Int J Syst Bacteriol

1996, 46:367–376.CrossRef 27. Torriani S, Van Reenen GA, Klein G, Reuter G, Dellaglio F, Dicks LM: Lactobacillus buy H 89 curvatus subsp. curvatus subsp. nov. and Lactobacillus curvatus subsp. melibiosus subsp. nov. and Lactobacillus sake subsp. sake subsp. nov. and Lactobacillus sake subsp. carnosus subsp. nov., new subspecies of Lactobacillus curvatus Abo-Elnaga and Kandler 1965 and Lactobacillus sake Katagiri, Kitahara, and Fukami 1934 (Klein et al. emended descriptions), respectively. Int J Syst Bacteriol 1996, 46:1158–1163.PubMedCrossRef 28. Berthier F, Ehrlich SD: Genetic diversity within Lactobacillus sakei and Lactobacillus curvatus and design of PCR primers for its detection using randomly amplified polymorphic DNA. Int J Syst BV-6 Bacteriol 1999, 49:997–1007.PubMedCrossRef 29. Chaillou S, Daty M, Baraige F, Dudez AM, Anglade P, Jones R, Alpert CA, Champomier-Vergès MC, Zagorec M: Intraspecies genomic diversity and natural population structure of the meat-borne lactic acid bacterium Lactobacillus sakei . Appl Environ Microbiol 2009, 75:970–980.PubMedCrossRef 30. McLeod A, Nyquist OL, Snipen L, Naterstad K, Axelsson L: Diversity of Lactobacillus sakei strains investigated by phenotypic and genotypic methods. Syst Appl Microbiol 2008, 31:393–403.PubMedCrossRef 31. Moretro T,

Hagen BF, Axelsson L: A new, completely defined medium for meat lactobacilli. J Appl Microbiol 1998, 85:715–722.CrossRef 32. Marceau A, Mera T, Zagorec M, BI 10773 chemical structure Champomier-Vergès MC: Protein expression under uracil privation in Lactobacillus sakei . FEMS Microbiol Lett 2001, 200:49–52.PubMedCrossRef 33. Champomier-Vergès MC, Marceau A, Mera T, Zagorec M: The pepR gene of Lactobacillus sakei is positively regulated by anaerobiosis at the transcriptional level. Appl Environ Microbiol 2002, 68:3873–3877.PubMedCrossRef Galactosylceramidase 34. Marceau A, Zagorec M, Chaillou S, Mera T, Champomier-Vergès MC: Evidence for involvement of at least six proteins in adaptation of Lactobacillus sakei to cold temperatures and addition of NaCl. Appl Environ Microbiol

2004, 70:7260–7268.PubMedCrossRef 35. Jofre A, Champomier-Vergès M, Anglade P, Baraige F, Martin B, Garriga M, Zagorec M, Aymerich T: Protein synthesis in lactic acid and pathogenic bacteria during recovery from a high pressure treatment. Res Microbiol 2007, 158:512–520.PubMedCrossRef 36. De Man JC, Rogosa M, Shape ME: A medium for the cultivation of lactobacilli. J Appl Microbiol 1960, 23:130–135.CrossRef 37. Blum H, Beier H, Gross HJ: Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 1987, 8:93–99.CrossRef 38. Shevchenko A, Wilm M, Vorm O, Mann M: Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem 1996, 68:850–858.PubMedCrossRef 39.

In this

latter case, the use of the small molecule RITA (reactivation of p53 and induction of tumor cell apoptosis) that inhibits MDM2/p53 interaction and induces expression of p53 target genes and massive apoptosis in various tumor cells lines [35], can be useful to counteract HIPK2 degradation and to reactivate p53 apoptotic function [38]. Interestingly, also zinc ions treatment has been shown to relapse the MDM2-induced HIPK2 downregulation, by counteracting the MDM2 E3 ubiquitin ligase activity finally reactivating the HIPK2-induced p53Ser46 phosphorylation and apoptotic activity [39], although the molecular mechanism needs to be elucidated. HIPK2 depletion has been shown to induce cancer cell resistance to different check details anticancer drugs even in p53-null see more cells, suggesting the involvement of additional HIPK2 targets other than p53. In particular, it has been found that HIPK2 phosphorylates and promotes proteasomal degradation of ΔNp63α, a prosurvival dominant negative (DN) isoform of the p53 family member p63. HIPK2 phosphorylates ΔNp63α at the T397 residue, thus, the nonphosphorylatable

