The tandem array multiple shRNAs expression vector contained four shRNA expression cassettes targeting two genes. In HCT116 cells, the

multiple shRNAs expression constructs could efficiently and simultaneously induce inhibition of RhoA and RhoC genes and markedly inhibit the invasion and migration potentials Paclitaxel order of cancer cells. The inhibitory effects of multiple shRNAs expression vectors were more effective than single shRNA expression vector (data not shown). Further research work is being done to evaluate the inhibition effects of multiple shRNAs expression vectors on nude mice. To our knowledge, this is the first study that 4-tandem shRNA construct targeting RhoA and RhoC genes was proved to be a successful approach in reducing the malignance of colorectal tumor cells. Recent accumulating evidences have shown that

co-expression PLX4032 manufacturer of multiple shRNAs can simultaneously inhibit multiple genes or target multiple sites on a single gene, which demonstrated that multiple shRNAs expression system could inhibit all six genes and was much more efficient in inducing apoptosis in PC3 cells [28]. Moreover, a tandem Ku-shRNA-encoding plasmid expression system can knock-down Ku70 and Ku80 at the same time [29]. Furthermore, the vector that expresses five shRNAs targeting on rat ventricular myocyte Kir2.1 gene in tandem is able to suppress the expression of Kir2.1 in rat ventricular myocytes [30]. All these results including ours implicate that such shRNA-induced in tandem RNA interference may be used for dissecting complex signaling pathways and even be applied to targeting multiple

Idoxuridine genes in cancer therapy. Acknowledgements This work was supported by grants from the Natural Scientific Foundation of Shandong Province (Grant code: 2006ZRB14274) and the Research Program of Qingdao South District Municipal Science and Technology Commission. References 1. Schoenwaelder SM, Burridge K: Bidirectional signalling between the cytoskeleton and integrins. Curr Opin Cell Biol 1999, 11: 274–286.PubMedCrossRef 2. Bar-Sagi D, Hall A: Ras and Rho GTPases: a family reunion. Cell 2000, 103: 227–238.PubMedCrossRef 3. Sahai E, Marshall CJ: RHO-GTPases and cancer. Nat Rev Cancer 2002, 2: 133–142.PubMedCrossRef 4. Takai Y, Sasaki T, Matozaki T: Small GTP-binding proteins. Physiol Rev 2001, 81: 153–208.PubMed 5. Horiuchi A, Imai T, Wang C, Ohira S, Feng Y, Nikaido T, Konishi I: Up-regulation of small GTPases, RhoA and RhoC, is associated with tumour progression in ovarian carcinoma. Lab Invest 2003, 83: 861–870.PubMed 6. Kamai T, Tsujii T, Arai K, Takagi K, Asami H, Ito Y, Oshima H: Significant association of Rho/ROCK pathway with invasion and metastasis of bladder cancer. Clin Cancer Res 2003, 9: 2632–2641.PubMed 7. Sun HW, Tong SL, He J, Wang Q, Zou L, Ma SJ, Tan HY, Luo JF, Wu HX: RhoA and RhoC-siRNA inhibit the proliferation and invasiveness activity of human gastric carcinoma by Rho/PI3K/Akt pathway. World J Gastroenterol 2007, 13: 3517–3522.PubMed 8.

Generally, local topography influences the distribution of palms (Kahn 1987), mainly indirectly through factors like soil conditions, disturbances, heterogeneity of the canopy, and biotic interactions (Svenning 2001). Indeed, the distribution of rattan palms in north Sulawesi seems to depend on topography (Clayton et al. 2002). On the other hand, a

more detailed survey in our study region only detected a relationship between the slope aspect and community composition of rattan palms, but neither directly with topographic position nor inclination (Getto 2009). Rattan palms occur on most types of rock and soil within their natural distribution area (Dransfield and Manokaran 1994). In fact, differences between upper lowland Compound Library and montane edaphic conditions in our study region do not appear to affect the rattan flora (Siebert BGB324 ic50 2005). Elevational ranges of rattan

species On average, rattan species in our study region had elevational range amplitudes of 515 m. This is likely an underestimate because not all elevations could be sampled and because it is likely that some species were not found in the study plots at elevations where they are not frequent. The gaps within the elevational ranges may likewise reflect the sampling methods which did not account for low population densities. In any case, an elevational range amplitude of 500 m is in accordance with previously documented range amplitudes of palms (400–1800 m) in Ecuador (Svenning et al. 2009). We observed a marked shift in species composition at around 1000 m, where many lowland species reached their upper and many montane species their lower distributional limits. Only eight species (23%) were recorded both below and above 1000 m. A similar elevational segregation at around 1000 m has been found among rattan palms in northern Borneo (Watanabe and Suzuki 2008). The shift from lowland dipterocarp forests to montane oak-laurel forests in Southeast Asia also occurs around 1000 m (Dransfield 1979), suggesting that this represents a fundamental vegetation limit in the region. Assemblage composition Overall, there was marked turnover in species composition between the study plots.

