Dimensions of the hexamers were measured using PyMOL


Dimensions of the hexamers were measured using PyMOL

(DeLano 2002), and all pore diameters were measured for this study using HOLE (Smart et al. 1996). Previously published pore diameters are in parenthesis if the difference was >0.5 Å between this analysis and published values Fig. 9 Electrostatic comparison of pores from structurally characterized BMC shell proteins, viewed from the concave side. Pore residues are shown as green sticks. Red denotes negative charge; blue denotes positive this website charge The pores of the pentamers are also narrow with diameters of ~5 and ~3.5 Å for CcmL and CsoS4A, respectively. They are also positively charged, even more so than the hexamers (Fig. 6). At its narrowest point, the pore for CcmL is formed by R-G-S-A-A and CsoS4A’s is formed by G-S-S-A-A (Table 2). Although the pore residues of carboxysome Pfam03319 orthologs are not as well conserved as their hexameric counterparts, sequence comparison reveals some conservation, with a pore motif of X-(G/S)-S-A-A (Fig. 4b). Table 2 List of structurally characterized pentameric Pfam03319 domain-containing proteins from the buy Inhibitor Library carboxysome and their dimensions Pfam03319 protein Carboxysome type Pentamer diametera (Å) Pentamer edge lengthb

(Å) Pore residues Pore diameter (Å) CcmL [2QW7] β 58 36 RGSAA 5 CsoS4A [2RCF] α 57 34 GSSAA 3.5 PDB IDs of the Mannose-binding protein-associated serine protease listed structures are in brackets. a Pentamer diameter was measured from one vertex to its opposite edged. b Pentamer edge length was measured from one vertex to its shared edge vertex. Dimensions of the pentamers were measured using PyMOL (DeLano 2002), and all pore diameters for this study

were measured using HOLE (Smart et al. 1996) Tandem BMC proteins Among the genes encoding components of both the α- and β-carboxysomes are some containing fusions of BMC domains (Fig. 3): CsoS1D in the α-carboxysome and CcmO and a CsoS1D ortholog (slr0169 in Synechocystis sp. PCC6803) in the β-carboxysome. In 2009, the first structure of a tandem BMC protein was determined, CsoS1D of Prochlorococcus marinus MED4 (Klein et al. 2009). This protein was not predicted to contain two BMC domains; the N-terminal domain lacks obvious sequence similarity to any other BMC domain. However, the α-carbon backbones of the two domains superimpose with an RMSD of 1.27 Å over 95 atoms; guided by a structure-based sequence alignment, the domains are 18% identical. CsoS1D forms trimers resulting in pseudohexamers that are similar in dimensions to hexameric shell proteins (Table 1), with pronounced concave and convex sides (Fig. 9). The edges of the pseudohexamers contain the conserved D-X-X-X-K edge motif and CsoS1D could be readily fitted into existing models of the facets of the α-carboxysome shell (Fig. 5) (Klein et al. 2009).

The remainder of the special issue was carefully crafted with res

The remainder of the special issue was carefully crafted with respect to Peek’s depiction of a “three world view” (Patterson

et al. 2002; Peek 2008). Peek, an innovator in behavioral health integration, has challenged those committed to healthcare to think about it from the viewpoints of clinical, operational, and financial perspectives. Healthcare’s clinical world is relevant to the models and approaches that providers use to deliver care to patients and families. The operational world is related to the workflow, procedural, and structural (re)design elements of healthcare. The financial world is about how healthcare systems sustain themselves economically, and on what we need to change across clinic-, state-, and federal- levels to do so. We have designed this issue to provide information and innovations at each selleck screening library AZD8055 research buy of these levels. Articles at the clinical levels include Lewis et al.’s biospsychorelational overview of military and veteran couples, Forbat et al.’s qualitative investigation regarding clinical support of caregivers at patients’ end-of-life, Fitzgerald and Thomas’ report regarding working with couples struggling with medical conditions through attachment perspectives and emotionally-focused couples therapy,