ΔNp63α-T397A mutant is not degraded in spite of either HIPK2 overexpression or ADR treatment. These findings underline ΔNp63α as a novel HIPK2 target in click here response to genotoxic drugs [33]. These data indicate that HIPK2 has a double commitment, working as activator for proapoptotic factors (i.e., p53) on one hand and inhibitor for antiapoptotic factors (i.e., CtBP, MDM2, ΔNp63α, HIF-1α) on the other hand. BCKDHA On the opposite side, these considerations would allow to suppose that tumor-associated inhibition of HIPK2 activity might strongly contribute to chemoresistance and tumor progression, in addition to other better-characterized events, such as p53 mutation/inactivation and MDM2 or ΔNp63α overexpression. Mechanisms of HIPK2 inhibition and its impact on both p53 function and tumor progression Several proteins have been shown to target the HIPK2/p53 axis and therefore to inhibit

stress- or drug-induced apoptosis to clear cancer. Recent studies demonstrated that High-mobility group A1 (HMGA1) proteins interact with p53 and inhibit its apoptotic activity [40]. Interestingly, HMGA1 overexpression is responsible for HIPK2 cytoplasmic sequestration and the subsequent inhibition of HIPK2/p53 interaction and apoptosis activation [41]. HMGA1 is frequently overexpressed in tumors and correlates with low apoptotic index in wild-type p53 breast cancer tissues [41]. Thus, immunostaining of breast ductal carcinomas with low HMGA1 expression and with high apoptotic index (not shown) results in HIPK2 nuclear localization (Figure 1A). On the other hand, breast ductal carcinomas with high HMGA1 expression and with low apoptotic index (not shown) show HIPK2 cytoplasmic localization (Figure 1B), meaning likely HIPK2 inactivation [41].

As shown in Figure 3c, the characteristic peaks of GO (green line) displayed the C=O stretching vibration peak at 1,730 cm-1, the vibration and deformation peaks of O-H groups at 3,428 and 1,415 cm-1, respectively, the C-O (epoxy groups) stretching vibration peak at 1,220 cm-1, and the C-O (alkoxy groups) stretching peak at 1,052 cm-1[25]. After the reaction is conducted for 48 h (red line), the intensities of the FTIR peaks corresponding to the C-O (epoxide groups) stretching vibration peak at 1,220 cm-1 disappeared nearly, the C=O stretching vibration

peak at 1,730 cm-1 decreased dramatically, and the vibration and deformation GDC 0068 peaks of O-H groups at 3,428 and 1,415 cm-1, respectively, and the C-O (alkoxy groups) stretching peak at 1,052 cm-1 increased slightly. These results further confirmed that some active functionalities Evofosfamide (epoxide groups) in GO have been removed. The mechanisms of tailoring GO Since the appearance of GO, the determination of GO structure has been challenging because of its nonstoichiometric chemical composition, which depends on the synthesis method and

the degree of reduction, and the oxygen functional groups in GO have been identified by various kinds of techniques. It is generally agreed that oxygen is present in GO mostly in the form of hydroxyl and epoxide groups on the basal plane, whereas smaller amounts of carboxyl, carbonyl, phenol, lactone, and quinone are present primarily at the sheet edges. The existence of the chemical groups confers new properties on GO such as the perfect monodispersity in water and weak reducibility. Based on the above facts and our experimental results, a probable mechanism is put forward as given in the schematic diagram (Figure 4). Firstly, part of Ag+ ions is preferentially absorbed on the sites of carboxylic groups at the edges of GO by the electrostatic interaction. Then Ag+ ions bonded on GO or freely dispersing in the solution further encounter the reducing groups (e.g., epoxy groups)

