e., DHEA, androstendione, etc.) or other purported ��-Nicotinamide datasheet anabolic or ergogenic nutritional supplements within 6 months prior to beginning the study and to not take any additional nutritional supplement or contraindicated prescription medication during the protocolParticipants agreed not to undertake any physical activity, nor seek any remedy for muscle soreness, other than the supplement provided, for the duration of the study.   All

participants were informed verbally and in writing, as to the objectives of the experiments, together with the potential associated risks. All participants signed an informed consent document approved by the Human Research Ethics Committee of Victoria University of Australia. All procedures conformed to National Health and Medical Research Council guidelines for the involvement of human participants for research 1. Table 1 Participant baseline characteristics

Characteristics CHO WPH P-value Age (yrs) 22 ± 4 24 ± 5 0.13 Weight (kg) 77 ± 14 81 ± 8 0.17 Leg Press 1RM (kgs) 125 ± 51 129 ± 40 0.92 Leg Extension 1RM (kgs) 88 ± 26 84 ± 25 0.70 Leg Flexion 1RM (kgs) Extension 40 ± 8 46 ± 22 0.54 Data are means ± standard deviations of mean. SI unit conversion factor: 1 kg = 2.2 lbs Experimental Design With the exception of the type and timing of the Cediranib supplement consumed, the experimental design and associated measurements were identical to our previous study [15]. Briefly, 2 weeks prior to the damage session, participants underwent unilateral (dominant limb) concentric 1 repetition maximum (RM) strength

assessments as prescribed by the National Strength and Conditioning Association (NSCA) [16], and a familiarisation session of the performance measurements. Isotretinoin On the morning of day 1, participants underwent performance measurements – voluntary isokinetic knee flexion and isokinetic/isometric knee extension of each leg using Cybex™ Testing and Rehabilitation System (Cybex International Inc. Ronkonkoma, New York). Strength values were expressed as percentage of pre-exercise values and normalised to contralateral controls as in our [15], and other [17, 18], previous studies. A 20-gauge Teflon catheter was placed in a forearm vein, and participants then performed a damage protocol on their dominant leg consisting of leg press, leg extension and leg curls at 120% of the participants’ HMPL-504 molecular weight predetermined 1RM for each exercise. The participant completed 40 repetitions (4 sets × 10, with 3 minutes rest between sets) of each exercise at a predetermined cadence (4 seconds), given verbally, which constituted 1 repetition.

0 Benign ovarian tumor serous 10 2 15.8   mucous 9 1     Age (years) < 50 12 8       ≥50 40 30     FIGO stage I/II 5/11 3/5       III/IV 24/12 19/11     Histological type Serous 30 21   Ovarian carcinoma

tissue   Mucous 22 17     Histological grade BAY 11-7082 G1 10 4       G2/G3 14/28 9/25     Ascites No 24 16       Yes 28 22     Lymph nodes metastasis No 32 20       Yes 20 18 73.1* * χ2 test. Compared with normal ovarian and benign ovarian tumor tissues P < 0.05. Figure 1 Immunohistochemistry analysis of MACC1 expression in different ovarian tissues. Normal ovary (A) and benign ovarian tumor (B) showed a lower staining of MACC1, but ovarian cancer (C) showed higher density staining (DAB staining, × 400). (D): Bar graphs show the positive rates of MACC1 protein. *P < 0.05 versus normal and benign ovarian tissues. Down-regulation of MACC1 expressions by RNAi After transfection GW3965 research buy 48 h, transfected cells with green fluorescence under fluorescence microscopy were observed (Figure 2). Expressions of MACC1 in stably transfected cells, which were selected by G418, were measured by RT-PCR and Western blot. Compared to control cells, levels of MACC1 mRNA and protein were significantly

down-regulated in OVCAR-3-s1, OVCAR-3-s2 and OVCAR-3-s3 cells, especially in OVCAR-3-s3 cells (Figure 3). According to these results, OVCAR-3-s3 cells which showed the highest inhibitory rate of MACC1 were used for further assay described below. Figure 2 Transfection of MACC1-shRNA into ovarian carcinoma OVCAR-3 cells. (A):

