Reactions with no addition of reverse transcriptase served as neg

Reactions with no addition of reverse transcriptase served as negative control and proved the absence of DNA contamination. Specificity of amplification was assessed by analyzing the melting curve of the amplification product. Primers to amplify lscB were used MRT67307 mouse for constructs lscB and lscA Up B while primers to amplify lscA were used for constructs lscA, lscB UpN A and lscB Up A. All the results were normalized to amplification of the cDNA of gyrA (PSPPH3667) as described previously [43]. Analysis of lscA gene expression by

Reverse-Transcriptase polymerase chain reaction (RT-PCR) Template-specific primers were designed for the respective lscA variants of P. syringae pv. selleck inhibitor glycinea PG4180, pv. phaseolicola 1448A, pv. syringae B728a, and pv. tomato DC3000. Bacterial cells were grown in HSC

medium and harvested at an OD600 of 0.5 as well as 2.0. RNA was extracted by acid phenol/chloroform extraction method [11]. An RT-PCR was performed on total mRNA using RevertAid First Strand cDNA Synthesis Kit (Fermentas) as recommended by the manufacturer. The strain-specific lscA primers were used to check for presence of an lscA mRNA by PCR using cDNA as template. Regular PCR with the same primer-pairs and genomic DNA as template were used as controls. The thermocycler program was as follows: 1 cycle of 95°C for 90 s; 25 cycles of 95°C for 15 s, 66°C for 15 s, 72°C for 30 s; 1 cycle of 72°C for 5 min. The results were analyzed by 1% agarose gel electrophoresis. Bioinformatics analyses Vector NTI Advance 10.1.1 (Life Technologies, California, USA) was used for the nucleotide, amino acid sequence alignments, as well as for generating genetic maps. BLAST-N and BLAST-P programs were used for online sequence analyses [44]. The website http://​www.​pseudomonas.​com was consulted for the determination of P. syringae gene orthologs and paralogs [45]. Authors’ information SK – Department of Molecular Microbiology, Molecular Life Sciences Research Center, Jacobs University Bremen,

Germany; ASr – Current Address: Department of Experimental Limnology, Leibniz-Institute of Freshwater Ecology and Inland Fisheries, Epothilone B (EPO906, Patupilone) Stechlin, Germany; DP – Department of Biochemical Engineering, Molecular Life Sciences Research Center, Jacobs University Bremen, Germany; ASt – Department of Molecular Microbiology, Molecular Life Sciences Research Center, Jacobs University Bremen, Germany; MU – Department of Molecular Microbiology, Molecular Life Sciences Research Center, Jacobs University Bremen, Germany. Acknowledgements We thank Helge Weingart for his helpful comments and Ramesh Mavathur for his help with Sanger sequencing. This study was supported by the Deutsche Forschungsgemeinschaft (UL-169/5-1). References 1.

Very recently, Kim et al [30] and Pan et al [31] reported on re

Very recently, Kim et al. [30] and Pan et al. [31] reported on reduced graphene oxide-ZnO nanocomposites for supercapacitor

electrodes by microwave-assisted method, which exhibited a specific capacitance of 109 F g−1 at a scan rate of 2 mV s−1 and 146 F g−1 at selleck chemical a scan rate of 2 mV s−1, respectively. But only approximately 30 F g−1 at a scan rate of 100 mV s−1. A sandwiched nanoarchitecture of reduced graphene oxide/ZnO/deducted graphene oxide is fabricated by Huang et al. [32] using chemical vapor deposition method, which exhibited a specific capacitance of 51.6 F g−1 at a scan rate of 10 mV s−1. Additionally, graphene-ZnO nanocomposites synthesized by other method such as ultrasonic spray pyrolysis method and their electrochemical performance were reported [33, 34]. However, these materials were limited by a low specific capacitance and poor stability at higher scan rate or high current densities. An effective regulation of graphene-ZnO

hybrid for high performance of supercapacitors is still challenging. On the other hand, the investigation ABT-888 manufacturer of solid-state supercapacitors based on graphene-ZnO hybrid is very limited. In this report, a simple and facile synthesis route is developed to prepare graphene-ZnO hybrid as an electrode material for supercapacitors using one-step hydrothermal technique. Initially, graphene oxide (GO) was synthesized using the well-known modified Hummer’s method. ZnO nanorods are inserted between the graphene nanosheets layer-by-layer rather than simply decorated on the surface Clomifene of graphene during GO hydrothermal reduction process. This strategy provides a novel method for the preparation of highly active materials (ZnO nanorods)

