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Fluoroquinolone resistance selection decreased the toxicity of 13124R and increased the toxicity of NCTRR. Conclusions Our study demonstrates that gatifloxacin resistance selection in C. perfringens was EPZ004777 solubility dmso associated with upregulation or downregulation of different genes involved in various aspects of metabolism and that the effect was strain-specific. The genes involved in transcription regulation, virulence and cell toxicity were among those that were upregulated in one resistant strain and downregulated in another. Hiscox et al. [47] surmised that “the regulation of virulence in C. perfringens

was a complex process” and we found that the nature of each strain adds yet another level of complexity to gene regulation in C. perfringens. Myer et al. [52] found Serine/threonin kinase inhibitor widely Momelotinib manufacturer variable large genomic islands in a large collection of C. perfringens strains and stated that considerable variation exists among the genomes of C. perfringens strains. It appears that this variation in gene structure of different C. perfringens strains also affects gene regulation and interaction of bacteria with fluoroquinolones. Fluoroquinolones have been implied to have a role in the development of C. difficile associated diarrhea [53]. Since virulent, drug-resistant clinical isolates of pathogenic

bacteria have an undefined genetic basis for their resistance and virulence, we used two wild types and otherwise isogenic resistant mutants, which are difficult to obtain in a clinical setting, to assess fluoroquinolone effects. Our results reflect clinical observations of

finding fluoroquinolone-resistant strains of bacteria that are more or less virulent than the susceptible strains. They underscore the role of fluoroquinolones in changing bacterial virulence and the importance of prudent use of fluoroquinolones. Further study is needed on the effect of fluoroquinolones on a larger number of C. perfringens strains, along with genomic analysis of the resistant mutants. Acknowledgments We thank Drs. Mark Hart and John B. Sutherland for their helpful comments on the manuscript, Dr. Carl E. Cerniglia for support of research and Drs. Donald Schwartz and Jean-Marie Rouillard for DNA microarray experiments. S.P. was supported by the FDA Commissioner’s Fellowship Program. The views presented in this article Amylase do not necessarily reflect those of the US Food and Drug Administration. Electronic supplementary material Additional file 1: Primers used for qRT-PCR. (PDF 23 KB) Additional file 2: Analysis of mRNA quality and expression. (PDF 81 KB) Additional file 3: Cytotoxicities of C. perfringens supernatants for macrophages. (PDF 31 KB) Additional file 4: Morphological examination of C. perfringens strains. (PDF 63 KB) References 1. Scallan E, Hoekstra RM, Angulo FJ, Tauxe RV, Widdowson MA, Roy SL: et al: Foodborne illness acquired in the United States—major pathogen s. Emerg Infect Dis 2011, 17:7–15.PubMed 2.

testosteroni S44 was cultured in LB broth with 1 mM Se(IV) at 26°C with shaking at 180 rpm, harvested at both log phase and stationary phase. Samples that were grown without Se(IV) were find more used as controls. Cultured samples were fixed using 2% v/v glutaraldehyde in 0.05 M sodium phosphate buffer (pH 7.2) for 24 h and were then rinsed three times in 0.15 M sodium cacodylate buffer (pH 7.2) for 2 h. The specimens were dehydrated in graded series of ethanol (70%, 96% and 100%) transferred to propylene oxide and embedded in Epon according to standard procedures. Sections, approximately 80 nm thick, were cut with a Reichert-Jung Ultracut E microtome and collected

on copper grids with Formvar supporting membranes. The sections were stained or unstained with uranyl acetate and lead citrate and then TEM-STEM-EDX (TITAN 120 kV) and EDS Mapping (QUANTA 200 F) were performed, respectively. Tungstate test on Se(IV) and Se(VI) reduction C. testosteroni S44 cells were incubated in CDM (chemically defined medium) [50], LB and TSB plates supplemented with 0.2 mM sodium

