Vector Borne Zoonotic Dis 2004,4(2):159–168.CrossRefPubMed 12. Steiner FE, Pinger SAHA HDAC molecular weight RR, Vann CN, Grindle N, Civitello D, Clay K, Fuqua C: Infection and co-infection rates of Anaplasma phagocytophilum variants, Babesia spp., Temsirolimus Borrelia burgdorferi , and the Rickettsial endosymbiont in Ixodes scapularis (Acari: Ixodidae) from sites in Indiana, Maine, Pennsylvania, and Wisconsin. J Med Entomol 2008, 289–297. 13. Hengge-Aronis R: Signal transduction and regulatory mechanisms involved in control of the σ S (RpoS) subunit of RNA

polymerase. Microbiol Mol Biol Rev 2002,66(3):373–395.CrossRefPubMed 14. Fikrig E, Narasimhan S:Borrelia burgdorferi -Traveling incognito? Microbes Infect 2006,8(5):1390–1399.CrossRefPubMed 15. Liang FT, Nelson FK, Fikrig E: Molecular adaptation of Borrelia burgdorferi in the murine host. J Exp Med 2002,196(2):275–280.CrossRefPubMed

16. Fraser CM, Casjens S, Huang WM, Sutton GG, Clayton R, Lathigra R, White O, Ketchum KA, Dodson R, Hickey EK, et al.: Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi. Nature 1997,390(6660):580–586.CrossRefPubMed 17. Caimano MJ, Eggers CH, Hazlett KRO, Radolf JD: RpoS is not central to the general stress response in Borrelia burgdorferi but does control expression of one or more essential virulence determinants. Infect Immun 2004,72(11):6433–6445.CrossRefPubMed 18. Fisher MA, Grimm D, Henion AK, Elias AF, Stewart PE, Rosa PA, Gherardini FC:Borrelia burgdorferi σ 54 is required for mammalian infection and vector transmission but not for tick colonization. PNAS learn more this website 2005,102(14):5162–5167.CrossRefPubMed 19. Hubner A, Yang X, Nolen DM, Popova TG, Cabello FC, Norgard

MV: Expression of Borrelia burgdorferi OspC and DbpA is controlled by a RpoN-RpoS regulatory pathway. PNAS 2001,98(22):12724–12729.CrossRefPubMed 20. Smith AH, Blevins JS, Bachlani GN, Yang XF, Norgard MV: Evidence that RpoS (σ S ) in Borrelia burgdorferi is controlled directly by RpoN (σ 54 /σ N ). J Bacteriol 2007,189(5):2139–2144.CrossRefPubMed 21. Caimano MJ, Iyer R, Eggers CH, Gonzalez C, Morton EA, Gilbert MA, Schwartz I, Radolf JD: Analysis of the RpoS regulon in Borrelia burgdorferi in response to mammalian host signals provides insight into RpoS function during the enzootic cycle. Mol Microbiol 2007,65(5):1193–1217.CrossRefPubMed 22. Hefty PS, Jolliff SE, Caimano MJ, Wikel SK, Radolf JD, Akins DR: Regulation of OspE-Related, OspF-Related, and Elp lipoproteins of Borrelia burgdorferi strain 297 by mammalian host-specific signals. Infect Immun 2001,69(6):3618–3627.CrossRefPubMed 23. Ge Y, Old I, Girons I, Charon N: The flgK motility operon of Borrelia burgdorferi is initiated by a σ 70 -like promoter. Microbiology 1997,143(5):1681–1690.CrossRefPubMed 24. Ge Y, Charon N: An unexpected flaA homolog is present and expressed in Borrelia burgdorferi.