Over half of the 34 rattan species were Cepharanthine found in only one or two study sites. We found that elevation was the main factor accounting for shifts in species composition of rattan assemblages. A difference of more than 900 m in elevation led to a complete species turnover of rattan palms. This agrees well with data on bryophytes, ferns, and angiosperms from other tropical mountains, which typically show changes of about 10% per 100 m elevational shift (Kessler 2000a; Bach et al. 2007). In addition, geographical distances between study plots accounted for a considerable proportion in the change of species composition between plots. The similarity of tropical tree assemblages generally tends to decrease with the geographical distance (Condit et al. 2002; Duivenvoorden et al. 2002).

The resistance of metal/PCMO/Pt junctions was evaluated click here by three techniques: (1) current–voltage (I-V) characteristics, (2) resistance measurements after pulsed voltage application, and (3) Cole-Cole plots by impedance spectroscopy. The positive voltage is defined as the current flows from the top electrode to the PCMO film, and the negative bias was defined by the opposite direction. The resistance switching of the PCMO films was measured by applying a single positive electric pulse and a single negative electric pulse alternately

to the top electrode. The width of the electrical pulse was 500 ns. The resistance values were read out at 0.1 V after each pulse. Impedance spectroscopy was performed in the frequency range of 100 Hz to 5 MHz. The Liproxstatin-1 cost oscillatory amplitude for the impedance measurements was 50 mV. Results and discussion The I-V characteristics and resistance switching behaviors of the PCMO-based devices with various kinds of electrode metals were studied by direct current (dc) voltage sweep measurements to evaluate the electrode material dependence of the memory effects. Figure  1a shows the I-V characteristic of the Al/PCMO/Pt device. The inset magnifies the behavior near the origin. The Al/PCMO/Pt device

has nonlinear and asymmetric I-V relations with hysteresis loops, resulting in resistance memory effect with high and low resistance states during the forward and backward sweeping of the voltage. By increasing the negative voltages, the switching from

the high resistance state to the low resistance state occurred. Subsequently, an opposite process was observed by sweeping the voltage reversely to positive values. The resistance change of the PCMO films was measured by applying electric CYTH4 pulses. Figure  1b shows the resistance switching in the Al/PCMO/Pt device. The pulse amplitude was 8 V. The positive or negative pulse reversibly switched the resistance of the PCMO films between the high resistance state and the low resistance state; the nonvolatile switching was achieved. Figure 1 I – V curves and resistance switching behavior of the Al/PCMO/Pt device. (a) I-V curves of the Al/PCMO/Pt device. The inset magnifies the behavior near the origin. (b) Resistance switching behavior of the Al/PCMO/Pt device. Figure  2a shows I-V characteristics in the initial state of the Ni/PCMO/Pt device. The I-V characteristics exhibited no hysteretic behavior. After adding an electric pulse of 5 V, however, the resistance of the device was decreased, and a hysteretic behavior shown in Figure  2b was observed. An increase in the negative voltages switched the high resistance state to the low resistance state with a negative differential resistance. Figure  2c shows the resistance switching in the Ni/PCMO/Pt device. The amplitude of the applied pulses was 5 V. The switching from the high resistance state to the low resistance state occurred.

