVs samples from the C.

Moreover, Zn-curc localized inside glioblastoma tissues suggesting its ability to cross the blood-tumor barrier. Materials

and methods Ethics statement All animals were handled in strict accordance with good animal practice as defined by the relevant national and/or local animal welfare bodies, and in accordance with the Italian and European legislation. All work was performed in accordance with the guidelines of the National Cancer Institute Regina Elena, where there is currently no active Ethical Committee for animal research, VS-4718 clinical trial and has been filed with the Veterinary Service Unit and the Italian Ministry of Health, in accordance with the Italian and European legislation. Cell culture and treatments The human colon cancer RKO (wtp53), glioblastoma U373MG (expressing R273H p53 mutation) and T98G (expressing M237I p53 mutation) cell lines were maintained in RPMI-1640 (Life Technology-Invitrogen), while human SKBR3 (expressing R175H p53 mutation), MD-MBA231 (expressing p53 mutation R280K) breast cancer cell lines and human fibroblasts (HF) (kindly provided by S. Soddu, Regina Elena National Cancer Institute, Rome, Italy) were maintained in DMEM (Life Technology-Invitrogen), all supplemented with 10% heat-inactivated fetal bovine serum plus glutamine and antibiotics. The following reagents were used: a heteroleptic pentacoordinated (bpy-9)Zn(curc, Cl) complex containing a

4,4′-disubstituted-2,2′-bipyridine as main ligand and curcumin (curc) and chloride (Cl) as ancillary ligands [13] was Liothyronine Sodium dissolved in DMSO and used at the Selleckchem BX-795 indicated concentrations; curcumin was prepared as previously reported [17]; pifithryn-α (PFT-α) (ENZO Life Sciences, Lausen Switzerland) was dissolved in DMSO and used at 30 μM; adryamycin (ADR) was used at 2 μg/ml and ZnCl2 was used at 100 μM. Viability and colony assays Subconfluent cells were plated in triplicate in 60 mm Petri dishes and 24 h later treated with Zn-curc complex (20-50-100 μM) for 24 and 48 h. Both floating and adherent cells were collected and cell viability was determined by Trypan blue exclusion by direct counting with a haemocytometer, as reported. The percentage

of cell viability, as blue/total cells, was assayed by scoring 200 cells per well three times. For long-term cell survival, subconfluent cells were plated in 60 mm Petri dishes and 24 h later treated with Zn-curc complex (20-50-100 μM). Twenty-four hours later, plates were washed with PBS and fresh medium was added. Death-resistant colonies were stained with crystal violet 14 days later. Cell death/PI staining Cell death was detected by cytofluorimetric analysis of propidium iodide (PI)-stained cells staining. Briefly, cells floating were collected by centrifugation and pooled with adherent cells recovered from the plates, fixed in 80% ethanol and stained in a PBS solution containing PI (62.5 mg/mL; Sigma-Aldrich), and RNase A (1.125 mg/mL; Sigma-Aldrich).

Authors’ contributions SL executed the Leptspiral isolation, MAT, PCR and MLST experiments, analyzed the data and drafted the manuscript; CZ participated in the analysis of MLST results; DW participated in the study design; XW participated the MLST experiments; KT participated in the rodents Trapping; XL and XJ provided the reference strains of L. interrogans; YN provided the rabbit anti-Leptospira serum; YL contributed to the culture of leptospiral strains and the MAT

experiments; GY and JZ participated in rodents trapping and Leptospira isolation. GT participated in the study design; JY critically revised the manuscript; all authors read and approved the final manuscript.”
“Background Periodontal CP673451 supplier disease is a bacterially induced and highly common chronic inflammatory condition OICR-9429 in humans, and severe periodontal disease (periodontitis)

remains the major cause of tooth loss in adult population worldwide [1]. Dysregulated host response to pathogenic plaque biofilm critically contributes to destructive inflammation resulting in tissue damage and alveolar bone loss [2]. Porphyromonas gingivalis is a keystone periodontal pathogen in the mixed microbial community and it releases copious amount of lipopolysaccharide (LPS) which perpetually interacts with host cells, thereby significantly contributing to periodontal pathogenesis [1–4]. LPS is a potent immuno-inflammatory modulator which causes serious complications in host. It is comprised of three major components viz. outermost O-antigen, core oligosaccharide regions and innermost lipid A [3]. Lipid A is the biologically most active component of LPS that imparts the endotoxin activity. Its structure differs widely among Gram-negative bacteria species depending on the differences in composition of attached