Universal tails were added to the 5′ end of the allelic primers during primer synthesis. See Figures 1 and S1 for branch location

of SNPs in phylogeny. SNP positions are given for B. melitensis 16 M genome and all are on chromosome I except assays 6214 and 2995 are on chromosome II. SNPs used in the CUMA were randomly selected from the various options available on each branch, with fewer options possible with shorter branches. If development of the assay failed to produce effective primer pairs based on standard primer design parameters we simply selected a new SNP locus. Using the CUMA assays, we genotyped a diverse set of isolates (n = 340), which included TGF-beta inhibitor all recognized biovars and type strains (except B. microti and B. suis biovars 3 and 5), against 17 SNP assays for 10 branches. For each sample we determined if the SNP allele for each locus was ancestral or derived on the corresponding branch and then verified where the sample was placed on the tree. When possible, we selected two SNPs from each of the major branches. We generated amplicons for the SNP regions in four PCR reactions for each of the two multiplex PCRs and then pooled the PF-6463922 order PCR product in one capillary injection.

If the CUMA assay failed any locus in multiplex reactions, we reran that locus in singleplex, which generally allowed for determination of the SNP allele. Samples with singleplex failure largely

appeared to be of poor DNA quality since there were typically failures across several different CUMA Tacrolimus (FK506) assays (Additional file 4: Table S2). Acknowledgements We thank numerous contributors of DNA to our Brucella collection, including Brian Bell, Bryan Bellaire, Wally Buchholz, Robert Burgess, Barun De, Mike Dobson, Linda Getsinger, Ted Hadfield, and William Slanta. We thank Jim Schupp, Molly Matthews, and Jodi Beaudry for assistance with CUMA primer design and Ray Auerbach, Jolene Bowers, and Josh Colvin for help with data analysis and running samples. Recent whole genomes for comparisons were generated by the Broad Institute under the direction of David O’Callaghan, Adrian Whatmore, and Doyle Ward. Funding from the U.S. Department of Homeland Security (DHS) supported this work. Use of product or trade names does not constitute endorsement by the U.S. Government. Electronic supplementary material Additional file 1 Figure S1.: Brucella phylogeny using maximum selleck screening library parsimony developed using 777 single nucleotide polymorphisms. Letters on branches refer to phylogenetic locations of CUMA assays developed in this work. Stars on branches represent phylogenetic locations of species or clade specific assays from Foster et al. 2008. In this figure we rooted with B.

bGenomic sequences are available through the NCBI genomic BLAST service. cThe putative signal sequence selleck chemicals cleavage sites were determined using the SignalP 4.1 server. *The B. pseudomallei strain DD503 is a derivative of isolate 1026b in which the AmrAB-OprA antibiotic efflux pump has been deleted to facilitate mutant construction [61]. The BMA1027 orthologs of strains DD503 and 1026b are identical (confirmed by nucleotide sequence analysis, data not shown). The published genomic sequence of the B. pseudomallei strain K96243 was

found to specify a BMA1027 ortholog (locus tag # BPSL1631, Figure  1B) that is 89% identical to that of B. mallei ATCC 23344. The BMA1027 ortholog was sequenced from the B. pseudomallei strain used HM781-36B in our laboratory, DD503, and was predicted to encode a protein that is 97% and 87% identical to that of B. pseudomallei K96243 and B. mallei ATCC 23344, respectively (Figure  1C). Database searches with the NCBI genomic BLAST service also identified orthologs in several B. pseudomallei and B. mallei isolates. Seven B. mallei and twenty-nine B. pseudomallei strains for which sequences are available through the service were found to have the gene. Characteristics of these ORFs are listed in the Additional files 1 and 2. Overall, the proteins are 87-100% identical and differ primarily in the number and/or arrangement

of SLST repeats, YadA stalk domains, and/or NSTA elements in their passenger domains. Based on these results, we conclude that BMA1027 orthologs are well-conserved gene products shared by B. mallei and B. pseudomallei. While preparing this article, Campos and colleagues published a report in which they functionally characterized autotransporter genes specified by the B. pseudomallei strain 1026b [51]. One of these molecules corresponds to the BMA1027 ortholog (locus tag # BP1026B_1575), which the authors designated bpaC. Henceforth, Nintedanib (BIBF 1120) BMA1027 and orthologs will be referred to as BpaC. Expression and functional properties of the BpaC protein in E. coli Because of sequence and structural similarities to known bacterial