on the basal plane of other GO sheets. Thus, Ag+ Docetaxel research buy ions themselves are reduced to Ag and then generate Ag nanoparticles; meanwhile, the carbon-carbon skeleton is broken which directly leads to the cutting of GO into little pieces. Figure 4 Schematic diagram of tailoring mechanism through solution-phase redox reaction by adding metal ions into solution. Although the feasibility conclusion has been verified through analysis results of UV-vis and FTIR data, we also elaborately investigated the chemical state find more change of carbon in GO by XPS technology. Figure 5a shows the C1s XPS of GO sheets. There are four different peaks detected that centered at 284.5, 288.4, 293.8, and 296.6 eV, corresponding to C=C/C-C in aromatic rings, C-O (epoxide and alkoxy), C=O, and COOH groups, respectively [26]. After adding Ag+ ions into solution for 48 h, the distinct changes of C1s XPS are detected in Figure 5b.

Comparative analysis of recombinant P1 protein fragments by western blotting In this experiment, equal amount (1 μg) of purified recombinant P1 protein fragments (rP1-I-IV) were run in two separate SDS-PAGE. SDS-PAGE of all the four purified P1 protein fragments was transferred to two separate nitrocellulose membrane to perform western blotting. After blocking with 5% skimmed milk in PBS-T one membrane was then incubated with primary antibody (pooled sera of M. pneumoniae infected patients, 1:50) and second membrane

was incubated with primary anti-M. pneumoniae antibody (1:3,000 dilutions) for 1 h. After washing with PBS-T first membrane was incubated with secondary antibody goat anti-human IgG and second membrane with secondary antibody goat anti-rabbit IgG conjugated with horseradish peroxidase (1:5000 dilutions) for 1 h. The membrane was developed with DAB EPZ015938 solubility dmso and H2O2. Reactivity of recombinant P1 protein fragments to patient sera All the Lazertinib mw four recombinant P1 protein fragments; rP1-I, rP1-II, rP1-III and rP1-IV were analyzed for their reactivity to twenty five sera of M. pneumoniae infected patients and sixteen healthy patient sera using ELISA assay as well as fifteen sera of M. pneumoniae

infected patients by western blot analysis. Western blot analysis was performed as described above using equal amount of recombinant proteins. For the ELISA analysis, 96-well microplates (Nunc, Roskilde, Denmark) were coated with 50 ng of either of the four P1 protein fragments in 0.06 M carbonate/bicarbonate buffer (pH 9.6) per well. The plates were kept overnight at 4°C and next day the well were washed with PBS-T and blocked with 5% skimmed milk in PBS-T for 2 h at room temperature. The antigen coated wells were next incubated with sera of M. pneumoniae infected patients (1:50 dilutions) for 1 h at 37°C. After incubation, plates were washed with PBS-T and incubated Benzatropine with

secondary goat anti-human antibody conjugated with horseradish-peroxidase (1:3,000 dilutions) for another 1 h at 37°C. The enzyme reaction was developed by addition of TMB/H2O2 substrate (Bangalore Genei) and was incubated in dark for 30 min at 37°C. The reaction was stopped with 2 N H2SO4 and the absorbance was read at 450 nm wavelength using micro-plate ELISA PERK modulator inhibitor reader (Bio-Tek Microplate Reader, USA). M. pneumoniae adhesion assay HEp-2 cells (5×104 HEp-2 cells ml−1), in RPMI-1640 medium with penicillin (100 U ml−1) 0.05% were added to 24-well Multi-dish plates (Nunc, Roskilde, Denmark) using sterile glass cover slips underneath. The plates were incubated overnight in 5% CO2 at 37°C. Next day, HEp-2 cells in each well were infected with the M. pneumoniae RPMI-suspension (50 μl well−1) and incubated for 6 h in 5% CO2 at 37°C. The infected HEp-2 cells were fixed in methanol 100% (1 ml well−1) at −20°C for 1 h and washed with PBS.

