buy HSP990 P128 Chen, K. O164 Chen, L. O126 Chen, Q. O43 Chen, W. P158 Chen, Y. P39 Chennamadhavuni, S. P189 DNA Damage inhibitor Cherfils-Vicini, J. O106, P62, P101 Chetrit, D. O152 Chia, S. O56 Chiang, C.-S. P223 Chiang, C.-S. P211 Chiappini, C. P204 Chiche, J. O7, O59 Chinen, L. P181 Chiodoni, C. P163 Chiquet-Ehrismann, R. O25 Cho, C.-F. P179 Cho,
N. H. P16, P186 Choi, I.-J. P129 Chong, J.-L. P155 Chouaib, S. O19 Chouaid, C. O106 Choudhary, M. P158 Choudhury, R. P. O154 Chow, F.-S. O24 Christofori, G. O88 Chu, E. S. P37 Chun, K.-H. P129 Chung, J.-J. P29 Chung, W.-Y. P84, P154 Ciampricotti, M. O104 Ciarloni, L. O130 Clark, R. O175 Clarke, P. P2 Clement, J. H. P118 Clemons, M. P159 Clottes. E. P32 Coffelt, S. O112, O144 Cognet, C. P161 Cohen, I. P142 Cohen, K. O79 Cohen, O. O11 Cohen-Kaplan, V. P73 Collins, T. P199, P203 Colombo, M. P. P163 Condeelis, J. O166 Conlon, S. P140 Contreras, L. O187 Cook, K. O127, O128 Cooks, T. O12 Cooper, J.
O187 Coopman, P. P42 Coquerel, B. P63 Cordelières, F. P. O66 Cormark, E. O181 Corvaisier, M. O107 Costa, É. P61 Costa, O. P108, P188 Courtiade, L. O50 Coussens, L. M. O77, O142 Cox, M. E. P195, P210 Cozzi, P. Epigenetics inhibitor J. P184 Craig, M. O99 Crawford, S. O60 Creasap, N. P155 Credille, K. O178 Cremer, I. O18, O106, P62, P101 Crende, O. O29 Crosby, M. O53 Cseh, B. O41 Csiszar, A. P138 Cuevas, I. O77 Currie, M. J. P51 Cussenot, O. P183 Cypser, J. O55 Czystowska, oxyclozanide M. O73 Dabrosin, C. O129 Dachs, G. U. P51 Dahlin, A. M. P149, P164 Damotte, D. O106, P62, P101, P165 Damour, O. P214 Dang,
T. O65 Dangles-Marie, V. O66, P69 Dantzer, F. O185 Daphu, I. K. P64 Darby, I. P102, P182 Dasgupta, A. O184 Dauscher, D. O17, P87 Daussy, C. P168 Dauvillier, S. O38, P144 David, E. P121 Davidsson, S. P174 Davies, H. P189 De Arcangelis, A. P65 de Bessa Garcia, S. A. P26 De Bondt, A. P124 de Chaisemartin, L. P165 De Clerck, Y. A. O13, O100 De Launoit, Y. O48, P194 De Thé, H. P69 de Visser, K. O104 Decouvelaere, A.-V. O48 Dedhar, S. O56 Degen, M. O25 Del Mare, S. O89 Del Villar, A. O151 Delhem, N. O48, P194 Delort, L. P214 Delprado, W. J. P184 Demehri, S. P29 Demers, B. P69 Demirtas, D. O92 Denny, W. O8 Depil, S. O48, P194 Derech-Haim, S. P5 Derocq, D. P42 Deroulers, C. P122 Desmouliere, A. P102, P182 Detchokul, S. P66 Dettmer, K. P49 Deutsch, D. O115 Devlin, C. O53 Dewhirst, M. W. O54 Dews, M. O21 Di Santo, J. O105 Dias, S. P60, P136 Diaz, R. P6 DiCara, D. P212 Dicko, A. P81 Diepart, C. P213 Dieu-Nosjean, M.-C. O106, P165 Diez, E. O107 Dinarello, C. A. O20, O105 Dirat, B. O38, P144 Djonov, V. O88 Dobroff, A. S. O108 Doglioni, C. O116 Dogné, J.-M. O57 Doherty, J. P29 Doleckova, I. O90 Doll, C. P6 Dolznig, H. P138 Domany, E. O81 Dominguez, A. L. O182, P150 Dominguez, G. P10 Donald, C. O180 Dong, Z. P33 Donnou, S. P168 Doratiotto, S. O161 Dörrie, J.