and Skorunka et al.’s family-based efforts with patients struggling with psychosomatic disorders. Articles at the operational levels include Fox et al.’s account regarding the opportunities and challenges for family therapists working in primary care and Marlowe et al.’s framework for making such integration work. Articles at the financial levels include Edwards et al.’s primer for Medical Family Therapists in healthcare policy and Crane and Christenson’s summary report of family therapy’s cost effectiveness. Articles tying Metalloexopeptidase all three of these worlds together include Tyndall et al.’s theoretical and empirical review of MedFT, Mendenhall et al.’s call to advance research in our field, and Tyndall et al.’s consideration of competencies core to our work. In 2010, the American Association

for Marriage and Family Therapy formulated a training track as part of its annual conference devoted to workforce development in MedFT. What is needed now is ongoing training across University training sites and at national conferences to help new and practicing clinicians and researchers grow and develop MedFT, so that they are more competitive in the marketplace. Empirical evidence is also needed that addresses the issues of health using a biopsychosocial-spiritual and systemic lens to generate outcomes that are transformative for patients and their families in-context. While Crane and Christenson (in this special issue) have provided us with some studies, we need more research to demonstrate the health benefits for the couple and family when the patient seeks treatment and members of their family/social systems are included as a part of it.

Thirteen isolates were assigned to species level with low demarca

Thirteen isolates were assigned to species level with low demarcation to the next species but supplemental conventional tests revealed a final identification to species GSK1120212 price level (Table 1). Conventional methods assigned 60% of the isolates to species level and 15% to genus level (Tables 1 and 2). However, only 40% were correctly assigned to species level and 13% correct to genus level considering the 16S rRNA gene sequencing as reference method. 47% of the isolates were misidentified or not identified

by conventional methods; nevertheless, 18 of the 31 isolates incorrectly assigned to species level were identified to the correct genus (Table 2). Table 1 Identification of clinical isolates (n=158) by conventional methods compared to 16S rRNA gene sequence analysis Conventional phenotyic methods   16S rRNA gene sequence analysis     Final identification (supplemental conventional tests if required) JAK pathway Identification (number of isolates) Level of identification and correctness of result Best reference species sequence % difference to reference species sequence GenBank accession numbers   Actinobacillus ureae (1) S 1; SI 2 Actinobacillus hominis Actinobacillus suis (low demarcation) 0.0, 0.4 KC866152 A. hominis (acidification of mannitol: A. hominis (positive), A. suis (negative) [1]) Aggregatibacter actinomycetemcomitans (2) S; SC Aggregatibacter actinomycetemcomitans 0.0, 0.3 KC866227; KC866228 A. actinomycetemcomitans

Aggregatibacter actinomycetemcomitans (1) S; SI Pasteurella bettyae 0.0 KC866143 P. bettyae Aggregatibacter aphrophilus (11) S; SC Aggregatibacter aphrophilus 0.0-0.8 KC866144; KC866145; KC866146; KC866147; KC866148; KC866149; KC866150; KC866229; KC866230; KC866231; KC866272 A. aphrophilus Aggregatibacter aphrophilus (2) NADPH-cytochrome-c2 reductase S; SI Aggregatibacter aphrophilus 3.8, 2.9 KC866151; KC866153 Aggregatibacter sp. Aggregatibacter aphrophilus (1) S; SI Neisseria sicca 0.8 KC866154 N. sicca (nitrate reduction: positive (N. mucosa), negative (N. sicca, N. subflava bv. flava); sucrose acidification: positive (N. sicca, N. mucosa),

