Importantly, even though we examined

colonization patterns by only a limited number of bacterial species, we found that the variable subgingival bacterial load by several -but clearly not all- species correlated significantly with tissue gene expression. In other words, and to paraphrase both Anton van Leeuwenhoek and George Orwell, our data indicate that all subgingival “”animalcules”" are not “”equal”" in this respect. In a recent publication [10], we presented transcriptomic data from a subset of patients involved in the present report (90 patients and 247 arrays out learn more of the total of 120 patients and 310 arrays included here) and compared

gene expression profiles of clinically healthy and diseased gingival tissues in patients with periodontitis. We documented substantial differential gene expression between states of gingival health and disease that was reflected both by genes that were a priori anticipated to be variably expressed based on current knowledge (e.g., several inflammatory, immune function- and apoptosis-related genes), but also by genes that are not readily associated with gingival inflammation (e.g., the transcription factor POU2AF1, the sperm associated antigen 4 which appears to be associated with apoptosis (own unpublished data), the cell adhesion-mediating Adriamycin solubility dmso protein desmocollin 1, and the signaling lymphocytic

activation molecule family member 7). In the present study, we sought to investigate whether the bacterial content of the selleck chemicals periodontal pocket is also a determinant of gene expression in the adjacent gingival tissues in order to enhance our understanding of the host-bacterial interactions that take place in the interface between the plaque biofilm and the periodontal pocket. We realize that the above question can ideally be addressed in a longitudinal prospective rather than a cross-sectional study. Thus, although our analyses considered bacterial colonization as the independent exposure and tissue gene expression as the outcome, it is impossible to rule out reverse causation, i.e., that the qualitative characteristics of the gingival tissue are the determinants of bacterial colonization. However, given that periodontitis is a bacterially-induced infection, the former approach is reasonable in the discussion of the observed correlations between colonization patterns and tissue gene expression signatures. We also want to draw the reader’s attention to the fact that, despite our inferences on each particular bacterial species’ effect on the gingival tissue transcriptome, we have not studied individual mono-infections.

To identify the level at which IpaB and InvE expression was regulated in response to changes in osmolarity, we analyzed the expression of virF. In the absence of salt, virF mRNA was detectable by RT-PCR (Fig. 1B, virF mRNA), although the level of mRNA expression was approximately 29.0 ± 4.6% of the maximum level observed in the presence of 150 mM NaCl. In an attempt to determine BIBW2992 solubility dmso the mechanism of regulation of virF transcription, we performed a reporter gene assay in which the expression of lacZ

was driven by the virF promoter [8]. In wild-type S. sonnei carrying the virF-lacZ reporter gene, the level of β-galactosidase activity in the absence of salt was 20.6% of that in the presence of 150 mM NaCl (Fig. 1C, Graph 1), which indicated that the virF promoter is partially active even in the absence of NaCl. We examined VirF-dependent expression of invE by Western blot and RT-PCR. The production of InvE protein was almost completely repressed under conditions of low osmolarity (Fig. 1B, α-InvE),

whereas under the same conditions, there was a significant level of invE mRNA detectable by RT-PCR (Fig. 1B, invE mRNA). Real-time RT-PCR analysis indicated that the amount of invE mRNA in the absence of NaCl was 9.5 ± 1.6% of the level in the presence of 150 mM NaCl. We carried out a reporter gene assay to examine the expression of invE at both the transcriptional and translational levels [13]. In low osmolarity, β-galactosidase activity Anacetrapib in wild-type S. sonnei that expressed the transcriptional fusion gene invETx-lacZ was moderately decreased, to 28.9% of that seen in the presence of 150 Rabusertib research buy mM NaCl (Fig. 1C, Graph 2). In contrast, β-galactosidase activity in cells that expressed the translational fusion gene invETL-lacZ was 7.3% of the level in the presence of 150 mM NaCl (Fig. 1C, Graph 3). These results indicated

that the expression of InvE protein is repressed in the absence of salt, a condition under which genes for at least two regulatory proteins are still transcribed, albeit at reduced levels. Thus, the repression of InvE synthesis occurs primarily at the post-transcriptional level. Post-transcriptional regulation of invE To examine the mechanism of post-transcriptional regulation of invE expression more directly, we replaced the native invE promoter with a promoter cassette containing the E. coli araC repressor and the araBAD promoter region [14]. In this system, we were able to examine VirF-independent expression of InvE under the control of the AraC-dependent araBAD promoter. Strain MS5512 carrying ΔpinvE::paraBAD [11] was cultured in the presence or absence of 150 mM NaCl, and the synthesis of InvE protein was induced by increasing the concentration of arabinose. Similar levels of invE mRNA were detected in the presence of 0.2 and 1.0 mM arabinose, independently of the presence or absence of NaCl (Fig. 2A, invE mRNA). However, the synthesis of InvE protein was significantly decreased in the absence of NaCl (Fig.