fatty acids, number of phosphorylation sites and substituted groups attached to the phosphate residues [3]. The canonical lipid A structure in Escherichia coli LPS is a hexa-acylated diphosphorylated glucosamine disaccharide. Previous studies have shown that P. gingivalis possesses highly heterogeneous lipid A structures containing penta-acylated LPS1690 and tetra-acylated LPS1435/1449, and this structural discrepancy may critically account for contrasting biological activities induced by P. gingivalis LPS [3, 4]. Human gingival fibroblasts (HGFs) are the major cell type Atezolizumab in human gingiva [5–7]. They play a key role in maintenance and remodeling of extra cellular matrix (ECM) by producing various structural components, such as collagen, elastin, glycoprotein and glycosaminoglycans. In addition, HGFs also synthesize and secrete various members of matrix metalloproteinases (MMPs) in response to P. gingivalis LPS challenge, which ultimately contribute to periodontal tissue destruction [8]. MMPs are a family of structurally and functionally related proteolytic enzymes containing a zinc-binding catalytic domain and they are active against the components of ECM [8–10].

J Biomol NMR 1995,6(3):277–293.PubMedCrossRef 61. Johnson BA, Blevins RA: Nmr View – a Computer-Program for the Visualization and Analysis of Nmr Data. J Biomol NMR 1994,4(5):603–614.CrossRef 62. Slupsky CM, Boyko RF, Booth VK, Sykes BD: Smartnotebook:

a semi-automated approach to protein sequential NMR resonance assignments. J Biomol NMR 2003,27(4):313–321.PubMedCrossRef P505-15 chemical structure 63. Marsh JA, Singh VK, Jia Z, Forman-Kay JD: Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation. Protein Sci 2006,15(12):2795–2804.PubMedCrossRef 64. Marcotte I, Separovic F, Auger M, Gagne SM: A multidimensional 1 H NMR investigation of the conformation of methionine-enkephalin in fast-tumbling bicelles. Biophys J 2004,86(3):1587–1600.PubMedCrossRef 65. Nan YH, Bang JK, Shin SY: Design of novel indolicidin-derived antimicrobial peptides with enhanced cell specificity and potent anti-inflammatory activity. Quisinostat supplier Peptides 2009,30(5):832–838.PubMedCrossRef 66. Peeters E, Nelis HJ, Coenye T: Comparison of multiple methods for quantification of microbial biofilms grown in microtiter plates. J Microbiol Methods 2008,72(2):157–165.PubMedCrossRef 67. Pedersen SS, Espersen F, Hoiby N, Shand GH: Purification, characterization, and immunological cross-reactivity of alginates produced by mucoid Pseudomonas

aeruginosa from patients with cystic fibrosis. J Clin Microbiol 1989,27(4):691–699.PubMed 68. Ambrosi C, Tiburzi F, Imperi F, Putignani L, Visca P: Involvement of AlgQ in transcriptional regulation of pyoverdine genes in Pseudomonas aeruginosa PAO1. J Bacteriol 2005,187(15):5097–5107.PubMedCrossRef Authors’ contributions

AB carried out the purification of peptides, prepared the samples for CD, NMR and SEM analyses, analyzed the spectra for backbone assignments and secondary structures, performed the experiments on the release of liposome-entrapped calcein and the expression of virulence factors and participated in drafting the manuscript. NV carried out the Depsipeptide concentration membrane depolarization studies, the confocal microscopy examinations with fluorescein-labeled pre-elafin/trappin-2 and drafted the manuscript. SM analyzed NMR data and drafted the manuscript. SMG designed and analyzed NMR experiments. YB conceived the study, participated in its design and wrote the manuscript. All the authors have read and approved the final manuscript. The authors declare no competing interest.”
“Background Periodontitis is a chronic destructive infectious disease of the tooth-supporting tissues. It is one of the most prevalent infectious diseases in the world. With percentages of moderate disease ranging from just below 20% in an age group of 30 to 40 year-olds in Swedish and Norwegian studies to even up to 38% of severe cases in the United States in an on average 75 year-old male population [1–3].