negative (N. subflava bv. flava) [18]) Neisseria subflava bv. flava 1.0 Neisseria mucosa (low demarcation) 1.1 Aggregatibacter sp. (1) G; GC Aggregatibacter aphrophilus 2.3 KC866155 Aggregatibacter sp. Bergeyella zoohelcum (1) S; SI Myroides odoratimimus 5.9 KC866156 Flavobacteriaceae Bergeyella zoohelcum (1) S; SI Neisseria zoodegmatis 0.3 KC866157 N. zoodegmatis Capnocytophaga canimorsus (2) S; SC Capnocytophaga canimorsus 0.5, 0.4 KC866158; KC866159 C. canimorsus Capnocytophaga ochracea (1) S; SI Capnocytophaga gingivalis 0.6 KC866160 C. gingivalis Capnocytophaga ochracea (1) S; SI Capnocytophaga ochracea 2.5 KC866161 Capnocytophaga sp. Capnocytophaga ochracea (5) S; SI Capnocytophaga sputigena 0.0-0.3 KC866162; KC866163; KC866164; KC866273; KC866274 C. sputigena 3 Capnocytophaga ochracea (1) S; SI Dysgonomonas mossii 0.6 KC866165 D. mossii Capnocytophaga ochracea (1) S; SI Leptotrichia trevisanii 0.

Levels of p65 was also determined in nuclear fractions β-actin w

Levels of p65 was also determined in nuclear fractions. β-actin was used as a control for equal loading. Data are the summary of averaged relative density units measured in 3 independent experiments.

*p < 0.05 compared with control. Effects of MAPK inhibitors on PCN-induced NF-κB signaling activation To determine whether MAPKs mediate PCN-activated NF-κB signaling pathway, we used PCN (50 μM) to stimulate U937 cells with or without pretreatment with MAPK and NF-κB inhibitors: SB 203580 (50 μM), PD98059 (50 μM) and PDTC 200 μM for 1 h. Cell proteins were collected at 30 min and NF-κB p65 protein translocation was detected by Western blotting. The results showed that there was abundant cytosol distribution of NF-κB p65 before stimulation. All the indicated blockers were able to reduce the localization Daporinad mw of SRT1720 in vitro NF-κB p65 in the cytosol (Figure 9). These data suggest that SB203580 and PD98059 can effectively inhibit PCN-induced NF-κB signaling activation. Therefore, it could be concluded that the activation of p38 and ERK MAPKs are signaling events that lie upstream of NF-κB activation. Figure 9 Effects of MAPK inhibitors on PCN-induced NF- κB signaling pathway. U937 cells were stimulated with PCN at 50 μM for the time periods indicated with or without pretreatment by MAPK and NF-κB inhibitors:

SB 203580 (50 μM), PD98059 (50 μM) and PDTC (200 μM) for 1 h. Cell proteins were then collected and NF-κB p65 protein expression was detected with Western Vitamin B12 blotting. Discussion The National Nosocomial Infection Surveillance indicates that P. aeruginosa is the

second most common cause of nosocomial pneumonia after Staphylococcus aureus[28]. Ventilator-associated pneumonia (VAP) caused by P. aeruginosa is a severe complication of intensive care, with mortality rates of 34 to 48% [28–30]. Therefore, it is critical to study the pathogenesis of P. aeruginosa. In recent years, with the development of technologies such as the gene chip and the protein chip, and the clarification of the genome sequence of the P. aeruginosa strain, it has been found that many elements such as pro-inflammatory cytokines, antimicrobial peptides, complements and epithelial cell receptors and their signal transduction systems (TLR2, 4, 5, CFTR, GM1, and its downstream NF-κB) participate in host defense and immune response induced by P. aeruginosa. It has also been found that P. aeruginosa components (flagella and pili) and virulence factors (such as the density-sensing system, type secretion system, toxins, alginate and cell toxin) play important roles in the pathogenesis [2, 16]. Among them, most P. aeruginosa strains secrete PCN (N-methyl-1-hydroxyphenazine), the pigment that gives blue-green color to the bacterial colonies [4].