selenite, 5.0 mM sodium selenate, respectively, and with or without 10 mM tungstate (Na2O4W.2H2O) at 26°C under aerobic condition for two days. The inhibiting effect of tungstate was shown by appearance or absence of the specific red color of SeNPs in comparison with control in absence of tungstate. Cellular fractionations and determination of Se(IV)-reducing activity Log-phase (12 hr) and stationary phase Birinapant molecular weight (20 hr) cells ADP ribosylation factor of C. testosteroni S44 were obtained by growth at 26°C, shaking at 180 rpm in 20 ml LB broth. The modified method was based on protocol of method No. 5 for subcellular fractionation [51]. All further parts of the procedure were carried out at 0 to 4°C unless differently noted. The cells in 20 ml LB cultures were harvested by

centrifugation for 20 min at 4,500 × g, and then the supernatant was removed. After being harvested, the cells were suspended in 2.0 ml 1 × PBS buffer (pH 7.0), GSK2118436 centrifuged three times for 10 min at 4,500 × g. The cells were then suspended in 1.0 ml 1 × PBS buffer (pH 7.0) containing 5% glycerol (v/v, final concentration). The suspension was treated with 1.0 mg ml−1 (final content) lysozyme for 5 min at room temperature and afterwards centrifuged for 20 min at 20,000 × g. The supernatant was periplasmic protein. In order to separate the membranes from the cytoplasm, the pellet was suspended in 1.0 ml 1 × PBS buffer containing 5% glycerol (v/v) and 125 units per ml (final concentration) DNase I. The suspension was treated with ultrasound for 20 min (20 amplitude microns, 5 s /5 s, Sanyo Soniprep). The broken-cell suspension was centrifuged for 6 min at 6000 × g to remove unbroken cells. The supernatant was centrifuged for 60 min at 20,000 × g. The supernatant contained the cytoplasmic fraction and the pellet contained the crude membranes (outer membrane and cytoplasmic membrane).

Strippoli GF, et al. BMJ. 2008;336:645–51. (Level 1)   7. Bianchi S, et al. Am J Kidney Dis. 2003;41:565–70. selleck screening library (Level 2)   8. Bianchi S, et al. Am J Kidney Dis. 2010;55:671–81. (Level 2)   9. Shepherd J, et al. Clin J Am Soc Nephrol. 2007;2:1131–9. (Level 4)   10. Keech A, et al. Lancet. 2005;366:1849–61. (Level 2)   11. Landray M, et al. Am J Kidney Dis. 2006;47:385–95. (Level 2)   12. Baigent C, et al. Lancet. 2011;377:2181–92. (Level

2)   13. Kimura K, et al. J Atheroscler Thromb. 2010;17:601–9. (Level 4)   14. Colhoun HM, et al. Am J Kidney Dis. 2009;54:810–9. (Level 4)   15. Fassett RG, et al. Atherosclerosis. 2010;213:218–24. (Level 4)   16. Tonelli M, et al. Circulation. 2005;112:171–8. (Level 4)   17. Vidt DG, et al. Clin Ther. 2011;33:717–25. (Level 4)   18. Ruggenenti P, et al. Clin J Am Soc Nephrol. 2010;5:1928–38. (Level 2)   19. Rahman M, et al. Am J Kidney Dis. 2008;52:412–24. (Level 4)   20. Huskey J, et al. Atherosclerosis. 2009;205:202–6. (Level 4)   21. Lemos PA, et al. Am BYL719 J Cardiol. 2005;95:445–51. (Level 4)   22. Renke M, et al. Acta Biochim Pol. 2010;57:547–2. (Level 2)   23. Nakamura T, et al. Oxid Med Cell Longev. 2010;3:304–7. (Level 4)   24. Inoue T, et al. Intern Med. 2011;50:1273–8. (Level 4)   Chapter 15: Obesity and Metabolic Syndrome in CKD Is the metabolic syndrome a risk factor for the development of CKD? The metabolic syndrome (MetS) is a cluster of risk factors for cardiovascular

diseases, and Glutathione peroxidase could affect kidneys through various pathways. This section summarizes the epidemiological data showing MetS as a risk factor for the development of CKD. The association of MetS with CDK varies with gender, race, and age, which should be considered in the interpretation of the studies. A recent meta-analysis has shown a significant association between MetS and the development of eGFR <60 ml/min per 1.73 m2. Each of the five components of

