Appl Environ Microbiol 1994,60(2):569–575.PubMedCentralPubMed 11. ten Have R, Hartmans S, Teunissen PJ, Field JA: Purification and characterization of two lignin peroxidase isozymes produced by Bjerkandera sp. strain BOS55. FEBS Lett 1998,422(3):391–394.PubMedCrossRef 12. Mester T, Tien M: Engineering of a

manganese-binding site in lignin peroxidase isozyme H8 from TH-302 cost Phanerochaete chrysosporium . Biochem Biophys Res Commun 2001,284(3):723–728.PubMedCrossRef 13. Timofeevski SL, Nie G, Reading NS, Aust SD: Addition of veratryl alcohol oxidase activity to manganese peroxidase by site-directed mutagenesis. Biochem Biophys Res Commun 1999,256(3):500–504.PubMedCrossRef 14. Camarero S, Sarkar S, Ruiz-Duenas FJ, Martinez MJ, Martinez AT: Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites. J Biol Chem 1999,274(15):10324–10330.PubMedCrossRef 15. Mester T, Field JA: Characterization of a novel manganese peroxidase-lignin peroxidase hybrid isozyme produced by Bjerkandera species strain BOS55 in the absence of manganese. J Biol Chem 1998,273(25):15412–15417.PubMedCrossRef 16. Puhse M, Szweda RT, Ma Y, Jeworrek C, Winter R, Zorn H: Marasmius scorodonius extracellular dimeric peroxidase – exploring its temperature and pressure stability. Biochim Biophys Acta 2009,1794(7):1091–1098.PubMedCrossRef 17. Missall TA, Pusateri

ME, Lodge

JK: Thiol peroxidase is critical for virulence and resistance to nitric oxide Buparlisib concentration and peroxide in the fungal pathogen, Cryptococcus neoformans . Mol Microbiol 2004,51(5):1447–1458.PubMedCrossRef 18. Molina L, Kahmann R: An Ustilago maydis gene involved in H 2 O 2 detoxification is required for virulence. Plant Cell 2007,19(7):2293–2309.PubMedCentralPubMedCrossRef 19. Chi MH, Park SY, clonidine Kim S, Lee YH: A Novel Pathogenicity Gene Is Required in the Rice Blast Fungus to Suppress the Basal Defenses of the Host. PLoS Pathog 2009,5(4):e1000401.PubMedCentralPubMedCrossRef 20. Segmuller N, Kokkelink L, Giesbert S, Odinius D, van Kan J, Tudzynski P: NADPH oxidases are involved in differentiation and pathogenicity in Botrytis cinerea . Mol Plant Microbe Interact 2008,21(6):808–819.PubMedCrossRef 21. Hunter S, Jones P, Mitchell A, Apweiler R, Attwood TK, Bateman A, Bernard T, Binns D, Bork P, Burge S, de Castro E, Coggill P, Corbett M, Das U, Daugherty L, Duquenne L, Finn RD, Fraser M, Gough J, Haft D, Hulo N, Kahn D, Kelly E, Letunic I, Lonsdale D, Lopez R, Madera M, Maslen J, McAnulla C, McDowall J, et al.: InterPro in 2011: new developments in the BAY 1895344 molecular weight family and domain prediction database. Nucleic Acids Res 2012,40(Database issue):D306–312.PubMedCentralPubMedCrossRef 22. Finn RD, Bateman A, Clements J, Coggill P, Eberhardt RY, Eddy SR, Heger A, Hetherington K, Holm L, Mistry J, Sonnhammer EL, Tate J, Punta M: Pfam: the protein families database.

The only exception to this is that phage P2 has a 786 bp ORF (orf30) with unknown function inserted between the S and V genes. There is no such insertion in WΦ and L-413C, but Pseudomonas phage ΦCTX (see below) has another uncharacterized ORF located at this position. Enterobacterial phages 186, PSP3, Fels-2, and SopEΦ also share their learn more overall gene order and many genes with P2, but the genes are more diverged. Unlike P2, these phages are UV-inducible

due to the presence of the tum gene. In addition, they have a different lysis-lysogeny switch region. P2 phages seem to have either of two different proteins for repression of the lytic cycle. P2, WΦ and L-413C have the repressor gene C whereas 186, PSP3, Fels-2, SopEΦ, HP1, HP2, and K139 (below) instead have the sequence-unrelated genes CI and CII, both of which are equally needed for establishing lysogeny. Mannheimia phage Φ-MhaA1-PHL101, Pseudomonas LY2874455 phageΦCTX, and Ralstonia phage RSA1 have many P2 genes and an overall order of structural genes that is P2-like, although interspersed with some uncharacterized genes. Their presumed regulatory gene regions include additional putative and uncharacterized ORFs. Phage ΦCTX has only the P2 regulatory gene ogr (transcriptional activator of