Antigenic drift leads to hemagglutinin variants within each HA su

Antigenic drift leads to hemagglutinin variants within each HA subtype from different globe

regions at different times. Certain Mabs that specifically target a given HA epitope of one type AIV, may not be able to recognize other AIV strains with a mutated antigenic epitope even if such a mutation is slight. Therefore, using one single Mab for H5 AIV antigen detection, in most cases, will not cover all the H5 subtype AIV circulating world around. Here we report the development of an antigen-capture dot ELISA based on a pair of Mabs targeting the same epitope on H5, however, by two different and dominant amino acids respectively, in an attempt to make a universal H5 AIV rapid detection test. Results Identification of monoclonal antibodies recognizing complementary epitopes on H5 hemagglutinin A panel of Mabs against influenza hemagglutinin was screened for efficient detection of different strains of H5N1 viruses. Based on see more the results of the HI assay, Mabs 6B8 and 4C2 MG-132 were chosen for further studies due to their high HI activity (Table 1) against a wide range of rescued reassortant viruses from different clades. Both Mabs were found to be of the IgM isotype. After the virus neutralizing activity has been confirmed (data not shown), the amino acids involved in forming the epitopes of the Mabs were analyzed using escape mutant analysis. All

HA amino acid numbering in this work uses H5 numbering excluding the signal peptide. Upon sequencing escape mutants from 3 different parental strains (Table 2), a few mutant clones of Mab 6B8 showed mutations at either Lys189 or Asn155, while clones of Mab 4C2 presented

mutations at Arg189, Ser155 or Asn155. The results indicated that the 189th and 155th amino acids were involved in the epitopes of both Mabs, but in different forms. Mab 6B8 is able to bind to H5 with either Lys189 or Asn155 independently. Mab 4C2 binds science to Arginine on 189th amino acid of H5, and it recognizes both Serine and Asparagine at position 155. Table 1 Hemagglutination Inhibition (HI) titers of the Mab 6B8 and 4C2 (1 mg/ml) against H5N1 influenza viruses. Virus Clade 6B8 4C2 A/Indonesia/CDC669/06 2.1 <8 512 A/Indonesia/CDC594/06 2.1 256 128 A/Vietnam/1203/04 1 512 <8 A/Hongkong/156/97 0 256 128 A/turkey/Turkey1/05 2.2 256 128 A/Anhui/1/05 2.3 256 <8 A/goose/Guiyang/337/06 4 128 128 A/chicken/Shanxi/2/06 7 256 256 A/chicken/Henan/12/04 8 256 128 Table 2 Amino acids on HA of H5N1 influenza viruses recognized by Mab 6B8 and 4C2, which identified in the comparison between parental virus and cloned escape mutants. Virus 6B8 4C2 A/Indonesia/CDC669/06 (155Ser, 189Arg) — 189Arg, 189Arg155Ser A/Indonesia/CDC594/06 (155Asn, 189Arg) 155Asn 155Asn A/Vietnam/1203/04 (155Ser, 189Lys) 189Lys — The number indicated the amino acid position in H5 HA. The amino acid type on the position was shown after the number. –: The Mab does not react with the parental virus.

Thus, the EXAFS contribution from each backscattering atom j is a

Thus, the EXAFS contribution from each backscattering atom j is a damped sine wave in k-space, with an amplitude, and a phase, which are both dependent on k. Additionally, S 0 2 is introduced as an amplitude reduction factor due to shake-up/shake-off processes at the central atom(s). This factor can be set for fits, on the basis of fits to model compounds. Thus, the following EXAFS equation is used to fit the experimental Fourier

isolates using N, R, and σ 2 as variable parameters, $$ \chi (k) = S_0^2 \sum\limits_j {{\frac{}kR_\textaj^2 }\,\texte^ – 2\sigma_\textaj^2 k^2 \texte^ – 2R_\textaj /\lambda_j (k)\,\sin (2kR_\textaj + a_\textaj (k))} . $$ (6)From the phase of each sine wave [2kR aj + α aj(k)], the absorber–backscatterer distance R aj can be determined if the phase FK506 solubility dmso shift α aj(k) is known. The phase shift is obtained