MetS showed a positive association with this risk, and the strength of association increased as the number of components increased. MetS was also selleck chemicals llc associated with the development of albuminuria. In the MAGIC study, it was concluded that concomitant occurrence of MetS and albuminuria increased the risk of kidney function loss more than five-fold compared to subjects with neither of these factors. Histologically, kidneys from MetS subjects showed a greater prevalence of tubular atrophy, interstitial fibrosis, arterial sclerosis, and global and segmental glomerulosclerosis than non-MetS subjects. MetS was also associated with renal dysfunction after kidney transplantation. In MetS subjects, non-alcoholic fatty liver disease (NAFLD), and especially liver fibrosis in non-alcoholic steatohepatitis (NASH) were associated with a decrease in kidney function. Change in body weight is better than body weight itself as a predictor of renal outcome. A retrospective cohort study showed that improvement of MetS was accompanied by reduced albuminuria and stable GFR in type 2 diabetes mellitus.

A total of approximately 30000 transposon mutants were screened and 14 phage resistant mutants were AR-13324 mouse isolated and analyzed. Since two mutants, TM20 and TM22 are defect in the same gene, rmlB, a total of 13 genes was identified, which are essential for phage infection. The transposon OSI-906 ic50 screen revealed genes important for LPS biosynthesis (see Table 4 for details) like the gene algC which is needed for a complete LPS core in P. aeruginosa [16]. It also revealed the genes rmlA and rmlB, which are involved in the biosynthesis of the LPS core sugars [39, 40]. These findings confirm that the phage JG004 uses LPS as receptor.

Other identified genes involved in LPS biosynthesis are wzz2, LCZ696 waaL, migA, PA5000 and PA5001 (Table 4) [40]. Since nine out of 13 identified genes encoded proteins involved in LPS biosynthesis, we additionally isolated LPS from all mutant strains and analyzed it by electrophoresis (see Materials and Methods). Figure 4 shows the LPS profiles of the transposon mutants. The lipid A, which migrates furthest due to its size, is seen as a dark grey spot at the end of the gel. The migration depends on changes in the LPS composition, mostly in the core polysaccharide which

is adjacent to the lipid A [41]. Not all LPS biosynthesis genes cause changes in the LPS which are visible by electrophorsis e.g. migA [42], which appears as wild type LPS. The black line in Figure 4 indicates the migration level of the wild type lipid A. Dramatic changes in the LPS profile which differs clearly from the P. aeruginosa wild type LPS can be seen for the algC, the wzz2 and the PA5001 mutant. Further analysis of the LPS for example Western blot analysis with antibodies specific to the different components of the LPS could provide a better understanding

of the mutants, www.selleck.co.jp/products/Paclitaxel(Taxol).html but was not involved in this phage characterization study. Figure 4 LPS profile of transposon mutants. Silver stained SDS-PAGE illustrating the isolated LPS of the wild type PAO1 and the transposon mutants. Only the gene, interrupted by the transposon of the respective mutant is indicated on top of the lanes, PAO1 is the P. aeruginosa wild type. The arrow points to the black line in the lower part of the gel. This line indicates the migration of wild type lipid A and core sugars of the LPS [42]. As indicated, the LPS of the speD, PA0534, PA0421, PA2555 and migA mutant strains appears similar to wild type LPS. The LPS profile of the remaining mutant strains is different and indicates an altered LPS structure. Interestingly, the biochemical analysis of LPS indicates that gene PA2200 might be involved in biosynthesis or modification of P. aeruginosa LPS due to altered migration. We also identified genes essential for phage infection, which encode proteins of unknown function.