directly grown on Gr surface that avoids the restacking of Gr sheets, which show high specific capacitance even at higher scan rate and excellent long-term cycle stability applied in a all solid-state supercapacitor device. Such high electrochemical properties provide important prospects for graphene-ZnO hybrid to be widely used as electrode material in supercapacitor. Methods Materials Graphite powder was purchased from Sigma Aldrich (St. Louis, MO, USA). All other reagents were commercially available and analytic grade and were used directly without any purification. Double-distilled water was used throughout the experiments. Synthesis of graphene oxide Graphite oxide was prepared from natural graphite powder through a modified Hummers method [35]. One gram of graphite powder, 1.1 g sodium nitrate, and 46 ml sulfuric acid were mixed and stirred for 10 min. Then, 3.0 g potassium permanganate was added slowly and temperature maintained below 20°C. DI water was added slowly and the temperature was raised to 90°C. The solution turned bright yellow when 3.0 ml of hydrogen peroxide (30%) was added. The mixture was filtered while warm and washed with warm DI water. Then GO was subjected to dialysis to completely remove metal ions and acids.

Then, the Cr-doped system can serve as a remarkably better photoc

Then, the Cr-doped system can serve as a remarkably better photocatalyst. Ti7MnO16, Ti7FeO16, Ti7CoO16, Ti7NiO16, and Ti7AgO16. The IELs occur in the middle of the band gap, namely the

intermediate level. They may reduce the energy required for electron transition, lower the threshold of photoexcitation, and thus expand the optical absorption spectrum without reducing the energy of electrons or holes. The electrons in the VB can be excited to the IELs and then subsequently excited to the CB by the visible light irradiation. So, IELs are beneficial for extending the sensitive light wavelength. The result gives a good explanation of the red shift [31–34]. However, for these find more kinds of IELs, high impurity doping concentration might form a recombination center for photoexcited electron–hole pairs and results in a decrease in the quantum yield for the photocatalytic reactions [21]. Therefore,

we must control the doping concentration to avoid them to act as Quisinostat datasheet the recombination center of photo-generated electrons and holes. Ti7CuO16. The IELs are located above the VB and partially overlap with the VBM. These kinds of IELs could act as trap centers for photoexcited holes, which can also reduce the recombination rate of charge carriers [10]. The holes generated in the VB produce an anodic photocurrent. Because the Cu t 2g level is close to the VB, the holes easily overlap in highly impure media [5]. Ti7ZnO16 and Ti7YO16. The IELs are located at the top of the VB and completely mixed with the O

2p states to form a new VBM (seen in Figures 3, 4, and 5). The band gaps of Zn- and Y-doped anatase TiO2 are narrowed to 2.69 and 3.15 eV, respectively, and smaller than that of pure TiO2, Buspirone HCl which is consistent with the experimental data on the red shift of the absorption edge [35, 36]. Figure 5 Calculated band structure. (a) Zn-doped anatase TiO2; (b) Y-doped anatase TiO2. Ti7ZrO16, Ti7NbO16. The IELs are not situated at band gap. The electronic structure of Zr-doped TiO2 exhibits similar to that of pure TiO2. Therefore, we can infer that the t2g level due to Zr does not contribute to the photo-response. Similarly, the band gap of Nb-doped anatase TiO2 is larger than that of undoped TiO2 by 0.09 eV, which may result in a blue shift of the absorption edge. Formation energy We analyzed the relative difficulty for different transition metal doping into anatase TiO2 using impurity formation energies, which is a widely accepted method. First-principles calculation for the relative stability of metal-doped TiO2 can help us understand the formation of the doped structures and provide useful guidance to prepare samples.

Significant growth retardance was exerted by p16INK4a compared wi

Significant growth retardance was exerted by p16INK4a compared with

the control. The protein was transduced the day before cell counting. Data shown are the mean ± standard deviation of triplicate wells or experiments. **p < 0.01. c. p16INK4a protein caused evident accumulation of A549 cells find more in G1 phase and a decrease of those in S phase at 48 h after subculture. Data shown are the mean ± standard deviation of three independent experiments. *p < 0.05. Discussion As a tumor suppressor, CDKN2A is an important gene because its inactivation abrogates two fundamental pathways, that of pRB and p53, both of which are involved in carcinogenesis and tumor progression. So far, the distinct tumor suppressive effects of p16INK4a and p14ARF have been established, but those of p12 have not. Furthermore, to the best of our knowledge, the effects of the three transcripts check details have not been compared.