either from theoretical calculations or empirically from compounds characterized BYL719 order by crystallography with the specific absorber–backscatterer pair of atoms. The phase shift α aj (k) depends on both the absorber and the scatterer atoms. As one knows the absorbing atom in an EXAFS experiment, an estimation of the phase shift can be used in identifying the scattering atom. The amplitude function contains the Debye–Waller factor and N j, the number of backscatterers at R aj. These two

parameters are highly correlated, which makes the determination of N j difficult. The backscattering PDK4 amplitude function f j(π, k) depends on the atomic number of the scattering atom, and scattering intensity increases with the electron density (i.e., atomic number) of the scattering atom. In principle, this can be used to identify the scattering atoms. In practice, however, the phase shift and backscattering amplitude function, both of which are dependent on the identity of the backscattering atom, can be used only to identify scattering atoms that are well separated by atomic number (Rehr and Albers 2000). The EXAFS fit-quality is evaluated using two different parameters Φ and ε 2 . $$ \Upphi = \sum\limits_1^N_\textT \left( \frac1s_\texti \right)^2 [\chi^\textexpt (k_\texti ) - \chi^\textcalc (k_\texti )]^2 , $$ (7)where N T is the total number of data points collected, \( \chi^\textexpt (k_\texti ) \) is the experimental EXAFS amplitude at k i, and \( \chi^\textcalc (k_\texti ) \) is the theoretical EXAFS amplitude at k i. The normalization factor s i is given by $$ \frac1s_\texti = \frack_\texti^3 \sum\nolimits_j^N_\textT k_\textj^3 \left .

The significance of the variables was tested with a Monte Carlo s

The significance of the variables was tested with a Monte Carlo simulation, run with 499 iterations. The software used was CANOCO 4.5 (Braak and Smilauer 1998). How much individual species were associated with a site ‘type’ was

tested with indicator species analysis (IndVal) (Dufrene and Legendre 1997). This analysis gives a value of 100 for a perfect indicator which means a species that occur on all sites with in a category (type) and not on any other site. Bad indicators get a value near 0. With 15,999 permutations in a Monte Carlo test the statistical significance of the indicator RG7422 values were calculated under the null hypothesis that the indicator value is not larger than would be expected by chance. Species present on four or more sites (n = 164) were analysed. PcOrd 6.0 was used for the calculations. Results In total 14,460 individuals of 323 saproxylic beetle species were found (Table 2). Of these, 56 were classified as living in hollows, and 259 as living in wood and bark. The eight remaining species live in sap-runs, but this category had too few species to allow further statistical analyses. Of all saproxylic species, 50 were red-listed (Table 2). Table 2 The total material of saproxylic beetles collected in the study Variable, species category All saproxylic Hollows Wood and bark

Sap-runs Small molecule library in vitro No. of individuals, all species 14,460 5,352 8,862 246 No. of species, all species 323 56 259 8 No. of individuals, red-listed species 1,429 331 1,098 0 No. of species, red-listed species 50 17 33 0 Number of

species ‘Open’ sites had the highest average number of species per site for all combinations of red-listed and non-red-listed species and substrate associations (Fig. 3). However, it was significantly higher than another category ‘Park’ only when “all saproxylic species” and “all wood and bark species” were compared (Fig. 3a, c; Table 3). Regarding species associated with hollows and red-listed species, the number of species in ‘Park’ was intermediate between ‘Open’ and ‘Re-grown’ sites, although these differences were not statistically significant (Fig. 3b, d–f; Table 3). Fig. 3 The average number of beetle species in the three stand types under comparison: a all saproxylic species, b species living in Arachidonate 15-lipoxygenase hollows, c species living in wood and bark, d all red-listed saproxylic species, e red-listed species in hollows, f red-listed species in wood and bark. Significant differences were found in (a) and (c) (see Table 3). Number of sites were: ‘Open’ n = 8, ‘Re-grown’ n = 11, ‘Park’ n = 8 Table 3 P values for each variable as tested in the final multiple regression models with the number of species per site as the dependent variable. The direction of the significant relationships are shown as (−) or (+) or for the variable ‘type’ in Fig. 3 All saproxylic species Variable All species Hollows Wood and bark Type 0.023 0.18 0.014 RT90N 0.008 (−) 0.