the late genes) and the recombination enzyme int (integrase), Φ-MhaA1-PHL101 has repressor (CI) and antirepressor (Cro) equivalents which are most closely related to the regulatory proteins Vorinostat molecular weight of the P22-like enterobacteria phage ST104 than to P2. Phage RSA1 seems to have only one P2-related regulatory gene, the ogr gene, although it is more related to the Ogr/Delta-like gene in ΦCTX. The RSA1 integrase is more similar to the integrases of the P2-like Burkholderia phages (ΦE202, Φ52237, and ΦE12-2 and P22-like viruses. 2. HP1-like viruses The genome architecture of HP1 [36] and its close relative, HP2, resembles that of P2 although

their cos sites, as with Pseudomonas ΦCTX [37], are located next heptaminol to attP rather than downstream of the portal protein-encoding gene as it is in P2. The P2 gene order is also conserved in Vibrio phages K139 [38] and κ and the Pasteurella phage F108 [39]. As in P2, the genomes can be divided into blocks of structural and regulatory genes. The structural genes are more similar in HP1 and HP2 than the regulatory genes. The six genes coding for capsid proteins are arranged in the same order in HP1 phages and many P2 phages. The other structural genes, coding mainly for tail components, show generally no similarity to those of P2 phages. Only some of the regulatory genes are similar in both HP1 and P2 phages, e.g., int, CI, and repA. Regulatory genes in general are more conserved within the HP1 group. Aeromonas phage ΦO18P [40] is included into the HP1 phages. It contains slightly more genes related to HP1 than to P2, although, when looking at individual proteins, it sometimes appears to have an intermediate position.

The bla content of the isolates analyzed had been determined in a past study [3]. Thirty seven (88%) of the 42 aac(6’)-lb-cr were borne on integrons containing the ISCR1 selleck products while 55% were borne on integrons linked to the IS26. Twenty four (71%) of the 34 isolates carrying a qnrA gene were resistant to nalidixic acid but not to ciprofloxacin while the other 10 isolates carrying this gene and 19 carrying the qnrB subtype were resistant to both antimicrobials,

Table 8. None of the isolates tested positive for qnrS. Majority (87%) of qnr genes were physically linked to either integron-associated ISCR1 or the IS26. All Isolates carrying aac(6’)-lb-cr Captisol solubility dmso or the qnr genes contained multiple genetic elements and were all MDR. Table 8 Carriage of aac(6′)-lb-cr and qnr genes among strains containing genetic elements and bla genes     Number (%) of strains carrying each gene and number (%) of strains containing genes linked to genetic elements Occurrence in strains carryingblagenesa   Total Strains containingintI1 Linked tointI1 Strains containing IS26 Linked to IS26 Strains containing ISCR1 Linked to ISCR1 Strains containing ISEcp1 Linked to ISEcp1 β-lactamase negative strains Strains containing TEM-1 or SHV-1 only Strains containing broad-spectrumblagenes aac(6’)-lb-cr

42 42 (100) 42 (100) 6 (14) 4 (9) 12 (29) 6 (14) 11

(26) 4 (10) 0 4 (9) 38 (91) qnrA 34 27 (79) 26 (75) 11 (32) 4 (12) 28 (82) 23 (68) 8 (24) 1 (3) 0 2 (6) 32 (94) qnrB 19 19 (100) 11 (58) 10 (53) 2 (11) 13 (64) 4 (21) 12 (63) 1 (5) 0 1 (5) 18 (95) Table shows the number of isolates carrying the three (fluoro)quinolone resistance genes and the proportion of such strains in which these genes were physically linked to various genetic elements and to bla genes. a: Distribution of the aac(6’)-lb-cr and qnr genes among strains fully susceptible to β-lactams, among those resistant to TEM-1 or SHV-1 Interleukin-3 receptor with a narrow substrate-range and among those carrying genes selleck kinase inhibitor encoding broad-spectrum β-lactamases such as bla SHV-5, bla SHV-12, bla CMY and bla CTX-Ms . Conjugative plasmids mediate en bloc transfer of multiple elements and resistance genes Multiple resistance genes and genetic elements associated with them were transferred en bloc to E. coli J53 in mating experiments, Table 9 . Majority of such transferred were mediated by plasmids containing I1, L/M, XI, HI2 and the F-type replicons. These experiments further revealed that genes conferring resistance to tetracylines and chloramphenicol were also harbored in the same plasmids encoding resistance to β-lactams, (fluoro)quinolones and aminoglycosides.