Normal OVCAR-3 cells under incandescent light (× 200). (B): After transfection 24 h, OVCAR-3-s3 cells under fluorescent light (× 100). (C): QNZ nmr Monoplast colony of OVCAR-3-s3 cells selected by G418 for three weeks (× 200). (D): G418 resistant OVCAR-3-s3 cell line (× 100). Figure 3 Down-regulation of MACC1 by MACC1-shRNA in ovarian carcinoma cells. The best inhibitory effects of MACC1 were identified in OVCAR-3-s3 cells by RT-PCR (A) 2-hydroxyphytanoyl-CoA lyase and Western blot (C), which were both performed for three times independently. Bar graphs show the relative expression levels of MACC1 mRNA (B) and protein (D).*P < 0.05 versus control groups. Inhibition of cell proliferation and colony formation by MACC1 RNAi According to Figure 4, the proliferation of OVCAR-3-s3 cells was obviously inhibited from the second day, when compared with control cells. There were no differences among OVCAR-3, OVCAR-3-neo and OVCAR-3-NC cells. In addition, OVCAR-3-s3 cells had lower rate of colony formation than control groups as shown in Figure 5. Thus, knockdown of MACC1 by RNAi could inhibit the growth of ovarian carcinoma cells. Figure 4 Suppression of proliferation by MACC1 RNAi in ovarian carcinoma cells measured by MTT assay. Obviously inhibitory effect of cell proliferation was observed from the second day after MACC1 knockdown.*P < 0.05 versus control groups. Figure 5 MACC1-shRNA inhibited the monoplast colony formation of ovarian carcinoma cells.

Collectively, these results FG-4592 revealed that the uptake of B. anthracis spores by mammalian cells is essentially the same within germinating and non-germinating in vitro environments. Figure 5 Uptake of B. anthracis spores into mammalian cells cultured

under germinating or non-germinating conditions. RAW264.7 cells (A, D), MH-S cells (B, E), or JAWSII cells (C, F) were incubated with B. anthracis spores (MOI 10) in DMEM, RPMI, or DMEM, respectively, in the presence (+, black bars) or absence (-, white bars) of FBS (10%), and then evaluated at 5 or 60 min by flow cytometry and in the presence of trypan blue (0.5%) for the percentage of cells with intracellular spores (A-C), and, for total cell associated spore fluorescence (D-F), as described under Materials and Methods. (A-C) The data are rendered as the percentage of infected cells with the entire population that has internalized spores. (D-F) The data are expressed as the change

in MFI, normalized to cells at 5 min post infection in FBS-free medium. To generate the bar graphs, data were combined from three independent experiments, each conducted in triplicate. Error bars indicate standard deviations. The P values were calculated to evaluate the statistical significance of the differences in percent infected cells (A) or total intracellular spores (B) between cells incubated in the absence or presence of FBS. Germination state of spores influences the number of viable, intracellular B. anthracis Although the uptake of B. anthracis spores Vorinostat into mammalian cells was independent of the presence or absence of FBS in the culture medium,

it was not clear whether the outcome of infection would also be similar under germinating and non-germinating conditions. To evaluate this issue, the recovery of viable, intracellular B. anthracis was compared subsequent to uptake by RAW264.7 cells in the absence or presence of FBS (10%), using the gentamicin protection assay PRKACG [11, 21, 46, 47]. These studies indicated that there were not significant differences in intracellular CFU after 5 min post-infection (Figure 6). However, after 60 or 240 min post infection, significantly greater CFU were recovered from cells in DMEM EVP4593 lacking FBS relative to cells incubated in the presence of FBS (Figure 6). To evaluate whether these differences might be attributed strictly to the presence or absence of FBS, similar studies were conducted in the absence of FBS, however this time using spores that had been pre-germinated for 30 min with DMEM supplemented with L-alanine/L-inosine (both at 10 mM). Similar to spore uptake in the presence of FBS, significantly fewer CFU were recovered from cells incubated with pre-germinated spores in the absence of FBS relative to cells incubated with dormant spores in DMEM lacking FBS (Figure 6).