For the proteomics analysis, the two groups of cells were cultured in the same conditions, maintained at 80% confluence and in exponential growth phase, harvested at the same time. Cells were washed with phosphate buffered saline (PBS) 3 times, solubilized in cell lysis buffer on ice for 30 min, followed by centrifugation at 100,000 g for 60 min at 4°C. The protein concentration was determined according to the method of Bradford. Samples were stored at -80°C. Two-dimensional electrophoresis (2-DE) Briefly, linear gradient 24-cm (pH 5-8) readystrip
#AC220 chemical structure randurls[1|1|,|CHEM1|]# (Bio-Rad) was rehydrated overnight at 17°C with 300 μg of protein samples in 500 μl of rehydration buffer (7 M urea, 2 M thiourea, 4% CHAPS, 65 mM DTT, and 0.2% Bio-Lyte). Isoelectric focusing (IEF) was performed by using PROTEAN IEF Cell (Bio-Rad). After IEF, the IPG strip was immediately equilibrated for 15 mins in equilibration buffer
I (6 M urea, 2% SDS, 0.375 M Tris-HCl pH 8.8, 20% glycerol, and 2% DTT) and then for 15 mins in equilibration buffer II (6 M urea, 2% SDS, 0.375 M Tris-HCl pH 8.8, 20% https://www.selleckchem.com/products/bix-01294.html glycerol, and 2.5% iodoaceta-mide). SDS-PAGE was carried out on 12% SDS-polyacrylamide gels (25 cm × 20.5 cm × 1.0 mm) by using the PROTEAN Plus Dodeca Cell (Bio-Rad) at a constant voltage of 200 V at 20°C. After electrophoresis, the gels were stained by using the Silver Stain Plus Kit (Bio-Rad). The above processes were performed in triplicate Resveratrol for each sample. Image Analysis The silver-stained 2-DE gels were scanned on a GS-800 Calibrated Imaging Densitometer (Bio-Rad) at a resolution of 300 dots per inch (dpi). Spot detection, quantification, and the analyses of 2-D protein patterns were done with the PDQuest software (version 7.1, BioRad). Then the report of quantitative differences between two gel images was generated. The gray values of the differentially expressed protein candidates were statistically analyzed by the nonparametric Wilcoxon test. Protein spots that showed more than
3-fold differential expression reproducible in the three gels were taken as differentially expressed candidates and selected. Spot Cutting and In-Gel Digestion Differentially expressed protein spots identified as described in the preceding text were excised from gels by Proteomeworks Spot Cutter (Bio-Rad), destained for 20 mins in 30 mM potassium ferricyanide/100 mM sodium thiosulfate (1:1 [v/v]), and washed in Milli-Q water until the gels shrank and were bleached. The gel pieces were incubated in 0.2 M NH4HCO3 for 20 mins and dried by lyophilization. To each gel piece, 20 μl of 20 μg/ml trypsin (proteomics grade, Sigma, St. Louis, MO) was added and incubated at 37°C overnight. The peptides were extracted three times with 50% ACN and 0.1% TFA and dried in a vacuum centrifuge.