vaccinii CBS 135436 = DF5032 Vaccinium corymbosum Ericaceae USA D.F. Farr JQ807303 KJ380964 KC849457 JQ807380 KJ381032 KJ420877 AF317570 KC843225 FAU633 Vaccinium macrocarpon Ericaceae USA F.A. Uecker JQ807338 KJ380966 KC849456 JQ807413 KJ381034 KJ420878 U11360,U11414 KC843226 FAU446 Vaccinium macrocarpon Ericaceae USA F. Caruso JQ807322 KJ380967 KC849455 JQ807398 KJ381035 KJ420882 U11317,U11367 KC843224 CBS 160.32 Vaccinium macrocarpon Ericaceae USA C.L. Shear JQ807297 KJ380968 KC343470 GQ250326 KJ381036 KC343712 AF317578 JX270436 FAU 468 Vaccinium macrocarpon Ericaceae USA F.A. Uecker JQ807323 KJ380965 KC849458 JQ807399 KJ381033 KJ420876

U113327,U11377 KC843227 *AR, DAN, DNP, FAU, DLR, DF, DP, LCM, M: isolates in SMML culture collection, USDA-ARS, Beltsville, MD, USA; CBS: CBS-KNAW Fungal Biodiversity Centre, Utrecht, The Netherlands; GSK1120212 in vivo Di-C005/1-10: obtained from Santos et al. 2010; MAFF: NIAS Genebank Project, Ministry of Agriculture, Forestry and Fisheries, Japan DNA extraction, PCR and sequencing DNA was extracted and the ITS, EF1-α, CAL, TUB and ACT genes were amplified

following the protocols outlined by Udayanga et al. (2014). The FG1093 (60s ribosomal protein L37) was amplified using the universal primers for Ascomycota, E1F1 and E3R1 (Walker et al. 2012) following the touch-down PCR protocol outlined by the same study. HIS (Histone-3) genes were amplified as described in Gomes et al. (2013) using the primer pair CYLH3F (Crous et al. 2004b) and H3-1b (Glass and Donaldson 1995). Apn2 primers for Diaporthe were designed and the conditions were optimised as described in this study learn more and amplified under conditions of 95 C° for 1 min, (95 °C : 30 s, 54 °C:50 s,72 °C:1 min) × 39 cycles, 72 °C for 10 min extension in PCR mixtures used for the other genes in Udayanga et al. (2014). PCR products were visualised in 1 % agarose gel electrophoresis

(Udayanga et al. 2014) and then purified with ExoSAP-IT (USB Corp., Cleveland, Ohio) according to the manufacturer’s instructions and sequenced with the BigDye Terminator 3.1 cycle sequencing kit (Applied Biosystems, Foster City, California) Florfenicol on an Applied Biosystems 3130xl Genetic Analyser using the same amplification primers for each of the gene regions. Apn2 (DNA lyase) primer design and assessment of utility within Diaporthe An alignment of the complete sequences of Apn2-Mat genes of Diaporthe W and G types in Kanematsu et al. (2007) (AB199324-27) with a selected set of homologous Apn2 genes available in GenBank including Colletotrichum caudatum (JX076930-32), C. cereale (EU365102, 365045, 365117), C. fragariae (FR719119), C. fructicola (FR719124), C. gloeosporioides (FR719121-22, FR719126), C. siamense (FR719125), and Thielavia terrestris chromosome A (XM003651303), Myceliophthora thermophila Chromosome 1 (CP003002), and the mating type A locus from Neurospora terricola (HE600070), N. pannonica (HE600067) and N.

