1 Specify whether the publications are open access (free access on Internet)   yes [] no [] – If yes: Enter the website address________________________________________________   8. Does your Institution agree to make its own scientific production freely accessible online on the open archive DSpace ISS http://​dspace.​iss.​it/​dspace set up by the Istituto Superiore di Sanità? yes [] no []   9. Please leave here any comments or notes if needed to clarify the answers given (by specifying the number of the related answer): Name and signature of the chief librarian or the person in charge at managing the publications

produced by your Institution Name_______________________________________________________________________ Signature____________________________________________________________________ Tel._________________________________________________________________________ selleckchem E-mail_______________________________________________________________________ Date________________________________________________________________________ Print the

questionnaire and send it to_____________________fax number_______________ within_____________________________ Thank you   PRIVACY POLICY Notice provided according to the terms of art. 13 of Italian Legislative Decree no. 196 of 30 June 2003 for the protection of personal data The data AR-13324 provided in the Questionnaire will be processed by means of automated equipment, only to fulfill the following tasks: to build up a unique reference access point to scientific information produced by the institutions surveyed through the digital archive DSpace ISS http://​dspace.​iss.​it/​dspace/​. Does the user grant her/his permission to processing their personal data according to the above mentioned tasks? Yes [] No [] Acknowledgements The authors wish to thank the colleagues 3-oxoacyl-(acyl-carrier-protein) reductase from the Italian institutions surveyed who actively collaborated by providing data through the questionnaire administered: Barbara Matrascia, Pellegrino Musto, Antonio Rosato, William Russell-Edu, Alessandra Trocino. Special GPCR & G Protein inhibitor thanks to Roberto Ricci

for his expert support in implementing data export procedures to DSpace ISS XML schema and to Roberto Rizzo for revising the manuscript and bibliography according to the Instructions. The authors are also very grateful to Norah May and Tania Merlino who revised the English text. References 1. Law D: Making science count: Open Access and its impact on the visibility of science. In Proceedings of the Conference Institutional archives for research: experiences and projects in Open Access. Istituto Superiore di Sanità. Rome, 30 November-1 December 2006. Edited by: De Castro P, Poltronieri E. Roma: Istituto Superiore di Sanità; 2007:6–14. (Rapporti ISTISAN 07/12) 2. Di Diodoro D: EBM ed editoria scientifica. In Etica conoscenza e sanità: Evidence-Based medicine fra ragione e passione. Edited by: Liberati A.

M.R. study of MurNAc- L -Ala- D -iGln (MDP) and its analogue murabutide: evidence for a structure involving two successive β-turns in MDP. Carbohydr Res 1987, 162:23–32.CrossRef 44. Sizun P, Perly B, Level M, Lefrancier P, Fermandjian S: Solution conformations of the immunomodulator muramyl

peptides. Tetrahedron 1988, 44:991–997.CrossRef 45. Adochitei A, Drochioiu G: Rapid characterization of peptide secondary structure by FT-IR spectroscopy. Rev Roum Chem 2011, 56:783–791. 46. Hering JA: FTIR spectroscopy for analysis of protein secondary structure. In Biological and Biomedical Infrared Spectroscopy. Edited by: Barth A, Haris PI. Amsterdam: IOS; 2009:129–167. 47. Wellman SE, Hamodrakas SJ, Kamitsos EI, Case ST: Secondary structure of synthetic peptides derived from the repeating selleck products unit of a giant secretory protein from Chironomus tentans . Biochim Biophys Acta Protein Struct Mol Enzymol 1992, 1121:279–285.CrossRef Competing interests The authors declare that they have no competing interests. Authors’ contributions LRA obtained the silica-supported SPhMDPOBn sample, carried out the electrospray

