Stat Appl Genet Mol Biol 2005., 4: 6. Yeung KY, Bumgarner RE, Raftery AE: Bayesian model averaging: development of an improved multi-class, gene selection and classification GSK2879552 tool for microarray data. Bioinformatics 2005, 21: 2394–2402.CrossRefPubMed 7. Li T, Zhang C, Ogihara M: A comparative study of feature selection and multiclass classification methods

for tissue classification based on gene expression. Bioinformatics 2004, 20: 2429–2437.CrossRefPubMed 8. Gordon GJ, Jensen RV, Hsiao LL, Gullans SR, Blumenstock JE, Ramaswamy S, Richards WG, Sugarbaker DJ, Bueno R: Translation of microarray data into clinically relevant cancer diagnostic tests using gene expression ratios in lung cancer and mesothelioma. Cancer Res 2002, 62: 4963–4967.PubMed 9. Alon U, Barkai N, Notterman DA, Gish K, Ybarra S, Mack D, Levine AJ: Broad

patterns of gene expression click here revealed by clustering analysis of tumor and normal colon tissues probed by oligonucleotide arrays. Proc Natl Acad Sci USA 1999, 96: 6745–6750.CrossRefPubMed 10. Singh D, Febbo PG, Ross K, Jackson DG, Manola J, Ladd C, Tamayo P, Renshaw AA, D’Amico AV, Richie JP, Lander ES, Loda M, Kantoff PW, Golub TR, Sellers WR: Gene expression correlates of clinical prostate Inhibitor Library in vivo cancer behavior. Cancer Cell 2002, 1: 203–209.CrossRefPubMed 11. Bhattacharjee A, Richards WG, Staunton J, Li C, Monti S, Vasa P, Ladd C, Beheshti J, Bueno R, Gillette M, Loda M, Weber G, Mark EJ, Lander ES, Wong W, Johnson BE, Golub TR, Sugarbaker DJ, Meyerson M: Classification of human lung carcinomas by mRNA expressionprofiling reveals distinct adenocarcinoma subclasses. Proc Natl Acad Sci USA 2001, 98: 13790–13795.CrossRefPubMed 12. Parmigiani G, Garrett-Mayer ES, Anbazhagan R, Gabrielson E: A cross-study Oxalosuccinic acid comparison of gene expression studies for the molecular classification of lung cancer. Clin Cancer Res 2004, 10: 2922–2927.CrossRefPubMed 13. Khan J, Wei JS, Ringnér M, Saal LH, Ladanyi M, Westermann F, Berthold F, Schwab M, Antonescu CR, Peterson C, Meltzer PS: Classification and diagnostic prediction of cancers using gene expression profiling and artificial

neural networks. Nat Med 2001, 7: 673–679.CrossRefPubMed 14. Pomeroy SL, Tamayo P, Gaasenbeek M, Sturla LM, Angelo M, McLaughlin ME, Kim JY, Goumnerova LC, Black PM, Lau C, Allen JC, Zagzag D, Olson JM, Curran T, Wetmore C, Biegel JA, Poggio T, Mukherjee S, Rifkin R, Califano A, Stolovitzky G, Louis DN, Mesirov JP, Lander ES, Golub TR: Prediction of central nervous system embryonal tumour outcome based on gene expression. Nature 2002, 415: 436–442.CrossRefPubMed 15. Opgen-Rhein R, Strimmer K: Accurate ranking of differentially expressed genes by a distribution-free shrinkage approach. Stat Appl Genet Mol Biol 2007, 6: Article9.PubMed 16. Schäfer J, Strimmer K: A shrinkage approach to large-scale covariance matrix estimation and implications for functional genomics.

MMPs contribute to this metastatic process by degrading basement membrane. In addition, MMPs can, due to their proteolytic activities, promote tumor growth by increasing the bioavailabilities of growth factors in the ECM [11]. Furthermore, it is becoming