Although GEI are assumed to have been acquired via horizontal gene transfer, for most of them self-transfer has not been tested BAY 63-2521 datasheet under experimental conditions. In some cases only GEI excision from its chromosomal location has been observed, which is presumed to be the first step in horizontal transfer [13]. A self-transferable GEI (e.g., ICE, conjugative transposons and other types) can move its excised DNA to a new host, where it can reintegrate with the help of an integrase enzyme at one or more specific insertion sites. GEI transfer can be ARS-1620 in vitro mediated by
conjugation or transduction, either by the element itself or via mobilization by another MGE. For some GEI the conjugation machinery closely resembles that of known plasmid-types, such as that of the SXT element of Vibrio cholerae [14] or the ICEMlSymR7A element of Mesorhizobium loti [15]. For others it is very distantly related to known plasmid conjugative systems, like for ICEHin1056 of Haemophilus influenzae, suggesting them to be evolutionary ancient elements [16]. The findings that many
GEI resemble phages by their integrase, but plasmids by their conjugative PX-478 cost system [10], suggests they are evolutionary hybrids, which may have global control mechanisms reminiscent of both phages and plasmids. To better understand the global control of such evolutionary hybrid elements and the consequences of the element’s behavior for its bacterial host, it would be helpful to have detailed information on their transcriptional organization and regulation, which is presently still very fragmented. The SXT-element, for example, displays a key regulator (SetR) similar to the phage λ CI repressor that is autocleaved Staurosporine manufacturer upon SOS response, after which
SXT transfer becomes strongly induced [17, 18]. Preliminary regulation studies were also performed on ICEHin1056 [16] and the Pseudomonas aeruginosa elements pKLC102 and PAGI-2 [19], but without attaining a global level. Our group has been studying a mobile GEI in Pseudomonas, Ralstonia and Burkholderia, called the clc element or ICEclc [20]. ICEclc has a size of 103 kilobase-pairs (kbp) and is integrated into the chromosome at the 3′ 18-bp extremity of one or more tRNAy Gly genes by the help of an unusually long P4-type integrase [21–23]. The first half of ICEclc encodes two catabolic pathways involved in chlorocatechol (clc genes) and 2-aminophenol (amn genes) degradation [20] (Figure 1A). The second half contains a large set of syntenic genes that were defined as life-style ‘core’ for sixteen GEIs originating from different Beta- and Gammaproteobacteria [24]. Among other things, this core has been proposed to encode a type IV conjugative secretion system distantly related to that of ICEHin1056 [16]. In addition, this part of ICEclc is assumed to encode the relaxosome complex needed for conjugation and was shown to bear a regulatory factor controlling excision and transfer [25, 26]. ICEclc is transferred from P.
1° from the American Xtal Technology (AXT, Inc., Fremont, find more CA, USA). Samples were initially indium bonded on an Inconel holder and degassed at 350°C for 30 min under 1 × 10−4 Torr in order to remove the contaminants. With the aim of investigating the effect of the Au thickness on the self-assembled Au droplets, various thicknesses of gold films were deposited at a growth rate of 0.5 Å/s with the ionization current of 3 mA as a function of time. The growth rate was calibrated by the XRD measurement. Gold films 2, 2.5, 3, 4, 6, 9, 12, and 20 nm thick were systematically deposited on GaAs (111)A and (100) at the same time in an ion-coater chamber under
1 × 10−1 Torr. Subsequently, substrate temperature (T sub) was ramped up to the target temperature of 550°C for an 4SC-202 mouse annealing process at a ramp rate of 1.83°C/s. The ramping was operated by a computer-controlled recipe in a PLD system, and the pressure was maintained below 1 × 10−4 Torr during the
annealing process. To ensure the uniformity of Au droplets after annealing for 150 s, the T sub was immediately quenched down to minimize the Ostwald ripening [30–32]. Subsequent to the fabrication of the self-assembled Au droplets, an Selleck HDAC inhibitor atomic force microscope (AFM) was utilized for the characterization of surface morphology under the non-contact (tapping) mode with the AFM tips (NSC16/AIBS, μmasch). The Al-coated tips were between 20 and 25 μm in length with a radius of the curvature of less than 10 nm. The tip had a spring constant of approximately 40 N/m and a resonant frequency of approximately 170 kHz. The convolution of tips more sensitively affects the lateral measurement when measuring objects with high aspect ratios as well as high density in general. Thus, to minimize the tip effect and maintain consistency of the analysis, the same type of tips from a single batch were utilized for the characterization of Au droplets. The XEI software (Park Baricitinib Systems, Suwon, South Korea, and Santa Clara, CA, USA) was utilized for the analysis of the acquired data including AFM images, cross-sectional surface line profiles, and
Fourier filter transform (FFT) power spectra. The acquired AFM images were processed by flattening along the x and y directions to improve the image quality. FFT power spectrum is generated by converting the height information from the spatial domain to the frequency domain using Fourier filter transform. Different colors represent different frequency intensities of height; thus, height distribution with directionality of nanostructures can be determined by the color distribution. For larger area surface characterization, a scanning electron microscope (SEM) under vacuum was utilized. The elemental analysis was performed using an energy-dispersive X-ray spectroscopy (EDS) system in vacuum with the spectral mode (Thermo Fisher Noran System 7, Pittsburgh, PA, USA).