Immunoblots show the result of SRT1720 cost T3S assays in which Selleck Crenigacestat proteins in culture supernatants (S, secreted proteins) and in bacterial pellets (P, nonsecreted proteins) from ~5×107 bacteria were loaded per lane. The first 15 amino acids of the Yersinia effector YopE correspond to an archetypal T3S signal [57, 58], and YopE15-TEM-1 was used as positive control; SycT and SycO are strictly cytosolic Yersinia T3S chaperones [44, 51]. SycT20-TEM-1 was a negative control for the T3S assays. Immunodetection of SycO ensured that the presence of TEM-1 hybrid proteins

in the culture supernatants was not a result of bacterial lysis or contamination. The percentage (%) of secretion of each TEM-1 hybrid was calculated by densitometry, as the ratio between the amount of secreted and total protein. The threshold to decide whether a protein was secreted was set to 5% (dashed line), based on the % of secretion of SycT20-TEM-1. Data are the mean ± SEM from at least 3 independent experiments. Identification of T3S

signals in C. trachomatis proteins To identify T3S signals in the selected 46 C. trachomatis proteins, we analyzed secretion of fusions to TEM-1 of the first 20 amino acids of each of these proteins by T3S-proficient Y. enterocolitica ΔHOPEMT. These experiments revealed 24 C. trachomatis proteins whose first 20 amino acids drove secretion AZD1480 clinical trial of TEM-1 hybrid proteins by Y. enterocolitica (Figure 2A). Owing to lack of expression, or very low expression levels, it was not possible to conclude if the TEM-1 hybrids comprising the N-terminal region of CT590, CT845 and CT863 were secreted (Figure 2A). By individually introducing the plasmids encoding the TEM-1 hybrid Carnitine dehydrogenase proteins that were secreted into T3S-deficient Y.

enterocolitica ΔHOPEMT ΔYscU and performing T3S assays, we confirmed that secretion of the proteins was dependent on a functional T3SS (Figure 2B). The percentage of secretion of the different hybrid proteins that were secreted varied considerable, between 56% (SEM, 4) for CT69420-TEM-1 to 5% (SEM, 2) for CT14320-TEM-1 (Figure 2B). Overall, this confirmed a T3S signal in CT203, which has been previously shown to be a T3S substrate [21], and revealed T3S signals in 23 previously T3S substrates of C. trachomatis. Figure 2 Identification of T3S signals in C. trachomatis proteins using Y. enterocolitica as a heterologous system. Y. enterocolitica T3S-proficient (ΔHOPEMT) (A) and T3S-defective (ΔHOPEMT ΔYscU) (B) were used to analyze secretion of hybrid proteins comprising the first 20 amino acids of selected C. trachomatis proteins or the first 20 amino acids of Y. enterocolitica SycT fused to the mature form of TEM-1 β-lactamase (TEM-1). Immunoblots show the result of T3S assays in which proteins in culture supernatants (S, secreted proteins) and in bacterial pellets (P, non-secreted proteins) from ~2.5×108 and ~5×107 bacteria, respectively, were loaded per lane. TEM-1 hybrids of the known C.