increasingly clear that MMPs play a central role in ECM degradation [13]. Among MMPs, MMP-2 (gelatinase A) and MMP-9 (gelatinase B), are present in large quantities in cancer tissues [14, 15], and accumulating evidence indicates that MMP-2 and MMP-9 play critical role during tumor invasion and metastasis [14, 16–20]. Furthermore, Matrix metalloproteinases (MMPs) and their endogenous inhibitors participate in the invasive process of human osteosarcoma [21]. Bisphosphonates (BPs) are stable analogues of pyrophosphonate, learn more and are potent inhibitors of osteoclast-mediated bone resorption. They are widely used to treat metabolic bone diseases, such as, Paget’s disease [22] and hypercalcemia [23] and to treat postmenopausal osteoporosis [24]. Recently, it was reported that BPs may significantly help control the pain associated with bone tumors [25]. Preclinical evidence suggest that BPs have direct antitumor effects on a variety of human cancer cells [26], and it is known that they

decrease cell proliferation in human osteosarcoma cell line panels, disturb the cell cycle, and induce the apoptosis of SaOS-2 cells [27, 28]. These findings suggest that BPs could play a QNZ solubility dmso beneficial 2-hydroxyphytanoyl-CoA lyase adjuvant role in the treatment of osteosarcoma. However, the inhibitory effects of BPs on osteosarcoma cell have not been HDAC inhibitor drugs comprehensively studied, and therefore, in the present study, we examined the effects of the third-generation BPs, risedronate, on osteosarcoma cell invasion. Methods Reagents Risedronate [1-hydroxy-2-(3-pyridinyl)ethylidene]bis [phosphonic acid] was purchased from (Sanofi-Aventis, Korea). A stock solution of risedronate was prepared in phosphate-buffer saline (PBS). All other chemicals and reagents

used were of analytical grade. Cell Culture SaOS-2 and U2OS were purchased from the Korean Cell Line Bank (KCLB). Cells were cultivated in Dulbecco’s Minimum Essential Medium (DMEM) supplemented with 10% heat-inactivated fetal bovine serum (Gibco BRL, Grand Island, NY). Cultures were maintained at 37°C in a 5% CO2/95% air atmosphere. The medium was changed every 2–3 days, and cells were passaged twice a week. Risedronate treatment of SaOS-2 and U2OS cells SaOS-2 and U2OS cells were seeded in 6-well plates at a density of 2 × 105cells/well in DMEM/10% FBS overnight. The cells were then washed and treated with different concentrations of risedronate (0, 0.1, 1, 10 μM) for 48-h at 37°C in 5% CO2. Conditioned media were then collected and cells were harvested. MTT cell viability assay SaOS-2 and U2OS cells were seeded onto a 96-well culture plate at a density of 1 × 104 cells/well in 100 μl of complete DMEM.

Our results indicated that the average rates of increasing body weight in mice injected with the complement strain GT01Δnga (pLZN2) https://www.selleckchem.com/products/gsk1120212-jtp-74057.html were lower than in mice injected with GT01Δnga (pLZ12-Km2), but this difference was not statistically significant (data not shown). GT01Δnga (pLZN-RBS) injection in the mouse model showed slightly lower increasing rates of body weight than did GT01Δnga (pLZN2) (data not shown) and GT01Δnga (pLZ12-Km2: control vector) (Figure 2A). In addition, when the body weight

on days 2 and 3 post-infection was analyzed, GT01Δnga (pLZN-RBSII2) with the highest NADase Capmatinib ic50 activity showed the slowest increasing rate of body weight (Figure 2B). Figure 2 Virulence (based on body weight change) to mouse of GT01 Δnga with or without cloned nga gene. (A) The change in body weight (% of the first weight) post-infection XMU-MP-1 in vitro was shown in a week (* as a reference, the parental strain was shown in three days, because most mice died within this period). (B) Relationship of body weight and NADase activity was shown on days 2 and 3. NADase activities (0.04, 1.28, 1.78 and 4.57 U, respectively) of (a) GT01Δnga (pLZ12-km2), (b) GT01Δnga (pLZN2), (c) GT01Δnga (pLZN-RBS) and (d) GT01Δnga (pLZN-RBSII2) was plotted on the horizontal axis, respectively (see Table 3 or the text for NADase activity of each strain). The gradual increase in body weight (%) depended on higher NADase activity of the strains. The error bars indicate the standard error of the means.