The ompR transcription is induced directly by its own gene product in Salmonella enterica [3]. OmpR consensus-like sequences are found in the upstream region of ompR in Escherichia coli, selleck kinase inhibitor Although there are still no reported experimental data for its autoregulation in this bacterium. Upon the elevation of medium osmolarity, cellular OmpR-P levels are likely enhanced by two distinct mechanisms, namely, post-translational phosphorylation/dephosphorylation by EnvZ and transcriptional auto-stimulation. Enterobacteriaceae express at least two major outer membrane (OM) porins, namely,

OmpF and OmpC, both of which form transmembrane pore structures and function as ion channel [4–6]. OmpF and OmpC in the cell of E. coli form water-filled pores that are poorly selective selleck chemicals to cations (so called non-specific porins), thereby allowing the diffusion of low-molecular-weight polar compounds (not over 600 daltons) into the cell to maintain cell permeability. They exist as homotrimers in the OM. The basic structural element of the porin monomer is an ellipsoid in the section cylinder consisting of 16 transmembrane β-strands (so-called β-barrel)

connected by short periplasmic and longer ‘external’ check details loops [7]. E. coli OmpX contains 8-stranded β-barrel, with polar residues on the inside and hydrophobic residues on the outside facing the membrane environment [8]. Enterobacter aerogenes OmpX is the smallest known channel protein with a markedly cationic selectivity [6, 9, 10]. Although several experiments have demonstrated that OmpX plays Ceramide glucosyltransferase roles that are similar to those of porin [6, 9–12], it is not yet clear whether or not OmpX forms porins on the

cell membrane. E. aerogenes OmpX forms channels in the lipid bilayer [6]; however, the NMR and crystal structures of OmpX do not show pores [8, 13]. The ompX expression in E. coli [12] or E. aerogenes [6] is enhanced during early exposure to environmental perturbations, such as high osmolarity, antibiotics and toxic compounds, that are accompanied by the repressed expression of non-specific porins (OmpF and/or OmpC). Over-expression of OmpX, with a channel structure that is much smaller than that of OmpF and OmpC [6], may stabilize cell OM and balance the decreased expression of the two non-specific porins for the exclusion of small harmful molecules. It is interesting to further investigate the roles of OmpX in modulating OM permeability and adaptability. OmpR consensus-like sequences have been found within the ompX upstream region in E. coli and E. aerogenes [6]; however, the regulation of ompX by OmpR has not yet been established experimentally in any bacterium. As shown in E. coli as a model, OmpF and OmpC are reciprocally regulated by medium osmolarity.

Immuno-detection has provided the basis for the development of powerful analytical tools for a wide range of targets. During the last years, the number of publications in this field has increased significantly [27]. Traditionally, the most common method applied to microorganism detection has been the enzyme-linked immunosorbent assay (ELISA). The main drawback of ELISA is the high detection limit generated;

which is often between 105 and 106 CFU/mL [28]. This limit may be improved to 103 and 104 cells/mL using more sensitive detection methods [29, 30]. The immobilization of antibodies onto the surface of magnetic beads to obtain immunomagnetic GSK2126458 beads (IMB) has promoted the development of immunomagnetic separation (IMS). Thereby, IMS provides a simple but powerful method for specific capture, recovery and concentration of the desired microorganism from heterogeneous INK128 bacterial suspension [23, 31–34]. A test based on IMS by anti-L. pneumophila immuno-modified magnetic beads (LPMB), coupled to enzyme-linked colorimetric detection has been proposed for the rapid detection of L. pneumophila cells in water samples [35]. In this study, intensive comparison of this immunomagnetic method (IMM) with the culture method is presented. Protein Tyrosine Kinase inhibitor results Comparative trial with natural samples The IMM test was applicable to detection of L. pneumophila in water samples. A total of 459 water samples, comprising both naturally contaminated

and artificially contaminated samples were examined for the presence of L. pneumophila using the reference culture method (ISO 11731-Part 1) and the IMM test in parallel.