Cloning, expression and purification of recombinant GapA-1 The gapA-1 gene from MC58 was cloned into the expression vector pCRT7/NT-TOPO to facilitate the expression and subsequent purification of 6 × histidine-tagged recombinant GapA-1 (Figure 1a). This was used to generate RαGapA-1. Immunoblot analysis confirmed that RαGapA-1 and anti-pentahistidine antibodies both reacted to the purified recombinant GapA-1 (Figure 1b &1c). Figure 1 SDS-PAGE and immunoblot analysis of

recombinant GapA-1. SDS-PAGE analysis confirms the purity of the recombinant GapA-1 purified under denaturing learn more conditions (a). Immunoblot analysis shows that recombinant GapA-1 is recognized by RαGapA-1 (b) and anti-pentahistidine antibodies (c). Construction of an N. meningitidis gapA-1 null mutant strain To examine the roles of GapA-1 in the meningococcus, a gapA-1 knockout derivative of N. meningitidis MC58 was generated. Immunoblotting using RαGapA-1 showed that GapA-1 could be detected in whole cell lysates of wild-type but not MC58ΔgapA-1 (Figure 2, lanes 1 & 2) confirming that GapA-1 was expressed under the conditions used and that expression had been abolished in the mutant. This analysis further confirmed that the Ro 61-8048 research buy RαGapA-1 sera did not recognize GapA-2 (37-kDa) under the conditions used. To further confirm that the immuno-reactive protein was GapA-1, a wild-type copy of

gapA-1 was introduced in trans into MC58ΔgapA-1 using plasmid pSAT-14 (Table 1). Introduction of gapA-1

at an ectopic site restored GapA-1 expression (Figure 2, lane 3). Further immunoblot analyses using Bay 11-7085 a panel of 14 N. meningitidis strains (Additional file 1) including representatives of differing serogroups and MLST-types showed that GapA-1 expression was conserved across all strains (data not shown). Expression was also conserved in N. gonorrhoeae FA1090 (data not shown). These data complement in silico predictions that GapA-1 is universally present and suggests that GapA-1 is constitutively-expressed across pathogenic https://www.selleckchem.com/products/az628.html Neisseria species. Figure 2 Immunoblot analysis of whole cell proteins from N. meningitidis using RαGapA-1. Analysis of MC58 wild-type, ΔgapA-1 mutant derivative and complemented mutant reveals the absence of GapA-1 in the ΔgapA-1 mutant preparation. Similar analysis shows the abolition of GapA-1 expression in the MC58ΔsiaD ΔgapA-1 mutant compared to the parental MC58ΔsiaD strain. Meningococcal GapA-1 is only surface-accessible to antibodies in the absence of capsule Grifantini et al showed using flow cytometry that GapA-1 was accessible to specific antibodies on the surface of meningococci [27]. However, the methodology used involved pre-treatment of the cells with 70% ethanol to permeabilize the capsule, making it unclear whether GapA-1 was accessible to antibodies in encapsulated bacteria.

We did not observe differences in oxidative response in IFN-γ induced MØ infected with wild type and mutant strains. However, the IFN-γ induces iNOS expression initiating the production of NO by MØ prior to their infection with Mtb (data not shown). The high level of NO reached in IFN-γ treated MØ cannot be subsequently lowered even by wild type Mtb

at least within the period of the experiment. Therefore, IFN-γ-activated MØ produced a similar, high amount of NO in response to the infection with wild-type or mutant strains. Phagocytosis of Mtb initiates the production of both TNF-α and IL-10 by MØ. It has been demonstrated by others that TNF-α together with IFN-γ participate in the killing of Mtb through the induction of NO and ROS production. TNF-α is also essential for granuloma check details formation [30–32]. We found here that the infection of resting and INF-γ-activated MØ with wild-type Mtb or ΔkstD mutant caused the release of equal amounts of TNF-α. At the same time however, we observed a greater increase in the production of IL-10 by IFN-γ-activated MØ infected with the ΔkstD strain compared to those infected with the wild-type or complemented strains. It has been reported that SRT2104 pathogenic strains of Mtb stimulate lower levels of TNF-α production by MØ than non-pathogenic