The human A549 cell line is a good model to investigate the suppression effects of each of the three transcript variants. The advantages of this cell line are as follows: First, the CDKN2A locus is homozygously deleted in this cell line, such that there is no interference from the endogenous proteins. This is an important consideration since the effects of p16INK4a were shown in a previous study to be associated with endogenous p16INK4a status [23, 24]. Previous research in our laboratory also demonstrated that introduction

of p16INK4a neither suppresses growth nor decreases colony formation rates by Anip973 and AGZY83-a cells expressing endogenous wild-type p16INK4a [25]. Second, the A549 cell line is wild-type in RB and p53. Therefore, p16INK4a and p14ARF plasmids can be expected to successfully act on the pRB and p53 pathways. As to the methods used in this study, the use of stable transfectants confers several advantages as it eliminates Rho a source of variability in transfection efficiency, which facilitated parallel comparison experiments. Furthermore, the characteristics of cells stably transfected with p16INK4a have been shown to differ from those transiently transfected with the vector; transient p16INK4a transfection induces apoptosis whereas stable transfection markedly suppresses cell growth and cloning efficiency [26]. Research on p12 has been hindered as the gene is expressed in normal pancreas tissue, which is difficult to obtain in a well-preserved state. We successfully constructed a eukaryotic expression vector carrying p12 and were thus able to show that the gene acts as a proliferation inhibitor in A549 cells. Thus, our research provides evidence that p12 has tumor suppressive effects not only in pancreatic and cervical cancer cell lines, as previously reported, but also in a lung cancer cell line. The effects of p12 on other cell types will be investigated in future studies.

Yang S, Land ML, Klingeman DM, Pelletier DA, Lu TS, Martin SL, Gu

Yang S, Land ML, Klingeman DM, Pelletier DA, Lu TS, Martin SL, Guo HB, Smith JC, Brown SD: A paradigm for industrial strain improvement identifies sodium acetate tolerance mechanisms in Zymomonas mobilis and Saccharomyces cerevisiae . Proc Natl Acad Sci USA, in press. 33. Joachimsthal EL, Rogers PL:

Characterization of a high-productivity recombinant strain of Zymomonas mobilis for ethanol production from glucose/xylose mixtures. Appl Biochem Biotechnol 2000, 84–86:343–356.PubMedCrossRef 34. Sambrook JaRD: Molecular Cloning: A Laboratory Manual (Third Edition). Cold Spring Harbor Laboratory selleck chemicals llc Press; 2000. 35. Pelletier DA, Hurst GB, Foote LJ, Lankford PK, McKeown CK, Lu TY, Schmoyer DD, Shah MB, Hervey WJ, McDonald WH, et al.: A general system for studying protein-protein interactions in gram-negative bacteria. J Proteome Res 2008,7(8):3319–3328.PubMedCrossRef 36. Kovach ME, Elzer

PH, Hill DS, Robertson GT, Farris MA, Roop RM, Peterson KM: Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes. Gene 1995,166(1):175–176.PubMedCrossRef Authors’ contributions SY and SDB designed the experiment, analyzed the data and wrote the manuscript. SY constructed the plasmid pBBR3DEST42 and mutant strains and performed the Bioscreen assays. DAP and TSL constructed the expression vector p42-0347 and carried out the Western-blot. All authors read and approved the final manuscript.”
“Background Periodontitis is a complex process affecting tooth-supporting tissues [1]. The pathogenesis of periodontal diseases is largely attributed to localized inflammation, which results from interaction between host and microbial factors [2]. MRT67307 The most

common etiological agent of chronic periodontitis is Porphyromonas gingivalis, a Gram-negative anaerobic black-pigmented bacterium [3]. On tooth surfaces, P. gingivalis is a constituent of the complex multispecies biofilm known as dental plaque, which has SPTBN5 properties of other biofilms found in the human body and in the environment. P. gingivalis can also colonize the tissues and cells of the gingival epithelium [4]. The bacterium can not only invade, but also accumulate inside gingival epithelial cells [5, 6]. Recent evidence demonstrates that the effect of periodontitis might have systemic consequences since the bacterium can spread systemically and locate to other tissues [7–10]. Bacteria living in a biofilm have a physiology different from that of planktonic cells and they generally live under nutrient limitation, including that of iron and heme. The uptake of heme as iron and protoporphyrin IX is an important mechanism by which P. gingivalis and other pathogenic bacteria obtain these compounds for their survival and their ability to establish an infection [11, 12]. Gram-negative bacteria utilize outer-membrane receptors to acquire heme from host hemoproteins directly or through a hemophore or lipoprotein and then transport the captured heme into the cell.