ionization ion trap mass spectrometric investigation click here and FT-IR spectroscopic investigation, and drafted the manuscript. LRA together with TVK conceived of the study and participated in its design and interpretation of TPD-MS and FT-IR investigation results. BBP obtained the TPD-MS spectra of SPhMDPOBn in the pristine state and on the silica surface. VNT together with LRA carried out the synthesis of SPhMDPOBn. AEZ together with VYC participated in the design and coordination of the synthesis of SPhMDPOBn. All authors read and approved the final manuscript. We declare that this manuscript is original, has not been published before Cediranib (AZD2171) and is not currently being considered for publication elsewhere.”
“Background Recently, field emitters using carbon

nanotubes (CNTs) have been utilized as cold electron sources for high-resolution X-ray apparatuses [1–3]. To use CNTs as electron sources, the turn-on electric field that triggers the field-driven electron emission must be low, and the generated emission see more current level must be high. Simultaneously, the stability of the emission current must be ensured during a long-term operation. Here, CNTs can be prepared on various types of substrates such as flat types and tip types either by direct [4–6] or indirect [7–10] methods. Practically, the indirect methods have certain advantages over the direct methods due to their simpler deposition systems, lower costs, lower processing temperatures, and easier scale-up. However, the indirect methods demonstrate weak adhesion often with the widely utilized metallic substrates [11, 12]. Under a prolonged emission condition, CNTs may be removed on substrates due to their weak adhesion. This makes it difficult to obtain uniform and consistent emission currents from the CNT emitter.

Their mutant showed increased stability relative to our T26N mutant but was completely non-motile under all conditions they assayed. Their Thermus MglA carrying this mutation showed a further decrease in hydrolysis relative to both WT and G21V activating mutation, but also showed a substantial decrease in affinity for mantGTP and the non-hydrolyzable analog mantGPPNHP [19]. A subset of mutations predicted to disrupt surface residues yielded strains with potentially informative phenotypes. The substitution at Leu124, which may be part of a LRR, might alter the interactions with an effector protein. One candidate is AglZ, a protein known to interact with MglA [43], which contains heptad repeats that are characteristic of

check details LRR-domain protein partners. Potential cycling of the MglA, AglZ, and FrzS triumvirate may yield clues to the regulation of A- and S-motility. Mauriello et al.

confirmed the interaction of AglZ and MglA, as well as FrzS and MglA using tandem affinity purification [4]. If the L124K substitution PRI-724 price altered the affinity of MglA for AglZ, this might perturb the interaction between AglZ and FrzS and might explain why the L124K mutant showed increased frequencies of cell reversal, however further investigation will be necessary to characterize the nature of this perturbation. Two mutations in MglA altered the ability to localize correctly as observed by immunofluorescence. Both of the mutations which appeared to disrupt correct localization were predicted to be located on the surface of the protein, and on one face. One critical residue, D52, is analogous to the D33 residue in Ras, which has been shown to interact with a lysine in the protein NORE1A. NORE1A is a cytoskeletal protein that has been shown to be a suppressor of growth and oncogenic properties of active Ras [44]. It is possible that mutation of D52 in MglA has disrupted a similar protein interaction which would PJ34 HCl account for its lack of proper localization and function in a complementation background, and also the mutation’s effects on the ability of M. xanthus to SB-715992 molecular weight control reversal. We posit that the surface containing both D52 and T54 is responsible

for proper recruitment of MglA to the cytoskeleton and that proper localization along the cytoskeleton is required for control of A-motility as well as regulating cell reversal. The failure of class III mutants to make detectable MglA was surprising as similar sets of mutations in other monomeric GTPases have not been reported to affect protein stability. Introduction of polar residues in critical residues of Ha-Ras (N116K/Y) created a protein that was unable to bind GTP correctly, but did not alter stability [45]. Replacement with other large nonpolar or charged groups also altered GTP binding, but mutant proteins were stable in vitro [35]. This suggests that GTP binding itself has the potential to regulate the function of MglA in motility and development.