adhesins, we speculated that BpaC mediates adherence to Protein Tyrosine Kinase inhibitor epithelial cells. To test this hypothesis, the bpaC gene of B. pseudomallei DD503 was cloned and expressed in the E. coli strain EPI300. This organism does not adhere well to epithelial cells [8, 53, 55, 62] and therefore provides a suitable heterologous genetic background to study the adherence properties of BpaC. To verify protein expression, whole cell lysates were prepared from E. coli EPI300 harboring the plasmid pCC1.3 (control) or pCCbpaC (specifies B. pseudomallei DD503 bpaC) and analyzed by western blot. Figure  2A shows that α-BpaC Abs (directed against aa 392–1098, part of surface-exposed passenger domain) react specifically with a band of 100-kDa in E.

In addition, the distribution of the gene duplications (Figure 4) revealed that clusters of gene duplications of the same COG function exist on both CI and CII and that most of the gene duplications in a cluster possessed roughly similar levels of sequence conservation. As such, it may be possible that these highlighted chromosomal segments are locally selected for, especially as these gene duplications possess similar functions.

The sequence similarity and evolutionary constraints of the duplicate gene-pair are indicative of the essential or nonessential nature of gene function. Previous studies have revealed shown that the type II topoisomerases gyrase and topoisomerase selleck chemicals IV demonstrated 40 to 60% amino acid sequence identity, but each protein has a distinct function essential for cell survival [55, this website 56] highlighting the limitations in bioinformatics approaches. In a similar note, duplicate protein pairs with very little amino acid identity can share similar functions. In Bacillus subtilis, the peptide defomylases (Def and YkrB) show similarity only across short sequences (motifs) but both independently carry a deformylase reaction

essential for cell viability [57]. Therefore, gene disruption analysis is further required to determine the definitive function of isologous gene-pairs. In the specific analysis involving the carbon metabolism genes, it is likely that the cluster in CI containing cbbA, cbbF, cbbM, cbbP duplicated first and then cbbG and cbbT duplications arose from CI and were inserted between the duplicated cbbA and cbbP genes on CII. In addition, the two genes that

code for hypothetical proteins found between cbbT and cbbG on CI may have arisen through an C59 cost additional Lepirudin insertion or transposition event. Although these duplicated genes exhibit varying levels of protein divergence, these protein-pairs are under negative selection as evidenced by the functional constraints analysis in Figure 10. Additionally, the identity between the cbbM genes was low (31%). This is most probably due to the high degree of difference between cbbM I and cbbM II . More specifically, it has been shown that cbbM, which performs the first critical step in carbon fixation, has two forms (cbbM I and cbbM II ). The form I enzymes possesses large and small subunits while the form II enzyme possesses only large subunits that are different from the form I large subunits [58]. The distinguishing between CO2/O2 is primarily accomplished by loop 6 of the large subunit, which contains a conserved element of 11 amino acid residues. Form II enzymes are primarily anaerobic and unable to function in aerobic environments whereas form I enzymes can function in aerobic environments [59, 60].

The holocene sants containing uniform holocene minerals occured. Grained show unusual biological/microbiological activity, like antifungal against Peronospora sp., Phytophthora sp. The entity of the patent invention lies in the use of the holocene grain wash-out and different Human Interferons and combinations between them in the prevention of growth and multiplication of Human neoplastic cells in vitro. 1) Grain samples (»Svijetli« (Light), »Tamni« (Dark)) and Human ATM Kinase Inhibitor chemical structure Interferons: HuIFN-αN3