IFS-inhibition of the virulence of the GAS strain GT01 If purified IFS is able to suppress GAS virulence in the mouse-infection

model, it would support the role of NADase in vivo. For this experiment, His-IFS was purified (Figure 3) and used in the mouse-model infection. Meanwhile, as an unrelated protein, His-TarC which is a His-tagged carboxyl terminal domain of an E. coli aspartate receptor was used. As shown in Figure 4-Aminobutyrate aminotransferase 4, the solution containing purified His-IFS, but not the control His-TarC, significantly reduced the virulence of GAS. The control protein was not effective for GAS virulence (Figure 4) because the mortality and the survival times did not decrease and prolong, respectively, compared with the result of GT01 infection without treatment (see GT01 strain in Table 2 for comparing the mortalities, data not shown for survival times). Figure 3 Purification of His-tagged IFS protein. The protein overexpressed with IPTG in E. coli JM109 having pHis-IFS (lane 2), but not in E. coli JM109 having the control vector pQE80L (lanes 5 and 6), was purified as shown in lane 3. The protein was detected by anti-RGS:His antibody to confirm the expected His-tagged product (lane 7). Figure 4 Inhibition of the mortality in mouse of a GAS GT01 clinical isolate by His-IFS. The solution including His-IFS reduced the virulence of the GAS to 42% mortality (5 death/12 trial) compared with 83% (10/12) of the control His-TarC (P = 0.008 for comparison of survival times).

The final product of IMP metabolism is urate.

There were no changes in the blood urate concentration between the groups either before or after the match (Figure 3C). None of the above metabolites showed changes in response to Arg supplementation when we compared the pre- and post-match levels (Figure 3). Figure 3 Glucose increases in response to exercise in a supplementation-independent manner (A). Neither supplementation nor exercise affects urea (B) or urate (C) after intense exercise. Control, n = 23 (PG, ●); Arginine, n = 16 (RG, Δ). (*) CX-5461 clinical trial denotes that the average ± SE is different from the pre-exercise values. Blood cells The six minutes this website of exercise induced an increase in leukocytes of approximately 75% in both groups. This elevated level did not decrease in the ten minutes following the experiment and was similar between the groups (Figure 4A). To avoid misinterpretations due to volemic variations, we also evaluated the red blood cell counts. The packed cell volume was not altered by exercise (Figure 4B). We did not detect any differences in the red blood cell count, volume or hemoglobin content in response to either exercise

or supplementation. Figure www.selleckchem.com/products/sbi-0206965.html 4 White blood cell counts increase (A) after intense exercise without changes in packed cell volume (B). Control, n = 23 (PG, ●); Arginine, n = 16 (RG, Δ). (*) denotes that the average ± SE is different from the pre-exercise values. The absolute pre-exercise WBC counts are 5.9 ± 0.2 cells × 109/L for the PG and 6.4 ± 0.5 cells × 109/L for the RG; the packed cell volumes are 47.5 ± 0.6% for the PG and 46.6 ± 0.6% for the RG. Differential white blood cell analyses showed a distinct response to both exercise and Arg supplementation. The basophil counts rose two-fold in the PG but did not change in the RG (Figure 5A). The eosinophil counts were significantly

different between the groups after the end of exercise (Figure 5B). However, neutrophils appeared not to respond significantly in either the PG or RG (Figure 5C). The exercise led to a 2.2-fold increase in the lymphocyte count. This increase was significantly reduced by Arg supplementation (Figure 6A). Calpain Figure 5 Granulocyte counts in response to exercise and supplementation. Basophils (A); eosinophils (B); neutrophils (C). Control, n = 23 (PG, ●); Arginine, n = 16 (RG, Δ). (*) denotes that the average ± SE is different from the pre-exercise values; (#) denotes a difference between the experimental groups. The absolute pre-exercise values for basophils are 2.6 ± 0.4 × 107 cells /L for the PG and 1.9 ± 0.9 × 107 cells /L for the RG; for eosinophils, 1.8 ± 0.3 × 108 cells /L for the PG and 2.0 ± 0.5 × 108 cells /L for the RG; and for neutrophils, 3.1 ± 0.2 × 109 cells /L for the PG and 2.7 ± 0.4 × 109 cells /L for the RG. Figure 6 Exercise induces an increase in lymphocytes in an arginine supplementation-dependent manner. Control, n = 23 (PG, ●); Arginine, n = 16 (RG, Δ).