The principle of these methods is based on the detection of IFN-γ

The principle of these methods is based on the detection of IFN-γ produced by the effectors memory T cells upon in vitro stimulation with the TB-specific antigens, early secretory antigen (ESAT) 6 and culture filtrate protein (CFP) 10. IFN can be measured using either ELISpot-based assay, represented by T-SPOT®.TB (Immunotech, Abingdon, UK), or an enzyme-linked immunosorbent assay (ELISA), represented by QFT-G and QFT-in-tube (QFT-IT; Cellestis, Victoria, Australia) [74]. Although QFT-G demonstrates

high specificity for LTBI FK228 order (96–99%), its sensitivity is still questionable (70–78%) [75]. In one study, LTBI treatment was avoided in 20% of patients with positive TST results but negative IGRA results [76]. The use of both methods in parallel can enhance both sensitivity and specificity. Furthermore, routine periodic retesting during therapy could allow for the detection of possible conversions. However, serial TST testing is not strictly I-BET151 molecular weight recommended due to the boosting effect [60]. There is also evidence that the TST can boost subsequent IGRA results. The effect is evident after the first 3 days post-TST testing and potentially wanes after a few months [77]. Furthermore, the use of IGRAs during immunosuppressive treatment (including biologic therapy) is controversial, because the immunosuppression might decrease the production

of IFN and interfere with the results [74]. Another inconvenience for both TST and IGRAs is the lack of discrimination between latent and active TB [60]. Positive TST/IGRAs tests at baseline often remain positive despite a successful anti-TB treatment. In these cases careful Cediranib (AZD2171) monitoring for clinical signs and symptoms of active TB is recommended [78]. According to the Tuberculosis Network European Trials Group (TBNET) consensus, the chemoprophylactic regimens recommended for LTBI include 6 or 9 months with isoniazid, 3 months of rifampicin plus isoniazid, or 4 months of rifampicin [79]. Another regimen used in the USA includes

rifampicin and pyrazinamide for 2 months, although this regimen has been associated with a high number of side effects [80]. The diagnostic tools for active TB infection include clinical assessment, cultures for M. tuberculosis, staining for acid-fast bacilli, chest X-rays, and nucleic acid amplification assays [9]. Although culture is considered the reference standard, in clinical practice the diagnosis and treatment of TB are usually based on the presence of abnormal radiologic findings or clinical suspicion [20]. The recommendations for resuming biologic therapy in active TB patients are controversial. According to the American College of Rheumatology (ACR), anti-TNF therapy can be initiated or resumed after 1 month of chemoprophylaxis for LTBI and after completion of therapy for active disease [78]. The British Society for Rheumatology (BSR) accepts the continuation of biologic therapy during TB treatment if clinically indicated [81]. Hernandez et al.

Also, the disparity between the activities of piperidinyl and mor

Also, the disparity between the activities of piperidinyl and morpholinyl derivatives shows that the oxygen atom in the morpholine molecule is important for the binding with a potential molecular target. This is probably caused by the fact that the oxygen atom can participate in the formation of hydrogen bonds in the drug-target site. Fig. 1 Chemical structures of compounds 22–25 Conclusions Our research showed that chemical character of the C-5 substituent significantly determines the antibacterial activity of the N2-aminomethyl derivatives of the SAR302503 cell line 1,2,4-triazole. This activity can be considerably increased by an introduction of an electron-withdrawing chlorine atom to the phenyl ring in the C-5 position.