Tunable plasmon resonance with varying incident angles can be observed. https://www.selleckchem.com/products/jph203.html Figure  3c shows the electric near-field distribution of a single nanopillar at 30° to the incidence normal at the wavelength of 430 nm calculated by using CST microwave studio. During simulations, one unit cell was considered BIRB 796 manufacturer which consisted of a vertically oriented cylindrical Au nanopillar. Periodic boundary conditions were assigned to the lateral walls and Floquet ports were imposed on top and bottom of the unit cell to

mimic an infinite periodic array with a periodicity of p = 450 nm. The nanopillar has a radius of r = 100 nm and a height of h = 200 nm. A fifth-order Drude-Lorentz model was employed to fit the measured permittivity of Au [42]. It is observed that at

the wavelength corresponding to the peak of specular reflection for each angle of incidence case, the electric field exhibits curl-like patterns, concentrating near the vertical surface of the nanopillar.As mentioned above, Ag has a much higher etching rate than Au under the same milling parameters using ion beams. Therefore, Ag has a larger selectivity than Au with the same resist mask (fixed thickness) for milling. Figure  4a,b shows the top-view and oblique-view SEM images of Ag nanopillar arrays with ultrasmall gap sizes, Volasertib solubility dmso respectively. The average measured smallest gap width is approximately 10 nm. Dome-shaped profiles can be observed from Figure  4b, which is mainly caused by materials redeposition during the milling process. Note that the gaps between neighboring nanopillars have been milled through to the surface of the substrate. Typical fabrication imperfections are highlighted with red circles.The measured absorbance spectra for two Ag nanopillar tuclazepam arrays with different periodicities

and ultrasmall inter-pillar separations are plotted in Figure  5. The LSPRs in nanopillars can be described as a series of longitudinal standing waves with an increasing number of harmonics at shorter wavelengths. In addition, the LSPRs are laterally confined and bounded between adjacent nanopillars. The spectra also show the effect of periodicity variation and reveal different regimes. Very little radiative coupling occurs when the diffraction edge is on the high-energy side of the main LSPR since the allowed diffracted orders have higher energy than the plasmon resonance. Most of the LSPRs confined within the nanopillar array exist as higher-order modes. Note that the standing waves within the nanopillars can be influenced by the coupling of transverse plasmon modes between nanopillars, leading to different resonances described for separate nanopillars. Additionally, Fano-type line shapes are observed which result from the interference between directly transmitted and scattered energy.

05) calculated by Fisher’s exact test and also by a ratio of the number of molecules from the experimental data set that Torin 2 maps to the pathway, divided by the total number of molecules that exists in that canonical pathway. Immunofluorescence microscopy Non-adherent THP-1 cells (CAM and mock treated) were analyzed by indirect immunofluorescent antibody (IFA) microscopy. Briefly, 1 × 105 cells were cytocentrifuged onto poly-L-lysine coated slides for 2 minutes at 1000 rpm using a Shandon Cytospin® 4 Cytocentrifuge (Thermo Scientific) [31]. The cytospun THP-1 cells were air dried and immediately fixed using ice cold acetone for 30 seconds. The fixed preparations were then washed with PBS and

stained with a rabbit antibody against whole killed C. burnetii NMII (primary antibody) followed by a goat anti-rabbit IgG Alexa Fluor-488 (Molecular Probes, Eugene, OR) secondary selleck antibody. Host and bacterial DNA were also stained using 4′,6-diamidino-2-phenylindole (DAPI). Microscopy was conducted using a Nikon Eclipse TE 2000-S microscope

with a Nikon DS FI1 camera and NIS-ELEMENTS F 3.00 software. IMAGEJ version 1.42n (Wayne Rasband, NIH) was also used for image processing [20]. RT-qPCR analysis RT-qPCR was performed using gene-specific primers (shown in Additional file 1-Table S1.I), and the SYBR Green Master Mix Kit (Applied Biosystems) on an Eppendorf Mastercycler ® ep realplex (Eppendorf, Hamberg, Germany) following the manufacturer’s recommendations.