The oxidized form of the redox molecule is reduced back to the reduced form OH- at the #buy SC75741 randurls[1|1|,|CHEM1|]# counter electrode (Pt/FTO) by the electrons that re-entered into the UV detector from the external circuit (e- + OH· → OH-). The circuit was completed in this manner, demonstrating a self-powered UV detection property. Overall, the ZnO nanoneedle
array/water solid-liquid heterojunction is one type of regenerative UV detector. Considering the tunability of the absorption edge of ZnO by simply changing the concentration of the doping element like Al [33, 34] or Mg [35, 36] and excellent spectral selectivity of this system, we suggest that the spectral response should be tailored by elemental doping [37] in a relatively wide range, which presents a promising versatile potential. In addition, the photoresponsivity and time performance of the solid-liquid heterojunction can also be improved by seeking for the optimized electrolyte solution. The simple fabrication technique, low cost, and environmental friendliness (nontoxic composition) further add to the solid-liquid UV detector’s commercial application. Conclusion In conclusion, c-axis-preferred ZnO nanoneedle Caspase inhibitor arrays have been successfully prepared on a transparent conductive FTO substrate via a simple hydrothermal
method. A new type of self-powered UV detector based on a ZnO nanoneedle array/water solid-liquid heterojunction structure is fabricated, which exhibits a prominent performance for UV light detection. The photocurrent responds rapidly with UV light on-off switching irradiation under ambient environment. The mechanism of the device
is suggested to be associated with the inherent built-in potential across the solid-liquid interface which works in a Schottky barrier manner that separates the electron-hole pairs generated under UV irradiation. The large relative surface and high crystal quality further promote the photoresponse. This new type of self-powered solid-liquid heterojunction-based UV detector can be a particularly suitable candidate for practical applications for its high photosensitivity; fast response; excellent spectral selectivity; uncomplicated, low-cost fabrication process; and environment-friendly feature. Acknowledgements This work was supported by the National Key Basic Research Program of China Florfenicol (2013CB922303, 2010CB833103), the National Natural Science Foundation of China (60976073, 11274201, 51231007), the 111 Project (B13029), and the Foundation for Outstanding Young Scientist in Shandong Province (BS2010CL036). References 1. Razeghi M, Rogalski A: Semiconductor ultraviolet detectors. J Appl Phys 1996, 79:7433.CrossRef 2. Munoz E, Monroy E, Pau JL, Calle F, Omnes F, Gibart P: III nitrides and UV detection. J Phys Condens Mat 2001, 13:7115.CrossRef 3. Soci C, Zhang A, Xiang B, Dayeh SA, Aplin DPR, Park J, Bao XY, Lo YH, Wang D: ZnO nanowire UV photodetectors with high internal gain.
Yin W, Cheepala S, Roberts JN, Syson-Chan K, DiGiovanni J, Clifford JL: Active Stat3 CH5183284 cost is required for survival of human squamous cell carcinoma cells in serum-free conditions. Mol Cancer 2006, 5:15.PubMedCrossRef 14. Kataoka K, Kim DJ, Carbajal S, Clifford J, DiGiovanni J: Stage-specific disruption of Stat3 demonstrates a direct requirement during both the initiation and promotion stages of mouse skin tumorigenesis. Carcinogenesis 2008,
29:1108–1114.PubMedCrossRef 15. Syed Z, Cheepala SB, Gill JN, Stein J, Nathan CA, Digiovanni J, Batra V, Adegboyega P, Kleiner HE, Clifford JL: All-trans retinoic acid suppresses Stat3 signaling during skin carcinogenesis. Cancer Prev Res (Phila Pa) 2009, 2:903–911.CrossRef 16. Bromberg JF, Wrzeszczynska MH, Devgan G, Zhao Y, Pestell RG, Albanese C, Darnell JE Jr: Stat3 as an oncogene. Cell 1999, 98:295–303.PubMedCrossRef 17. Chan KS, Sano S, Kataoka K, Abel E, Carbajal S, Beltran L, Clifford J, Peavey M, Shen J, Digiovanni J: Forced expression of a constitutively active form of Stat3 in mouse epidermis enhances malignant progression of skin tumors induced by two-stage carcinogenesis. Oncogene 2008, 27:1087–1094.PubMedCrossRef 18. Karin M: Nuclear factor-kappaB in cancer development and progression. Nature 2006, 441:431–436.PubMedCrossRef 19. Aggarwal S, Takada Y, Singh S, Myers JN, Aggarwal BB: Inhibition of growth and survival of human head
and neck squamous cell carcinoma cells by curcumin via modulation of nuclear factor-kappaB signaling. Int J Cancer 2004, 111:679–692.PubMedCrossRef 20. Loercher see more A, Lee TL, Ricker JL, Howard A, Geoghegen J, Chen Z, Sunwoo JB, Sitcheran R, Chuang EY, Mitchell JB, Baldwin AS Jr, Van