In addition to this, the number of atoms which form the aminomethyl STA-9090 molecular weight substituent seems to be important. The activity of the obtained Mannich bases was particularly strong toward opportunistic bacteria. The antibacterial activity of some compounds was similar or higher than the activity of commonly used antibiotics such as ampicillin and cefuroxime. Experimental General comments All reagents and solvents were purchased from Alfa Aesar (Ward Hill, USA) and Merck Co. (Darmstadt, Germany). Melting points were determined using Fisher-Johns apparatus

(Fisher Scientific, Schwerte, Germany) and are uncorrected. The 1H-NMR and 13C-NMR spectra were recorded on a Bruker Avance spectrometer (Bruker BioSpin GmbH, Rheinstetten, Germany) using TMS as an internal standard. The IR spectra (KBr) were obtained on a Perkin-Elmer 1725X FTIR spectrophotometer. Elemental analyses were performed on an AMZ 851 CHX analyzer (PG, Gdańsk, Poland) and the results were within ±0.2 % of the theoretical value. All the compounds were purified by flash chromatography (PuriFlash 430evo, Interchim, USA). Synthesis of thiosemicarbazide derivatives (4–6) Three derivatives of thiosemicarbazide: 1-benzoyl-4-(4-bromophenyl)thiosemicarbazide (4), 4-(4-bromophenyl)-1-[(2-chlorophenyl)carbonyl]thiosemicarbazide click here (5), and 4-(4-bromophenyl)-1-[(4-chlorophenyl)carbonyl]thiosemicarbazide

(6) were synthesized according to the procedure described earlier (Plech et al., 2011a). Their spectral and physicochemical properties were consistent with (Li et al., 2001; Oruç et al., 2004). Synthesis of 1,2,4-triazole derivatives (7–9) Appropriate thiosemicarbazides (4–6) were dissolved in 2 % solution of NaOH. Next, the resulting solution was heated under reflux for 2 h. After cooling, the reaction mixture was neutralized with HCl. The precipitated product was filtered off, washed with distilled water, and recrystallized from EtOH. 4-(4-Bromophenyl)-5-phenyl-2,4-dihydro-3H-1,2,4-triazole-3-thione (7) Yield: 87 %, CAS Registry Number: 162221-97-8. 4-(4-Bromophenyl)-5-(2-chlorophenyl)-2,4-dihydro-3H-1,2,4-triazole-3-thione (8) Yield: 83 %, m.p. 282–284 °C, 1H-NMR (250 MHz) (DMSO-d 6) δ (ppm): 7.08–7.76 (m, 8H, Ar–H), 14.03 (s, 1H, NH, exch. D2O).

Cells were harvested by centrifugation

(5,000 × g, 10 min

Cells were harvested by centrifugation

(5,000 × g, 10 min), washed twice with 0.1 M PBS (pH 7.2) and adjusted to 108 CFU ml-1 using McFarland standard. Bacterial cells were heated at 80°C for 20 min in a water bath and were subsequently used for immunization of mice and screening of hybridoma cells for MAbs production using ELISA. Several Cronobacter strains see more used in the study were isolated from Jordan (Table 1). These isolates were identified and characterized by several traditional and molecular methods [19]. The 16S rRNA sequences of the isolates were deposited in the GenBank (MD, USA) (Table 1), while the isolates were deposited in the Egyptian Microbial Culture Collection (Ain Shams University, Cairo, Egypt). Table 1 Cronobacter and Non-Cronobacter strains used in this study. Isolate # Isolate

identity Source Isolate ID GenBank ID based on 16S rRNA sequence – C. muytjensii – ATCC 51329 – C4 C. sakazakii Clinical –   C6 C. sakazakii Clinical CDC 407-77 – C13 C. sakazakii Clinical ATTC 29004 – Jor* 44 C. sakazakii Food EMCC 1904 FJ906902 Jor* 93 C. sakazakii Food EMCC1905 FJ906906 Jor* 112 C. muytjensii Food EMCC1906 FJ906909 Jor* 146A C. sakazakii Food EMCC1907 FJ906897 Jor* 146B C. sakazakii Food EMCC1908 FJ906910 Jor* 149 C. muytjensii Food EMCC1909 FJ906912 Jor* 160A C. sakazakii learn more Environment EMCC1910 FJ906914 Jor* 170 C. turicensis Food EMCC1912 FJ906916 None -Cronobacter         – C. freundii – ATCC 43864 – - E. coli – ATCC 35218 – - L. ivanovii – ATCC 19119 – - P aeruginosa – ATCC 27833 – - S. enterica Choleraesuis – CIP 104220 – - S. sonnei – ATCC 9290 – Jor*: Strains were isolated from food and environmental samples collected in Jordan and were deposited in the Egyptian Microbial Culture Collection (EMCC; Ain Shams University, Cairo, Egypt) and their 16S rRNA sequences were deposited in the GenBank. C: clinical samples isolated from patients obtained