Nonoguchi N, Ohta T, Oh JE, Kim YH, Kleihues P, Ohgaki H: TERT promoter mutations in primary and secondary glioblastomas. Acta Neuropathol 2013, 126:931–937.PubMedCrossRef 23. Remke M, Ramaswamy V, Peacock J, Shih DJ, Koelsche C, Northcott PA, Hill N, Cavalli FM, Kool M, Wang X, Mack SC, Barszczyk M, Morrissy AS, Wu X, Agnihotri S, Luu B, Jones DT, Garzia L, Dubuc AM, Zhukova Erastin manufacturer N, Vanner R, Kros JM, French PJ, Van Meir EG, Vibhakar R, Zitterbart K, Chan JA, Bognar L, Klekner A, Lach B, et al.: TERT promoter mutations are highly recurrent in SHH subgroup medulloblastoma. Acta Neuropathol

2013, 126:917–929.PubMedCentralPubMedCrossRef 24. Scott GA, Laughlin TS, Rothberg PG: Mutations of the TERT promoter are common in basal cell carcinoma and squamous cell carcinoma. Mod Pathol 2014, 27:516–523.PubMedCrossRef

25. Vinagre J, Almeida A, Populo H, Batista R, Lyra J, Pinto V, Coelho R, Celestino R, Prazeres H, Lima L, Melo M, da Rocha AG, Preto A, Castro P, Castro L, Pardal F, Lopes JM, Santos LL, Reis RM, Cameselle-Teijeiro J, Sobrinho-Simoes M, Lima J, Maximo V, Soares P: Frequency of TERT promoter mutations in human cancers. Nat Commun 2013, 4:2185.PubMedCrossRef 26. Goutagny S, Nault JC, Mallet M, Henin D, see more Rossi JZ, Kalamarides M: High incidence of activating TERT promoter mutations in meningiomas undergoing malignant progression. Brain Pathol 2014, 24:184–189.CrossRef 27. Schneider-Stock R, Jaeger V, Rys J, Epplen JT, Roessner A: High learn more telomerase activity and high HTRT mRNA expression differentiate pure myxoid Epothilone B (EPO906, Patupilone) and myxoid/round-cell liposarcomas. Int J Cancer 2000, 89:63–68.PubMedCrossRef 28. Costa A, Daidone MG, Daprai L, Villa R, Cantu S, Pilotti S, Mariani L, Gronchi A, Henson JD, Reddel

RR, Zaffaroni N: Telomere maintenance mechanisms in liposarcomas: association with histologic subtypes and disease progression. Cancer Res 2006, 66:8918–8924.PubMedCrossRef 29. Matsuo T, Shimose S, Kubo T, Fujimori J, Yasunaga Y, Sugita T, Ochi M: Correlation between p38 mitogen-activated protein kinase and human telomerase reverse transcriptase in sarcomas. J Exp Clin Cancer Res 2012, 31:5.PubMedCentralPubMedCrossRef 30. Schneider-Stock R, Boltze C, Jager V, Epplen J, Landt O, Peters B, Rys J, Roessner A: Elevated telomerase activity, c-MYC-, and hTERT mRNA expression: association with tumour progression in malignant lipomatous tumours. J Pathol 2003, 199:517–525.PubMedCrossRef 31. Yan P, Benhattar J, Coindre JM, Guillou L: Telomerase activity and hTERT mRNA expression can be heterogeneous and does not correlate with telomere length in soft tissue sarcomas. Int J Cancer 2002, 98:851–856.PubMedCrossRef 32. Ulaner GA, Hu JF, Vu TH, Giudice LC, Hoffman AR: Telomerase activity in human development is regulated by human telomerase reverse transcriptase (hTERT) transcription and by alternate splicing of hTERT transcripts. Cancer Res 1998, 58:4168–4172.PubMed 33.

By comparing three SEM images of Figure 3, one can see that the concentration of PVP has less influence on the yield of silver nanowires when PVPMW=1,300,000 was used. However, it is found that the concentration of PVP contributes to the control of diameter

of the synthesized nanowire. In Figure 3a, there are short nanorods, long nanowires, and some nanoparticles selleck chemicals (<10%). Figure 3b shows the yield of silver nanowires with uniform diameter and length increased to about 95% which is similar to the result shown in Figure 3c. From the above comparison study, it should be noted that varying the MWs of PVP is more efficient on the shape control of silver nanocrystals than varying the concentrations of PVP. Figure 3 SEM images of silver nanocrystals obtained by varying the concentration of PVP MW=1,300,000 . (a) 0.143 M, (b) 0.286 M, and (c) 0.572 M. Optical property