(Human leukocyte Interferon) (1000 I.U./ml) (reference value) and rHuIFN-α2 (1000 I.U./ml) (reference value) were used. Samples from river Drava sants, near Koprivnica, grained by »Star mix« technology giving fine grain with 60–80 μm size were used. The following

wash-out (»suspensions«) were prepared: (1) 10% Monoethylene-glycole, (2) 10% PBS (Phosphate buffer saline).CaCo-2 Gilteritinib mouse (Colon cancer carcinom) cells were used and WISH (Human amniotic cell line) cells as control. Cells were treated either with grain wash-out (Monoethylene glycole, PBS), HuIFN-αN3, rHuIFN-α2 or with different combinations between them in ratio: 1:1, 1:2, 2:1. The 50% cell growth inhibition test was used. The meaning of the data: The higher is the dillution till well giving 50% cell growth inhibition, beter is the substance. The conclusions:(1)The holocene grain wash-out (10% suspension) show the AP (Antiproliferative) activity against CaCo-2 cells in vitro.(2)The AP actvitiy of Monoethylene glicole wash-out is higher than these obtained from PBS (3)The obtained AP activity can be enhanced up to 4x by combination with HuIFN-αN3 but not with rHuIFN-α2.(4)For

the optimal enhancement of Holocene grain wash-out AP activity in vitro different natural subtypes contained in HuIFN-αN3 are needed. 1)Kesteli B., Filipič B., Šooš E. (2007): Ways of use of natural extracts of Holoce- ne minerals and Interferons on the growth of neoplastic cells.(In Croatian) IPO; Republic of Croatia, Patent No.: P20080400A Poster No. Calpain 148 Toxicity Studies of Cancer Drugs in Engineered Cell Environments Maria Håkanson 1 , Mirren Charnley1, MAPK inhibitor Marcus Textor1 1 Laboratory for Surface Science and Technology, Department of Material Science, ETH Zurich, Zurich, Switzerland It is widely acknowledged that cancer progression and behavior is affected by the microenvironment [1]. Furthermore, substantial evidence exists that demonstrates the dependence of the drug response in cancer cells on cues of the surrounding environment, such as dimensionality [2] and ECM composition [3].

Small increments of AsH3 partial pressure MK-4827 nmr by increasing V/III ratio to 35, 37, 40, and 50 result in rapid increases of well-developed QDs. The QD density increases nearly by five orders of magnitude, from 5 × 105 cm−2 (V/III ratio = 30) to 1.2 × 1010 cm−2 (V/III ratio = 50). Also, the base diameters decrease correspondingly from 90 to 46 nm. Phase II. By further increasing the V/III ratio from 50 to 140, the densities

of QDs increase slowly from 1.2 × 1010 cm−2 to 3.8 × 1010 cm−2, and the corresponding base diameters decrease from 46 to 29 nm. Also, we notice that the uniformity of QDs gets worse and the bimodal size distribution of QDs gets more obvious with increasing V/III ratio. Phase III. The density Selleckchem LDN-193189 of QDs decreases significantly by one order of magnitude when the V/III ratio is increased up to 200, and then increases slowly again with higher V/III ratio. During this phase, the average base diameters also undergo abrupt change, increasing to 121 nm and then decreasing to 90 nm. To explain the above complicated behaviors of QDs, several competing mechanisms should be taken into account. Phase I is in the margin of 2D to 3D transition which is reasonable to conclude from the AFM images;

therefore, a minor increase of coverage can facilitate the growth changing from 2D to 3D, thus resulting in significant change of QDs. As the AsH3 partial pressure increases, the rate of the chemical Selleckchem PCI-32765 reaction of TMIn+AsH3→InAs+3CH4 is increased by providing more available AsH3 molecules, leading to the increasing coverage of InAs. As a result, the QD density increases dramatically. A similar behavior of increasing dot density

with increasing coverage can be found in many other reports [9, 15, 16]. Meanwhile, the increased AsH3 partial pressure can limit the migration length of In adatoms; therefore, the base diameter tends to decrease. Accordingly, in phase I, with the increasing of V/III ratio, the QD densities increase dramatically and the corresponding QD average diameters decrease. In phase II, the chemical reaction rate as well as the InAs coverage keeps increasing due to the increasing AsH3 partial pressure, but the increase of the growth rate is limited by the fixed TMIn GBA3 flow rate. Furthermore, phase II is beyond the 2D to 3D transition; therefore, the QD density increases with decreasing rate. Similarly, the average base diameters decrease due to the limited In migration length with increasing AsH3 partial pressure. In addition, considering the kinetics of MOCVD growth, the initial formation of QDs is not in the thermal equilibrium; thus, increasing coverage also leads to the development of small QDs into energetically favorable large-sized QDs. In our case, the bimodal size distribution starts occurring at V/III ratio of 50 and gets more obvious with increasing V/III ratio. In phase III, the QD density decreases significantly at V/III ratio of 200.