Waes C: Nuclear factor-kappaB is an important modulator of the altered gene expression profile and malignant phenotype in squamous cell carcinoma. Cancer Res 2004, 64:6511–6523.PubMedCrossRef 21. Kobielak A, Fuchs E: Links between alpha-catenin, learn more NF-kappaB, and squamous cell carcinoma in skin. Proc Natl Acad Sci USA 2006, 103:2322–2327.PubMedCrossRef 22. Mukhtar H, Agarwal R: Skin cancer chemoprevention. J Investig Dermatol Symp Proc 1996, 1:209–214.PubMed 23. Gupta S, Mukhtar H: Chemoprevention of skin cancer: current status and future prospects. Cancer Metastasis Rev 2002, 21:363–380.PubMedCrossRef 24. Bickers DR, Athar M: Novel approaches to chemoprevention of skin cancer. J Dermatol 2000, 27:691–695.PubMed 25. Fenbendazole Kondo A, Ohigashi H, Murakami A, Suratwadee J, Koshimizu K: 1′-Acetoxychavicol Acetate as a Potent inhibitor of Tumor Promoter-induced Epstein-Barre Virus Activation from Languas galanga, a Traditional Thai Condiment. Biosci. Biotech. Biochem 1993, 57:1344–1345.CrossRef 26. Murakami A, Kuki W, Takahashi Y, Yonei H, Nakamura Y, Ohto Y, Ohigashi H, Koshimizu K: Auraptene, a citrus coumarin, inhibits 12-O-tetradecanoylphorbol-13-acetate-induced tumor promotion in ICR mouse skin, possibly through suppression of superoxide generation in leukocytes. Jpn J Cancer Res 1997, 88:443–452.
Long-term effects were assessed by the total amount
of prednisolone, duration to achieve <20 mg/day of prednisolone, and duration of sustained remission (defined as no relapse). Major adverse effects caused by steroids, including diabetes mellitus, peptic ulcers, infections, bone fractures, and psychiatric symptoms were recorded. These adverse effects were defined by the following criteria: diabetes mellitus; use of anti-diabetic medication, peptic ulcer; based on positive endoscopic findings, infection; requiring medication, bone fracture; induced by steroids including vertebra fracture and femoral neck fracture, psychiatric symptoms; requiring medication, and hypertension; systolic blood pressure >140 mmHg, diastolic blood pressure >90 mmHg or
the initiation of antihypertensive medication. Statistical analysis Data are expressed as the mean ± standard this website NSC 683864 chemical structure deviation. Statistical analyses were performed using a one-way analysis of variance (ANOVA) followed by Tukey’s post Roscovitine clinical trial hoc test. Chi-squared tests were used for comparisons between categorical variables. Remission curves were evaluated by Kaplan–Meier method. A possible predictor of the LOS after the treatment, durations of remission, and major adverse effects were tested by multivariate analysis. Statistical analyses were performed using SPSS statistics 19 (IBM) or Stat-View J version 5.0 (SAS institute Inc). Values of P < 0.05 were considered significant. Results Patient characteristics From 53 patients with MCNS identified in the initial screening, we selected 46 patients who fulfilled the inclusion criteria of this study and divided them into IMP dehydrogenase three groups according to the treatment regimen. The clinical characteristics of patients in the three groups are shown in Table 2. No significant differences were observed in any of the parameters examined. The mean dose of cyclosporine required to maintain the
whole-blood trough level between 50 and 150 ng/ml was 118 ± 30 mg/day (range 50 and 200 mg/day) during the first 6 months of treatment. The average doses of prednisolone initiated immediately after MPT were 30.0 ± 0.0 and 39.0 ± 6.3 mg/day in Groups 1 and 2, respectively. The initial dose of prednisolone in Group 3 was 47.9 ± 7.0 mg/day. The dose of prednisolone was tapered by 5–10 mg every 4–8 weeks. No significant differences were observed in the average doses of prednisolone at discharge among three groups (27.9 ± 3.6 mg/day in Group 1; 30.7 ± 4.6 mg/day in Group 2; 30.4 ± 1.3 mg/day in Group 3; P = 0.062). Table 2 Patients characteristics Characteristic Group 1 (n = 17) Group 2 (n = 15) Group 3 (n = 14) P value Age at diagnosis (years) 37 ± 18 37 ± 16 39 ± 19 0.949 Sex (male:female) 8:9 9:6 9:5 0.596 Body mass index 25.2 ± 5.1 23.7 ± 3.2 22.7 ± 3.4 0.247 Selectivity index 0.12 ± 0.05 0.13 ± 0.10 0.13 ± 0.05 0.890 Systolic blood pressure (mmHg) 119 ± 17 120 ± 17 122 ± 13 0.866 Diastolic blood pressure (mmHg) 73 ± 11 78 ± 11 74 ± 11 0.419 Body weight (kg) 67 ± 17 65 ± 13 63 ± 13 0.