Briefly, first strand cDNA was synthesized using Eltanexor random hexamers, 1 μg of total RNA, and the SuperScript III First-Strand Synthesis System for RT-PCR (Invitrogen) as suggested by the manufacturer. Oligonucleotide primers were designed using Primer3Plus [32, 33]. The primer efficiency of each primer set was determined to be within the efficiency window for the 2-ΔΔCT relative fold calculation method [34]. The human β-actin gene was used as the reference gene. Paired T-Test was performed to identify statistical differences between any Ergoloid two conditions. Differences were considered significant at a P < 0.05. Results SPV morphology within CAM treated C. burnetii infected THP-1 cells As the transient inhibition of C. burnetii protein synthesis within infected THP-1 cells using CAM is pivotal to testing our hypothesis, we sought to confirm that morphological changes occur to the PV of infected THP-1 cells after transient CAM treatment in a manner consistent with that observed in other cell types [35]. Using phase contrast and IFA microscopy analysis, we assessed the effect of bacteriostatic levels of CAM (10 μg/ml) on infected THP-1 cells during the log growth phase of the C. burnetii infectious cycle in order to coincide with subsequent microarray analysis. Robust infections (≥90% infected cells) were produced using C. burnetii NMII at a genome equivalent MOI of 15. Infections were either mock or CAM treated at 48 hours post infection (hpi), and then compared at 72 hpi.

OMVs alter antibiotic resistance phenotype in ETEC Adaptive (longer-term) bacterial resistance to polymyxin is typically based

on the upregulation of genes which lead to the modification of LPS [27, 33]. We wondered whether OMV-mediated defense would affect the onset of adaptive resistance of ETEC to polymyxin #ITF2357 randurls[1|1|,|CHEM1|]# B. A mid-log liquid culture of ETEC was treated with polymyxin B (3.5 μg/mL) and concurrently supplemented with either a relatively high concentration of ETEC OMVs (2 μg/mL) or buffer. Samples were taken hourly for up to 7 h post treatment, spread on LB agar and LB agar containing polymyxin B, and the plates inspected after 12 h incubation at 37°C (Figure 4). As expected from the results described earlier, ETEC cultures supplemented

with OMVs survived better compared to cultures that did not contain added OMVs (Figure 4B, C). However, we further observed that these bacteria were not able to grow on plates containing polymyxin B (Figure 4D). This suggests that the bacteria survived to a greater extent but did not become adapted to resist polymyxin. Figure 4 Acquisition of ETEC resistance to polymyxin B is reduced by co-incubation with high concentrations of OMVs. At hourly time-points for 0-7 h of co-incubation, equivalent Caspase inhibitor volumes of the samples described below were streaked on each plate in a pattern indicated by the template diagram. Top row: ETEC co-incubated with (A) nothing, (B, D) a high concentration of ETEC OMV (2 μg/mL) and polymyxin B (3.5 μg/ml), or (C) polymyxin B alone (3.5 μg/mL). Samples were streaked either on LB agar C1GALT1 (A-C), or LB containing 5 μg/ml polymyxin B (D-E). (E) ETEC co-incubated with ETEC OMV (3 μg/mL) and polymyxin B (3.5 μg/mL) for 5 h, then an additional 5 μg/mL polymyxin B was added, and plated on LB containing 5 μg/mL polymyxin B. Resistance was

seen by hour 7 without decreasing cell population significantly. Bottom row: ETEC co-incubated with (F) nothing, or (G, I) 1.4 μg/mL ETEC OMV and 3.5 μg/ml polymyxin B, and (H, J) polymyxin B alone (3.5 μg/mL), streaked on LB (F-H) or LB containing 5 μg/mL polymyxin B (I-J). (n = 9 for all experiments). To test if the bacteria in the OMV-supplemented culture were simply incapable of becoming adaptively resistant, an additional 5 μg/ml polymyxin B was added at hour 5 after the OMV-polymyxin B co-incubation and the culture was then plated on polymyxin B-containing agar. Resistant ETEC were observed without a detectable decrease in cell number after 7 h (Figure 4E). This result demonstrated that the OMV-protected ETEC had the capacity to adapt to high levels of antibiotic and achieve resistance if the polymyxin dose was increased beyond the amount the OMVs could protect. This reasoning was confirmed in further experiments in which we used a lower OMV concentration (0.7 μg/ml) with the same concentration of polymyxin B.