MC58 wild-type and MC58ΔgapA-1 Selleck GW786034 treated with RαGapA-1 followed by anti-rabbit IgG-Alexa Fluor 488 conjugate showed no demonstrable shift in fluorescence signal compared to the same strains incubated with RαGapA-1 or secondary antibody alone showing that GapA-1 was not

detectable on whole cells of these strains (Figure 3a &3b). However, identical experiments using MC58ΔsiaD demonstrated a clear Lazertinib purchase shift in fluorescence when cells were treated with RαGapA-1 followed by anti-rabbit IgG-Alexa Fluor 488 conjugate (Figure 3c). This demonstrated that, in the absence of capsule, surface exposed GapA-1 was accessible to antibody. From the MC58ΔsiaD cells probed with both antibodies, 25% were found in the M2 region (Figure 3c), suggesting that in broth-grown cells Selleckchem NCT-501 unexposed to human epithelial cells only a minority of the population had GapA-1 was present on the cell surface. Pre-immune sera showed no reactivity against wild-type MC58 or MC58ΔsiaD, and RαGapA-1 specifically recognized only GapA-1 in immunoblot experiments confirming that the binding of RαGapA-1 to MC58ΔsiaD observed by flow cytometry was GapA-1 specific. Figure 3 Flow cytometry of MC58 wild-type (a), MC58Δ gapA-1 (b) or MC58Δ siaD (c) for GapA-1 surface localization. Cells were stained with RαGapA-1 (primary alone), anti-rabbit IgG-Alexa Fluor 488 conjugate (secondary alone) or both. Fluorescence was displayed as a

histogram. In panel c, the histogram area in M2 represents the population of fluorescently labelled meningococci. GapA-1 is required for optimal adhesion to host cells The capacity of the wild-type, GapA-1 mutant and complemented mutant strains to associate with, and invade into human brain microvascular endothelial (HBME) cells were then determined. GapA-1 deficient meningococci had a significantly reduced

capacity to adhere to monolayers of HBME cells (Figure 4). No significant reduction was observed in the ability of the GapA-1 mutant to invade monolayers of HBME cells (data PD184352 (CI-1040) not shown). Similar results were also obtained using HEp-2 cells confirming that the effect was not limited to endothelial cells (data not shown). To confirm that the observed effects were not due to an impairment of in vitro growth, the growth rate of the strains was compared by measuring the optical density at 600 nm (OD600) and determining the viable counts of broth cultures sampled during exponential growth over 24 h in triplicate on three separate occasions. No significant difference between strains was observed (data not shown). Figure 4 MC58Δ gapA-1 has a reduced ability to associate with HBMEs compared to the wild-type or complemented strains. The number of GapA-1-deficient meningococci associating was significantly lower than the wild-type (*P = 0.0018). Mean levels shown from three independent experiments, each using triplicate wells. Bars denote standard deviation. Cfu denotes colony forming units.

Nat Biotechnol 2003,21(6):639–644.PubMedCrossRef 14. Shlomai A, Shaul Y: Inhibition of hepatitis B virus expression and replication by RNA interference. Hepatology 2003,37(4):764–770.PubMedCrossRef 15. Ying RS, Zhu C, Fan XG, Li N, Tian XF, Liu HB, Zhang BX: Hepatitis B virus is inhibited by RNA interference in cell

culture and in mice. Antiviral Res 2007,73(1):24–30.PubMedCrossRef 16. Giladi H, Ketzinel-Gilad M, Rivkin L, Felig Y, Nussbaum O, Galun HDAC inhibitor review E: Small interfering RNA inhibits hepatitis B virus replication in mice. Mol Ther 2003,8(5):769–776.PubMedCrossRef 17. Chen Y, Cheng G, Mahato RI: RNAi for treating hepatitis B viral infection. Pharm Res 2008,25(1):72–86.PubMedCrossRef 18. Ely A, Naidoo T, Mufamadi S, Crowther C, Arbuthnot P: Expressed anti-HBV primary microRNA beta-catenin assay Pitavastatin solubility dmso shuttles inhibit viral replication efficiently in vitro