Figure 4 LPS induces early histone H3 methylation and acetylation changes at the promoter region of IL-8 gene. Chromatin from HT-29 cells was harvested at the indicated time points after LPS exposure. (A) Schematic representation of IL-8 promoter region, as in Figure 3. Positions of the primers used for ChIP analyses are shown. Presented are the results of ChIP analyses using anti-acetyl-H3 MM-102 mw (B) anti-dimethyl-H3K4 (C), anti-dimethyl-H3K9

(D) and anti-trimethyl-K27 (E) antibodies. DNA sequences recovered after the indicated times of LPS treatment were quantified by real-time PCR using the primers indicated above. Average% input ± S.D from 4 independent experiments are plotted. *, p < 0.01; **, p < 0.05; n.s.= not significant, compared to control cells. Very interestingly, H3K27me3 levels were initially very low but then increased substantially starting at 6 hours and remained high 24 hours after LPS stimulation (Figure 4E). H3K27 trimethylation is catalyzed by Polycomb group (PcG) protein complexes [21, 22], which have been shown to be involved in cytokines genes

reprogramming occurring in both epithelial and macrophage cells in response to bacterial products and inflammation-related stimuli [23, 24]. It is also worth to note that when all the above ChIP assays were performed in unprimed HT-29 cells (not pre-treated with interferon-γ) we did not detect significant changes in histone H3 methylation VX-680 state during the same time course (data not shown) suggesting that the observed chromatin modifications are dependent on the MD2/TLR4 pathway. However, because it

is well known that even “”pure”" LPS preparations may be contaminated with lipoproteins, we cannot Selleckchem SB431542 definitively exclude that the observed chromatin modifications could be influenced by TLR2 signaling. Taken together our data indicate that while changes of H3-acetyl, H3K4me2 and H3K9me2 state in the IL-8 promoter region occur rapidly, transiently and correspond to transcription activation, the changes of H3K27me3 levels MRIP occur at a later time and are long lasting. Finally it should be considered that a strong mark of gene repression, such as H3K27me3, could predispose to a more repressed state of IL-8 gene and, thus, could render the gene less responsive to further LPS stimulation. Moreover, H3K27me3 is also related to DNA hypermethylation that has been shown to occur in intestinal cancer at PcG target genes. In particular, it has been recently demonstrated that hypermethylation of PcG target genes in intestinal cancer is mediated by inflammation [24]. Thus, although our data indicate that DNA methylation is not directly involved in LPS response, such phenomenon may occur later, after prolonged exposure to LPS, as a consequence of PcG proteins recruitment at IL-8 gene.

By exploiting the chemo-enzymatic synthesis

developed by DSM Pharmaceutical Products (Sonke et al., 1999), we prepared enantiomerically pure isovaline and Cα-methylvaline in large amounts. The corresponding racemic α-amino amides, synthesized by partial Strecker synthesis, were enzymatically resolved with appropriate α-amino amidases. Then, homo-peptides (di- and tetra-) from the sterically hindered isovaline and Cα-methylvaline were synthesized step-by-step in solution. The highly effective EDC/HOAt or acyl fluoride C-activation procedures EPZ-6438 in vivo were employed in peptide bond formation. Results of the catalysis experiments showed MAPK inhibitor the all Cα-methylated peptides exhibit significant chiral influence on the synthesis of tetroses