Inflammatory responses and chemokine/cytokine production elicited by WT FT proceeds with much slower kinetics than typically observed for other bacterial pathogens. In contrast, the kinetics of chemokine/cytokine

expression and neutrophil recruitment is more rapid following infection with the galU mutant strain, likely resulting in more rapid uptake and killing of bacteria by neutrophils. These studies also revealed that disruption of the galU gene results in a hypercytotoxic phenotype that could be due (at least in part) to activation of the AIM-2 inflammasome. The accelerated death of cells infected with the galU mutant P5091 strain presumably interferes with the normal replicative cycle of the bacterium, resulting in the significant difference in bacterial burdens in the liver and spleen of mice infected with the galU mutant vs. WT strains of FTLVS observed 4 days post-infection and contributing to the reduction in FTLVSΔgalU virulence. These findings underscore the need for studies designed to understand the mechanisms used by WT FT to alter the kinetics of innate immune responses following infection. A thorough comparative analysis of the outer envelope of the WT and galU mutant strains of FTLVS coupled with a more detailed analysis of the innate signaling that results following infection with these two strains of FT could lead to a better understanding of the ability of FT to avoid detection by the

innate immune system during the early stages of infection. SB-715992 The findings SAR302503 research buy presented here also suggest that a galU mutant strain of FT has high potential as a platform for

development of a live attenuated tularemia vaccine strain. Methods Bacteria and Culture Conditions FTLVS was a kind gift of Dr. Karen Elkins (FDA, Bethesda, MD). The FTLVS galU mutant strain was identified by screening a LVS transposon mutant library for mutants exhibiting elevated susceptibility to polymyxin B. Transposon insertion in to the galU gene was verified by DNA sequencing and the polymyxin B hypersensitive phenotype was verified by complementation. The results of this screen will be described in a future publication. FT strains were grown at 37°C in Mueller-Hinton (DIFCO/Becton Dickinson, Sparks, MD) broth modified with 2.5% ferric pyrophosphate, 0.1% glucose, and 10% cysteine (MMH). Monoiodotyrosine The galU mutant was grown under kanamycin selection (10 μg/mL). Complementation studies were performed as follows. The galU gene was amplified by PCR from the LVS genome using primers: forward primer: 5′-CTCGTGGATCCGCTAAAATGAAAATAAGAAAAGC-3′ and reverse primer: 5′-ATCGCTAATCGATAAGCTATCTATTTTGAAGG-3′. The resulting amplicon was digested with BamHI and ClaI restriction endonucleases before being ligated to similarly digested pXB167 [65], which placed the galU gene downstream and in the same orientation as the constitutively expressed orf5 promoter. The resulting plasmid, pXB167-galU, was then introduced into the indicated strains by electroporation as previously described [15, 65].

The lethal effect occurred only on the protozoan parasites and the erythrocytes remained unaffected by the peptide action. Histopathological findings suggest that the extent of damage

was negligible at the tissue level. 1 GSK2118436 manufacturer Introduction Malaria, caused by a protozoan parasite, is considered one of the most important endemic diseases afflicting subtropical countries and is the ninth most significant cause of mortality globally [1, 2]. Of the four human malaria parasite species, Plasmodium falciparum has been rated as the most malignant and causative Nirogacestat in vivo agent of cerebral malaria [3]. During the last few decades, there has been an emergence of clinical resistance to first-line treatment of antimalarial drugs. The widespread resistance of P. falciparum to chloroquine has rendered the drug ineffective against the most dangerous Plasmodium strain. Moreover, chloroquine resistance is associated with cross-resistance Selleck Stattic to other quinoline drugs, such as quinine and amodiaquine [4]. In the fight against resistance, artemisinin-based combination therapies (ACT) and its derivatives have provided a respite [5]. However, the search for novel lead compounds that can be developed as a cure for malaria is still active. One