Serum amylase and lipase levels were unchanged during the present study, though serum trypsin levels increased after the ASNase injection. Serum PSTI levels increased after the ASNase injection as well. Acute pancreatitis develops with unregulated trypsin activity after breakdown

of critical protective mechanisms and copious secretion of pancreatic enzymes such as amylase and lipase.[21,22] The present results indicate that inhibitors of trypsin could potentially prevent development of pancreatitis, and suggest the presence of subclinical pancreatitis in cases who do not develop pancreatitis during administration of ASNase. Not only ASNase but also prednisolone has been implicated as an agent capable of inducing pancreatitis.[23] Previous reports suggest that ASNase is the more likely source of pancreatitis on the basis of histologic examination of the pancreas, the relative infrequency of prednisolone-induced www.selleckchem.com/products/azd9291.html pancreatitis, and a negative result after rechallenge with prednisolone.[14,18,24] In the present study, one of 29 patients (3%) developed ASNase-induced pancreatitis, similar to the morbidity rates in previous reports.[4,6,9,16,25] Since the patient developed NCT-501 clinical trial severe pancreatitis, ASNase was contraindicated during the rest of her treatment for ALL. The results of her blood tests were similar to the results from those patients

who did not develop AR-13324 order acute pancreatitis, so there was no parameter that could be used to predict acute pancreatitis. When ASNase-induced pancreatitis

occurs, treatment with Erwinia chrysanthemi asparaginase is an option. As it can also lead to pancreatitis, Erwinia asparaginase is a second-line therapy for ALL after hypersensitivity to Escherichia coli asparaginase.[26] Furthermore, there are no widely accepted guidelines for use of Erwinia asparaginase, and such treatment is not covered by health insurance providers in Japan. Previous reports have shown that there is a mean of almost 10 days from the last administration of ASNase to diagnosis of pancreatitis.[5,9,16] Similarly, Japanese case reports of ASNase-induced pancreatitis have shown that 50 of 56 patients (89%) who developed tuclazepam ASNase-induced pancreatitis did so within 10 days (median 2 days, range 0–23 days) after administration of ASNase.[27] This period is similar to the time period in the present study when the levels of plasma amino acids, serum trypsin, and serum PSTI changed. In the rat model, it has been proposed that ASNase-induced pancreatic injury can involve disruption of the plasma amino acid balance that is caused by ASNase. Disruption of protein synthesis in acinar cells then causes inhibition of exocytosis following the histologic morphologic changes.[28] The present results imply that the plasma amino acid level imbalance could also be a factor in ASNase-induced pancreatitis in humans.

The O–I STI571 solubility dmso 1 curves measured

with the five different colors were fitted together with the restriction of common values of J and Tau(reox), as these parameters are unlikely to depend on the color of light. Calculation of Sigma(II)λ by the multi-color-PAM-software is based on the fitted value of the time constant Tau and the value of incident PAR, using the following general equation: $$ \textSigma(\textII)_\lambda = \frack(\textII)L \cdot \textPAR = \frac1\tau \cdot L \cdot \textPAR, $$ (1)where k(II) is the rate constant of PS II turnover and Tau the time constant of QA-reduction during the O–I 1 rise, L is Avogadro’s constant, PAR is the photon fluence rate of the light driving the O–I 1 rise and Sigma(II)λ the wavelength- and sample-dependent absorption cross section of PS II (for further explanations, see “Results and interpretation” section). Measurement of absorptance Sample absorptance was measured using the same Optical Unit ED-101US/MD as for fluorescence GSI-IX measurements (see Fig. 1), but with the detector-unit

MCP-D being moved from the 90° position (relative to the emitter-unit) to the 180° position. The long-pass filter in front of the detector was exchanged against suitable neutral buy BKM120 density filters and pin-hole diaphragms, so that pulse-modulated transmittance signals could be measured both with the suspension medium as such, I medium, and with the suspension medium containing Chlorella or Synechocystis, I sample. The absorptance a (=1 − transmittance) was calculated as a = 1 – I sample/I medium. With the given optical geometry almost all light entering the 10 × 10 mm cuvette via the emitter-perspex-rod is picked up by the detector-perspex-rod,

unless absorbed by the sample. Photosynthetic cAMP organisms and sample preparation Experiments were carried out with dilute suspensions of green unicellular algae Chlorella vulgaris and cyanobacteria Synechocystis PCC 6803. Chlorella was cultured in natural day light (north window) at 20–40 μmol/(m2 s) and room temperature (25 °C) in an inorganic medium (Pirson and Ruppel 1962) under ambient air. Synechocystis was grown photoautotrophically in artificial light (tungsten) at 30  μmol/(m2 s) and 30 °C in Allen’s (1968) medium under ambient air. Both cultures were shaken manually at least four times per day. Cultures were frequently diluted so that chlorophyll content did not exceed 5–10 mg/L. Experiments were carried out at room temperature with diluted suspensions at 200–300 μg/L, as determined with a calibrated WATER-PAM chlorophyll fluorometer (Walz). For sample preparation the cuvette was first filled with 1.4 mL of culture medium and then stock suspension was added dropwise to the stirred sample until signals corresponding to 200–300 μg/L were reached.