characterization UV-visible NIR spectrophotometer can also be used to confirm the morphologies of silver nanocrystals. The resonance bands of the plasmonic nanocrystals are mainly dependent on the distribution of the electromagnetic field on the surface of the metal nanocrystals. In other words, metal nanoparticles with selleckchem different shapes and sizes should have different optical signatures. Figure 4a exhibits the extinction spectra of the silver solution with different PVPs at 0.286 M. As shown in Figure 4a, the rodlike shape prepared with PVPMW=8,000 has a broad scattering Carnitine palmitoyltransferase II band from the visible to the near-infrared wavelengths leading to the white color shown in the inset in Figure 1a. Because the structure joined together can trap light effectively [30], such rodlike nanostructure can be used as a hot spot. The extinction

spectra of the silver nanostructure solution using PVPMW=29,000 have a main resonance peak at 430 nm and a shoulder peak at 360 nm corresponding to the nanosphere [17]. In comparison, that of PVPMW=40,000 exhibits a redshift and broader absorption range GDC 0068 ascribed to the irregular shapes of the products. In the extinction spectrum of the solution with PVPMW=1,300,000, there are two resonance peaks at 390 and 350 nm belonging to the optical signature of silver nanowire [19]. Figure 4 The optical characteristics of the silver solution. (a) The extinction spectra of the silver nanostructure solution obtained with different PVPs of 0.286 M. (b) The extinction spectra of the silver nanostructure solution obtained at different concentrations of PVPMW=29,000, (c) The extinction spectra of the silver nanostructure solution obtained at different concentrations of PVPMW=40,000. (d) The extinction spectra of the silver nanostructure solution obtained at different concentrations of PVPMW=1,300,000. Figure 4b,c,d shows the extinction spectra of the silver nanostructure solution obtained at different concentrations of PVPMW=29,000, PVPMW=40,000, and PVPMW=1,300,000, respectively.

Table 2 Primer sets used for the 16S rRNA gene quantification of A. muciniphila , F. prausnitzii , Enterobacteriaceae , Clostridium cluster IV, Bifidobacterium and Entospletinib in vivo Lactobacillus group by qPCR. Amplicon size, annealing and

fluorescence acquisition temperature are also reported Target microorganism Primer set Sequence (5′ to 3′) Product size (bp) Annealing temp (°C) Fluorescence acquisition temp (°C) Reference Akkermansia muciniphila AM1 CAGCACGTGAAGGTGGGGAC 349 63 88 [31]   AM2 CCTTGCGGTTGGCTTCAGAT         Faecalibacterium prausnitzii Fprau223F GATGGCCTCGCGTCCGATTAG 199 67 85 [32]   Fprau420R CCGAAGACCTTCTTCCTCC Evofosfamide research buy         Enterobacteriaceae Eco1457F CATTGACGTTACCCGCAGAAGAAG 195 63 87 [32]   Eco1652R CTCTACGAGACTCAAGCTTGC         Clostridium

Cl_IV S-*-Clos-0561-a-S-17 TTACTGGGTGTAAAGGG 588 60 85 [33]   S-*-Clept-1129.a-A-17 TAGAGTGCTCTTGCGTA         Bifidobacterium bif-164 GGGTGGTAATGCCGGATG 523 60 90 [34]   bif-662 CCACCGTTACACCGGGAA         Lactobacillus group Lac1 AGCAGTAGGGAATCTTCCA 327 61 85 [35]   Lac2 ATTYCACCGCTACACATG         Results Faecal microbiota profile of atopic children and healthy controls The faecal microbiota of 19 atopic children and 12 healthy controls living in Italy was characterized by means of the HTF-Microbi.Array platform (Additional files 4 and 5) [24]. Hybridization experiments were performed in two replicates. Pearson’s correlation OSI-906 in vivo coefficients ranging from 0.95 and 0.99 were achieved between the two replicates, proving the high reproducibility of the phylogenetic profiles obtained by the HTF-Microbi.Array platform. A PCA of the fluorescence signals from atopics and controls was carried out.

