Cell 2006, 127:1109–1122 PubMedCrossRef 8 Alexander SP: Flavonoi

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of the psychostimulant effects of caffeine. J Neurochem 2008, 105:1067–1079.PubMedCrossRef 10. Cheuvront SN, Ely BR, Kenefick RW, Michniak-Kohn BB, Rood JC, Sawka MN: No effect of nutritional adenosine receptor antagonists on exercise performance in the heat. Am J Physiol Regul Integr Comp Physiol 2009, 296:R394-R401.PubMedCrossRef 11. Nieman DC, Henson DA, Davis JM, Angela Murphy E, Jenkins DP, Gross SJ, Carmichael MD, Quindry JC, Dumke CL, Utter AC, McAnulty SR, McAnulty LS, Tripplett NT, Mayer EP: Quercetin´s influence on exercise-induced changes in plasma cytokines and muscle and leukocyte cytokine mRNA. J Appl Physiol 2007, 103:1728–1735.PubMedCrossRef 12. Davis JM, Murphy EA, McClellan JL, Carmichael MD, Gangemi JD: Quercetin reduces susceptibility to influenza infection following stressful exercise. Am J Physiol Regul Integr Comp Physiol 2008, 295:R505-R509.PubMedCrossRef 13. Vlachodimitropoulou E, Naftalin RJ, Sharp PA: Quercetin is a substrate for the transmembrane

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Br J Haematol 2004,125(6):749–755 PubMed 160 Eisenbarth GS: Upda

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CM, Palmer M, Schvarcz E, Aman J: Prevalence of urinary tract symptoms in long-standing type 1 diabetes mellitus. Diabetes Metab 1998,24(4):351–354.PubMed 164. Couri CE, Oliveira MC, Stracieri AB, Moraes DA, Pieroni F, Barros GM, Madeira MI, Malmegrim KC, Foss-Freitas MC, Simoes BP, et al.: C-peptide levels and insulin independence following autologous nonmyeloablative hematopoietic stem cell transplantation in newly diagnosed type 1 diabetes mellitus. JAMA 2009,301(15):1573–1579.PubMed 165. Snarski E, Torosian T, Paluszewska PARP inhibitor M, Urbanowska E, Milczarczyk A, Jedynasty K, Franek E, Jedrzejczak WW: Alleviation of exogenous insulin requirement in type

1 diabetes mellitus after immunoablation selleck and transplantation of autologous hematopoietic stem cells. Pol Arch Med Wewn 2009,119(6):422–426.PubMed 166. Trivedi HL, Vanikar AV, Thakker U, Firoze A, Dave SD, Patel CN, Patel JV, Bhargava AB, Shankar V: Human adipose tissue-derived mesenchymal stem cells combined with hematopoietic stem cell transplantation synthesize insulin. Transplant Proc 2008,40(4):1135–1139.PubMed 167. Wijesekera LC, Leigh PN: Amyotrophic lateral sclerosis. Orphanet http://www.selleck.co.jp/products/Docetaxel(Taxotere).html J Rare Dis 2009, 4:3.PubMed 168. Janson CG, Ramesh TM, During MJ, Leone P, Heywood J: Human intrathecal transplantation of peripheral blood stem cells in amyotrophic lateral sclerosis. J Hematother Stem Cell Res 2001,10(6):913–915.PubMed 169. Mazzini L, Ferrero I, Luparello V, Rustichelli D, Gunetti M, Mareschi K, Testa L, Stecco A, Tarletti R, Miglioretti M, et al.: Mesenchymal stem cell transplantation

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For A niger

and previously characterized gene products,

For A. niger

and previously characterized gene products, given names are also included. This phylogenetic tree was built using the neighbor joining algorithm with 32 000 Entospletinib bootstrap replicates. Based on sequence identities, the S. cerevisiae Tps1 protein was selected by the software as outgroup. Optional settings or use of other algorithms gave identical, or very similar, results. Two-hybrid assay to reveal putative protein-protein interactions In order to determine whether the homologous proteins physically interact, as has been reported in S. cerevisiae[39], we performed a bacterial-based two-hybrid assay screening for interactions between all six A. niger proteins. For each protein, the full-length open reading frame was cloned into an expression vector and co-transformed into E. coli cells. All 36 possible combinations of A. niger proteins were screened, together with two clones containing different subunits of the leucine zipper GCN4 serving as a positive control and four combinations of one A. niger