1). The symptoms associated with extrapyramidal effects often start soon after the initiation of treatment and may be transient [35]. In addition, the sedative and orthostatic hypotensive side effects of antipsychotics often occur immediately after

the start of treatment. The NVP-BGJ398 second period of increased risk after several months of use may reflect the effects of long-term hyperprolactinemia on bone density. Indeed, Hugenholtz et al. [20] found an increased risk only among long-term users of antipsychotics and attributed this to the prolactin-raising properties of antipsychotics. We did not find an association between the sedative and orthostatic hypotensive side effects and fracture risk in our analyses. One of the VEGFR inhibitor strengths of our study is the size of the study population (6,763 cases and 26,341 controls) and that it is representative for the general population of the Netherlands, although the absolute number of users of atypical antipsychotics was low. All prescribing information was collected routinely and we do not expect our findings to be Geneticin biased with regards to exposure status. Also, as fractures

invariably result in hospitalization, we are confident that cases, controls, and index dates were identified reliably. Nevertheless, given the observational nature of this study, the results should be interpreted with knowledge of its limitations. First, cases and controls were not matched on the period of observation available in the database and the results could be affected by information bias. However, the exclusion of patients with less than 1 year of follow-up did not affect the results substantially. Second, information about relevant diagnoses and co-morbidities may have been recorded upon hospitalization for a fracture and it is likely that the information available for cases was more complete and up-to-date than that available for controls. It could be argued that

we did not consider the use of bisphosphonates as a potential confounder. However, there should be a priori evidence, that a confounder is associated PDK4 both with antipsychotic exposure and hip fracture risk. As far as we know, there is no clear evidence that antipsychotic users are more likely to be exposed to bisphosphonates, compared to non-users. Moreover, in a case–control study, the use of bisphosphonates may act as an intermediate variable between exposure and outcome, rather than a confounder. This is supported by the positive association between bisphosphonate use and hip fracture (crude OR 1.71 [95% CI 1.47, 1.99], Table 2). Another potential limitation is the unavailability of data on smoking and alcohol consumption for a population that may include individuals with high levels of nicotine and/or alcohol consumption. Both are well-known risk factors of fracture risk [36, 37].

This application Wortmannin molecular weight might be useful for systems that are sensitive to genetically modified organisms according to (GMO)-rules. Conclusions Bacteriophage M13 is suitable for phage display not only with a modified gp3 but also with a modified gp9 which is a minor coat protein at the phage tip. The modified gp9 protein can be supplied in trans from a plasmid and fully complements an amber 9 phage mutant. The modified phage tip is very well accessible to specific antibodies. Methods Phage,

plasmid and bacterial strains M13 phage was from our lab collection [16]. M13am9 with an amber mutation in the second codon of gIX was constructed by site-directed mutagenesis [17]. For the construction of gp9-T7, gp9-DT7, gp9-HA and gp9-DHA RF-DNA of M13mp19 served as template for PCR amplification. DNA Damage inhibitor The PCR amplified gIX was subcloned into pMS119 [18] and an unique MunI restriction site was introduced by QuikChangeTM in vitro mutagenesis between the codons 2 and 3. Into this site RF-DNA of M13mp19 served as template for the amplification of gIX by PCR. The gIX fragment was subcloned into pMS119, DNA fragments LY2835219 clinical trial encoding the T7 and HA tag sequences were introduced by ligation, resulting in pMS-g9-T7 and pMS-g9-HA. Also, longer