species [32]. IL-10 is an immunosuppressive cytokine that blocks phagosome maturation and antigen presentation and also limits the Th1 response [33]. Thus, our finding that MØ infected with the ΔkstD strain produce higher Methane monooxygenase level of IL-10 than MØ infected with wild-type Mtb and that similar amount of TNF-α is released by MØ after infection with both strains may suggest that certain aspects of the virulence activity of the wild-type strain are in fact not affected in the ΔkstD mutant. Interestingly, we found that blocking the TLR2-mediated signaling pathway

prior to infection restored the phenotype of the ΔkstD mutant in resting MØ to a level similar to that of the wild-type strain. However, neither anti-TLR2 blocking mAb nor IRAK1/4 inhibitor altered the response of MØ to wild-type Mtb. These results suggest that TLR2 signaling is disrupted in MØ infected with wild-type Mtb, but not in MØ infected with the mutant strain. The essential role of the TLR2-mediated pathway in the production of NO and ROS in Mtb-infected MØ is well documented [5, 6, 26, 34]. Further study is needed to elucidate the complete mechanism by which Mtb affects TLR2 signaling whether the ability of Mtb to catabolize AZD2171 supplier cholesterol might be important for this process. It has been demonstrated by others that Mtb is able to modulate macrophage signaling pathways by stimulating phosphorylation of the Bcl-2 family member Bad as well as AKT kinase [35].

Environ Microbiol 2003, 5:1350–1369.PubMedCrossRef 38. Firoved AM, Deretic V: Microarray analysis of global gene expression in mucoid Pseudomonas aeruginosa . J Bacteriol 2003, 185:1071–1081.PubMedCrossRef 39. Rao J, DiGiandomenico A, Unger J, Bao Y, Smad inhibitor Polanowska-Grabowska RK, Goldberg JB: A novel oxidized low-density lipoprotein-binding protein from Pseudomonas aeruginosa . Microbiology 2008, 154:654–665.PubMedCrossRef 40. Winklhofer-Roob BM, Ziouzenkova O, Puhl H, Ellemunter H, Greiner P,

Muller G, van’t Hof MA, Esterbauer H, Shmerling DH: Impaired resistance to oxidation of low density lipoprotein in cystic fibrosis: improvement during vitamin E supplementation. Free Radic Biol Med 1995, 19:725–733.PubMedCrossRef 41. Folders J, Algra J, Roelofs MS, van Loon LC, Tommassen J, Bitter W: Characterization of Pseudomonas aeruginosa chitinase, a gradually secreted protein. J Bacteriol click here 2001, 183:7044–7052.PubMedCrossRef 42. Marquart ME, Caballero AR, Chomnawang M, Thibodeaux BA, Twining SS, O’Callaghan RJ: Identification of a novel secreted protease from Pseudomonas aeruginosa that causes corneal erosions. Invest Ophthalmol Vis Sci 2005, 46:3761–3768.PubMedCrossRef 43. Upritchard HG, Cordwell SJ, Lamont IL: Immunoproteomics to examine cystic fibrosis host interactions with extracellular Pseudomonas aeruginosa proteins. Infect Immun 2008, 76:4624–4632.PubMedCrossRef

44. Rada B, Leto TL: Redox warfare between airway epithelial cells and Pseudomonas : dual oxidase versus pyocyanin. Immunol Res 2009, 43:198–209.PubMedCrossRef 45. Rada B, Lekstrom K, Damian RGFP966 cell line S, Dupuy C, Leto TL: The Pseudomonas toxin pyocyanin inhibits the dual oxidase-based antimicrobial system as it imposes DOK2 oxidative stress on airway epithelial cells. J Immunol 2008, 181:4883–4893.PubMed 46. Price-Whelan A, Dietrich LE, Newman DK: Pyocyanin alters redox homeostasis and carbon flux through central metabolic pathways in Pseudomonas aeruginosa PA14. J Bacteriol 2007, 189:6372–6381.PubMedCrossRef 47. Wilson R, Pitt T, Taylor G, Watson D, MacDermot J, Sykes D, Roberts D, Cole P: Pyocyanin and 1-hydroxyphenazine produced by Pseudomonas

aeruginosa inhibit the beating of human respiratory cilia in vitro. J Clin Invest 1987, 79:221–229.PubMedCrossRef 48. Lauredo IT, Sabater JR, Ahmed A, Botvinnikova Y, Abraham WM: Mechanism of pyocyanin- and 1-hydroxyphenazine-induced lung neutrophilia in sheep airways. J Appl Physiol 1998, 85:2298–2304.PubMed 49. Usher LR, Lawson RA, Geary I, Taylor CJ, Bingle CD, Taylor GW, Whyte MKB: Induction of neutrophil apoptosis by the Pseudomonas aeruginosa exotoxin pyocyanin: a potential mechanism of persistent infection. J Immunol 2002, 168:1861–1868.PubMed 50. Mowat E, Paterson S, Fothergill JL, Wright EA, Ledson MJ, Walshaw MJ, Brockhurst MA, Winstanley C: Pseudomonas aeruginosa population diversity and turnover in cystic fibrosis chronic infections.