05 (1.00 to 4.18) 0.04 Osteoarthritisa contralateral (n, %) 61/349 (18%) 8/110 (7%) 2.40 (1.19 to 4.87) 0.01 MJS contralateral (mean, SD) 3.55 (0.95) 3.74 (0.87) −0.20 (−0.39 to 0.00) 0.06 aOsteoarthritis is defined as either an MJS ≤2.5 mm or a K&L grade II EPZ015666 clinical trial or higher or previous surgery for osteoarthritis (total hip replacement) Table 2 Osteoarthritis measured by MJS and/or K&L in the case group comparing femoral neck fractures and trochanteric fractures   Cases, femoral neck fractures Cases, trochanteric fractures

Mean difference or RR with 95% confidence interval p MJS ≤2.5 mm ipsilateral (n, %) 8/96 (8%) 23/154 (15%) 0.56 (0.26 to 1.19) 0.12 K&L grade II or higher ipsilateral (n, %) 10/96 (10%) 30/154 (20%) 0.54 (0.27 to 1.04) 0.06 Osteoarthritisa ipsilateral (n, %) 14/96 (15%) 34/154 (22%) 0.66 (0.37 to 1.17) 0.14 MJS ipsilateral (mean, SD) 3.72 (0.90) 3.42 (1.03) 0.30 (0.05 to 0.55) 0.02 MJS ≤2.5 contralateral, mm (n,%) 15/177 (9%) 27/172 (16%) 0.54 (0.30 to 0.98) 0.04 K&L grade II or higher contralateral (n, %) 25/177 (14%) 27/172 (16%) 0.90 (0.55 to 1.49) 0.68 Osteoarthritisa

contralateral (n, %) 26/177 (15%) 35/172 (20%) 0.72 (0.46 to 1.15) 0.16 MJS contralateral (mean, SD) 3.62 (0.97) 3.47 (0.91) 0.14 (−0.06 to 0.34) 0.16 aOsteoarthritis is defined as either an MJS ≤2.5 mm or a K&L grade II or higher or previous surgery for osteoarthritis (total hip replacement) When comparing OA as defined by MJS and K&L, the Pearson correlation coefficient was r = 0.67 (p < 0.01) on the injured selleckchem side and r = 0.72 (p < 0.001) on Vildagliptin the non-injured side. The Pearson correlation coefficient of the overall OA between the injured and non-injured side was 0.24 (p < 0.001). Six patients in the fracture group, all with trochanteric fractures, and five patients in the contusion group,

had bilateral osteoarthritis. Three patients in the contusion group had osteoarthritis only on the non-injured side. Discussion In this study, we did not find a difference in the prevalence of OA on the injured side in patients with hip fractures compared to patients with hip contusion. Hence, we found no support for the theory that OA may protect against a hip fracture. The relative risk was close to 1 with narrow confidence intervals for all comparisons, and the difference in mean MJS was very close to 0 (Table 1). The relationship between OA and osteoporotic proximal femoral fractures is of special relevance to the ageing population because both conditions are common and both increase with age. It is of particular interest to investigate OA in the hip because it is often the only affected joint, suggesting that local biomechanical risk factors are important [21]. In this model, the fracture group represent patients with osteoporotic fractures and the contusion group represents patients with less osteoporosis, as their hip did tolerate a fall without fracturing.

One of the genes up-regulated at late-log growth phase was the locus BMEI0402. Veliparib cell line The product of this gene has not yet been characterized in B. melitensis;

however, it has high homology (63% sequence identity) to an immunogenic outer membrane protein, Omp31 (BMEII0844) [37]. Omp31 is a haemin-binding protein [38], which binds to, and extracts iron from, the host. Iron has been identified as a required element for epithelial invasion in microbial pathogens [39–41], and the expression of this locus, along with other iron-related genes in late-log phase cultures (BMEI0176–0177, BMEII0536, BMEII0567, BMEII0583, BMEII0704, BMEII0883, BMEII1120, BMEII1122), may influence the internalization ability of brucellae. SP41 is another surface-exposed outer membrane protein with a critical role in Brucella suis adherence to, and invasion of, non-phagocytic cells [13]. The role of this protein, which is encoded by the ugpB gene (BMEII0625) present in the chromosome