PubMedCrossRef 45. Dever TE, Chen JJ, Barber GN, Cigan AM, Feng L, Donahue TF, London IM, Katze MG, Hinnebusch AG: Mammalian eukaryotic initiation factor 2 alpha kinases functionally substitute for GCN2 protein GSK1904529A manufacturer kinase in the GCN4 translational control mechanism of yeast. Proc Natl Acad Sci

USA 1993, 90:4616–4620.PubMedCrossRef 46. Carroll K, Elroy-Stein O, Moss B, Jagus R: Recombinant vaccinia virus K3L gene product prevents activation of double-stranded RNA-dependent, initiation factor 2 alpha-specific protein kinase. J Biol Chem 1993, 268:12837–12842.PubMed 47. Davies MV, Chang HW, Jacobs BL, Kaufman RJ: The E3L and K3L vaccinia virus gene products stimulate translation through inhibition of the double-stranded RNA-dependent protein kinase by different mechanisms. J Virol 1993, 67:1688–1692.PubMed 48. Nonato MC, Widom J, Clardy J: Crystal structure

of the N-terminal segment of human eukaryotic translation initiation factor 2alpha. J Biol Chem 2002, 277:17057–17061.PubMedCrossRef 49. Rothenburg S, Seo EJ, Gibbs JS, Dever TE, Dittmar K: Rapid evolution of protein kinase PKR alters sensitivity to viral inhibitors. Nat Struct Mol Biol 2009, 16:63–70.PubMedCrossRef 50. Dar AC, Dever TE, Sicheri F: Higher-order substrate recognition of eIF2alpha by the RNA-dependent protein kinase PKR. Cell 2005, 122:887–900.PubMedCrossRef 51. Seo EJ, Liu F, Kawagishi-Kobayashi M, Ung TL, Cao C, Dar AC, Sicheri F, Dever TE: Protein kinase PKR mutants resistant to the poxvirus pseudosubstrate selleck chemicals llc K3L protein. Proc Natl Acad Sci USA 2008, 105:16894–16899.PubMedCrossRef 52. Dever TE, Feng L, Wek RC, Cigan AM, Donahue TF, Hinnebusch AG: Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast. Cell 1992, 68:585–596.PubMedCrossRef 53. Reid GA, Schatz G: Import of proteins into mitochondria. Extramitochondrial pools and post-translational import ofmitochondrial protein precursors in vivo. J Biol Chem 1982, Lenvatinib price 257:13062–13067.PubMed 54. Edgar RC: MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 2004, 32:1792–1797.PubMedCrossRef

55. Pollastri G, McLysaght A: Porter: a new, accurate server for protein secondary structure prediction. Bioinformatics 2005, 21:1719–1720.PubMedCrossRef Authors’ contributions SR and TED devised this study with important input from VGC. All experiments were performed by SR. The manuscript was drafted by SR with essential contributions from TED and VGC. All authors read and approved the final manuscript.”
“Background Pasteurella pneumotropica is a Gram-negative rod-shaped bacterium that is frequently isolated from the upper respiratory tract of laboratory rodents. This bacterium is a major causative agent of opportunistic infection in rodents, and almost all infected immunocompetent rodents exhibit unapparent infection. An earlier study reported that coinfection by P.

K. and U.Sch.). Both systems are commercially available (Heinz Walz GmbH, Germany). The experimental setup is depicted schematically BMN 673 purchase in Fig. 1. Fig. 1 Block scheme of experimental setup for simultaneous measurements of dual-wavelength (550–520 nm) difference signal (P515) and CO2 uptake. For further explanations, see text The leaf was enclosed

in a gas-exchange cuvette (3010-DUAL, Walz), with an illuminated area of 1.3 cm2 and 1 mm chamber depth. Leaf temperature was kept close to 20 °C (between 19.5 and 21.5 °C). Within the cuvette the leaf was sandwiched between the end-pieces of two 10 × 10 mm perspex light guides connected to emitter (DUAL EP515) and detector (DUAL DP515) units of the Dual-PAM-100. CO2 and H2O concentration of the incoming gas was controlled via the GFS-3000 Gas Exchange System. A carrier gas with 2.1 % O2 in N2 was provided. The gas stream (400 μmol s−1) passed the leaf twice, at lower and upper sides before entering the Infrared Gas Analyzer for assessment selleck of CO2-uptake and H2O-release. The emitter unit consisted of an array of 8 white LEDs equipped with interference filters. While the “550 nm” ML was derived from 3 white LEDs with 3 individual 550 nm interference filters