Thirty healthy subjects, 50% male and 50% female, were randomized into 45, 90, and 180 μg dose groups (ten subjects in each) for the determination of the pharmacokinetic profile of a single-dose BCQB by the investigator. Another ten subjects, 50% male A-769662 clinical trial and 50% female, were administrated 120 μg of BCQB by intranasal sprays on day 1; received no treatment on day 2; and continued to receive the study drug three times daily (at 7:30am, 12:00pm and 7:00pm) from days 3 through 7 to assess multiple-dose

pharmacokinetics (see table II). The subjects were required to fast overnight (12 hours) before administration, while standard meals and water intake were provided 2 hours post-dose. Blood samples (5 mL) were collected at 0 hours (pre-dose), 2, 5, 10, 15, 30 minutes, 1, 2, 3, 5, 7, 12, 24, and 48 hours post-dose

for the single-dose study. For the www.selleckchem.com/products/Roscovitine.html multiple-dose study, blood samples (5 mL) were collected prior to dosing on days 1, 5, 6, and 7 (0 hours prior to dosing) and 2, 5, 10, 15, 30 minutes, 1, 2, 3, 5, 7, 9, 12, 15, 24, and 36 hours post-dose on day 1 and day 7. Plasma was separated and stored at −20°C for analysis. Urine samples were collected at 0 hours (pre-dose), 0–2, 2–4, 4–6, 6–8, 8–10, 10–12, 12–24, 24–36, and 36–48 hours post-dose for the single-dose study. The total volume of urine in each time interval was recorded and stored at −20°C for analysis. Safety Monitoring Throughout the study, all subjects remained in the study unit under continuous observation. Details of adverse events (AEs) were obtained and recorded by the study physicians.

Routine safety and tolerability were evaluated through AE reporting Orotidine 5′-phosphate decarboxylase by the investigators and subjects, on the basis of vital signs, physical examination, laboratory examination (routine blood, urine and feces test, occult blood test and blood biochemical test) and ECG, which were performed at scheduled intervals during the studies. AEs that occurred during the study were classified as mild (awareness of a sign or symptom but comfortably tolerated), moderate (discomfort that may interfere with daily activities) or serious (death, life-threatening, requiring hospitalization or incapacitating). AEs were recorded and reported according to GCP. Pharmacokinetic Measurement The concentrations of BCQB in plasma and urine were determined by validated liquid chromatography-mass spectrometry methods,[20,21] . The lower limit of quantitation (LLOQ) of BCQB in plasma was 5 pg/mL, while in urine it was 0.02 ng/mL. The pharmacokinetic parameters were calculated by WinNonlin Professional software (Version 6.1, Pharsight Corporation, Mountain View, CA, USA) using non-compartmental methods.

As the standard of care for stage G3b-5 CKD, we recommend that patients be encouraged to lower their dietary protein intake to 0.6–0.8 g/kg·standard body weight (SBW)/day. Actual protein intake should be estimated by analyzing the urea content in the 24-h urine sample using the Maroni formula; it should then be evaluated by comparing it with the results of previously published studies, which showed that the achieved protein intakes were 0.75–0.9 g/kg/day in clinical trials with protein restriction of 0.6–0.8 g/kg/day. Several studies also demonstrated both the efficacy and potential hazards of a very low protein diet. Therefore, the potential

benefits selleck inhibitor and risks of severe protein restriction should be specifically assessed for each patient. Digestibility and the amino acid score of protein sources should be taken into consideration when prescribing protein restriction diets. For early CKD with the risk of progression, we suggest encouraging patients to lower their protein intake to 0.8–1.0 g/kg·SBW/day. The extent of protein restriction should be individualized in accordance with each patient’s specific clinical condition, including severity, risk of progression, nutritional status, and adherence. Bibliography 1. Pan Y, et al. Am J Clin Nutr. 2008;88:660–6. (Level 1)   2. Gansevoort RT, et al. Nephrol Dial Transplant. 1995;10:497–504. (Level 3)

  3. Williams PS, et al. Q J Med. 1991;81:837–55. (Level selleck 2)   4. D’Amico G, et al. Nephrol Dial Transplant. 1994;9:1590–4. (Level 2)   5. Mircescu G, et al. J Ren Nutr. 2007;17:179–88. (Level 2)   6. Rosman JB, et al. Kidney Int Suppl. 1989;27:S96–102. (Level 2)   7. Cianciaruso B, et al. Am J Kidney Dis. 2009;54:1052–61. (Level 2)   8. Fouque D, et al. Cochrane Database Syst Rev. 2009:CD001892. (Level 1)   9. Pedrini MT, et al. Ann Intern Med. 1996;124:627–32. (Level 1)   10. Hansen HP, et al. Kidney Int. 2002;62:220–8. (Level 2)   11. Kasiske BL, et al. Am J Kidney Dis. 1998;31:954–61. (Level 1)   12. Robertson L, et al. Cochrane Database Syst Rev. 2007;CD002181.