II of B. melitensis 16 M genome, was not previously described for B. melitensis adhesion to and/or penetration of epithelial cells. The transcript from the ugpB gene was not identified as differentially expressed in our cDNA microarray analysis between the most and the least invasive cultures. Therefore, under our experimental Ro 61-8048 cost conditions, this OMP seems not to be involved in the higher invasiveness of the late-log phase cultures. It is possible that the composition of the cell culture medium does not induce the expression of ugpB, or it is also possible that ugpB is constitutively expressed and/or act in concert with other factors. Although genetic analysis reveals that ugpB may belong to an operon (BMEII0621 to II0625) that encodes for a sn-glycerol-3-phosphate ABC transporter [42], the experimental evidence does not support this hypothesis. A previous study showed that

the product of ugpB in B. suis is indeed a surface-exposed protein with adhesion and invasion activity [13]. In fact, in this study, three of the transcripts predicted to encode the transport system [ugpC (BMEII00621) (ATP-binding thiprotein), ugpE (BMEII0622) and ugpA (BMEII0624) (permease proteins)] were highly up-regulated (> 50 fold) in late-log phase cultures, when compared to stationary Bay 11-7085 phase cultures. In concordance with previous experimental evidence, our microarray data would support the finding of others that ugpB does not belong to an operon that encodes for a sn-glycerol-3-phosphate ABC transporter. In addition, our results support growth-phase regulation of the sn-glycerol-3-phosphate ABC transport system, which has been implicated in Brucella pathogenesis [24, 43]. The ability of Brucella to invade host cells is linked to its OM properties. B. melitensis OMP profile changes during culture growth [44], as gene expression is transcriptional regulated by environmental conditions [12, 45].

“
“Introduction The glutamatergic system is an attractive molecular target for pharmacological intervention (Kaczor and Matosiuk, 2010). Ligands acting on ionotropic glutamate receptors (iGluRs: NMDA, AMPA, and kainate receptors) or

metabotropic glutamate receptors (mGluRs) are potential drug candidates for the treatment of neurodegenerative diseases (Alzheimer’s disease, Parkinson’s disease, Huntington’s disease), epilepsy, as well as schizophrenia, anxiety, and memory disorders (Kew and Kemp, 2005). Although only a few glutamate receptor ligands have turned out to be clinically useful (firstly, because of the crucial role of the glutamatergic system in many physiological processes, and secondly, due to the unfavorable psychotropic side effects, traditionally linked with high-affinity NMDA receptor antagonists), ligands of kainate receptors seem to be especially promising. Kainate receptors are involved www.selleckchem.com/products/Trichostatin-A.html in epileptogenesis and inducing synaptic plasticity, mainly via the mossy fiber long-term potentiation mechanism. Thus, antagonists of kainate receptors are potential anti-seizure and neuroprotective agents. Moreover, non-competitive antagonists of AMPA receptors are well tolerated in preclinical and clinical studies (Szénási et al., 2008),

thus it may be expected that this will also be the case for such ligands of kainate Selonsertib concentration receptors. Research on non-competitive antagonists Interleukin-2 receptor of kainate receptors is hindered by the fact that only three series of such compounds have been obtained up to now (Kaczor et al., 2012; Valgeirsson et al., 2003, 2004). Recently, we have reported 1,2,3,5-tetrasubstituted

indole derivatives which are among the most active non-competitive antagonists of the GluK1 receptor and are the first known such ligands of the GluK2 receptor, Fig. 1 (Kaczor et al., 2012). We have also suggested a binding site for them in the receptor transduction domain (Kaczor et al., 2014) which was enabled by the construction of whole receptor models (Kaczor et al., 2008, 2009, 2014). Here we present further modifications, 2–7, of the lead compound E099-25011, (1-ethyl-5-methoxy-2-(4-methoxyphenyl)-3-methylindole), 1. The lead compound was identified by searching the internal databases of compounds at the Elbion Institute, Radebul, Germany. 1 is an analog of Zindoxifene, an anti-estrogen, tumor-inhibiting compound (Schneider et al., 1991). We have previously optimized compound 1 by changing substituents in positions 1, 2, 3, and 5 of the indole system (Fig. 1) (Kaczor et al., 2012, 2014). Compounds 3 and 5–7 were tested for their affinity to the GluK2 receptor, and compounds 3 and 5 were found to be non-competitive antagonists at this receptor. Furthermore, we show how novel non-competitive antagonists 3 and 5 of the GluK2 receptor interact with the transduction domain of the previously constructed homology model of this receptor (Kaczor et al., 2014). Fig.