(resulting wavelength 550.5 nm, 5.5 nm HBW), 4 white LEDs equipped with 4 individual 520 nm interference filters (resulting wavelength 518.5 nm, 8.5 nm HBW) provided “520 nm” ML. A single white LED with a 535 nm interference filter (5.5 nm HBW) gave 535 nm ML (not used for the measurements presented in this study). The 8 LEDs were arranged in a ring and focused via a central 6.5 mm hole in a chip-on-board (COB) LED array (featuring 635 nm Power-LEDs for actinic illumination) on a 10 × 10 mm Perspex rod, which served for mixing the various light qualities and guiding the randomized light to the leaf sample. In addition, a single 730 nm LED equipped with a 1 mm RG9 filter in the center of the LED array served for far-red

illumination (FR). The COB array consisted of 24 Power-LED-Chips which for short times PDGFR inhibitor can be driven with high currents (up to 1.5 A). It provided not only continuous actinic illumination, but also saturating single turnover flashes (ST). The LED array (1) was powered by LED drivers in the DUAL-C control unit, containing dedicated hard- and firm-ware. The pulse-modulated green ML originating from the emitter unit was partially transmitted via the leaf into the outgoing 10 × 10 mm perspex rod and guided to the detector unit. Before reaching the 10 × 10 mm PIN-photodiode (2), it passed a blue-green filter (3) (1 mm BG39, Schott), which served for absorption of AL, ST, and FR lights. After pre-amplification, the pulse-modulated difference signal was processed with the help of a selective window amplifier within the DUAL-C control unit. Two settings of hardware damping of the signal were provided for fast and slow kinetics measurements, with 10 μs and 1 ms time constants, respectively.

The values of the intensity ratios shown between parentheses were obtained from the Raman spectra of CNTs on the electrodes, while values outside parentheses were taken in between the electrodes. The obtained local intensities of the G+ band are displayed in the Raman map shown in Figure 5. The I D/I G ratio for CNT bundles between the electrodes and on the electrodes DMXAA order is shown in the mapping of Figure 6. The I D/I G ratio appears similar for different excitation wavelengths having a value of 0.29 ± 0.02 for CNTs on the bundles between the electrodes and a I D/I G ratio of 0.30 ± 0.01 for

CNTs on the electrode. The shape of the three peaks (D, G+, and G−) does not change throughout the investigated region. Given that the Raman imaging shows a homogeneous CNT quality along the FET, differences in resistance observed by CS-AFM between different bundles can most certainly be attributed to the quality of the Pd electrode/CNT contact, and not to the CNT quality. A slightly higher defect concentration observed at the CNTs on the electrodes might come from welding of the CNT onto the Pd electrode during deposition, although such small difference in I D/I G ratio is within the experimental error. Conclusions Raman spectroscopy and imaging Trichostatin A ic50 in addition to current sensing AFM were used in order to investigate

a CNT-based device. Semiconducting single-walled CNTs were deposited and aligned using dielectrophoresis. The semiconducting character of the CNT bundles was proved by Raman spectroscopy, and the SWCNT diameter was determined to be 2.5 ± 0.3 nm. It is shown that an Ohmic contact between the palladium electrodes and the CNTs is realized using this fabrication method without any significant increase in

defect density at the GABA Receptor CNT/electrode contact. Acknowledgments The work is supported by the following projects: DFG Research Unit 1713 ‘Sensorische Mikro- und Nanosysteme’ and DFG project ZA146/22-1 Raman investigations of In(Ga)As/Al(Ga)As self-assembled quantum dot structures: from ensembles to single quantum dots’. Alexander Villabona is acknowledged for the implementation of the stage for Raman imaging. We also acknowledge the staff of the ZfM for the help with structure fabrication and SEM measurements. References 1. Hueso LE, Pruneda JM, Ferrari V, Burnell G, Valdes-Herrera JP, Simons BD, Littlewood PB, Artacho E, Fert A, Mathur ND: Transformation of spin information into large electrical signals using carbon nanotubes. Nature 2007, 445:410–413.CrossRef 2. Kuemmeth F, Ilani S, Ralph DC, McEuen PL: Coupling of spin and orbital motion of electrons in carbon nanotubes. Nature 2008, 452:448–452.CrossRef 3. Sgobba V, Guldi DM: Carbon nanotubes-electronic/electrochemical properties and application for nanoelectronics and photonics. Chem Soc Rev 2009, 38:165–184.CrossRef 4.