RAS p21 protein activator 1 (Level 1)   13. Koya D, et al. Diabetologia. 2009;52:2037–45. (Level 2)   14. Feiten SF, et al. Eur J Clin Nutr. 2005;59:129–36. (Level 2)   15. Jungers P, et al. Kidney Int. 1987;22(Suppl):S67–71. (Level 2)   16. Cianciaruso B, et al. Nephrol Dial Transplant. 2008;23:636–44. (Level 2)   17. Malvy D, et al. J Am Coll Nutr. 1999;18:481–6. (Level 2)   18. Di Iorio BR, et al. Kidney Int. 2003;64:1822–8. (Level 2)   19. Ihle BU, et al. N Engl J Med. 1989;321:1773–7. (Level 2)   20. Levey AS, et al. Am J Kidney Dis. 1996;27:652–63. (Level 4)   21. Zeller K, et al. N Engl J Med. 1991;324:78–84. (Level 2)   22. Klahr S, et al. J Am Soc Nephrol. 1995;5:2037–47. (Level 3)   23. Walser M, et al. Am J Kidney Dis. 1996;28:354–64. (Level 5)   24. Chauveau P, et al. J Ren Nutr. 2007;17:250–7.

(Bertrand et al. 2008). We present the different preparation steps of samples for the EXPOSE missions and the first analytical results of the ground experiments. Barbier. B., Chabin, A., Chaput, D., and Brack, A. (1998). Photochemical processing of amino acids in Earth orbit. Planet. Space Sci., 46: 391–398. Barbier, B., Henin, O., Boillot, F., Chabin, A., Chaput, D., and Brack, A. (2002) Exposure of amino acids and derivatives in the Earth orbit. Planet. Space Sci., 50:353–359. Bertrand,

M., Chabin, A., Brack and Westall, F. (2008) Separation of amino acid enantiomers VIA chiral derivatization and non-chiral gas chromatography. Journal of Chromatography, A 1180: 131–137. Boillot, F., Chabin, A., Buré, C., Venet, M., Belsky, click here A., Bertrand-Urbaniak, M., Delmas, A., Brack, A., and Barbier, B. (2002) The Perseus Exobiology Mission on MIR: Behaviour of amino acids and peptides in Earth orbit. Origins of Life and Evolution of the Biosphere, 32: 359–385. Cottin, HDAC activity assay H., Coll, P., Coscia, D., Fray,; N., Guan, Y.Y., Macari, F., Raulin, F., Rivron, C., Stalport, F., Szopa, C., Chaput,

D., Viso, M., Bertrand, M., Chabin, A., Thirkell, L., Westall, F., and Brack A, (in press) Heterogenous solid/gas chemistry of organic compounds related to comets, meteorites, Titan, and Mars: Laboratory and in lower Earth orbit experiments. To appear in the Adv. Space Res. E-mail: annie.​chabin@cnrs-orleans.​fr Experimental Fossilization Induced in Modern Microbial Mats Elizabeth Chacón B1, Mariajose Peña1, Felipe Torres de la Cruz1, A. Negrón-Mendoza2 1Facultad de Ciencias de la Tierra, UANL; 2Instituto de Ciencias Nucleares, UNAM Microbial

fossilization is a key geobiological process to understand the sedimentary record and to design new strategies in the extraterrestrial life search. Although several analysis have been proposed to identify and describe in situ fossilization of different types of microorganisms (Jones et al 1999; Westfall et al 2001), the many factors involved in this complex process still wait for elucidation. By far, the most common microbial fossil preservation process is by silicification, as during the numerous ancient cyanobacterial microfossils from Precambrian strata testify. Other less common fossilization processes include phosphate and carbonate replacement. Among the main factors inducing fossilization are a rapid lithification, a rapid burial after cell death, cooling and evaporation of supersaturated mineral waters (mainly in the case of silicification) as well as the biological mediation on the nucleation of specific minerals input from the environment (Konhauser et al 2001). Previous works have suggested that biological organic matter mediates biomineralization; in contrast, other recent observations indicate that mineralization of cyanobacteria is an inorganically controlled process, induced by rapid cooling and evaporation of the spring waters, occurring independent of microorganisms.