and in vivo. Mol Ther 2008,16(6):1105–1112.PubMedCrossRef 19. Olinger CM, Jutavijittum P, Hubschen JM, Yousukh A, Samountry B, Thammavong T, Toriyama K, Muller CP: Possible new hepatitis B virus genotype, southeast Asia. Emerg Infect Dis 2008,14(11):1777–1780.PubMedCrossRef 20. Tran TT, Trinh TN, Abe K: New complex recombinant genotype of hepatitis B virus identified in Vietnam. J Virol 2008,82(11):5657–5663.PubMedCrossRef 21. Colson P, Roquelaure B, Tamalet C: Detection of a newly identified hepatitis B virus genotype in southeastern France. J Clin Virol 2009,45(2):165–167.PubMedCrossRef

22. Sugiyama M, Tanaka Y, Kato T, Orito E, Ito K, Acharya SK, Gish RG, Kramvis A, Shimada T, Izumi N, et al.: Influence of hepatitis B virus genotypes on the intra- and extracellular expression of viral DNA and antigens. Hepatology 2006,44(4):915–924.PubMedCrossRef 23. Wu HL, Huang LR, Huang CC, Lai HL, Liu CJ, Huang YT, Hsu YW, Lu CY, Chen DS, Chen PJ: RNA interference-mediated control of hepatitis B virus and emergence of resistant mutant. Gastroenterology 2005,128(3):708–716.PubMedCrossRef 24. Medina MF, Joshi S: RNA-polymerase III-driven expression cassettes in human gene therapy. Curr Opin Mol Ther 1999,1(5):580–594.PubMed 25. Interleukin-2 receptor Grimm D, Streetz KL, Jopling CL, Storm TA, Pandey K, Davis CR, Marion P, Salazar F, Kay MA: Fatality in mice due to oversaturation of cellular microRNA/short hairpin RNA pathways. Nature 2006,441(7092):537–541.PubMedCrossRef 26. Keck K, Volper EM, Spengler RM, Long DD, Chan CY, Ding Y, McCaffrey AP: Rational design leads to more potent RNA interference against hepatitis B virus: factors effecting silencing efficiency. Mol Ther 2009,17(3):538–547.PubMedCrossRef 27. Bredehorst R, von Wulffen H, Granato C: Quantitation of hepatitis B virus (HBV) core antigen in serum in the presence of antibodies to HBV core antigen: comparison with assays of serum HBV DNA, DNA polymerase, and HBV e antigen. J Clin Microbiol 1985,21(4):593–598.PubMed 28.

TDF/FTC/RPV is a second-generation STR containing 300 mg of TDF, 200 mg of FTC and 25 mg of RPV. It is licensed both in the US and in Europe for the use in HIV-infected subjects naïve or experienced (with a limitation referring to a viral load <100,000 copies/ml). More recently, TDF/FTC/COBI (cobicistat)/EVG (elvitegravir) has been approved. It is the first non-NNRTI-based STR containing 300 mg of TDF,

200 mg of FTC, 150 mg of EVG and 150 mg of COBI. EVG is an integrase inhibitor that selectively inhibits the strand-transfer step of integration process of viral DNA into the nucleic acid of the host [40, 41]. COBI is a pharmacokinetic enhancer that does not exert any ARV activity [42]. TDF/FTC/EFV is currently one of the first choices for PR-171 nmr the treatment of HIV infection both in the US [43] and in the main European Guidelines [3, 44, 45]. It is the STR most widely used in clinical practice and the experience gained over years on the single components is much more extensive if compared to newer STR formulations. The US Guidelines have recently added TDF/FTC/COBI/EVG as a preferred regimen and the European Guidelines have

added TDF/FTC/RPV as a recommended regimen as well. Different studies have demonstrated that virologically suppressed patients receiving a wide array of NRTI backbones given with NNRTI- or PI-based therapies can be safely switched to the TDF/FTC/EFV STR [16, JNK inhibitor nmr 20, 21, 46]. Longer term data up to week 144 support the high durability of the use of TDF/FTC/EFV STR and a continued immunological recovery [41, 47]. TDF/FTC/EFV STR has been considered as the comparator arm in the trials leading to registration of new STRs. from It showed high efficacy in naïve subjects coupled with a favorable toxicological profile (Tables 1, 2; [48–59]). Table 1 Tolerability profile of FK228 single-tablet