The parameters for this comparison study were calculated from the results summarized in Table 1 as it is described in the Methods section. Sensitivity and specificity were estimated as 96.6% (284/294) Protein tyrosine phosphatase and 88% (145/165), respectively for the IMM. This means that a proportion of actual positives and negatives are correctly assigned by the IMM test. False positives and false negatives were estimated as, respectively, 12.0% (20/304) and 3.4% (10/294). Some “false” positives could be related to problems in the culture method, as stated in the background that presents some limitations under different circumstances [12, 15, 21]. In fact, the PCR analysis of some of the samples initially considered false positives confirmed later the existence of DNA from L. pneumophila in those samples (results not shown), suggesting a failure of the culture method. From the point of view of the IMM as a screening test with culture confirmation, presumptive test negative results can be added to the true negatives. In this case sensitivity and specificity were estimated as, respectively, 96.6% (284/294) and 100% (0/165) for the IMM. False positives and false negatives were estimated as, respectively, 0% (0/324) and 3.4% (10/294). The low false negative ratio suggests that the IMM is very reliable.

For translation into the clinic it is important to observe that besides NK cells, relatively small numbers of NKT and T cells are HSP inhibitor expanded in this system. These cell populations may mediate GvHD when infused together with NK cells in adoptive allogeneic immunotherapy protocols. GvHD is a serious, potentially life-threatening, condition resulting from transplanted or infused allogeneic donor cell recognition of the recipients’ tissues as non-self, and is predominantly mediated by CD3+ T cells [30]. These cells are often depleted to prevent GvHD, as could be accomplished with the cells expanded by the protocol

presented here. Depletion of T cells from the NK cell product before administration to the host is likely to be less critical in the autologous setting. An important observation selleck screening library in our studies was that the expanded NK cells did not kill autologous and allogeneic PBMC, an indication that despite the increase in surface expression of activating receptors on the NK cells, the inhibitory ligands expressed on normal PBMC were dominant and able to control cytolytic activity against non-malignant cells. This is further illustrated in that both find more gastric tumor

cell lines were susceptible to autologous cytotoxicity BCKDHB despite the expression of high levels of inhibitory classical and non-classical HLA class I molecules. These data suggest that, under certain conditions, activating receptor-ligand recognition may override receptor-ligand interactions that inhibit NK activity. Emerging data indicates that important triggers in this

interaction are surface structures (ligand) that are expressed on cells that have undergone malignant transformation. In addition, it is well recognized that HLA class I expression the major NK cell inhibitory structure, is often down regulated in many solid tumors. In the case of autologous NK cell cytotoxicity against PBMC, inhibitory signals still predominated over activating signals, since no cytotoxicity of NK cells against autologous or allogeneic PBMC was observed. Our results indicate that the NK cells expanded and activated by the methods described do not recognize and kill non-transformed cells. In addition, while significantly higher levels of the inhibitory CD94/NKG2A complex were expressed after ex-vivo cell expansion, it did not affect the potential of autologous gastric tumor cell recognition. The CD94/NKG2A complex is reported to directly inhibit NK cell cytotoxicity through recognition of HLA-E [31].

Typhimurium. The LPI™ FlowCell is a single use device with a membrane-attracting surface that allows for the immobilisation of intact proteoliposomes (phospholipid vesicle incorporating membrane AR-13324 mouse proteins [19]) directly produced from membrane. The proteins are kept in their native state with retained structure and function. The LPI™ FlowCell, allows for multiple rounds of chemical treatment and a wide variety of applications since the membrane vesicles are attached directly to the surface. The work-flow starts with the preparation of small membrane vesicles from S. Typhimurium. The membrane vesicles are washed and are then injected

into the LPI™ FlowCell, allowing attachment to the surface. The immobilised CBL0137 in vivo membranes are then subjected to enzymatic digestion of proteins, in one or multiple steps to increase sequence coverage. By using proteases such as trypsin, Selleck XAV939 the surface exposed parts of the membrane associated proteins are digested into smaller peptide fragments which can be eluted from the flow cell and analysed by liquid