such group of compounds are peptides produced naturally or which are synthetic in nature [2, 6]. For its successful existence and to protect itself from other pathogens, bacteria synthesize antimicrobial peptides (AMPs). These AMPs are ribosomally synthesized and are generally known as bacteriocins [7]. They form an innate part of the lactic acid bacteria defense system [8, 9]. These peptides have remained effective Dapagliflozin weapons since times immemorial against bacteria and fungi. It is generally believed that resistance can be developed in microorganisms in response to a therapeutic molecule/compound; however, there are very few studies reporting the development of resistance against bacteriocins/AMPs. The reasons for this are that

they are highly selective against the negatively charged bacterial membrane versus the zwitterionic mammalian membranes of a human host, and, secondly, the non-specificity in targeting is unlikely to evoke resistance [10]. The majority of reports suggest an association of these bacteriocins with the killing of pathogenic Gram-positive and Gram-negative bacteria as well as fungi [11–13]. Considering the inhibitory spectrum of these AMPs, they are turning out to be powerful agents for targeting bacteria, fungi, and parasites, and there may be other targets that they can be tested upon [6]. For any such application, it is mandatory to test and provide information on toxicity/ill effects of the compound under consideration.

“
“Introduction What did Darwin think about the origin of life? His opinion seems to have changed over time from his original remark in the 1861 3rd edition of The Origin of Species «…it is no valid objection that science as yet throws no light on the far higher problem of the essence or origin

of life», which he reiterated in a letter he mailed to his close friend Joseph Dalton Hooker on March 29, 1863, in which he wrote that GSK2118436 cost «…it is mere rubbish thinking, at present, of origin of life; one might as well think of origin of matter». But yet, in a now famous paragraph in the letter sent to the same addressee on February 1st, 1871, he stated that «it is often said that all the conditions for the first production of a living being are now present, which could ever have been present. But if (and oh what a big if) we could conceive in some warm little pond with all sort of ammonia and phosphoric salts,—light, heat, electricity present, that a protein compound was chemically formed, ready to undergo still more complex changes, at the present such matter would be instantly devoured, or absorbed, which would not have been the case before living

creatures were formed [...]». Darwin’s opinions on the origin of the first organisms thus varied somewhat during his life, but never lead to the dramatic shift that could be implied by reading only the two paragraphs included. Indeed, a careful examination and critical reading of his public and private writings shows that what appear to be contradictory opinions on the problem of the emergence of life are the result of texts read out of context, sometimes maliciously, as shown by some this website publications of creationist groups and advocates of the so-called intelligent design. Darwin was a meticulous writer who kept detailed diaries

and excellent records of his extensive correspondence. This allows a detailed examination of the development of his ideas, a task facilitated not only by examining the books and articles he published during his lifetime, but also by the online availability of his correspondence and notebooks, including the pages that Darwin himself excised from buy Decitabine them but which have survived. Any attempt to study in detail Darwin’s ideas on the origin of life must consider the work of Farley (1977) and Strick (2000). Our own analysis has been greatly facilitated by the detailed cross-references and bibliographical analyses available at The Darwin Correspondence Project (Jim Secord, http://​www.​darwinproject.​ac.​uk/​) and The Complete Work of Charles Darwin Online (John van Wyhe, http://​darwin-online.​org.​uk/​). What we report here is not an exhaustive examination of all the phrases, sentences, letters or paragraphs in which Darwin touched in one way or another on the problem of the origins of life, or related issues like spontaneous generation or archebiosis. We have not included, for NVP-LDE225 chemical structure instance, his epistolary exchanges with W. H.