protein and one bacterial protein serving as negative controls. Results with no interactions were repeated at least once in an additional independent two-hybrid assay. Where interactions were detected, the assay was repeated in at least two independent assays. Results indicated that TpsB interacts click here with TpsA, TpsB and TppA, and that all Tps units Adriamycin molecular weight interact with themselves (Table 4). All putative interactions involving either TppB or TppC did not score any signals above the negative controls (data not shown). why Table 4 Protein-protein interactions assayed by Bacterial adenylate cyclase two-hybrid system Protein TpsA TpsB TpsC TppA TpsA 418 (210–863)* 1746 (1582–1799) 113 (77–135) 71 (43–89) TpsB 1593 (1467–1832) 1776 (1658–1988) 441 (341–560) 581 (322–714) TpsC 172 (101–244) 688 (315–980) 1214 (861–1551) 80 (67–102) TppA 429 (167–656) 691 (462–987) 156 (133–198) 83 (58–98) *Estimated values are in units/mg dry weight

bacteria. Values in parentheses are the highest and lowest scores for each based on three to four independent assays. The positive control zip-zip (T18 and T25 fragments of the leucine zipper of GCN4) was scored to 3429 (2938–4270). Negative controls and remaining protein interactions scored at maximum 220 (zip-tpsA) but usually less than 50. Values in bold are considered true protein-protein interactions. Gene expression during conidial outgrowth Gene expressions were quantified during different stages of A. niger development. Preliminary results showed that due to the extractability of different structures, two RNA extraction protocols (see Methods) were required: The first included high force to break the tough cell walls of conidia and early germination structures; and, the second was more efficient for fragile structures. Notably, the second protocol was not vigorous enough to extract any RNA from spores (data not shown).

Thin sections (100 nm) were

Thin sections (100 nm) were obtained using Leica Ultracut (Leica, Germany) and collected on Nickel grids (200 mesh; Electron Microscopy Sciences). For localization, monoclonal anti-PLG antibody (1:100) (Sigma) was used. The grids were washed and subsequently treated with gold (10 nm) conjugated – anti mouse IgG. Mice pre-immune

serum was used as a negative control. The immunolabeled sections Autophagy Compound Library chemical structure were stained with uranyl acetate and viewed using a Jeol 2100 F transmission electron microscope (Jeol Analytic Instruments) at an acceleration voltage of 120 KV. Biofilm formation Biofilm formation was observed by growing static cultures of mycobacteria without shaking in 7H9 medium without Tween 80 at 37°C. Biofilm formation was assayed by crystal violet staining method developed by Reicht et al.[19, 20]. Briefly, 200 μl of stationary phase cultures (A600 normalized to 1) were added to 7H9 medium in polystyrene culture plates for biofilm formation and in culture tubes for pellicle formation. After incubation of static culture of M. smegmatis strains for 2 days and M. bovis for 2–3 weeks, biofilm was quantified by removing the medium carefully and staining with 1% crystal violet for 45 min. PCI-34051 research buy The wells were washed three times with water and air-dried. The dye was solubilized with 80% ethanol and A550 was measured. Results Generation

of glnA1 promoter Selleckchem Crenolanib variants Figure 2 shows a schematic representation of the deletion variants of the promoter. M. bovis contains two native promoters P1 and P2 within 320 bp upstream of glnA1 gene

(start codon designated as +1). 124 bp upstream of glnA1 start codon was taken as P1 promoter. Further, from 320 bp upstream sequence, 31 bp (-46 to -76) was deleted from Branched chain aminotransferase the native promoter and taken as P2 promoter. The native, P1 and P2 promoter with glnA1 gene were used for further characterization in response to nitrogen limitation and excess. Figure 2 Schematic representation of glnA1 promoter. glnA1 gene with two promoters P1 and P2. +1 represents glnA1 translational start site. The red arrow represents the transcriptional start site. The black arrow represents the position of primers used to make deletion variants of the glnA1 promoter. Growth characteristics M. bovis strain was grown in low and high nitrogen medium and growth profile was studied by measuring optical density at 600 nm. No significant difference was observed in the growth of M. bovis when cultured in low nitrogen medium as compared to growth in high nitrogen medium (Figure 3A). This indicated that M. bovis was able to acquire nitrogen from other sources in the medium (L-glutamic acid, ferric ammonium citrate and ammonium sulphate). Same was the case when growth of wild type M. smegmatis and MSFP was studied in low and high nitrogen conditions (Figure 3B).