from CDC (Atlanta, GA, USA) and were a gift from Dr. Ben Davies Tall from U.S. FDA. All the other isolates were obtained from the American Type Culture Collection (ATCC) except for Salmonella which obtained from the Collection of Institute Pasteur (CIP) and S. sonnei which was a local strain Lipopolysaccharide (LPS) Astemizole extraction and antigen preparation LPS was prepared following the method described by Jaradat and Zawistowski [23], with minor modifications. Briefly, C. muytjensii ATCC 51329 cells were harvested from an overnight culture by centrifugation (5,000 × g, 10 min) and resuspended in 50 ml of 50 mM sodium phosphate buffer, pH 7.0. The cells were sonicated 5 times for 45 s intervals at 300 Watts (Branson Sonifier). The sonicated suspension was incubated with pancreatic RNase and DNase (0.1 μg ml-1) in 20 mM MgCl2 at 37°C for 10 min, followed by 10 min at 60°C and then mixed with an equal volume of preheated 90% phenol.

PubMed 4 Versalovic J, Shortridge D, Kibler K, Griffy MV, Beyer

PubMed 4. Versalovic J, Shortridge D, Kibler K, Griffy MV, Beyer J, Flamm RK, Tanaka PD0332991 mw SK, Graham

DY, Go MF: Mutations in 23S rRNA are associated with clarithromycin resistance in Helicobacter pylori. Antimicrob Agents Chemother 1996,40(2):477–480.PubMed 5. De Francesco V, Margiotta M, Zullo A, Hassan C, Giorgio F, Burattini O, Stoppino G, Cea U, Pace A, Zotti M, et al.: Prevalence of primary clarithromycin resistance in Helicobacter pylori strains over a 15 year period in Italy. J Antimicrob Chemother 2007,59(4):783–785.PubMedCrossRef 6. National Committee for Clinical Laboratory Standards: Performance standards for antimicrobial susceptibility testing- Sixth informational supplement. Wayne, Pa; 1999. Tariquidar cell line M100 S9.19,1 7. Piccolomini R, Di Bonaventura G, Catamo G, Carbone F, Neri M: Comparative evaluation of the E test, agar dilution, and broth microdilution for testing susceptibilities

of Helicobacter pylori strains to 20 antimicrobial agents. J Clin Microbiol 1997,35(7):1842–1846.PubMed 8. Osato MS, Reddy R, Reddy SG, Penland RL, Graham DY: Comparison of the Etest and the NCCLS-approved agar dilution method to detect metronidazole and clarithromycin resistant Helicobacter pylori. Int J Antimicrob Agents 2001,17(1):39–44.PubMedCrossRef 9. Oleastro M, Menard A, Santos A, Lamouliatte H, Monteiro L, Barthelemy P, Megraud F: Real-time PCR assay for rapid and accurate detection of point mutations conferring resistance to clarithromycin in Helicobacter pylori. J Clin Microbiol 2003,41(1):397–402.PubMedCrossRef 10. Gerrits MM, van Vliet AH, Kuipers EJ, Kusters JG: Helicobacter pylori and antimicrobial resistance: molecular mechanisms and clinical implications. Lancet Infect Dis 2006,6(11):699–709.PubMedCrossRef 11. Morris JM, Reasonover AL, Bruce MG, Bruden DL, McMahon BJ, Sacco FD, Berg DE, Parkinson AJ: Evaluation of seaFAST, a rapid fluorescent in

situ hybridization test, for detection of Helicobacter pylori and resistance to clarithromycin Isotretinoin in paraffin-embedded biopsy sections. J Clin Microbiol 2005,43(7):3494–3496.PubMedCrossRef 12. van Doorn LJ, Glupczynski Y, Kusters JG, Megraud F, Midolo P, Maggi-Solca N, Queiroz DM, Nouhan N, Stet E, Quint WG: Accurate prediction of macrolide resistance in Helicobacter pylori by a PCR line probe assay for detection of mutations in the 23S rRNA gene: multicenter validation study. Antimicrob Agents Chemother 2001,45(5):1500–1504.PubMedCrossRef 13. Cambau E, Allerheiligen V, Coulon C, Corbel C, Lascols C, Deforges L, Soussy CJ, Delchier JC, Megraud F: Evaluation of a new test, genotype HelicoDR, for molecular detection of antibiotic resistance in Helicobacter pylori. J Clin Microbiol 2009,47(11):3600–3607.PubMedCrossRef 14. Almeida C, Azevedo NF, Iversen C, Fanning S, Keevil CW, Vieira MJ: Development and application of a novel peptide nucleic acid probe for the specific detection of Cronobacter genomospecies (Enterobacter sakazakii) in powdered infant formula.