chromatography – tandem mass spectrometry (LC-MS/MS). A multi-step protocol can then be designed to increase the total sequence coverage of proteins identified, and so adding more confidence to the results generated using the LPI™ FlowCell. This approach allowed to identify a larger number of outer membrane proteins expressed by S. Typhimurium than previously reported [20] where many of which are associated with virulence. Results Preparation of outer membrane vesicles PLEKHM2 A key step for the successful isolation of outer membrane proteins when using the LPI technology is the generation of outer membrane vesicles (OMVs). Here cells were converted into osmotically sensitive spheroplasts in triplicates by digesting the peptidoglycan layers of the cell wall with lysozyme. This was followed by osmotic shock treatment which induced the formation of vesicles at the outer membrane. Some were freely liberated as judged by electron microscopy. However, many were still attached to cells and were released by vigorous shaking. Intact, unbroken cells were removed

from the vesicles by a low centrifugation step and the outer membrane vesicles were collected by ultracentrifugation. The process of vesiculation and the purity of the vesicle suspension was monitored using electron microscopy (EM) (Figure 1). The various stages were monitored, that is from untreated washed cells to pure outer membrane vesicles to exclude as far as possible the presence of whole cells prior to loading on the LPI™ FlowCell. The images obtained by EM demonstrated the morphological changes the cell undergoes during the vesiculation process and the efficiency of the procedures used to generate OMVs. Figure 1 Electron microscopy images illustrating the various stages of vesicle formation of Salmonella Typhimurium. a) An intact washed Salmonella cell prior vesiculation treatment.

Metagenome sequence data (i.e. singleton reads) were processed using two fully automated open source systems: (1) the MG-RAST v3.0 pipeline (http://​metagenomics.​anl.​gov) [18] and (2) the

Rapid Analysis of Multiple Metagenomes with a Clustering and Annotation Pipeline (RAMMCAP) [19], available from the Community Cyberinfrastructure for Advanced Microbial Ecology Research and Analysis (CAMERA, http://​camera.​calit2.​net). MK-8931 price The analysis included phylogenetic comparisons and functional annotations. All analyses were performed with an expected e-value cutoff of 1e-05 without preprocessing filtering. The metagenomes generated in this paper are freely available from the SEED platform (Projects: 4470638.3 and 4470639.3). Taxonomic relationships between metagenomes were analyzed by two complementary analyses using the MG-RAST pipeline. First, 16S rRNA gene sequences were retrieved and compared to a database of known 16S rRNA

gene sequences (e.g. SSU SILVA rRNA database project). Each read that matched a known sequence was MLN2238 assigned to that organism. In the second analysis putative BI 2536 nmr open reading frames (ORF) were identified and their corresponding protein sequences were searched with BLAST against the M5NR database [18]. The M5NR is an integration of many sequence databases into one single, searchable database. This approach provided us with information for assignments to taxonomic units (e.g. class, families and species) with the caveat a protein sequence could be assigned to more than one closely related organism. Taxonomic assignments were resolved using the lowest common ancestor (LCA) approach [18]. Functional analysis and reconstruction of metabolic

pathways ORFs were identified Thalidomide and their corresponding protein sequences were annotated (i.e. assigned functions) by comparison to SEED, Pfam, TIGRfam and COG databases [18, 19]. Identified proteins were assigned with their respective enzyme commission number (EC). Prior to quantitative characterization, counts were normalized (relative abundance) against the total number of hits in their respective database (e.g. SEED, COG, etc.) using effective sequence counts, a composite measure of sequence number and average genome size (AGS) of the metagenome as described by Beszteri et al.[20]. Raes and colleagues [21] defined the AGS as an ecological measure of genome size that also includes multiple plasmid copies, inserted sequences, and associated phages and viruses. Previous studies [20, 21] demonstrated that the relative abundance of genes will show differences if the AGS of the community fluctuate across samples. The ChaoI and ACE estimators of COG richness were computed with the software SPADE v2.1 (http://​chao.​stat.​nthu.​edu.​tw) [22] using the number of individual COGs per unique COG function. The proportion of specific genes in metagenomes also provides a method for comparison between samples.