The reaction products were examined by electron microscopy and X-

The reaction products were examined by electron microscopy and X-ray diffraction in order to identify their chemical compositions and microstructures. Methods Alumina-passivated Al nanoparticles with a diameter range of 50 to 120 nm were purchased from Sigma-Aldrich Corporation (St. Louis, MO, USA). These nanoparticles were handled in an argon-filled glove box before being mixed with the oxidizer. The thickness of the oxide shell was about 5 to 8 nm which agrees with the reported data on passivated Al nanoparticles [41, 42]. By assuming the averaged nanoparticle diameter of 80 nm, this shell thickness indicates that the content of Al is about 50%. NiO nanowires were synthesized by

a hydrothermal method; their average diameters were approximately 20 nm, and their lengths were several microns. Hydrothermal synthesis involved two see more major steps. First, NiOH PRN1371 nanostructures were formed at 120°C in a weak GSK126 supplier alkaline solution when Ni(NO3) reacted with a Ni source. NiO nanowires were then produced by annealing NiOH nanostructures at 500°C

for 1 h at ambient atmosphere. The two reactants were then mixed together and ground in a 50-mL beaker in air; 10 mL of isopropanol was then added to the beaker, and the suspension was mixed in an ultrasound bath for 2 h. The suspension was then stir dried on a hot-plate stirrer. The dried powder was carefully scraped from the beaker wall and ground in an alumina mortar. Subsequently, the powder was pressed into

a stainless steel die to make a pellet with a diameter of 3 mm and a height of 0.7 mm. It is worthwhile to mention that a few thermogravimetric analysis (TGA) trails were made in order to fully oxidize the Al nanoparticles in air for determining the content of Al in those particles. The results were however quite uncertain due to the low penetration of O2 into the core of these nanoparticles. Six different compositions indicated in Table 1 were prepared. For each composition, two MTMR9 samples were tested. The weight ratios of NiO in these composites were used to calculate the fuel-to-oxidizer equivalence ratio Φ, defined in this study by the following: (1) where is the measured mass ratio of the fuel to oxidizer and is the stoichiometric ratio calculated from the following thermite reaction between Al and NiO: (2) Table 1 Compositions of six Al nanoparticle and NiO nanowire composites Sample Composition Weight percentage of NiO nanowires (%) Equivalence ratio ( Φ )a A Al-NiO 9 18 B Al-NiO 20 7 C Al-NiO 26 5 D Al-NiO 33 3.5 E Al-NiO 38 2.8 F Al-NiO 50 1.7 aCalculated by the Al content of 42%. In this study, the equivalence ratios were calculated from the mass ratio of Al nanoparticles to oxidizer nanowires by taking into account the mass of the alumina shell. For this purpose, a base hydrolysis method was used to determine the amount of active aluminum in Al nanoparticles [43].

J Chin Med Assoc 2007, 70:324–330 PubMedCrossRef 6 Alijani A, Ha

J Chin Med Assoc 2007, 70:324–330.PubMedCrossRef 6. Alijani A, Hanna GB, Cuschieri A: Abdominal wall lift versus positive-pressure selleckchem capnoperitoneum for laparoscopic cholecystectomy: randomized controlled trial. Ann Surg 2004, 239:388–394.PubMedCrossRef 7. Tai YP, Wei CK, Lai YY: Intraoperative pneumothorax during laparoscopic cholecystectomy. Acta