and mimic the effect of the L-Val-L-Val catalyst in having a larger erythrose ee than threose ee, as well as in their configuration relationship with the sugars (the product erythrose acquires ee of configuration opposite to that of the catalyst in case of peptides, while it is the same for amino acids). Interestingly, the largest ee (45% for erythrose) was obtained with the homo-tetrapeptide of isovaline under mild conditions (sodium acetate buffer, pH 5.4, 25°C, 18 h). The homo-dipeptides of both isovaline and Cα-methylvaline also produced a significant ee (41% for erythrose) that appears to increase with time. Because Cα-methylated amino acids are non-racemic in meteorites, do not racemize in aqueous environments, and are known to be (310)-helix (Toniolo and Benedetti, 1991) Flavopiridol (Alvocidib) formers in peptides with as few as four residues (Toniolo et al., 2001),

these results suggest that meteoritic, Cα-methylated, α-amino acids may have contributed to molecular evolution upon delivery to the early Earth by catalytically transferring their asymmetry to other prebiotic molecules. Pizzarello, S., Weber, A. (2004). VS-4718 Meteoritic amino acids as asymmetric catalysts. Science, 303:1151. Sonke, T., Kaptein, B., Boesten, W. H. J., Broxterman, Q. B., Schoemaker, H. E., Kamphuis, J., Formaggio, F., Toniolo, C., Rutjes, F. P. J. T. (1999). In Patel, R. N., editor, Stereoselective Biocatalysis, pages 23–58. Dekker, New York, NY. Toniolo, C., Benedetti, E. (1991) The polypeptide 310-helix. Trends Biochem. Sci., 16:350–353. Toniolo, C., Crisma, M., Formaggio, F., Peggion, C. (2001). Control of peptide conformation by the Thorpe-Ingold effect (Cα-tetrasubstitution). Biopolymers (Pept. Sci.), 60:396–419. Weber, A., Pizzarello, S. (2006). The peptide catalyzed stereospecific synthesis of tetroses: a possible model for prebiotic molecular evolution. Proc. Natl.

Compared with S. aureus RN4220, the transformant carrying pHNLKJC2 had elevated MICs against chloramphenicol (8-fold), florfenicol (16-fold), clindamycin (64-fold), tiamulin (32-fold), valnemulin (32-fold),

and linezolid (4-fold) (Table  1), supporting the presence and the functional activity of cfr. In addition, the transformant carrying pUC18-cfr exhibited 2-fold-elevated MICs for chloramphenicol and florfenicol as compared to E. coli DH5α. Analysis of the genetic environment of cfr in the plasmid pHNTLD18 and pHNLKJC2 JSH-23 molecular weight Southern blotting confirmed that, in Staphylococcus equorum TLD18, cfr was located on a plasmid designed as pHNTLD18. An approximately 5.7-kb EcoRI fragment containing cfr was cloned and sequenced. A Tn558 variant was identified on the plasmid pHNTLD18, in which parts of the Tn558-associated transposase genes tnpA and tnpB were replaced by a cfr-carrying segment and the insertion Selleck ARS-1620 sequence IS21-558 (Figure  1A). Another resistance gene, fexA, encoding an exporter that mediates the active efflux of phenicols, was found to be located downstream of Tn558. Figure 1 Genetic environment of cfr in plasmids pHNTLD18 and pHNLKJC2 and comparison with other similar plasmids. The arrows indicate the positions and directions

of the transcription of the genes. Regions of >98% homology are shaded in grey. Δ indicates a truncated gene. A. genetic environment of cfr in pHNTLD18; B. genetic environment of cfr in pHNLKJC2. The sequences 1,926-bp find more upstream and 2,659-bp downstream of cfr on the plasmid pHNLKJC2 were obtained by primer walking. Basic local alignment search tool (BLAST) analysis of these sequences revealed a 3′-truncated segment of the gene pre/mob upstream of cfr. Further upstream, an incomplete rep gene was detected. Analysis of the region downstream of cfr revealed the presence of a complete pre/mob gene. Immediately downstream of eltoprazine the pre/mob gene, an incomplete macrolide-lincosamide-streptogramin B (MLSB) resistance gene ermC was detected (Figure  1B). Discussion Lack of previous studies on the distribution of the multiresistance gene cfr among staphylococci in retail meat led us to screen 118 meat samples for the same. In our analysis,