The antibiotics were serially diluted in 1 mL of M79 medium at concentrations from 256 μg/mL to 0.5 μg/mL. An overnight culture of A. amazonense was diluted to 4 × 104 cells/mL. One milliliter of this dilution was added to one milliliter of M79 medium containing the appropriate antibiotic concentration. The cells were cultivated in a rotary shaker at 150 rpm for 40 h at 35°C. Conjugation Conjugation was basically carried out as described by Clerico et al. (2007) [42]. However, some modifications were made as follows: overnight cultures of A. amazonense Y2 (receptor), E. coli XL1-Blue containing the plasmid pRK2013 (helper), and E. coli XL1-Blue containing the appropriate plasmid (donor) were used.

Approximately 1 mL of the A. amazonense culture with an OD600 = 2 (1.3 × 109 cfu/ml) was mixed with 1 mL of each helper and donor cultures with an OD600 = 0.2 (2 × 108 cfu/mL) LCZ696 in vivo (ratio 10:1:1), unless stated otherwise. This mixture was harvested by centrifugation at 6000 g for 2 min and then resuspended in 100 μL of MLB medium (LB and M79 mixture at a proportion of 8:2), and this volume was then spotted onto MLB agar and incubated for 20 h at 35°C. Following this, the cell mass

was resuspended in 200 μL of M79 medium and plated on M79 medium containing the appropriate antibiotic. Electroporation The preparation of cells was based on the protocol described by Schultheiss and Schüler (2003) [27]. A 3 mL GDC-0941 in vitro overnight culture of A. amazonense was inoculated in 250 mL of M79 and the cells were cultivated to an OD600 of ~0.12 (early-log growth phase), unless stated otherwise. From this point, all manipulations were conducted on ice. The cells were incubated in ice for 30 min and then harvested by Branched chain aminotransferase centrifugation at 5000 g for 20 min at 10°C. The cells were resuspended in 100 mL of electroporation buffer (pH 6.5 HEPES 1 mM, MgCl2 1 mM, and sucrose 200 mM) and again harvested by centrifugation (20 min at 5000 g). Subsequently, the cells were resuspended in 40 mL of electroporation buffer and again harvested by centrifugation. At the end, the cells were resuspended

in 250 μL of electroporation buffer (final concentration of ~1010 cfu/mL), distributed in aliquots of 40 μL, and frozen in liquid nitrogen. Cell electroporation was carried out as follows: the 40 μL aliquot was mixed with 50 ng of the pHRGFPGUS vector and electroporated through a Gene Pulser apparatus (Bio-Rad Laboratories Inc.) with 12.5 kV/cm, 25 μF and 200 Ω, unless stated otherwise. After electrical discharge, the cells were resuspended in 500 μL of M79 medium and incubated at 35°C for 3 h in a rotary shaker at 150 rpm. Subsequently, the cells were plated on solid M79 medium containing 20 μg/mL of kanamycin and incubated for 2 days at 35°C. Gene mutagenesis Site-directed mutagenesis was based on a protocol described by Eggeling and Reyes (2005) [43].

However, nothing is known about metabolites of the tryptophan catabolism on DC function. CD14+ cells were isolated from periperal blood and activated to fully mature DC in vitro. In parallel cultures, DCs were generated in the presence of different concentrations of kynurenine and quinolinic acid. These mature DC were used to analyse expression of differentiation markers by FACS, to stimmulate naïve T-cells to proliferation, and to induce Th-1 T-cell LY3039478 price response. Kynurenine, but not quinolinic acid, had a dramatic effect on the expression of the DC maturation marker CD83, suggesting that kynurenine has an impact on DC maturation.

The expression of MHC-class I molecules, the co-stimulatory receptors CD80/CD86 and CCR7 on DC was not affected by kynurenine or quinolinic acid. In further analysis we found that kynurenine treated DC dramatically decrease the ability of T-cells to produce INF-gamma a key cytokine indicating a Th-1 immune response. Subsequently T-cell subpopulations were analysed and found that the portion of CD4+CD25+ T-cells was significantly increased in the T-cell population generated by kynurenine treated DC, which indicate an increase in a suppressor Thiazovivin cell line T-cell population. In summary, these data suggest that kynurenine “primed” mDC induce generation of suppressor T-cells. Based on the data

presented above we hypothesize that metabolites of the kynurenine pathway are important determinants in turning the immune system especially DC to a tolerogenic phenotype. Poster No. 54 Impact of Hypoxia on Furin Trafficking and the Formation of Invadopodia Dominique Arsenault 1 , Sébastien GrandMont1, Martine Charbonneau1, Kelly Harper1, Claire M. Dubois1 1 Department of Pediatric, Immunology Division, Université de Sherbrooke, Sherbrooke,