Anaesthesiol Taiwan 2006, 44:231–234.PubMed 8. Hasson HM, Galanopoulos C, Langerman A: Ischemic necrosis of small bowel following laparoscopic surgery. JSLS 2004, 8:159–163.PubMedCentralPubMed 9. Smith HJ: BI 2536 cost Carbon dioxide embolism during pneumoperitoneum for laparoscopic surgery: a case report. AANA J 2011, 79:371–373.PubMed 10. Korndorffer JR Jr, Fellinger E, Reed W: SAGES guideline for laparoscopic appendectomy. Surg Endosc 2010, 24:757–761.PubMedCrossRef 11. Smith RS, Fry WR, Tsoi EK, Henderson VJ, Hirvela ER, Koehler RH, Brams DM, Morabito DJ, Peskin GW: Gasless laparoscopy and conventional instruments. The next phase of minimally invasive surgery. Arch Surg 1993, 128:1102–1107.PubMedCrossRef 12. Chen D, Shi H, Dong H, Liu K, Ding K: Gasless single-incision laparoscopic appendectomy. Surg Endosc 2011, 25:1472–1476.PubMedCrossRef 13. McKinlay R, Mastrangelo MJ Jr: Current status of laparoscopic appendectomy. Curr Surg 2003, 60:506–512.PubMedCrossRef 14. Tiwari MM, Reynoso JF,

Tsang AW, Oleynikov D: Comparison of outcomes of laparoscopic and open appendectomy in management of uncomplicated CB-839 solubility dmso and complicated appendicitis. Ann Surg 2011, 254:927–932.PubMedCrossRef 15. Kheirabadi BS, Tuthill D, Pearson R, Bayer V, Beall D, Drohan W, MacPhee DNA ligase MJ, Holcomb JB: Metabolic and hemodynamic effects of CO2 pneumoperitoneum in a controlled hemorrhage model. J Trauma 2001, 50:1031–1043.PubMedCrossRef 16. Holzman M, Sharp K, Richards W: Hypercarbia during carbon dioxide gas insufflation for therapeutic laparoscopy: a note of caution. Surg Laparosc Endosc 1992, 2:11–14.PubMed 17. Davidson BS, Cromeens DM, Feig BW: Alternative methods of exposure minimize cardiopulmonary risk in experimental animals during minimally

invasive surgery. Surg Endosc 1996, 10:301–304.PubMedCrossRef 18. Paolucci V, Gutt CN, Schaeff B, Encke A: Gasless laparoscopy in abdominal surgery. Surg Endosc 1995, 9:497–500.PubMedCrossRef 19. Goldberg JM, Maurer WG: A randomized comparison of gasless laparoscopy and CO2 pneumoperitoneum. Obstet Gynecol 1997, 90:416–420.PubMedCrossRef 20. Fingerhut A, Millat B, Borrie F: Laparoscopic versus open appendectomy: time to decide. World J Surg 1999, 23:835–845.PubMedCrossRef 21. Raja AS, Wright C, Sodickson AD, Zane RD, Schiff GD, Hanson R, Baeyens PF, Khorasani R: Negative appendectomy rate in the era of CT: an 18-year perspective. Radiology 2010, 256:460–465.PubMedCrossRef 22. Petroianu A: Diagnosis of acute appendicitis. Int J Surg 2012, 10:115–119.PubMedCrossRef 23.

7%) Escherichia coli 105 (41 8%) (Escherichia coli resistant

7%) Escherichia coli 105 (41.8%) (Escherichia coli resistant

to third generation cephalosporins) 35 (13.%) Klebsiella pneuumoniae 41 (15.3%) (Klebsiella pneumoniae resistant to third generation cephalosporins) 13 (4.8%) Pseudomonas 20 (7.4%) Others 29 (10.8%) Aerobic Gram-positive bacteria 41 (15.3%) Enterococcus faecalis 16 (6%) Enterococcus faecium 10 (3.4%) Staphylococcus Aureus 7 (4%) Others 8 (3%) Bacteroides 8 (3%) Candida albicans 17 (6%) Non candida albicans 6 (2.2%) CB-839 nmr Other yeats 2 (0.7%) All the microorganisms isolated in both intraoperative and subsequent samples from peritoneal fluid are reported in Table 7. Table 7 Total of microorganisms identified from both intraoperative and subsequent peritoneal samples Total 1826 (100%) Aerobic Gram-negative bacteria 1152 (63%) Escherichia coli 653 (35.7%) (Escherichia coli resistant to third generation cephalosporins) 110 (6%) Klebsiella pneuumoniae