cfr was detected in 22 samples. The detection rate was 18.6%, which is higher than the detection rates of food animal samples in China [10, 11]. The low fitness cost of cfr acquisition observed in staphylococcal isolates may account for the persistence of this multiresistance gene in retail meat even in the absence of an antimicrobial selection pressure [12]. The high detection rate found in this study suggested that cfr may be widely disseminated among staphylococci in the meats sold in China, increasing the possibility of this gene entering the food chain. In this study, S. equorum (n = 8) was the predominant species among the 22 cfr-carrying isolates obtained from animal food sources. To the best of our knowledge, this is the first report of cfr in S. equorum. S.

A cluster of six nanoparticles was analyzed with similar results. The use of EELS unveiled bright and dark plasmon modes. The low-energy ones are located on the extremes of the long axis and the high-energy ones on the short axis. The sharper areas of the cluster present higher intensity in the resonance peak. The results presented in this manuscript contribute to the design of plasmonic circuits by metal nanoparticle paths. Authors’ information CDE is a Ph. D. student at the Universidad de Cádiz. WS is a Research

scientist at the Stuttgart Center for Electron Microscopy (StEM), Max Plank Institute for intelligent systems, PAvA is head of the Stuttgart Center for Electron Microscopy

(StEM), Max Planck Institute for intelligent systems. SIM is a full professor at the Departamento de Ciencia de los Materiales e Ingeniería Metalúrgica y Química Inorgánica, NSC23766 Universidad de Cádiz. Acknowledgments This work was supported by the Spanish MINECO (projects TEC20011-29120-C05-03 and CONSOLIDER INGENIO 2010 CSD2009-00013) and the Junta de Andalucía (PAI research group TEP-946 INNANOMAT). We would like to thank Giovanni Scavello for helping us on the layout of the figures. References 1. Maier SA: Plasmonics: Fundamentals and Applications. 1st edition. New York: Springer; 2007. 2. Duan HG, Fernandez-Dominguez AI, Bosman M, Maier SA, Yang JKW: Nanoplasmonics: Masitinib (AB1010) classical down to the nanometer scale. Nano Lett 2012, 12:1683–1689.CrossRef 3. Barrow SJ, Funston selleck chemical AM, Gomez DE, Davis TJ, Mulvaney P: Surface plasmon resonances in strongly coupled gold nanosphere chains from monomer to hexamer. Nano Lett 2011, 11:4180–4187.CrossRef 4. Warner MG, Hutchison JE: Linear assemblies of nanoparticles electrostatically organized on DNA scaffolds. Nat Mater 2003, 2:272–277.CrossRef 5. Woehrle GH, Warner MG, Hutchison JE: Molecular-level

control of feature separation in ARN-509 mouse one-dimensional nanostructure assemblies formed by biomolecular nanolithography. Langmuir 2004, 20:5982–5988.CrossRef 6. de Abajo FJG, Kociak M: Probing the photonic local density of states with electron energy loss spectroscopy. Phys Rev Lett 2008, 100:06804. 7. Nelayah J, Kociak M, Stephan O, de Abajo FJG, Tence M, Henrard L, Taverna D, Pastoriza-Santos I, Liz-Marzan LM, Colliex C: Mapping surface plasmons on a single metallic nanoparticle. Nat Phys 2007, 3:348–353.CrossRef 8. Sigle W, Gu L, Talebi N, Ögüt B, Koch C, Vogelgesang R, van Aken P: EELS and EFTEM of surface plasmons in metallic nanostructures. Microsc Microanal 2011, 17:762–763.CrossRef 9. Guiton BS, Iberi V, Li SZ, Leonard DN, Parish CM, Kotula PG, Varela M, Schatz GC, Pennycook SJ, Camden JP: Correlated optical measurements and plasmon mapping of silver nanorods. Nano Lett 2011, 11:3482–3488.CrossRef 10.