J Med Entomol 1998, 35:222–226.PubMed 11. Jadin J,

Vincke IH, Dunjic A, Delville JP, Wery M, Bafort J, Scheepers-Biva M: Role of Pseudomonas in the sporogenesis of the hematozoon of malaria in the mosquito. Bull Soc Pathol Exot Filiales 1966, 59:514–525.PubMed 12. Gonzalez-Ceron L, Santillan F, Rodriguez MH, Mendez D, Hernandez-Avila JE: Bacteria in midguts of field-collected Anopheles albimanus block Plasmodium vivax sporogonic development. J Med Entomol 2003, 40:371–374.PubMedCrossRef 13. Briones AM, Shililu J, Githure J, Novak R, Ras L:Thorsellia anophelis is the dominant bacterium in a Kenyan population of adult CP690550 Anopheles gambiae mosquitoes. The ISME Journal 2008, 2:74–82.PubMedCrossRef 14. Favia G, Ricci I, Damiani C, Raddadi N, Crotti E, Marzorati M, Rizzi A, Urso R, Brusetti L, Borin S, Mora D, Scuppa P, Pasqualini L, Clementi E, Genchi M, Corona S, Negri I, Grandi G, Alma A, Kramer L, Esposito https://www.selleckchem.com/products/Lapatinib-Ditosylate.html F, Bandi C, Sacchi L, Daffonchio D: Bacteria

of the genus Asaia stably associate with Anopheles stephensi , an Asian malarial mosquito vector. Proc Natl Acad Sci USA 2007, 104:9047–9051.PubMedCrossRef 15. Seitz HM, Maier WA, Rottok M, Becker-Feldmann H: Concomitant infections of Anopheles stephensi with Plasmodium berghei and Serratia marcescens : additive detrimental effects. Zentralbl Bakteriol Hyg 1987, 266:155–166. 16. Lindh JM, Terenius O, Faye I: 16S rRNA Gene-Based Identification of Midgut Bacteria from Field-Caught Anopheles gambiae sensu lato and A. funestus mosquitoes reveals new species related to known insect symbionts. Appl

Environ Microbiol 2005, 71:7217–7223.PubMedCrossRef 17. Lozupone CA, Knight R: Global patterns Depsipeptide in vitro in bacterial diversity. Proc Natl Acad Sci USA 2007, 104:11436–11440.PubMedCrossRef 18. Magurran AE:Ecological diversity and its measurement. Prinston University Press, Prinston, NJ 1998. 19. Durvasula RV, Gumbs A, Panackal A, Kruglov O, Aksoy S, Merrifield RB, Richards FF, Beard CB: Prevention of insect borne diseases: an approach using transgenic symbiotic bacteria. Proc Natl Acad Sci USA 1997, 94:3274–3278.PubMedCrossRef 20. Beard CB, Durvasula RV, Richards FF: Bacterial symbiosis in arthropods and the control of disease transmission. Emerg Infect Dis 1998, 4:581–591.PubMedCrossRef 21. Marzorati M, Alma A, Sacchi L, Pajoro M, Palermo S, Brusetti L, Raddadi N, Balloi A, Tedeschi R, Clementi E, Corona S, Quaglino F, Bianco PA, Beninati T, Bandi C, Daffonchio D: A novel bacteroidetes symbiont is localized in Scaphoideus titanus , the insect vector of Flavescence Doree in Vitis vinifera. Appl Environ Microbiol 2006, 72:1467–1475.PubMedCrossRef 22. Zabalou S, Riegler M, Theodorakopoulou M, Stauffer C, Savakis C, Bourtzis K:Wolbachia -induced cytoplasmic incompatibility as a means for insect pest population control. Proc Natl Acad Sci USA 2004, 101:15042–15045.PubMedCrossRef 23.

As seen in Figure 5, the cleavage sites in the mRNA, which was purified from the cells with over-expression of the nucleases MqsR and HicA, are distributed all over the operon. Several specific cutting sites of the MazF nuclease are found in the RelB-encoding part. No cleavage is detected in response to production of the protein kinase HipA, as expected. Most of the cutting sites were unique for each toxin indicating that the cleavage in vivo was a result of primary activity of the over-produced toxin. RNA from MazF and MqsR over-expression samples was mostly cleaved at the specific cutting sites of these toxins, i.e. ACA [51] and GCU

[16]. However, selleck chemicals llc several unique cleavage sites in the MazF and MqsR over-expression samples do not contain these sequences and might be generated by MAPK inhibitor unidentified ribonuclease(s), possibly cross-activated toxins (Additional file 1: Table S3). We also observed that not all ACA and GCU sequences were cleaved in the relBEF mRNA by MazF and MqsR, respectively.