181 (9.9%) (Klebsiella pneumoniae resistant to third generation cephalosporins) 39 (2.1%) Klebsiella oxytoca 11 (0.6%) (Klebsiella oxytoca resistant to third generation cephalosporins) 2 (0.1) Enterobacter 75 (4.1%) Proteus 52 (2.8%) Pseudomonas 94 (5.1%) Others 102 (5.6%) Aerobic Gram-positive bacteria 414 (22.7%) Enterococcus faecalis 169 (9.2%) Enterococcus faecium 68 (3.7%) Staphylococcus Aureus 46 (2.5%) Streptococcus spp. 85 (4.6%) Others 47 (2.6%) Anaerobes 141 Screening Library datasheet (7.7%) Bacteroides 108 (5.9%) (Bacteroides resistant to Metronidazole) 3 (0.2%) Clostridium 11 (0.6%) Others 22 (1.2%) Candida spp. 117 (6.4%) Candida albicans 90 (4.9%) (Candida albicans resistant to Fluconazole) 2 (0.1%) Non-albicans Candida 27 (1.4%) (non-albicans Candida resistant to Fluconazole) 3 (0.1%) Other yeats 2 (0.1%) The major pathogens involved in intra-abdominal infections were found to be Enterobacteriaceae. Among the intra-operative

isolates, Extended-Spectrum Beta-Lactamase (ESBL)-producing Escherichia coli STA-9090 ic50 isolates comprised 13.7% (75/548) of all Escherichia coli isolates, while ESBL-positive Klebsiella pneumoniae isolates represented 18.6% (26/140) of all Klebsiella pneumoniae isolates. ESBL-positive Enterobacteriaceae were more prevalent in patients with healthcare associated infections IAIs than they Adenosine were in patients with community-acquired IAIs. ESBL-positive Escherichia coli isolates comprised 20.6% (19/92) of all identified Escherichia coli isolates, while ESBL-positive Klebsiella pneumoniae isolates made up 42.8% (15/35) of all identified Klebsiella pneumoniae isolates. Among all the microorganisms isolated in both intraoperative and subsequent samples from peritoneal fluid, there were 110 isolates of Escherichia coli ESBL, 39 isolates of Klebsiella pneumoniae ESBL, 2 isolates of Klebsiella Oxytoca ESBL. There were 5 isolates of Klebsiella pneumoniae resistant to Carbapenems. Among the microorganisms isolated in the intraoperative samples, there were 74 isolates of Pseudomonas aeruginosa, comprising 5.

670 m, on decorticated branches of Sambucus nigra 1–2 cm thick in

670 m, on decorticated click here branches of Sambucus nigra 1–2 cm thick in leaf debris, 21 Nov. 2009, H. Voglmayr & W. Jaklitsch (WU 30191, culture S 94 = CBS 126958). Notes: Hypocrea sambuci is well characterised by its occurrence on decorticated branches of Sambucus nigra, by minute fresh stromata that appear waxy or gelatinous, similar to those of H. tremelloides, and flat pulvinate to discoid dry stromata that often look like a miniature of H. subalpina. H. tremelloides differs e.g. by incarnate stromata that are typically densely aggregated in large

groups, and by faster growth at higher temperatures. Stromata of H. sambuci are usually accompanied by different green-conidial species of Trichoderma, such as T. harzianum or T. cerinum. Several attempts to prepare a culture under standard conditions failed, because the germ tubes died shortly after germination. Only one specimen (WU 29103) yielded an unstable culture (C.P.K. 3718) upon ascospore isolation Epigenetics inhibitor on CMD at 20°C. The short description above is based on this culture. Conidiophores are similar to those of T. tremelloides, albeit somehow simpler and more regular in structure than the latter. It has not Lazertinib solubility dmso yet been possible to obtain the sequence of tef1 introns of H. sambuci, due to priming issues. Other sequences were obtained using DNA extracted from stromata (WU 29467) and from the culture C.P.K. 3718. ITS, rpb2 and tef1

exon sequences show that H. sambuci is phylogenetically distinct from, but closely related to, H. tremelloides. Hypocrea schweinitzii (Fr. : Fr.) Sacc., Syll. Fung. 2: 522 (1883a). Fig. 94 Fig. 94 Teleomorph of Hypocrea schweinitzii. a–c. Fresh stromata (a. immature).