Mol Cancer Ther 2006, 5 (5) : 1239–1247.CrossRefPubMed

Competing interests The authors declare that they have no competing interests. Authors’ contributions LX and LW carried out cell treatments and radiosensitivity assay; BS, XW and LL contributed to MTT cell viability assay and flow cytometry analysis. LX, XS and JY supervised experimental work and BVD-523 chemical structure wrote the manuscript. All authors read and approved the final manuscript.”
“Background Integrins are an important class of cell surface receptors that recognize extracellular matrix proteins and allow the cell’s microenvironment to help regulate intracellular signaling events[1, 2]. Binding to multivalent ligands results in integrin crosslinking, which activates a signaling process that induces integrin clustering within the plasma membrane[3, 4]. Clustering of integrins in vitro can also be investigated with crosslinking antibodies, which provide greater specificity than most integrin ligands[5]. In the process of integrin clustering, integrins that are diffusely distributed throughout the membrane dissociate from their cytoskeletal contacts and aggregate in particular regions of the membrane, where they form large complexes with new attachments to the cytoskeleton[6,

7]. In addition to activating the individual integrin heterodimers, the clustering of integrins leads to recruitment of other signaling molecules to the plasma membrane [1–4]. Activated integrins are known to regulate growth Crenigacestat mw factor receptor signaling in normal and malignant cells[8, 9]. Integrin-growth factor receptor crosstalk is important for many growth factor receptor-mediated GSK2879552 supplier functions, including cell proliferation, survival, motility and invasion[8, 9]. The α6β4 integrin, a receptor for most laminins that is normally expressed in the myoepithelial cell layer of benign breast epithelium[10], is upregulated in the aggressive basal subtype of invasive breast cancer[11]. EGFR is also overexpressed in this subgroup of breast cancers[11], and in-vitro data suggest that crosstalk between α6β4 integrin

Beta adrenergic receptor kinase and EGFR may be important in the progression of this basal subtype of breast cancers [12–14]. EGFR converts from an inactive monomeric form to an active homodimer upon stimulation by its ligand[15, 16], and cell surface clusters of activated EGFR homodimers are known to occur [17–19]. We showed previously that α6β4 integrin crosslinking induces PI3K-dependent cell surface clustering of α6β4 integrin in breast carcinoma cells[20]. Because integrin clusters are known to recruit other molecules to membrane complexes, we hypothesized that α6β4 clustering might lead to the redistribution and clustering of EGFR on the tumor cell surface. Moreover, because cell surface clustering of a variety of receptors, including EGFR, has been shown to augment receptor function[5, 17–19], we hypothesized that α6β4 integrin-induced EGFR clustering might augment particular tumor cell responses to EGF.

On examination, he was hypoxic (94% oxygen saturation), hypothermic (35.6°C) and tachycardic with new onset, fast atrial fibrillation (rate 142/minute), but normotensive. In addition, he was diffusely tender in the supra-pubic region and in both loins, especially on the right. Neurological examination was normal other than MRC grade 4/5 power in the lower limbs. Blood tests demonstrated a marked inflammatory response with raised CRP (373 mg/L) C646 in vitro and predominantly neutrophilic

leucocytosis (20.5 × 109/L). Acute kidney injury (urea 31.4 mmol/L; creatinine 244 μmol/L) and mildy deranged liver function tests (alkaline phosphatase 343 IU/L; GGT 183 IU/L; ALT 52 IU/L; bilirubin 14 μmol/L) were evident. Arterial blood gases demonstrated a metabolic acidosis P505-15 clinical trial (pH 7.32; base excess −8 mEq/L). A chest radiograph was normal. Urinalysis was positive for leucocytes and erythrocytes only. Blood cultures were taken and broad spectrum antibiotics were commenced for presumed urosepsis. 24 hours after admission, the right hand became diffusely swollen, erythematous and tender, and the patient continued to experience pyrexia. His urine cultures yielded Serratia marcescens sensitive to the antibiotics. Ultrasonography of the urinary tract failed to demonstrate hydronephrosis. Ultrasonography of the right