regimens (STRs) Reason for drug discontinuation TDF/FTC/EFV STaR (%) (n = 392) TDF/FTC/EFV 102 (%) (n = 352) TDF/FTC/RPV STaR (%) (n = 394) TDF/FTC/COBI/EVG 102 (%) (n = 348) TDF/FTC/COBI/EVG 103 (%) (n = 353) Renal events 0 0 0 2.0 0.8 Rash and skin reactions 0.5 1.4 0 0 0 Diarrhea 0.5 0 0 0 0.6 Nausea 0 0 0 0 0.3 Vomiting 0 0 0 0 0.3 Fatigue 0.5 0.6 0 0.3 0 Pyrexia 0.5 0 0 0 0.6 Hepatitis C 0 0 0 0 0.3 Dizziness 1.5 0 0 0 0 Abnormal dreams 1.8 0.6 0 0 0 Insomnia 1.0 0.6 0.3 0 0 Depression 2.0 1.1 0 0.3 0 Suicidal ideation 0.8 0 0 0 0 Reasons for drug discontinuation due to intolerance (%) as reported by the studies STaR, 102 and 103.

All strains were maintained at −80°C in Luria-Bertani liquid medium (LB medium) [42] containing a final concentration of 15% (v/v) glycerol. Annual bluegrass seeds (Poa annua L.) were obtained from 1996 mid-Willamette Valley grass seed screenings and were provided by International Seeds, Halsey, OR, and by C and R Farm, Tangent, OR. Prior to use, the seeds were cleaned to remove straw and seeds of other species. Culture filtrate production Pseudomonas fluorescens cells were inoculated into the modified Pseudomonas Minimal Salts Medium (PMS medium) described by Banowetz et al. [10], and cultured and harvested as described in the same reference. To prepare culture

filtrates, the 7-day P. fluorescens cultures were centrifuged (3000 × g, 15 min), and the supernatant was passed through a bacteriological filter (Millipore GP Express Steritop, Talazoparib nmr 0.22 μM pore size, Millipore, Billerica, MA). The resulting sterile culture filtrate

was stored at 4°C prior to use. Agar diffusion assays for antimicrobial {Selleck Anti-infection Compound Library|Selleck Antiinfection Compound Library|Selleck Anti-infection Compound Library|Selleck Antiinfection Compound Library|Selleckchem Anti-infection Compound Library|Selleckchem Antiinfection Compound Library|Selleckchem Anti-infection Compound Library|Selleckchem Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|Anti-infection Compound Library|Antiinfection Compound Library|buy Anti-infection Compound Library|Anti-infection Compound Library ic50|Anti-infection Compound Library price|Anti-infection Compound Library cost|Anti-infection Compound Library solubility dmso|Anti-infection Compound Library purchase|Anti-infection Compound Library manufacturer|Anti-infection Compound Library research buy|Anti-infection Compound Library order|Anti-infection Compound Library mouse|Anti-infection Compound Library chemical structure|Anti-infection Compound Library mw|Anti-infection Compound Library molecular weight|Anti-infection Compound Library datasheet|Anti-infection Compound Library supplier|Anti-infection Compound Library in vitro|Anti-infection Compound Library cell line|Anti-infection Compound Library concentration|Anti-infection Compound Library nmr|Anti-infection Compound Library in vivo|Anti-infection Compound Library clinical trial|Anti-infection Compound Library cell assay|Anti-infection Compound Library screening|Anti-infection Compound Library high throughput|buy Antiinfection Compound Library|Antiinfection Compound Library ic50|Antiinfection Compound Library price|Antiinfection Compound Library cost|Antiinfection Compound Library solubility dmso|Antiinfection Compound Library purchase|Antiinfection Compound Library manufacturer|Antiinfection Compound Library research buy|Antiinfection Compound Library order|Antiinfection Compound Library chemical structure|Antiinfection Compound Library datasheet|Antiinfection Compound Library supplier|Antiinfection Compound Library in vitro|Antiinfection Compound Library cell line|Antiinfection Compound Library concentration|Antiinfection Compound Library clinical trial|Antiinfection Compound Library cell assay|Antiinfection Compound Library screening|Antiinfection Compound Library high throughput|Anti-infection Compound high throughput screening| activity To test the antimicrobial activity of P. fluorescens SBW25 filtrate, bacterial strains were grown overnight in LB medium (6 mL) at 28°C (except for Escherichia coli, which was grown at 37°C) with shaking (225 rpm). The following morning, the stationary phase bacterial suspensions were adjusted with sterile water to an optical density of 0.2 at 600 nm (or 0.8 in the case of E. coli) as measured with a Superspec 3000 (Biorad Inc., Hercules, CA). A 300-μL