As before [19], the cleavage preferences of HicA could not be identified. Figure 5 Cleavage of the relBEF mRNA in vivo . The same RNA samples that were analyzed by northern blotting (Figure 1) were subjected to primer extension analysis shown in (Additional file 1: Figure S4). Detected 5′ ends, localization of the extension primers and hybridization probes are mapped on to the relBEF operon. Dotted lines mark cleavage sites that occur in response to several over-produced toxins. The gray bar indicates the region where detection of the cleavage sites in the relBEF mRNA was Amobarbital impossible owing to the plasmidal relE mRNA transcribed from pVK11. To confirm our notion of TA cross-activation, we hoped to see

some cleavage hotspots. At those sites, strong cleavage by an overproduced toxin occurs at its specific cutting sequence (e.g. ACA in the case of MazF). Cleavage at the same site in response to expression of another toxin would indicate activation of the primary cutter by the over-produced toxin. We tested possible cross-activation at three of these sites. At position 174 (ˇACA), the relBEF transcript is cut by MazF and in response to the over-produced HicA. The MqsR-specific cleavage sites at positions 399 (GCˇU) and 431 (GˇCU) are also cleaved in the samples from HicA over-production (Additional file 1: Figure S4). We found that these cuts were not due to the activation of MazF and MqsR, since they occurred in RNA extracted from the BW25113ΔmazEF and BW25113ΔmqsRA cells (data not shown). ChpBK, a homolog of MazF with similar but relaxed sequence specificity [52] may be accountable for the cleavage at 174 (ˇACA).

Acknowledgements We thank Alistair Graham for providing NSCLC sections, Stewart Church for assistance with phase-contrast microscopy and the Northern Ireland Leukaemia Research Fund for financial support. Electronic supplementary material Additional file 1: Loss of UCH-L1 expression did not affect cell proliferation of H838 cells. CyQUANT® assays were performed at two different time points of 24 and 48 hr post-transfection with UCH-L1

siRNA in H838 cells. The results from 3 experiments are shown graphically. Statistical analysis showed no significant difference between UCH-L1 siRNA-treated and controls. (TIFF 444 KB) Additional file 2: Kaplan-Meier analysis in the GSE13213 dataset based on UCH-L1 expression. A. Kaplan-Meier analysis for patients separated into above and below the median of UCH-L1 expression in the GSE13213 dataset. B Kaplan-Meier analysis PD98059 mw for patients separated into quartiles Y-27632 research buy based on UCH-L1 expression. The first and fourth quartiles are included in the graph. The UCH-L1 gene is represented by a single probe (A-23P132956). (TIFF 101 KB) Additional file 3: Kaplan-Meier analysis in the GSE3141 dataset based on UCH-L1 expression represented by probesets 1555834_at and 201387_s_at. A. Kaplan-Meier analysis for patients separated into above and below the median expression of UCH-L1 based on probeset 1555834_at signal intensities. B. Kaplan-Meier analysis for patients separated into quartiles based

on UCH-L1 expression represented by probeset 1555834_at. The first and fourth quartiles are included in the graph. C. Kaplan-Meier analysis for patients separated into above and below the median expression of UCH-L1 based on probeset Ceramide glucosyltransferase 201387_s_at signal intensities. D. Kaplan-Meier analysis for patients separated into quartiles based on UCH-L1 expression represented by 201387_s_at. The first and fourth quartiles are included in the graph. (TIFF 190 KB) Additional file 4: Kaplan-Meier analysis in the GSE8894 dataset based on UCHL-1 expression represented by 2 probesets 1555834_at and 201387_s_at. A. Kaplan-Meier analysis for patients separated into above

and below the median expression of UCH-L1 based on probeset 1555834_at signal intensities. B. Kaplan-Meier analysis for patients separated into quartiles based on UCH-L1 expression represented by probeset 1555834_at. The first and fourth quartiles are included in the graph. C. Kaplan-Meier analysis for patients separated into above and below the median expression of UCH-L1 based on probeset 201387_s_at signal intensities. D. Kaplan-Meier analysis for patients separated into quartiles based on UCH-L1 expression represented by 201387_s_at. The first and fourth quartiles are included in the graph. (TIFF 204 KB) References 1. Mani A, Gelmann EP: The ubiquitin-proteasome pathway and its role in cancer. J Clin Oncol 2005, 23:4776–4789.PubMedCrossRef 2. Mukhopadhyay D, Riezman H: Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science 2007, 315:201–205.

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