Exactly at the end of 120 min of heating, the flow of reactant an

Exactly at the end of 120 min of heating, the flow of reactant and carrier gases were stopped and the furnace was set to cool down to room temperature before removing the sample. Once the furnace got cooled to near room temperature, the sample was removed from it. Grayish white

deposits were observed on the silicon substrate. The same procedure was repeated for all samples of different dopant concentrations. Doping mechanism of ZnO:Al Due to their confined electronic states to a very small volume in nanocrystals, doping leads to phenomena not found in the bulk counterparts. Although the underlying mechanism responsible for these observations are still under investigation, we believe that the following reactions spontaneously occur during the deposition of ZnO:Al NSs. (2.1) (2.2) It is expected that doubly charged donors including oxygen EPZ-6438 mouse vacancies (V o) and zinc interstitials (Zn i ) would be formed by the extrinsic doping selleckchem of Al. This is possible if the incorporated Al atoms take oxygen from ZnO and form either or inside the ZnO matrix. As the standard Gibbs-free energy change of these reactions is largely negative (-618 kJ mole-1) [3], it is believed that the formation of m */m o is responsible for the extrinsic doping of ZnO:Al, which

is contrary to the conventional doping mechanism based on the substitution of foreign elements. Doping takes place by incorporating Al atoms in which charged donors would be formed at or near the Al2O3/ZnO interface in compensation for free electrons. The electrons around these donors could be localized within the Bohr radius (aH) of ZnO as stated below: (2.3) where a o = Bohr radius of H atom (0.53 Å), ϵ r = relative permittivity of ZnO (81), m * = effective mass of an electron in ZnO (0.318), m o = mass of an electron, and a H = Bohr radius of ZnO. Theory in reference [3] suggests that of ZnO in Equation (2.3) is approximately nearly 14 Å. Since donated electrons orbit around charged donor with the radius, the repulsion force between electrons belonging to adjacent donors could suppress the donation of additional electrons. The Coulomb repulsion force between

adjacent charged donors may also cause decrease of carrier concentration in the same manner. Thus, these repulsion forces could cause the effective field for doping around each donor. These effective fields probably limit the doping efficiency of Al atoms within a single Al2O3 layer. Alloying evaporation method According to the self-catalytic growth mechanism proposed by Dang et al. [4], the process completes in four major steps. Figure 2 best explains the particular growth mechanism. It can be understood as follows: (A) As soon as the temperature of the furnace reaches the melting point of the Zn powder, it starts to melt and form a large quantity of melting liquid drops of size approximately identical to those of the original solid metal particles.

Indirect ELISA technique The indirect ELISA technique, modified f

Indirect ELISA technique The indirect ELISA technique, modified from Kishinevsky and Maoz [55], was tested here for its ability to identify Cyclopia rhizobia under both glasshouse and field conditions. In the indirect ELISA method, the this website antigen is adsorbed, followed by the application of purified primary antibody and a single secondary antibody-conjugate. The antibody-conjugate (usually goat anti-rabbit conjugate) is commercially available and can be used in conjunction with a number of strain-specific antibody preparations. The

method is simpler, but has lower analytical sensitivity than the direct method [55, 56]. Production of strain-specific primary antibodies The four test strains used in this study were grown in a defined broth medium containing 0.5 g K2HPO4, 0.2 g MgSO4.7H20, Seliciclib nmr 0.1 g NaCl, 0.5 g KHPO4 and 10 g mannitol in 1 l distilled water53 and incubated at 20°C to obtain 0.4 OD600. To remove exopolysaccharides (produced in large quantities by strains UCT44b and UCT61a), the bacterial cells were washed three times by repeated centrifugation in phosphate-buffered saline (PBS) solution. The final sediment was suspended in 10 ml saline solution (150 mM NaCl) to a final concentration of > 109 CFU ml-1. Antibodies were prepared against each test strain using adult New Zealand White rabbits. The rabbits were bled prior to inoculation to assess their pre-inoculation antibody levels.