Tornatore, L., Borgani, S., Dolag, K. and Matteucci, F. (2007). Chemical enrichment of galaxy clusters from hydrodynamical

simulations. MNRAS, 382:1050–1072. AZD1152 molecular weight Vladilo, G. (2004). Dust and planet formation in the early Universe. In Seckbach, J. et al., editors, Life in the Universe, pages 167–168, Kluwer Academic Publishers E-mail: vladilo@oats.​inaf.​it Adaptability of Bacillus subtilis 168 Cells to High UV Stress Marko Wassmann, Ralf Moeller, Günther Reitz, Petra Rettberg German Aerospace Center (DLR), Institute of Aerospace Medicine, Radiation Biology Department, Research Group Photo- and Exobiology, Linder Hoehe, D-51147 Cologne, Germany Previous experiments have shown that vegetative cells of Bacillus subtilis are capable to repair large amounts of DNA photolesions directly after irradiation. But no DNA repair process is error-free, leading to mutations which will be inherited to the following generations (Sung et al., 2003). In a precursory study for the space experiment ADAPT (Molecular adaptation strategies of microorganisms selleck chemicals llc to different space and planetary UV climate conditions)*, cells of Bacillus subtilis 168 were continuously cultured under periodical 16.8 kJ/m2-polychromatic UV irradiation

at 200–400 nm (Wasserman et al., 2007). Approximately 700 generations of B. subtilis had been periodically exposed to UV radiation. Cells evolved under UV stress were 3-fold more resistant to UV-C compared to the ancestral and equally evolved but not UV-irradiated populations. Spores of both cell types respond similar to UV irradiation and exhibit ancestor UV survival characteristics. UV-evolved cells were 7-fold more resistant to ionizing radiation than their non-UV exposed

evolved relatives and ancestor, whereas no changes in the spore survival after ionizing radiation exposure of all three populations were detectable. Current investigations on the molecular mechanisms, e.g. transcriptional profiling, will allow understanding changes on the adaptation level. Sung, H. M., Yeamans, G., Ross, C. A., and Yasbin, R. E. (2003). Roles of YqjH and YqjW, homologs of the Escherichia next coli UmuC/DinB or Y superfamily of DNA polymerases, in stationary-phase mutagenesis and UV-induced mutagenesis of Bacillus subtilis. J. Bacteriol., 185:2153–2160. Wassmann, M., Moeller, R., Nellen, J., Reitz, G., Rabbow, E., and Rettberg, P. (2007). Bacillus subtilis’ ability to adapt to extreme UV stress. Int. J. Astrobiol., 6:71. *NASA homepage—Exposure Experiment (Expose/ADAPT) http://​www.​nasa.​gov/​mission_​pages/​station/​science/​experiments/​Expose.​html E-mail: Marko.​Wassmann@dlr.​de Historical and Philosophycal Aspects Santiago Ramón y Cajal and His Endosymbiotic Metastructures Within Neurons Ulises Iturbe1,3, Juli Peretó2, Antonio Lazcano1 1Facultad de Ciencias, UNAM. Apartado Postal 70-407, Cd. Universitaria, Mexico, D.

5. To increase knowledge in generalb 5. Participant would use the test to increase knowledge in general  6. Selection of education or work typeb 6. Participant would use the test result as advice in their choice of education or type of work. Test content  1. Test messagea 7. Participant would use the test if the results contain clear and useful statements on personal HE susceptibility

and tailored advice on possible preventive measures (from advice on the type and price of effective skin products Etomoxir in vitro and gloves to advice on strategies to reduce exposure at work).  2. Low test effortb 8. Participant would use the test because it takes no effort: a buccal swab is easy, fast learn more and not painful. Feelings and emotions  1. Curiositya 1. Participant would use the test just out of curiosity about their personal HE susceptibility  2. Feara 2. Participant would not use the test because they fear their personal HE susceptibility  3. “Need” to know personal HE riska 3. Participant would use the test because they feel a need to know their personal HE susceptibility  4. (In)security

about developing HEb 4. Participant would use the test because he/she thinks that a test result would give a feeling of security, or as a confirmation of his/her own suspicions about susceptibility. Participant would not take the test if he/she thinks that

it would only give rise to feelings of insecurity about if and when HE will develop (especially with a positive test result) Involvement with HE  1. Interest Aspartate in genetic diseases in generala 1. Participant would use the test because he/she has an interest in genetics, genetic diseases or genetic testing in general.  2. Have HEa 2. Participant would use the test because he/she has HE now or has had it in the past and consequently knows how unpleasant HE can be.  3. Have acquaintance with HEa 3. Participant would use the test because he/she has an acquaintance with HE and knows how unpleasant HE can be.  4. Professional involvementb 4. Participant would use the test because he/she works in health care. He/she is nurse and, therefore, feels acquainted with health innovations.  5. Only for contribution to scienceb 5. Participant would only use the test to contribute to science. He/she does not want to know their test results. Principles and beliefs  1. Religious beliefsa 1. Participant would not use the test because of his/her religious beliefs.  2. Principally in favour of or against genetic testinga 2. Participant would not use the test because he/she is principally against genetic testing: you should not interfere with nature.

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