aliquot of selleckchem the diluted culture was spread onto the surface TCL of a 925 Minimal Medium plate (100 × 15 mm, containing 25 mL of medium). The 925 Minimal Medium [43] was prepared with the modifications described by Halgren et al.[25]. After spreading the bacterial lawn, central wells were punched in the agar with a No. 9 cork borer, and a 300-μL aliquot of SBW25 culture filtrate was dispensed into the well. The plates were incubated for 48 h at 28°C, examined, and scored. Zones of inhibition in the area adjacent to the well were quantified with Able Image Analyzer® software (MU Labs, Ljublijana, Slovenia). Three replicate plates were prepared for each bacterial strain tested, and the experiment was repeated for any strain that appeared sensitive to the SBW25 filtrate. Germination arrest assays The ability of SBW25 culture filtrate to inhibit the germination of Poa annua seeds was tested according to the protocol described by Banowetz et al.[10]. Ethanol extraction of culture filtrate Measured volumes of P. fluorescens culture filtrate were taken to dryness in vacuo at a temperature ≤ 45°C. After evaporation, the dry solids were extracted three times (5 min per extraction) with 90% or 85% (v/v) ethanol as indicated. Each of the three extractions was performed by swirling the solids with a volume of ethanol solution equal to one-third of the original volume of culture filtrate.

Figure 1 AFM images of ZnO seed layers. They are prepared by (a) RF magnetron sputtering (40 nm in thickness) and (b) dip coating. Figure 2a,b,c shows the SEM images of ZnO nanostructures grown on bare Si substrate, on the Si selleck compound substrate coated with seed layer deposited by RF magnetron sputtering (40 nm in thickness), and on the Si substrate coated with seed layer deposited by dip coating method, respectively,

at 0.05 M, at 95°C for 5 h. As can be seen, there are ZnO nanostructures grown on all of the three substrates. Among them, there are randomly oriented ZnO nanoflowers at low density on the bare Si substrate, as shown in Figure 2a. Without the seed layer, the nucleation density is remarkably lower than that grown with seeds because nucleation of ZnO MLN8237 LY2874455 ic50 nanostructures on seeds has a lower free energy barrier of activation than on the bare Si substrate [9]. In contrast, Figure 2b,c presents that ZnO nanorods grown on the Si substrate coated with the seed layer deposited by RF magnetron sputtering and dip coating are c-axis-oriented at high density, indicating

that the seed layer plays an essential role in promoting nucleation and guiding oriented growth. Especially, the nanorods grown on the RF-sputtered seed layer is perfectly aligned normal to the substrate with uniform height,

which is due to the low roughness and even distribution of the RF-sputtered Methamphetamine seed layer, while the broad size distribution and large surface roughness of the dip-coated seed layer lead to poor orientation and surface roughness of the ZnO nanorods as shown in Figure 2c, which will be further confirmed by the following XRD measurement. Figure 2 SEM images of ZnO nanostructures. They are grown on (a) bare Si substrate, the Si substrate coated with the seed layer deposited by (b) RF magnetron sputtering (40 nm in thickness) and (c) dip coating, at 0.05 M, at 95°C for 5 h (insets are corresponding cross-sectional images). The crystal structure on the ZnO nanostructures grown on bare Si substrate (sample 1), RF-sputtered seed layer (sample 2), and dip-coated seed layer (sample 3) was studied using XRD measurements in a θ-2θ configuration, as shown in Figure 3. Except for the peaks caused by the Si substrate and the non-monochromaticity of the X-ray source, the XRD patterns of the three samples share two peaks at 34.44° and 72.56°, corresponding to ZnO (002) and (004), respectively. The absence of any other peaks from the XRD pattern of sample 2 within the experimental resolution indicates the high c-axis orientation of ZnO nanostructures grown on RF-sputtered seed layer.