QC, Canada Recent studies indicate that tumoral invasion and metastasis, triggered by the hypoxic microenvironment, involves strategic relocalization of convertases, adhesion molecules, and metalloproteases. We used the highly invasive human Reverse transcriptase fibrosarcoma cells HT-1080, stably transfected with eGFP-tagged-furin in order to study the impact of hypoxia on the cellular localization of the convertase furin. Our results indicate that in hypoxic cells, furin is relocalized at the plasma membrane and is internalized via both clathrin- and caveolin/raft dependent endocytosis. Using furin trafficking mutants, we demonstrate that filamin-A, a cytoskeletal tethering protein, is essential for the membrane localization of furin under hypoxia. We further demonstrate that in hypoxic cells, furin and its substrate MT1-MMP relocalize to specific pericellular compartments and this relocalisation is associated with an increased cell ability to convert pro-MT1-MMP into its active form.

A crosslinked SAM of 5,5′-bis (mercaptomethyl)-2,2′-bipyridine-Ni2+ (BPD-Ni2+) has been prepared on top of the pre-patterned Au bottom contacts. Then the top Au contacts were evaporated. A two-electrode probe station

was used to assess the fidelity of the molecular junctions. Additionally, to elucidate the molecular transport in the device junctions, temperature-dependent I-V examinations were performed. Methods Fabrication of the crossbar molecular devices Fabrication of the bottom electrode Lithography of bottom electrodes was accomplished by starting with a clean single-side polished SiO2 substrate. Photoresist TPCA-1 mw PMMA 950 was spin-coated on SiO2 at 2,000 rpm for 90 s and baked at 180°C for 3 min (Figure 1a). Then, to avoid the charge-up of PMMA, 15 nm of conductive polymer (ESPACER 300Z; Showa Denko K.K., Minato, Tokyo, Japan) was spin-coating on the top of the PMMA at 2,000 rpm for 60 s. RO4929097 The

100-nm bar patterns were fabricated using an electron beam lithography system (50 kV, 100 mC/cm2; Elionix Co. Ltd., Hachioji, Tokyo, Japan). The resist was developed in MIBK methyl isobutyl ketone + IPA isopropanol 1:3 solution (MIBK-IPA) for 30 to 40 s to remove the irradiated zones and to form a pattern for the bottom electrode bars (Figure 1b). Finally, using electron-beam deposition, 10 nm of titanium and 150 nm of gold were deposited on the photoresist-patterned wafer. The wafer was immersed in acetone to remove the photoresist and the excess metal which adhered on the resist (Figure 1c). Figure 1 Scheme process flow for fabrication of crossbar molecular devices. (a) Photoresist patterning for bottom contacts on SiO2. (b) The 100-nm bar patterns were created

using electron beam lithography. (c) Deposition of 10 nm of Ti and 150-nm Au over patterned substrate and lift-off excess Au with photoresist removal. (d) Deposition of SAM over the entire substrate. (e) Preparation and deposition of top electrodes. Preparation of the crosslinked BPD-Ni2+ SAM The SAM of BPD films was fabricated in the following manner: 5,5′-bis(mercaptomethyl)-2,2′-bipyridine was purchased from Aldrich and used as received. The SAM of 5,5′-bismercaptomethyl-2,2′-bipyridine (BPD) was prepared by Carnitine palmitoyltransferase II immersing the bottom electrodes in freshly prepared 1-mM solution of n-hexane for 1 h at 60°C. Solutions were well-degassed using Ar. All preparation steps were performed in the absence of ambient light, which is the same as the process in our previous studies [4, 6]. Subsequently, the bottom gold bar was modified with a layer of BPD and immersed for 3 h in a 50-mM aqueous solution of NiCl2 (see Figure 2a,b). Figure 2 Preparation of the cross-linked BPD-Ni 2+ SAM. (a) Preparation of the BPD SAM. (b) Encapsulation of Ni on the BPD SAM. (c) A BPD-Ni system was employed as a negative resist for e-beam lithography. Microscope image of etched BPD-Ni/Au template, preliminary patterned by electrons in proximity printing geometry using a metal mesh as mask.

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