Biochemistry 2005, 70: 576–583 PubMed 7 Ayadi W, Karray-Hakim H,

Biochemistry 2005, 70: 576–583.PubMed 7. Ayadi W, Karray-Hakim H, Khabir A, Feki L, Charfi S, Boudawara T, Ghorbel A, Daoud J, Frikha M, Busson P, Hammami A: Aberrant methylation of p16, DLEC1, BLU and E-cadherin gene promoters in nasopharyngeal carcinoma biopsies from Tunisian

patients. Anticancer Res 2008, 28 (4B) : 2161–7.PubMed 8. Lo PH, Xie D, Chan KC, Xu FP, Kuzmin I, Lerman MI, Law S, Chua D, Sham J, Lung ML: Reduced expression of RASSF1A in esophageal and nasopharyngeal carcinomas significantly correlates with tumor stage. Cancer Lett 2007, 257 (2) : 199–205.CrossRefPubMed 9. Zhou Wen, Feng Xiangling, Li Hong, Wang Lei, Zhu Bin, Liu Weidong, Zhao Ming, Yao Kaitai, Ren Caiping: Inactivation of LARS2, located at the commonly deleted region 3p21.3, by both epigenetic and genetic mechanisms in nasopharyngeal carcinoma. Acta Biochim Biophys Sin (Shanghai). 2009, 41 (1) : 54–62.CrossRef 10. Liu Z, Zhao J, Chen XF, Li W, Liu R, Lei Z, Liu X, Peng X, Xu K, Chen J, Liu H, Zhou QH, Zhang HT: CpG island methylator phenotype involving tumor suppressor genes located on chromosome 3p in non-small cell lung cancer. Lung Cancer 2008, 62 (1) : 15–22.CrossRefPubMed

11. Agathanggelou A, Honorio S, Macartney DP, Martinez A, Dallol A, Rader J, et al.: Methylation associated inactivation of RASSF1A from region 3p21.3 in lung, breast and ovarian tumours. Oncogene 2001, 20: 1509–1518.CrossRefPubMed 12. Ye M, Xia B, Guo Q, Zhou F, Zhang X: Association of XL184 diminished expression of RASSF1A with promoter methylation in primary gastric cancer from patients of central

China. BMC Cancer 2007, 7: 1–7.CrossRef 13. Steinmann K, Sandner A, Schagdarsurengin U, Dammann RH: Frequent promoter hypermethylation of tumor-related genes in head and neck squamous cell carcinoma. Oncol 17-DMAG (Alvespimycin) HCl Rep 2009, 22 (6) : 1519–26.PubMed 14. Thaler S, Hähnel PS, Schad A, Dammann R, Schuler M: RASSF1A mediates p21Cip1/Waf1-dependent cell cycle arrest and senescence through modulation of the Raf-MEK-ERK pathway and inhibition of Akt. Cancer Res 2009, 69 (5) : 1748–57.CrossRefPubMed 15. Shen WJ, Dai DQ, Teng Y, Liu HB: 5-Aza-CdR regulates the expression of RASSF1A gene in human gastric cancer cell line and inhibits the growth of cells. Zhonghua Wei Chang Wai Ke Za Zhi 2009, 12 (1) : 57–60.PubMed 16. Xue WJ, Li C, Zhou XJ, Guan HG, Qin L, Li P, Wang ZW, Qian HX: RASSF1A expression inhibits the growth of hepatocellular carcinoma from Qidong County. J Gastroenterol Hepatol 2008, 23 (9) : 1448–58.CrossRefPubMed 17. Vos MD, Dallol A, Eckfeld K, Allen NPC, Donninger H, Hesson L, et al.: The RASSF1A Tumor Suppressor Activates Bax via MOAP-1. The Journal of biological chemistry 2006, 281: 4557–4563.CrossRefPubMed 18. Dammann R, Li C, Yoon J-H, Chin PL, Bates S, Pfeifer GP: Epigenetic inactivation of a RAS association domain family protein from the lung tumour suppressor locus 3p21.3. Nature genetics 2000, 25: 315–319.