Drug Discov Today 2005, 10:35–43.Fludarabine molecular weight CrossRef 40. Lakshminarayanan A, Ravi VK, Tatineni R, Rajesh YB, Maingi V, Vasu KS, Madhusudhan

N, Maiti PK, Sood AK, Das S, Jayaraman N: Efficient dendrimer-DNA complexation and gene delivery vector properties of nitrogen-core poly(propyl ether imine) dendrimer in mammalian cells. Bioconjug Chem 2013,24(9):1612–1623.CrossRef 41. Liang GF, Zhu YL, Sun B, Hu FH, Tian T, Li SC, Xiao ZD: PLGA-based gene delivering nanoparticle enhance suppression effect of miRNA in HePG2 cells. Nanoscale Res Lett 2011,6(447):6–447. 42. Kabanov AV, Kabanov VA: DNA complexes with polycations for the delivery of genetic material into cells. GDC-0994 cell line Bioconjug Chem 1995,6(1):7–20.CrossRef 43. Sun X, Zhang N: Cationic polymer optimization for efficient gene delivery. Mini Rev Med Chem 2010,10(2):108–125.CrossRef 44. Xu W, Ling P, Zhang T: Polymeric micelles, a promising drug delivery system to enhance bioavailability of poorly water-soluble drugs. J Drug Deliv 2013, 2013:1–15.CrossRef 45. Dufresne M-H, Gauthier MA, Leroux J-C: Thiol-functionalized

polymeric micelles: from molecular recognition to improved mucoadhesion. Bioconjug Chem 2005,16(4):1027–1033.CrossRef 46. Harris TJ, Green JJ, Fung PW, Langer R, Anderson DG, Bhatia SN: Tissue-specific gene delivery via nanoparticle coating. Biomaterials 2010,31(5):998–1006.CrossRef 47. Lian J, Xin Z, Ming L, Yan D, Nongyue H: Current progress in gene delivery technology based on chemical methods and nano-carriers. Theranostics 2014,4(3):240–255.CrossRef 48. Ramos-Perez V, Cifuentes A, Coronas selleck N, Pablo A, Borrós S: Modification of carbon nanotubes for gene delivery vectors: nanomaterial interfaces in biology. Methods Mol Biol 2013, 1025:261–268.CrossRef 49. Shi Kam NW, Jessop TC, Wender PA, Dai H: Nanotube molecular transporters: internalization of carbon nanotube-protein conjugates into

mammalian cells. J Am Chem Soc 2004,126(22):6850–6851.CrossRef 50. Katragadda CS, Choudhury PK, Murthy P: Nanoparticles ADAM7 as non-viral gene delivery vectors. Indian J Pharm Educ Res 2010,44(2):109–111. 51. Isobe H, Nakanishi W, Tomita N, Jinno S, Okayama H, Nakamura E: Gene delivery by aminofullerenes: structural requirements for efficient transfection. Chem An Asian J 2006,1(1–2):167–175.CrossRef 52. Huang F-W, Wang H-Y, Li C, Wang H-F, Sun Y-X, Feng J, Zhang X-Z, Zhuo R-X: PEGylated PEI-based biodegradable polymers as non-viral gene vectors. Acta Biomater 2010,6(11):4285–4295.CrossRef 53. Tang Z, Zhou Y, Sun H, Li D, Zhou S: Biodegradable magnetic calcium phosphate nanoformulation for cancer therapy. Eur J Pharm Biopharm 2014, 2014. 54. Tiwari PK, Soo Lee Y: Gene delivery in conjunction with gold nanoparticle and tumor treating electric field. J Appl Phys 2013,114(5):5.CrossRef 55. Colvin VL, Goldstein AN, Alivisatos AP: Semiconductor nanocrystals covalently bound to metal surfaces with self-assembled monolayers. J Am Chem Soc 1992, 114:5221–5230.