The diagnosis of atopy was considered as a dummy environmental variable. As shown in Figure 1A, the principal components Chloroambucil PC2 and PC3, which collectively represented only a minor fraction of the total variance (9.7%), resulted in the separation of samples according to the health status. In order to identify the bacterial lineages showing differences in abundance between atopics and controls, probe fluorescence signals obtained from the HTF-Microbi.Array in atopics and controls were compared by box plot analysis (Additional file 6). Probes showing P < 0.3 are represented in Figure 1B. Atopic children showed a tendency towards reduction of A. muciniphila F. prausnitzii et rel. and Ruminococcus bromii et rel. (Clostridium cluster IV), and Clostridium cluster XIVa, and were enriched in Enterobacteriaceae Bacillus clausii and Veillonella parvula. Figure 1 Analysis of the HTF-Microbi.Array fluorescence signals. A: PCA of the HTF-Microbi.Array fluorescence signals. Atopy or health status were considered as dummy environmental variables (green triangles) and indicated as atopic and control, respectively.

The graphene sheet cannot make a complete recovery, and there exited broken covalent bonds after the unloading process. In the reloading process, the maximum force exerting on graphene is much smaller than that in Figure  3, which denotes the fracture of graphene lattices. Figure  4b describes the state where the unloading process begins, and Figure  4c describes the state where the unloading process ends. After the loading process, there exited broken bonds and fractured lattices in the middle of the graphene film and these defective structures did not recover during the unloading process.

Therefore, the deformation of the graphene described in this figure can be considered as a plastic type. Figure 4 Loading-unloading-reloading process with the maximum indentation depth smaller than the critical indentation depth. (a) Load–displacement curve, (b) local atom click here configuration when the loading process is finished, and OSI-906 in vitro (c) local atom configuration when the unloading process is finished. Young’s modulus and strength of the

graphene film According to the available correlation for the indentation experiments of a circular single-layer graphene film in [18, 22, 37], one new formula is constructed to describe the relationship between indention depth and load, (1) where d is the indentation depth and F denotes the concentrated force gotten by the graphene film. In Equation 1, the load F consists of two parts: the first part, F σ (d), represents the term due to the axial tension of the two-dimensional (2-D) film, (2) where σ 0 2D is the pre-tension of the single-layer graphene film, r

is the indenter radius, β denotes the aspect ratio and is equal to L/b, and R equ represents the equivalent radius of the rectangular graphene sheet, (Lb/π)1/2. RVX-208 The second one, F E(d), represents the large deformation term, (3) where E 2D is the 2-D elastic modulus, i.e., Young’s modulus, of the single layer graphene film. The strain energy density of graphene, as a standard 2-D material, can be represented by the energy of per unit area. Then, the corresponding pre-tension and elastic modulus can be expressed as σ 0 2D and E 2D, respectively, with the unit N/m. The common pre-tension and elastic modulus of a 3-D bulk material can be obtained through these 2-D ISRIB mw values divided respectively by the effective thickness which is always treated as the layer spacing of the graphite crystal, i.e., 3.35 Å. q is an nondimensional value, q = 1/(1.05 - 0.15ν - 0.16ν 2) = 0.9795, where ν denotes Poisson’s ratio, ν = 0.165 [3, 18, 21]. It is reported that when r/R > 0.1, the indenter radius has a significant influence on the load–displacement properties [38, 39]. In our simulations, r/R > 0.1; thus, Equations 2 and 3 are corrected by a factor of (r/R)3/4 and (r/R)1/4, respectively.