Prog Brain Res 2004, 146:451–476.CrossRef 6. Ponder KP: Vectors in gene therapy. In An Introduction to Molecular Medicine and Gene Therapy. Edited by: Kresina TF. New York: Wiley; 2002:77–112. 7. Philippi C, Loretz B, Schaefer UF, Lehr CM: Telomerase as an emerging target to fight cancer–opportunities and challenges for nanomedicine. J Control Release 2010,146(2):228–240.CrossRef 8. Higashi T, Khalil IA, Maiti KK, Lee WS, Akita H, Harashima H, Chung SK: Novel lipidated sorbitol-based molecular transporters for non-viral gene delivery. J Control Release 2009,136(2):140–147.CrossRef 9. Kostarelos K, BAY 80-6946 clinical trial Miller AD: Synthetic, Anlotinib clinical trial self-assembly ABCD nanoparticles;

a structural paradigm for viable synthetic non-viral vectors. Chem Soc Rev 2005,34(11):970–994.CrossRef 10. Mastrobattista E, van der Aa MA,

Hennink WE, Crommelin DJ: Artificial viruses: a nanotechnological approach to gene delivery. Nat Rev Drug Discov 2006,5(2):115–121.CrossRef 11. Lu Y: Transcriptionally regulated, prostate-targeted gene therapy for prostate cancer. Adv Drug Deliv Rev 2009,61(7–8):572–588.CrossRef 12. Bharali DJ, Klejbor I, Stachowiak EK, this website Dutta P, Roy I, Kaur N, Bergey EJ, Prasad PN, Stachowiak MK: Organically modified silica nanoparticles: a nonviral vector for in vivo gene delivery and expression in the brain. Proc Natl Acad Sci U S A 2005,102(32):11539–11544.CrossRef 13. Conwell CC, Huang L: Recent advances in non ‒ viral gene delivery . Adv Genet 2005, 53:1–18.CrossRef 14. Niidome T, Huang L: Gene therapy

progress and prospects: nonviral vectors. Gene Ther 2002,9(24):1647–1652.CrossRef 15. Bigger BW, Tolmachov O, Collombet JM, Fragkos M, Palaszewski I, Coutelle C: An araC-controlled bacterial cre expression system to produce DNA minicircle vectors for nuclear and mitochondrial gene therapy. J Biol Chem 2001,276(25):23018–23027.CrossRef 16. Mayrhofer P, Schleef M, Jechlinger W: Use of minicircle plasmids for gene therapy. Methods Mol Biol 2009, 542:87–104.CrossRef 17. Deelman L, Sharma K: Mechanisms of kidney fibrosis and the role of antifibrotic therapies. Curr Opin Nephrol Hypertens GNA12 2009,18(1):85–90.CrossRef 18. Lee JM, Yoon TJ, Cho YS: Recent developments in nanoparticle-based siRNA delivery for cancer therapy. Biomed Res Int 2013,782041(10):17. 19. Dobson J: Gene therapy progress and prospects: magnetic nanoparticle-based gene delivery. Gene Ther 2006,13(4):283–287.CrossRef 20. Liu C, Zhang N: Chapter 13 – nanoparticles in gene therapy: principles, prospects, and challenges. Prog Mol Biol Transl Sci 2011, 104:509–562.CrossRef 21. Sinha R, Kim GJ, Nie S, Shin DM: Nanotechnology in cancer therapeutics: bioconjugated nanoparticles for drug delivery. Mol Cancer Ther 2006,5(8):1909–1917.CrossRef 22. Morachis JM, Mahmoud EA, Sankaranarayanan J, Almutairi A: Triggered rapid degradation of nanoparticles for gene delivery. J Drug Deliv 2012, 2012:1–7.CrossRef 23.