Nucleic Acids Res 2009,37(22):7678–7690.PubMedCrossRef 51. Rojo F: Carbon catabolite repression in Pseudomonas : optimizing metabolic versatility and interactions with the environment. FEMS Microbiol Rev 2010,34(5):658–684.PubMed 52. Daniels C, Godoy P, Duque E, Molina-Henares MA, de la Torre J, Del Arco JM, Herrera C, Segura A, Guazzaroni ME, Ferrer M, Ramos JL: Global regulation of food supply by Pseudomonas putida DOT-T1E. J Bacteriol 2010,192(8):2169–2181.PubMedCrossRef
Cell Cycle inhibitor 53. Moreno R, Martinez-Gomariz M, Yuste L, Gil C, Rojo F: The Pseudomonas putida Crc global regulator controls the hierarchical assimilation of amino acids in a complete medium: evidence from proteomic and genomic analyses. Proteomics 2009,9(11):2910–2928.PubMedCrossRef 54. Jaouen T, Coquet L, Marvin-Guy L, Orange N, Chevalier S, De E: Functional characterization
of Pseudomonas fluorescens OprE and OprQ membrane proteins. Biochem Biophys Res Commun 2006,346(3):1048–1052.PubMedCrossRef 55. Yamano Y, Nishikawa T, Komatsu Y: Cloning and nucleotide sequence of anaerobically induced porin protein E1 (OprE) of Pseudomonas aeruginosa PAO1. Mol Microbiol 1993,8(5):993–1004.PubMedCrossRef 56. Shrivastava R, Basu B, Eltanexor nmr Godbole A, Mathew MK, Apte SK, Phale PS: Repression of the glucose-inducible outer-membrane protein OprB during utilization of aromatic compounds and organic acids in Pseudomonas putida CSV86. Microbiology 2011, 157:1531–1540.PubMedCrossRef 57. Wylie JL, Worobec EA: The OprB porin plays a central role in carbohydrate uptake in Pseudomonas Bafilomycin A1 mouse aeruginosa . J Bacteriol 1995,177(11):3021–3026.PubMed 58. Görke B, Stülke J: Carbon catabolite repression
in bacteria: many ways to make the most out of nutrients. Nat Rev Microbiol 2008,6(8):613–624.PubMedCrossRef 59. Reimann SA, Wolfe AJ: A critical process controlled by MalT and OmpR is revealed through synthetic lethality. J Bacteriol 2009,191(16):5320–5324.PubMedCrossRef 60. Reimann SA, Wolfe AJ: Constitutive Expression of the Maltoporin LamB in the Absence of OmpR Damages the Cell Envelope. J Bacteriol 2011,193(4):842–853.PubMedCrossRef 61. Yan Q, Wang N: The ColR/ColS Two-Component System Plays Multiple Roles in the Pathogenicity of the Citrus Canker Pathogen Xanthomonas citri subsp. citri . J Bacteriol 2011,193(7):1590–1599.PubMedCrossRef 62. Lugtenberg triclocarban BJ, Kravchenko LV, Simons M: Tomato seed and root exudate sugars: composition, utilization by Pseudomonas biocontrol strains and role in rhizosphere colonization. Environ Microbiol 1999,1(5):439–446.PubMedCrossRef 63. Lugtenberg B, Kamilova F: Plant-growth-promoting rhizobacteria. Annu Rev Microbiol 2009, 63:541–556.PubMedCrossRef 64. Herrero M, de Lorenzo V, Timmis KN: Transposon vectors containing non-antibiotic resistance selection markers for cloning and stable chromosomal insertion of foreign genes in gram-negative bacteria. J Bacteriol 1990,172(11):6557–6567.PubMed 65.