J Nanopart Res 2013, 15:1–29.CrossRef 48. Khlebtsov BN, Panfilova EV, Terentyuk GS, Maksimova IL, Ivanov AV, Khlebtsov NG: Plasmonic nanopowders for photothermal therapy

of tumors. Langmuir 2012, 28:8994–9002.CrossRef 49. Khlebtsov BN, Khanadeev VA, Panfilova EV, Pylaev TE, Bibikova OA, Staroverov SA, Bogatyrev VA, Dykman LA, Khlebtsov NG: New types of learn more nanomaterials: powders of gold nanospheres, nanorods, nanostars, and gold–silver nanocages. Nanotechnologies in Russia 2013, 8:209–219.CrossRef 50. Tsvetkov MY, Khlebtsov BN, Panfilova EV, Bafratashvili VN, Khlebtsov NG: Gold nanorods as a promising technological platform for SERS-analytics. Selleckchem ABT 737 Russian Chem J 2012, 56:83–90. (in Russian) 51. Stockman MI: Nanoplasmonics: past, present, and glimpse into future. Opt Express 2011, 19:22029–22106.CrossRef 52. Nikoobakht B, El-Sayed MA: Preparation and growth mechanism of gold 4EGI-1 datasheet nanorods (NRs) using seed-mediated growth method. Chem Mater 2003, 15:1957–1962.CrossRef 53. Khlebtsov B, Khanadeev V, Khlebtsov N: A new T-matrix solvable model for nanorods: TEM-based ensemble simulations supported by experiments. J Phys Chem C 2011, 115:6317–6323.CrossRef 54. Stöber W, Fink A, Bohn E: Controlled growth of monodisperse silica spheres in the micron size range. J Colloid Interface Sci 1968, 26:62–69.CrossRef 55. Tsvetkov MY,

Bagratashvili VN, Panchenko VY, Rybaltovskii AO, Samoylovich MI, Timofeev MA: Plasmon resonances of silver nanoparticles in silica based mesostructured films. Nanotechnologies in Russia 2011, 6:619–624.CrossRef 56. Glycogen branching enzyme Khlebtsov BN, Khanadeev VA, Khlebtsov NG: Observation of extra-high depolarized light scattering spectra from gold nanorods. J Phys Chem C 2008, 112:12760–12768.CrossRef 57. Ratto F, Matteini P, Rossi F, Pini R: Size and shape control in the overgrowth of gold nanorods. J Nanopart Res 2010, 12:2029–2036.CrossRef 58. Khlebtsov BN, Khanadeev VA, Khlebtsov NG: Determination

of the size, concentration, and refractive index of silica nanoparticles from turbidity spectra. Langmuir 2008, 277:107–110. 59. Busch K, John S: Photonic band gap formation in certain self-organizing systems. Phys Rev E 1998, 58:3896–3908.CrossRef 60. Lopez C: Materials aspects of photonic crystals. Adv Mater 2003, 15:1679–1704.CrossRef 61. Bertone JF, Jiang P, Hwang KS, Mittleman DM, Colvin VL: Thickness dependence of the optical properties of ordered silica-air and air-polymer photonic crystals. Phys Rev Lett 1999, 83:300–303.CrossRef 62. Jain PK, El-Sayed MA: Plasmonic coupling in noble metal nanostructures. Chem Phys Lett 2010, 487:153–164.CrossRef 63. Zong S, Wang Z, Yang J, Wang C, Xu S, Cui Y: A SERS and fluorescence dual mode cancer cell targeting probe based on silica coated Au@Ag core–shell nanorods. Talanta 2012, 97:368–375.CrossRef 64.

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