d, e, g–j. Dry stromata (d, e. immature; e. with anamorph; i. stroma initial). Benzatropine f, k. Rehydrated stromata (f. in section; k. in face view). l. Stroma surface in face view. m. Perithecium in section. n. Cortical and subcortical tissue in section. o. Subperithecial tissue in section. p. Non-attached stroma base in section. q–t. Asci with ascospores (s, t. in cotton blue/lactic acid). a. WU 29473. b, c, r. WU 29471. d, e. WU 29472. g. WU 29476. h, i. WU 29475. k–q, s. WU 29470. f, j. PRM (leg. Pouzar). t. WU 29474. Scale bars: a, e–g = 1 mm. b, i, k = 0.7 mm. c, d = 1.5 mm. h = 0.4 mm. j = 2.5 mm. l = 10 μm. m = 20 μm. n–p = 15 μm. q–t = 5 μm ≡ Sphaeria schweinitzii Fr. : Fr., Elench. Fungorum 2: 60 (1828). = Sphaeria rigens Fr., Elench. Fung. 2: 61 (1828). ≡ Hypocrea rigens (Fr. : Fr.) Sacc., Michelia 1: 301 (1878). = Sphaeria lenta Schwein., Schriften Naturf. Ges. Leipzig 1: 4 (1822). = Sphaeria contorta Schwein., Trans. Amer. Phil. Soc. II, 4(2): 194 (1832). ≡ Hypocrea contorta (Schwein.) Berk. & M.A. Curtis, Grevillea 4: 14 (1875). = Hypocrea atrata P. Karst., Mycol. Fenn. 2: 207 (1873). = Hypocrea repanda Fuckel, Symb. Mycol. Nachtr. 1: 312, 3: 23 (1871). = Hypocrea rufa * umbrina Sacc., Atti Soc. Venet.-Trent. Sci. Nat., Padova 4: 124 (1875).

6e-05) However, although inactivation of crc alleviated repressi

6e-05). However, although inactivation of crc alleviated repression of OprB1 on 0.8% glucose medium, the OprB1/OprF ratio was still higher on 0.2% glucose medium (Figure 7D, compare results for the crc mutant on 0.2 and 0.8% glucose, p = 6.7e-04). Therefore we conclude that in addition to the Crc some other factor(s) as yet unknown should be implicated in hunger-induced up-regulation of OprB1. Figure 7 Post-transcriptional

regulation of OprB1 depends High Content Screening on the glucose concentration. A. β-Galactosidase (β-Gal) activity expressed from the gtsA promoter was measured in the wild-type P. putida grown on solid medium with 0.2 or 0.8% glucose or 0.2% gluconate. B. SDS-PAGE of the outer membrane protein https://www.selleckchem.com/products/Tipifarnib(R115777).html preparations from P. putida wild-type PaW85 (wt) and from OprB1-overexpressing strain PaWoprB1-tacB1 (B1tacB1) grown 24 hours over the whole Petri plate. The growth medium contained 0.2 or 0.8% glucose (glc) as a carbon source. Plus (+) mark above the lane indicates that the bacterial growth medium contained also 0.5 mM IPTG. C and D. Analysis of the effect of the crc inactivation on the hunger-induced up-regulation

of OprB1. The outer membrane proteins were prepared from P. putida wild-type selleck chemicals (wt) and crc mutant strains (crc) grown for 24 hours as a lawn over the entire Petri plate. The growth medium contained 0.2 or 0.8% glucose (glc). The ratio of OprB1 to OprF was calculated from the data of at least two independent

protein preparations and five independent gel runs. Mean values and 95% confidence intervals are presented. Discussion Previous studies on ColRS signaling system have revealed a peculiar Megestrol Acetate subpopulation lysis phenotype of the colR mutant grown on glucose solid medium [25]. In this study we clarified the reasons for glucose-specific cell lysis and revealed that the ColRS system is necessary for P. putida to survive the hunger response which includes up-regulation of sugar channel OprB1. Several lines of evidence obtained in this study suggest that the glucose-growing colR mutant experiences envelope stress caused by the accumulation of membrane proteins. This was first indicated by the collection of mutants suppressing the lysis phenotype of the colR-deficient strain. These data demonstrated that the loss of ColR can be suppressed by down-regulation of certain OM proteins like OprB1 and OprF, as well by hindering the SecB-dependent protein secretion. Second, artificial overexpression of sugar channel protein OprB1 further highlighted the specifically increased sensitivity of the colR mutant to this particular OM protein.

Int J Syst Bacteriol 1998, 48:107–116 PubMedCrossRef 31 Maiden M

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