One rabbit was used for each test strain and was injected with the appropriate antigen according to the following protocol: Day 1: 0.5 ml intramuscular injections into each hind leg (with equal parts Freund’s complete adjuvant mixed prior to injection); Day 14: 1 ml intravenous injection; Day 21: 1 ml intravenous injection; Day 28: 1 ml intravenous injection; Day 35: trial bleed to check antiserum titre; Day 37: bleed by cardiac puncture after 0.15 ml intravenous acetylpromazine (sedative) injection. Intravenous

injections and trial bleeds were done via the marginal ear vein. Collected blood was incubated for 1 h at 37°C to facilitate clotting and then held at 4°C overnight to Cyclin-dependent kinase 3 extrude serum. The serum was removed, centrifuged to remove residual cells and stored at -20°C in 0.5 ml aliquots. Antiserum titres were tested using the long agglutination test of Vincent [52]. No precipitation reactions occurred with the pre-inoculation sera, but strong agglutinations occurred with the test antisera. Antisera agglutination titres were 1:600, 1:200, 1:400 and 1:500 for strains PPRICI3, UCT40a, UCT44b and UCT61a, respectively. Antigen preparation from roots nodules Cyclopia maculata seedlings were grown on nutrient-agar slants in individual sterile tubes. After three weeks of growth, the tubes were inoculated with test strains using three replicate tubes per strain and three uninoculated tubes as a negative control.

Urol Oncol 2011,31(1):115–123 PubMed 29 Chiyomaru T, Enokida H,

Urol Oncol 2011,31(1):115–123.PubMed 29. Chiyomaru T, Enokida H, Tatarano S, Kawahara K, Uchida Y, Nishiyama K, Fujimura L, Kikkawa N, Seki N, Nakagawa M: miR-145 and miR-133a function as tumour suppressors and directly regulate FSCN1 expression in bladder cancer. Br J Cancer 2010,102(5):883–891.PubMedCrossRef 30. Ichimi

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2010,29(7):1073–1084.PubMedCrossRef 35. Fei X, Qi M, Wu B, Song Y, Wang Y, Li T: MicroRNA-195–5p suppresses glucose uptake and proliferation of human bladder cancer T24 cells by regulating GLUT3 expression. FEBS Lett 2012,586(4):392–397.PubMedCrossRef 36. Shatseva T, Lee DY, Deng Z, Yang BB: MicroRNA miR-199a-3p regulates cell proliferation and survival by targeting caveolin-2. J Cell Sci 2011,124(Pt 16):2826–2836.PubMedCrossRef 37. Wiklund ED, Bramsen JB, Hulf T, Dyrskjot L, Ramanathan R, Hansen TB, Villadsen SB, Gao S, Ostenfeld MS, Borre M, Peter ME, Orntoft TF, Kjems J, Clark SJ: Coordinated epigenetic repression of the miR-200 family and miR-205 in invasive bladder cancer. Int J Cancer 2011,128(6):1327–1334.PubMedCrossRef 38. Adam L, Zhong M, Choi W, Qi W, Nicoloso M, Arora A, Calin G, Wang H, Siefker-Radtke A, McConkey D, Bar-Eli M, Dinney C: miR-200 expression regulates epithelial-to-mesenchymal transition in bladder cancer cells and reverses resistance to epidermal growth factor receptor therapy. Clin Cancer Res 2009,15(16):5060–5072.PubMedCrossRef 39. Bo J, Yang G, Huo K, Jiang H, Zhang L, Liu D, Huang Y: microRNA-203 suppresses bladder cancer development by repressing bcl-w expression.