hand showed generalised soft tissue oedema with a 1 cm deep fluid filled collection containing echogenic material overlying the MCP joints.The following day, the acute kidney injury worsened (urea 43.4 mmol/L; creatinine 351 μmol/L). An urgent CT thorax/abdomen/pelvis demonstrated an unexpected finding of bilateral iliopsoas NVP-BSK805 cost abscesses, most extensive on the right side which contained a considerable volume

of gas (Figures 1 and 2). Figure 1 Transverse view on CT of the bilateral iliopsoas abscesses. Figure 2 CT demonstrated Sagittal View of Abdomen and Pelvis demonstrating gas locules in Right Iliopsoas Region. The patient proceeded to theatre for drainage of the abscesses. During intubation the anaesthetist noted the oropharynx was sloughy and inflamed and accordingly biopsies were taken. Bilateral groin incisions were used to approach the iliopsoas muscles in the extra-peritoneal MYO10 plane. On the right side the abscess cavity involved the entire length of the iliopsoas muscle and contained 100 ml of cream coloured pus as well as gas. On the left side an estimated 40 ml of pus was contained within the lower psoas muscle. There was no evidence of communication with the replaced hip joints on either side. Drains were placed into the cavities. The hand abscess was also drained and samples from all sites were sent to microbiology. The patient was then transferred post-operatively to ICU for inotropic support (noradrenaline) and ongoing fluid resuscitation. 72 hours after admission the blood cultures returned a yield of F. necrophorum and subsequently tazocin and metronidazole were commenced.

The indium droplet deposition was calibrated in terms of growth rate, deposition thickness and growth temperature by growing a series of samples at various temperatures of 145°C to 310°C using In-flux in the range of 2.2 to 6.0 × 10−7 mbar. Results and discussion Figure 1a is the atomic force microscope (AFM) image of optimal sample showing that the droplets have an average diameter of approximately 70 nm, height of approximately 20 nm and density of approximately 6 × 108 cm−2. We found that 3 ML indium deposition selleck grown at 220° with a growth rate of 0.01 ML/s gives uniform droplets suitable for NWs’ growth. Figure 1b shows the 45°-tilted SEM image of InAs NWs grown on HOPG for 20 min. All

the NWs are vertically aligned on the surface without tapering, i.e. highly uniform diameter along the entire length. The NWs also have a homogeneous diameter distribution with a hexagonal cross-section, and no metal droplets are present on the top of the NWs. The ACY-1215 ic50 average diameter, length and number density of the NWs are 78 ± 5 nm, 0.82 ± 0.28 μm and approximately 4 × 108 cm−2 respectively. The SEM image also shows that parasitic InAs islands were formed on the surface during growth.

Based on an estimate from large-area SEM images, the InAs islands cover 38% of the surface. As the areal coverage of NWs is approximately 2%, almost 60% of the surface remains bare. As growths on graphite without indium droplets led to NWs with a density one order of magnitude lower than that with droplets, we assume that droplets activate the growth of NWs. Figure 1 AFM image of pre-calibrated In droplets and SEM image of grown InAs NWs. A 1 × 1 μm AFM image of pre-calibrated indium droplets grown at optimal conditions (a) and 45°-tilted SEM image of InAs NWs grown for 20 min on (b) graphite and Si (111) (c). The scale bar is 400 nm. The vertical alignment of the NWs is due to the low surface Mannose-binding protein-associated serine protease energy along the (111) orientation. The morphological

parameters of the resulting NWs are similar to those of GaAs NWs on graphite by MBE [6]. However, in comparison with MOCVD grown InAs NWs on graphite (diameter of approximately 42 nm [2] and 30 nm [4] with a density of 6 to 7 × 108 cm−2), our MBE-grown InAs NWs are doubled in diameter with half the density. This is probably because of the non-requirement of activation and dissociation at the surface during the growth in MBE leading to longer surface diffusion of the adatoms, resulting in larger diameter and lower density [26]. In addition, the VE-822 solubility dmso absence of surface dangling bonds on the graphite surface gives rise to van der Waals epitaxy which is proposed to be different from general Frank-van der Merwe growth mode in MBE (layer-by-layer growth). In order to understand this effect, a few samples of InAs NWs were grown on Si (111) under identical growth conditions. These led to repeatable NWs as shown in SEM image (Figure 1c) for typical resulting NWs.

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