epitopes were introduced to construct pMS-g9-DT7 and pMS-g9-DHA, respectively. For protein expression and complementation experiments E. coli K38 (HfrC T2R relA1 pit-10 about spoT1 tonA22 ompF627 phoA4 λ-) [19] was transformed as a non-suppressor strain. E. coli K37 (HfrC supD32 relA1 pit-10 spoT1 tonA22 ompF627 phoA4 T2R λ-) [19, 20] was used as a suppressor strain and E. coli JS7131 (MC1060 ΔyidC attB::R6Kori ParaBADyidC + Specr) as a depletion

strain of the membrane insertase YidC [4]. Complementation test of phage expressing modified gp9 proteins On agar plates 4 mL melted LB top agar (47°C) containing 1 mM IPTG was mixed with 500 μL of a fresh E. coli K38 overnight culture bearing either pMS-g9/7 pMS-g9-T7, pMS-g9-DT7, pMS-g9-HA or pMS-g9-DHA. After solidification of the top agar, 10 μL of a phage suspension was applied on top of the agar from serial dilutions of a phage stock. Plaque formation was observed after incubation at 37°C overnight. Expression of the modified gp9 proteins 2 mL cultures of E. coli K38 bearing plasmids encoding a respective gp9 variant were grown at 37°C to the early exponential phase in M9 minimal medium. Protein expression was induced by adding 1 mM IPTG and 10 min later the newly synthesised proteins were pulse-labelled for 10 min with 20 μCi 35S-methionine. To remove the non-incorporated 35S-methionine the total bacterial proteins were precipitated with 12% TCA on ice overnight, washed with cold acetone and resuspended in 10 mM Tris/HCl 2% SDS, pH 8.0.

Zinn KR, Chaudhuri TR, Szafran AA, O’Quinn D, Weaver C, Dugger K, Lamar D, Kesterson RA, Wang X, Frank SJ: Noninvasive bioluminescence imaging in small animals. ILAR J 2008, 49:103–115.PubMedCentralPubMedCrossRef Competing interests The authors declare that they have no competing interests. Authors’ contributions MJJ participated in study design, in vivo studies, data analysis, and manuscript drafting. CHA participated in study design, in vitro studies, data analysis, and manuscript drafting. HK and JWC participated in study design, and interpretation of data. IJC and SJ participated

in in vitro studies, and data analysis. YHK and HY participated in in vivo studies, and data acquisition. YlK participated in study design, in vivo studies, data analysis, and manuscript drafting, and critical revision of the manuscript. All authors read and approved the final manuscript. Funding This work was supported in part by the Basic Science Research Program find more through the

National Research SN-38 nmr Foundation of Korea funded by the Ministry of Education, Science and Technology (2011–0010250), and the Korean Health Technology R&D Project, Ministry of Health & Welfare, Republic of Korea (HI12C1148).”
“Background Pituitary adenomas (PAs) account for about 15% of intracranial tumors. Although PAs are mostly benign lesions, about 30-55% of them are confirmed to locally invasive, and some of them infiltrate dura, bone and sinuses, are designated highly 3-oxoacyl-(acyl-carrier-protein) reductase aggressive [1,2]. The conventional treatment of large pituitary adenomas consists of surgery, and radiotherapy when it is hard to achieve total resection. The use of additional radiotherapy is limited by the risk of radiation necrosis of surrounding structures. Thus, medication treatment, although unlikely to be curative immediately, might lead to certain clinically therapeutic effect, as a useful supplement [3]. Currently, first-line clinical medication for PAs generally consists of dopamine agonists (DAs), somatostatin

analogs (SSAs) or combinations [4]. Recently, some routine chemotherapeutics such as Temozolomide (TMZ) and Bevacizumab have been selleck inhibitor carefully studied to treat PAs and considered to be potential for aggressive PAs’ medical therapy [5-8]. DAs were widely used for the treatment of prolactinomas and some somatotropinomas, and the responsiveness depends on the expression of dopamine D2 receptors (D2R) on tumor cells. Abnormal expression of D2R in prolactinoma was considered to confer resistance to DA treatment. Fadul et al. [7] first reported two cases of pituitary carcinoma received TMZ treatment, concluding that TMZ may be effective in treating pituitary carcinomas. After that, more and more studies demonstrated the inspiring therapeutic effect of TMZ on pituitary carcinomas and aggressive PAs. As a DNA repairase, O6-methylguanine DNA methyltransferase (MGMT) confers chemoresistance to TMZ [9]. Thus, tumors with low expression of MGMT are usually sensitive to TMZ.

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